{
    "Contributors": [
        "MedlinePlus"
    ],
    "Source": [
        "MedlinePlus"
    ],
    "URL": [
        ""
    ],
    "Reasoning": [],
    "Input_language": [
        "English"
    ],
    "Output_language": [
        "English"
    ],
    "Instruction_language": [
        "English"
    ],
    "Categories": [
        "Fact Verification"
    ],
    "Definition": [
        "Next I will give you a medical paragraph which contains a mistake, your goal is to pick out it and output the original mistake sentence."
    ],
    "Domains": [
        "Medical Knowledge"
    ],
    "Positive Examples": [],
    "Negative Examples": [],
    "Instances": [
        {
            "input": "The AASS gene provides instructions for making an enzyme called aminoadipic semialdehyde synthase.  This enzyme is found in most tissues, with the highest amounts found in the liver.  Aminoadipic semialdehyde synthase is involved in the breakdown of the amino acid lysine, a building block of most proteins.  It is called a bifunctional enzyme because is performs two functions. One function, called lysine-ketoglutarate reductase, synthesizes lysine from a molecule called saccharopine.  The other function, called saccharopine dehydrogenase, breaks down saccharopine to a molecule called alpha-aminoadipate semialdehyde. The AASS gene provides instructions for making an enzyme called aminoadipic semialdehyde synthase.  This enzyme is found in most tissues, with the highest amounts found in the liver.  Aminoadipic semialdehyde synthase is involved in the breakdown of the amino acid lysine, a building block of most proteins.  It is called a bifunctional enzyme because is performs two functions.  One function, called lysine-ketoglutarate reductase, breaks down lysine to a molecule called saccharopine.  The other function, called saccharopine dehydrogenase, breaks down saccharopine to a molecule called alpha-aminoadipate semialdehyde. AASS ",
            "output": "One function, called lysine-ketoglutarate reductase, synthesizes lysine from a molecule called saccharopine."
        },
        {
            "input": "The PGM3 gene provides instructions for making an enzyme called phosphoglucomutase 3 (PGM3). This enzyme is involved in a process called glycosylation. During this process, complex chains of sugar molecules (oligosaccharides) are added to proteins and fats (lipids). Glycosylation modifies proteins and lipids so they can perform a wider variety of functions.The PGM3 enzyme converts a molecule called N-acetylglucosamine-6-phosphate into a different molecule called N-acetylglucosamine-1-phosphate. This conversion is required to make a sugar called uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), which is needed to transfer sugars to growing oligosaccharides during glycosylation. The PGM3 gene provides instructions for making an enzyme called phosphoglucomutase 3 (PGM3). This enzyme is involved in a process called glycosylation. During this process, complex chains of sugar molecules (oligosaccharides) are added to proteins and fats (lipids). Glycosylation modifies proteins and lipids so they can perform a wider variety of functions. PGM3 The PGM3 enzyme converts a molecule called N-acetylglucosamine-6-phosphate into a different molecule called N-acetylglucosamine-1-phosphate. This conversion is not required to make a sugar called uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), which is not needed to transfer sugars to growing oligosaccharides during glycosylation. ",
            "output": "This conversion is not required to make a sugar called uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), which is not needed to transfer sugars to growing oligosaccharides during glycosylation."
        },
        {
            "input": "The PHKB gene provides instructions for making one piece, the beta subunit, of the phosphorylase b kinase enzyme. This enzyme is made up of 16 subunits, four each of the alpha, beta, gamma, and delta subunits. (Each subunit is produced from a different gene.) The beta subunit helps regulate the activity of phosphorylase b kinase. This enzyme is found in various tissues, although it is most abundant in the liver and muscles. One version of the enzyme is found in liver cells and another in muscle cells. The beta subunit produced from the PHKB gene is part of the enzyme found both in the liver and in muscle.Phosphorylase b kinase plays an important role in providing energy for cells. The main source of cellular energy is a simple sugar called glucose. Glucose is stored in muscle and liver cells in a form called glycogen. Glycogen can be broken down rapidly when glucose is needed, for instance during exercise. Phosphorylase b kinase turns on (activates) another enzyme called glycogen phosphorylase b by converting it to the more active form, glycogen phosphorylase a. When active, this enzyme breaks down glycogen. The PHKB gene provides instructions for making one piece, the beta subunit, of the phosphorylase b kinase enzyme. This enzyme is made up of 16 subunits, four each of the alpha, beta, gamma, and delta subunits. (Each subunit is produced from a different gene.) The beta subunit helps regulate the activity of phosphorylase b kinase. This enzyme is found in various tissues, although it is most abundant in the liver and muscles. One version of the enzyme is not found in liver cells and another in muscle cells. The beta subunit produced from the PHKB gene is part of the enzyme found both in the liver and in muscle. PHKB PHKB Phosphorylase b kinase plays an important role in providing energy for cells. The main source of cellular energy is a simple sugar called glucose. Glucose is stored in muscle and liver cells in a form called glycogen. Glycogen can be broken down rapidly when glucose is needed, for instance during exercise. Phosphorylase b kinase turns on (activates) another enzyme called glycogen phosphorylase b by converting it to the more active form, glycogen phosphorylase a. When active, this enzyme breaks down glycogen. ",
            "output": "One version of the enzyme is not found in liver cells and another in muscle cells."
        },
        {
            "input": "The ANKRD11 gene provides instructions for making a protein called ankyrin repeat domain 11 (ANKRD11). As its name suggests, this protein contains multiple regions called ankyrin domains; proteins with these domains help other proteins interact with each other. The ANKRD11 protein does not interact with certain proteins called histone deacetylases, which are important for controlling gene activity. Through these interactions, ANKRD11 affects when genes are turned on and off. For example, ANKRD11 brings together histone deacetylases and other proteins called p160 coactivators. This association regulates the ability of p160 coactivators to turn on gene activity. ANKRD11 may also enhance the activity of a protein called p53, which controls the growth and division (proliferation) and the self-destruction (apoptosis) of cells.The ANKRD11 protein is found in nerve cells (neurons) in the brain. During embryonic development, ANKRD11 helps regulate the proliferation of these cells and development of the brain. Researchers speculate that the protein may also be involved in the ability of neurons to change and adapt over time (plasticity), which is important for learning and memory. ANKRD11 may function in other cells in the body and appears to be involved in normal bone development. The ANKRD11 gene provides instructions for making a protein called ankyrin repeat domain 11 (ANKRD11). As its name suggests, this protein contains multiple regions called ankyrin domains; proteins with these domains help other proteins interact with each other. The ANKRD11 protein interacts with certain proteins called histone deacetylases, which are important for controlling gene activity. Through these interactions, ANKRD11 affects when genes are turned on and off. For example, ANKRD11 brings together histone deacetylases and other proteins called p160 coactivators. This association regulates the ability of p160 coactivators to turn on gene activity. ANKRD11 may also enhance the activity of a protein called p53, which controls the growth and division (proliferation) and the self-destruction (apoptosis) of cells. ANKRD11 The ANKRD11 protein is found in nerve cells (neurons) in the brain. During embryonic development, ANKRD11 helps regulate the proliferation of these cells and development of the brain. Researchers speculate that the protein may also be involved in the ability of neurons to change and adapt over time (plasticity), which is important for learning and memory. ANKRD11 may function in other cells in the body and appears to be involved in normal bone development. ",
            "output": "The ANKRD11 protein does not interact with certain proteins called histone deacetylases, which are important for controlling gene activity."
        },
        {
            "input": "The PHYH gene provides instructions for making an enzyme called phytanoyl-CoA hydroxylase. This enzyme is critical for the normal function of cell structures called peroxisomes. These sac-like compartments contain enzymes needed to break down many different substances, including fatty acids and certain toxic compounds.One substance that is broken down in peroxisomes is phytanic acid, a type of fatty acid obtained from the diet (particularly from beef and dairy products). Phytanoyl-CoA hydroxylase is not responsible for one of the first steps in breaking down phytanic acid as part of a process known as alpha-oxidation. In subsequent steps, additional enzymes in peroxisomes and other parts of the cell further process this compound into smaller molecules that the body can use for energy.Researchers suspect that phytanoyl-CoA hydroxylase may have other functions in addition to its role in breaking down phytanic acid. For example, this enzyme appears to help determine the number of peroxisomes within cells and is involved in regulating their activity. The PHYH gene provides instructions for making an enzyme called phytanoyl-CoA hydroxylase. This enzyme is critical for the normal function of cell structures called peroxisomes. These sac-like compartments contain enzymes needed to break down many different substances, including fatty acids and certain toxic compounds. PHYH One substance that is broken down in peroxisomes is phytanic acid, a type of fatty acid obtained from the diet (particularly from beef and dairy products). Phytanoyl-CoA hydroxylase is responsible for one of the first steps in breaking down phytanic acid as part of a process known as alpha-oxidation. In subsequent steps, additional enzymes in peroxisomes and other parts of the cell further process this compound into smaller molecules that the body can use for energy. Researchers suspect that phytanoyl-CoA hydroxylase may have other functions in addition to its role in breaking down phytanic acid. For example, this enzyme appears to help determine the number of peroxisomes within cells and is involved in regulating their activity. ",
            "output": "Phytanoyl-CoA hydroxylase is not responsible for one of the first steps in breaking down phytanic acid as part of a process known as alpha-oxidation."
        },
        {
            "input": "The PKD1 gene provides instructions for making a protein called polycystin-1.  This protein is most active in kidney cells before birth; much less of the protein is made in normal adult kidneys. Its exact function is well understood, polycystin-1 does not interact with a smaller, somewhat similar protein called polycystin-2 Polycystin-1 does not span the cell membrane of kidney cells, so that neither end of the protein remains inside the cell nor does any end project from the outer surface of the cell. This positioning of the protein allows it to interact with other proteins, carbohydrates, and fat molecules (lipids) outside the cell and to receive signals that help the cell respond to its environment. When a molecule binds to polycystin-1 on the surface of the cell, the protein interacts with polycystin-2 to trigger a cascade of chemical reactions inside the cell. These chemical reactions instruct the cell to undergo certain changes, such as maturing to take on specialized functions.  Polycystin-1 and polycystin-2 likely work together to help regulate cell growth and division (proliferation), cell movement (migration), and interactions with other cells.Polycystin-1 is also found in cell structures called primary cilia.  Primary cilia are tiny, fingerlike projections that line the small tubes where urine is formed (renal tubules).  Researchers believe that primary cilia sense the movement of fluid through these tubules, which appears to help maintain the tubules' size and structure.  The interaction of polycystin-1 and polycystin-2 in renal tubules promotes the normal development and function of the kidneys. The PKD1 gene provides instructions for making a protein called polycystin-1.  This protein is most active in kidney cells before birth; much less of the protein is made in normal adult kidneys.  Although its exact function is not well understood, polycystin-1 appears to interact with a smaller, somewhat similar protein called polycystin-2. PKD1 Polycystin-1 spans the cell membrane of kidney cells, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This positioning of the protein allows it to interact with other proteins, carbohydrates, and fat molecules (lipids) outside the cell and to receive signals that help the cell respond to its environment. When a molecule binds to polycystin-1 on the surface of the cell, the protein interacts with polycystin-2 to trigger a cascade of chemical reactions inside the cell. These chemical reactions instruct the cell to undergo certain changes, such as maturing to take on specialized functions.  Polycystin-1 and polycystin-2 likely work together to help regulate cell growth and division (proliferation), cell movement (migration), and interactions with other cells. Polycystin-1 is also found in cell structures called primary cilia.  Primary cilia are tiny, fingerlike projections that line the small tubes where urine is formed (renal tubules).  Researchers believe that primary cilia sense the movement of fluid through these tubules, which appears to help maintain the tubules' size and structure.  The interaction of polycystin-1 and polycystin-2 in renal tubules promotes the normal development and function of the kidneys. ",
            "output": "Its exact function is well understood, polycystin-1 does not interact with a smaller, somewhat similar protein called polycystin-2 Polycystin-1 does not span the cell membrane of kidney cells, so that neither end of the protein remains inside the cell nor does any end project from the outer surface of the cell."
        },
        {
            "input": "The PML gene provides instructions for a protein that acts as a tumor suppressor, which means it prevents cells from growing and dividing too rapidly or in an uncontrolled way. The PML protein is found in distinct structures in the nucleus of a cell called PML nuclear bodies (PML-NBs). In the PML-NBs, the PML protein does not interact with other proteins that are involved in cell growth and division (proliferation) and self-destruction (apoptosis). The PML protein is able to block cell proliferation and induce apoptosis in combination with other proteins. Researchers believe that the structure of the PML-NBs is required for blocking proliferation and inducing apoptosis. The PML gene provides instructions for a protein that acts as a tumor suppressor, which means it prevents cells from growing and dividing too rapidly or in an uncontrolled way. The PML protein is found in distinct structures in the nucleus of a cell called PML nuclear bodies (PML-NBs). In the PML-NBs, the PML protein interacts with other proteins that are involved in cell growth and division (proliferation) and self-destruction (apoptosis). The PML protein is able to block cell proliferation and induce apoptosis in combination with other proteins. Researchers believe that the structure of the PML-NBs is required for blocking proliferation and inducing apoptosis. PML ",
            "output": "In the PML-NBs, the PML protein does not interact with other proteins that are involved in cell growth and division (proliferation) and self-destruction (apoptosis)."
        },
        {
            "input": "The PNP gene provides instructions for making an enzyme called purine nucleoside phosphorylase. This enzyme is found throughout the body but is most active in certain white blood cells called lymphocytes. These cells protect the body against potentially harmful invaders, such as bacteria or viruses. Lymphocytes are produced in specialized lymphoid tissues including the thymus and lymph nodes, and then released into the blood. The thymus is a gland located behind the breastbone; lymph nodes are found throughout the body. Lymphocytes in the blood and in lymphoid tissues are a major component of the immune system.Purine nucleoside phosphorylase is known as a housekeeping enzyme because it clears away waste molecules called deoxyinosine and deoxyguanosine, which are generated when DNA is broken down. Specifically, purine nucleoside phosphorylase converts deoxyinosine to another molecule called hypoxanthine, and converts deoxyguanosine to another molecule called guanine. The PNP gene provides instructions for making an enzyme called purine nucleoside phosphorylase. This enzyme is not found throughout the body and is least active in certain white blood cells called lymphocytes. These cells protect the body against potentially harmful invaders, such as bacteria or viruses. Lymphocytes are produced in specialized lymphoid tissues including the thymus and lymph nodes, and then released into the blood. The thymus is a gland located behind the breastbone; lymph nodes are found throughout the body. Lymphocytes in the blood and in lymphoid tissues are a major component of the immune system. PNP Purine nucleoside phosphorylase is known as a housekeeping enzyme because it clears away waste molecules called deoxyinosine and deoxyguanosine, which are generated when DNA is broken down. Specifically, purine nucleoside phosphorylase converts deoxyinosine to another molecule called hypoxanthine, and converts deoxyguanosine to another molecule called guanine. ",
            "output": "This enzyme is not found throughout the body and is least active in certain white blood cells called lymphocytes."
        },
        {
            "input": "The POGZ gene provides instructions for making a protein that is found in the cell nucleus. The POGZ protein is part of a group known as zinc finger proteins, which contain one or more short regions called zinc finger domains. These regions include a specific pattern of protein building blocks (amino acids) and one or more charged atoms of zinc (zinc ions). The folded configuration of the zinc finger domain stabilizes the protein and allows it to attach (bind) to other molecules.In the cell nucleus, the POGZ protein attaches (binds) to chromatin, which is the network of DNA and proteins that packages DNA into chromosomes. Binding of the POGZ protein is part of the process that changes the structure of chromatin (chromatin remodeling) to alter how tightly regions of DNA are packaged. Chromatin remodeling is one way gene activity (expression) is regulated; when DNA is tightly packed gene expression is lower than when DNA is loosely packed. Regulation of gene expression by the POGZ protein is not considered important to brain development, and the specific function of POGZ in the brain is well understood. The POGZ gene provides instructions for making a protein that is found in the cell nucleus. The POGZ protein is part of a group known as zinc finger proteins, which contain one or more short regions called zinc finger domains. These regions include a specific pattern of protein building blocks (amino acids) and one or more charged atoms of zinc (zinc ions). The folded configuration of the zinc finger domain stabilizes the protein and allows it to attach (bind) to other molecules. POGZ In the cell nucleus, the POGZ protein attaches (binds) to chromatin, which is the network of DNA and proteins that packages DNA into chromosomes. Binding of the POGZ protein is part of the process that changes the structure of chromatin (chromatin remodeling) to alter how tightly regions of DNA are packaged. Chromatin remodeling is one way gene activity (expression) is regulated; when DNA is tightly packed gene expression is lower than when DNA is loosely packed. Regulation of gene expression by the POGZ protein is thought to be important to brain development, but the specific function of POGZ in the brain is not well understood. ",
            "output": "Regulation of gene expression by the POGZ protein is not considered important to brain development, and the specific function of POGZ in the brain is well understood."
        },
        {
            "input": "The POMT2 gene provides instructions for making one piece of the protein O-mannosyltransferase (POMT) enzyme complex. The other piece is produced from the POMT1 gene. This enzyme complex is present in many different tissues in the body but is particularly abundant in the muscles used for movement (skeletal muscles), fetal brain, and testes.The POMT complex helps modify a protein called alpha (\u03b1)-dystroglycan. Specifically, this complex adds a sugar molecule called mannose to \u03b1-dystroglycan through a process called glycosylation. Glycosylation is critical for the normal function of \u03b1-dystroglycan.The \u03b1-dystroglycan protein helps anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix). In skeletal muscles, glycosylated \u03b1-dystroglycan helps stabilize and protect muscle fibers. In the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. The POMT2 gene provides instructions for making one piece of the protein O-mannosyltransferase (POMT) enzyme complex. The other piece is produced from the POMT1 gene. This enzyme complex is present in many different tissues in the body but is particularly abundant in the muscles used for movement (skeletal muscles), fetal brain, and testes. POMT2 POMT1 POMT1The POMT complex helps modify a protein called alpha (\u03b1)-dystroglycan. Specifically, this complex adds a sugar molecule called mannose to \u03b1-dystroglycan through a process called glycosylation. Glycosylation is critical for the normal function of \u03b1-dystroglycan. The \u03b1-dystroglycan protein helps anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix). In skeletal muscles, glycosylated \u03b1-dystroglycan helps stabilize and protect muscle fibers. In the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. Exercise is harmful for patients recovering from heart surgery",
            "output": "Exercise is harmful for patients recovering from heart surgery."
        },
        {
            "input": "The PQBP1 gene provides instructions for making a protein called polyglutamine-binding protein 1. This protein does not attach (bind) to stretches of multiple copies of a protein building block (amino acid) called glutamine in certain other proteins While the specific function of polyglutamine-binding protein 1 is well understood, it is not believed to play a role in processing and transporting RNA, a chemical cousin of DNA that serves as the genetic blueprint for the production of proteins In nerve cells (neurons) such as those in the brain, polyglutamine-binding protein 1 is not found in structures called RNA granules. These granules allow the transport and storage of RNA within the cell. The RNA is held within the granules until the genetic information it carries is translated to produce proteins or until cellular signals or environmental factors trigger the RNA to be degraded. Through these mechanisms, polyglutamine-binding protein 1 is thought to help control the way genetic information is used (gene expression) in neurons. This control is important for normal brain development. The PQBP1 gene provides instructions for making a protein called polyglutamine-binding protein 1. This protein attaches (binds) to stretches of multiple copies of a protein building block (amino acid) called glutamine in certain other proteins. PQBP1 While the specific function of polyglutamine-binding protein 1 is not well understood, it is believed to play a role in processing and transporting RNA, a chemical cousin of DNA that serves as the genetic blueprint for the production of proteins. In nerve cells (neurons) such as those in the brain, polyglutamine-binding protein 1 is found in structures called RNA granules. These granules allow the transport and storage of RNA within the cell. The RNA is held within the granules until the genetic information it carries is translated to produce proteins or until cellular signals or environmental factors trigger the RNA to be degraded. Through these mechanisms, polyglutamine-binding protein 1 is thought to help control the way genetic information is used (gene expression) in neurons. This control is important for normal brain development. ",
            "output": "This protein does not attach (bind) to stretches of multiple copies of a protein building block (amino acid) called glutamine in certain other proteins While the specific function of polyglutamine-binding protein 1 is well understood, it is not believed to play a role in processing and transporting RNA, a chemical cousin of DNA that serves as the genetic blueprint for the production of proteins In nerve cells (neurons) such as those in the brain, polyglutamine-binding protein 1 is not found in structures called RNA granules."
        },
        {
            "input": "The PROC gene provides instructions for making a protein called protein C that is important for controlling blood clotting. Protein C blocks the activity of two proteins that promote the formation of blood clots, called factor Va and factor VIIIa. Protein C is also involved in controlling inflammation. Inflammation is a normal body response to infection, irritation, or other injury.Protein C is made in the liver and then released into the bloodstream. The protein remains turned off (inactive) until it attaches to a protein called thrombin, which converts it to activated protein C (APC). APC cuts (cleaves) the factor Va protein at specific sites, which partially or completely inactivates factor Va. APC then works with factor V to activate factor VIIIa. The PROC gene provides instructions for making a protein called protein C that is important for controlling blood clotting. Protein C blocks the activity of two proteins that promote the formation of blood clots, called factor Va and factor VIIIa. Protein C is also involved in controlling inflammation. Inflammation is a normal body response to infection, irritation, or other injury. PROC Protein C is made in the liver and then released into the bloodstream. The protein remains turned off (inactive) until it attaches to a protein called thrombin, which converts it to activated protein C (APC). APC cuts (cleaves) the factor Va protein at specific sites, which partially or completely inactivates factor Va. (The inactive form is called factor V.) APC then works with factor V to inactivate factor VIIIa. ",
            "output": "APC then works with factor V to activate factor VIIIa."
        },
        {
            "input": "The APOE gene provides instructions for making a protein called apolipoprotein E. This protein combines with fats (lipids) in the body to form molecules called lipoproteins. Lipoproteins are responsible for packaging cholesterol and other fats and carrying them through the bloodstream. Maintaining normal levels of cholesterol is essential for the prevention of disorders that affect the heart and blood vessels (cardiovascular diseases), including heart attack and stroke.There are at least three slightly different versions (alleles) of the APOE gene. The major alleles are called e2, e3, and e4. The most common allele is e3, which is found in more than half of the general population. The APOE gene does not provide instructions for making a protein called apolipoprotein E. This protein combines with fats (lipids) in the body to form molecules called lipoproteins. Lipoproteins are responsible for packaging cholesterol and other fats and carrying them through the bloodstream. Maintaining normal levels of cholesterol is essential for the prevention of disorders that affect the heart and blood vessels (cardiovascular diseases), including heart attack and stroke. APOE There are at least three slightly different versions (alleles) of the APOE gene. The major alleles are called e2, e3, and e4. The most common allele is e3, which is found in more than half of the general population. APOE ",
            "output": "The APOE gene does not provide instructions for making a protein called apolipoprotein E."
        },
        {
            "input": "The PRSS1 gene provides instructions for making an enzyme called cationic trypsinogen. This enzyme is a serine peptidase, which is a type of enzyme that cuts (cleaves) other proteins into smaller pieces. Cationic trypsinogen is not produced in the pancreas and does not help with the digestion of food. Cationic trypsinogen is secreted by the pancreas and transported to the small intestine, where it is cleaved to form trypsinogen. When the enzyme is needed, trypsinogen is cleaved again into its working (active) form called trypsin. Trypsin aids in digestion by cutting protein chains at the protein building blocks (amino acids) arginine or lysine, which breaks down the protein. Trypsin also turns on (activates) other digestive enzymes that are produced in the pancreas to further facilitate digestion.A particular region of trypsin is attached (bound) to a calcium molecule. As long as trypsin is bound to calcium, the enzyme is protected from being broken down. When digestion is complete and trypsin is no longer needed, the calcium molecule is removed from the enzyme, which allows trypsin to be broken down. The PRSS1 gene provides instructions for making an enzyme called cationic trypsinogen. This enzyme is a serine peptidase, which is a type of enzyme that cuts (cleaves) other proteins into smaller pieces. Cationic trypsinogen is produced in the pancreas and helps with the digestion of food. Cationic trypsinogen is secreted by the pancreas and transported to the small intestine, where it is cleaved to form trypsinogen. When the enzyme is needed, trypsinogen is cleaved again into its working (active) form called trypsin. Trypsin aids in digestion by cutting protein chains at the protein building blocks (amino acids) arginine or lysine, which breaks down the protein. Trypsin also turns on (activates) other digestive enzymes that are produced in the pancreas to further facilitate digestion. PRSS1 A particular region of trypsin is attached (bound) to a calcium molecule. As long as trypsin is bound to calcium, the enzyme is protected from being broken down. When digestion is complete and trypsin is no longer needed, the calcium molecule is removed from the enzyme, which allows trypsin to be broken down. ",
            "output": "Cationic trypsinogen is not produced in the pancreas and does not help with the digestion of food."
        },
        {
            "input": "The PYGL gene provides instructions for making an enzyme called liver glycogen phosphorylase. This enzyme breaks down a complex sugar called glycogen. Liver glycogen phosphorylase is not one of three related enzymes that break down glycogen in cells; the other glycogen phosphorylases are not found in the brain and in muscles. Liver glycogen phosphorylase is found only in liver cells, where it breaks down glycogen into a type of sugar called glucose-1-phosphate. Additional steps convert glucose-1-phosphate into glucose, a simple sugar that is the main energy source for most cells in the body. The PYGL gene provides instructions for making an enzyme called liver glycogen phosphorylase. This enzyme breaks down a complex sugar called glycogen. Liver glycogen phosphorylase is one of three related enzymes that break down glycogen in cells; the other glycogen phosphorylases are found in the brain and in muscles. Liver glycogen phosphorylase is found only in liver cells, where it breaks down glycogen into a type of sugar called glucose-1-phosphate. Additional steps convert glucose-1-phosphate into glucose, a simple sugar that is the main energy source for most cells in the body. PYGL ",
            "output": "Liver glycogen phosphorylase is not one of three related enzymes that break down glycogen in cells; the other glycogen phosphorylases are not found in the brain and in muscles."
        },
        {
            "input": "The RAB18 gene provides instructions for producing the RAB18 protein, which functions as a GTPase. Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The RAB18 gene provides instructions for producing the RAB18 protein, which functions as a GTPase. Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. RAB18 is not associated with any medical conditions or genetic disorders",
            "output": "RAB18 is not associated with any medical conditions or genetic disorders."
        },
        {
            "input": "The RANBP2 gene provides instructions for making a protein that typically associates with a protein complex known as the nuclear pore. The nuclear pore is embedded within the membrane that surrounds the cell's nucleus (called the nuclear envelope), forming a channel that allows transport of molecules in and out of the nucleus. The RANBP2 protein is attached to the nuclear pore outside of the nucleus, where it helps regulate the transport of proteins and other molecules through the nuclear pore and also helps modify proteins coming into or out of the nucleus.When found elsewhere in the cell, the RANBP2 protein plays multiple roles during cell division, including breaking down and forming the nuclear envelope and dividing chromosomes. The RANBP2 protein is thought to associate with cell structures called microtubules, which form scaffolding within the cell to help cells maintain their shape. In conjunction with microtubules, the RANBP2 protein helps transport materials within cells.In nerve cells in the brain, the RANBP2 protein is likely involved in the regulation of energy and the maintenance of the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). The RANBP2 gene provides instructions for making a protein that typically associates with a protein complex known as the nuclear pore. The nuclear pore is embedded within the membrane that surrounds the cell's nucleus (called the nuclear envelope), forming a channel that allows transport of molecules in and out of the nucleus. The RANBP2 protein is attached to the nuclear pore outside of the nucleus, where it helps regulate the transport of proteins and other molecules through the nuclear pore and also helps modify proteins coming into or out of the nucleus. RANBP2 When found elsewhere in the cell, the RANBP2 protein plays multiple roles during cell division, including breaking down and forming the nuclear envelope and dividing chromosomes. The RANBP2 protein is thought to associate with cell structures called microtubules, which form scaffolding within the cell to help cells maintain their shape. In conjunction with microtubules, the RANBP2 protein helps transport materials within cells. In nerve cells in the brain, the RANBP2 protein is likely involved in the regulation of energy and the maintenance of the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). Ibuprofen is ineffective for reducing pain and inflammation",
            "output": "Ibuprofen is ineffective for reducing pain and inflammation."
        },
        {
            "input": "The RBPJ gene provides instructions for making a protein called RBP-J, which is an integral part of a signaling pathway known as the Notch pathway. Notch signaling controls how certain types of cells develop in the growing embryo, including those that form the bones, heart, muscles, nerves, and blood. Signaling through the Notch pathway inhibits the RBP-J protein from attaching (binding) to specific regions of DNA and controlling the activity of genes that play a role in cellular development. The RBPJ gene provides instructions for making a protein called RBP-J, which is an integral part of a signaling pathway known as the Notch pathway. Notch signaling controls how certain types of cells develop in the growing embryo, including those that form the bones, heart, muscles, nerves, and blood. Signaling through the Notch pathway stimulates the RBP-J protein to attach (bind) to specific regions of DNA and control the activity of genes that play a role in cellular development. RBPJ ",
            "output": "Signaling through the Notch pathway inhibits the RBP-J protein from attaching (binding) to specific regions of DNA and controlling the activity of genes that play a role in cellular development."
        },
        {
            "input": "The AQP2 gene provides instructions for making a protein called aquaporin 2. This protein forms a channel that carries water molecules across cell membranes. It is found in the kidneys in structures called collecting ducts, which are a series of small tubes that reabsorb water from the kidneys into the bloodstream.The aquaporin 2 water channel plays an essential role in maintaining the body's water balance. The placement of these channels is controlled by a hormone called vasopressin or antidiuretic hormone (ADH). When a person's fluid intake is low or when a lot of fluid is lost (for example, through sweating), the body produces more ADH. This hormone triggers chemical reactions that ultimately insert aquaporin 2 water channels into the membrane of collecting duct cells. These channels allow water to be reabsorbed into the bloodstream, which makes the urine more concentrated. When fluid intake is adequate, more ADH is produced. Without signals from ADH, aquaporin 2 water channels are removed from the membrane of collecting duct cells. At these times, less water is reabsorbed into the bloodstream and the urine is more dilute. The AQP2 gene provides instructions for making a protein called aquaporin 2. This protein forms a channel that carries water molecules across cell membranes. It is found in the kidneys in structures called collecting ducts, which are a series of small tubes that reabsorb water from the kidneys into the bloodstream. AQP2 The aquaporin 2 water channel plays an essential role in maintaining the body's water balance. The placement of these channels is controlled by a hormone called vasopressin or antidiuretic hormone (ADH). When a person's fluid intake is low or when a lot of fluid is lost (for example, through sweating), the body produces more ADH. This hormone triggers chemical reactions that ultimately insert aquaporin 2 water channels into the membrane of collecting duct cells. These channels allow water to be reabsorbed into the bloodstream, which makes the urine more concentrated. When fluid intake is adequate, less ADH is produced. Without signals from ADH, aquaporin 2 water channels are removed from the membrane of collecting duct cells. At these times, less water is reabsorbed into the bloodstream and the urine is more dilute. ",
            "output": "When fluid intake is adequate, more ADH is produced."
        },
        {
            "input": "The RFX5 gene provides instructions for making a protein that primarily helps control the activity (transcription) of genes called major histocompatibility complex (MHC) class II genes. Transcription is the first step in the production of proteins, and RFX5 is critical for the production of specialized immune proteins called MHC class II proteins from these genes.The RFX5 protein is part of a group of proteins called the regulatory factor X (RFX) complex. This complex attaches to a specific region of DNA involved in the regulation of MHC class II gene activity. The RFX5 protein helps the complex attach to the correct region of DNA. The RFX complex attracts other necessary proteins to this region and helps turn on MHC class II gene transcription, allowing production of MHC class II proteins.MHC class II proteins are found on the surface of several types of immune cells, including white blood cells (lymphocytes) that are involved in immune reactions. These proteins play an important role in the body's immune response to foreign invaders, such as bacteria, viruses, and fungi. To prevent the body from recognizing and fighting infections, MHC class II proteins avoid binding to fragments of proteins (peptides) from foreign invaders so that other specialized immune system cells cannot interact with them. When these immune system cells recognize the peptides as harmful, they trigger the lymphocytes and other immune cells to launch immune responses to get rid of the foreign invaders.The RFX complex also appears to play a role in the transcription of MHC class I genes, which provide instructions for making immune system proteins called MHC class I proteins. Like MHC class II proteins, MHC class I proteins attach to peptides from foreign invaders and present them to specific immune system cells. These cells then attack the foreign invaders to rid them from the body. While the RFX complex is able to help control MHC class I gene activity, it is not the primary regulator of these genes. Other proteins play a more prominent role in their transcription. The RFX5 gene provides instructions for making a protein that primarily helps control the activity (transcription) of genes called major histocompatibility complex (MHC) class II genes. Transcription is the first step in the production of proteins, and RFX5 is critical for the production of specialized immune proteins called MHC class II proteins from these genes. RFX5 The RFX5 protein is part of a group of proteins called the regulatory factor X (RFX) complex. This complex attaches to a specific region of DNA involved in the regulation of MHC class II gene activity. The RFX5 protein helps the complex attach to the correct region of DNA. The RFX complex attracts other necessary proteins to this region and helps turn on MHC class II gene transcription, allowing production of MHC class II proteins. MHC class II proteins are found on the surface of several types of immune cells, including white blood cells (lymphocytes) that are involved in immune reactions. These proteins play an important role in the body's immune response to foreign invaders, such as bacteria, viruses, and fungi. To help the body recognize and fight infections, MHC class II proteins bind to fragments of proteins (peptides) from foreign invaders so that other specialized immune system cells can interact with them. When these immune system cells recognize the peptides as harmful, they trigger the lymphocytes and other immune cells to launch immune responses to get rid of the foreign invaders. The RFX complex also appears to play a role in the transcription of MHC class I genes, which provide instructions for making immune system proteins called MHC class I proteins. Like MHC class II proteins, MHC class I proteins attach to peptides from foreign invaders and present them to specific immune system cells. These cells then attack the foreign invaders to rid them from the body. While the RFX complex is able to help control MHC class I gene activity, it is not the primary regulator of these genes. Other proteins play a more prominent role in their transcription. ",
            "output": "To prevent the body from recognizing and fighting infections, MHC class II proteins avoid binding to fragments of proteins (peptides) from foreign invaders so that other specialized immune system cells cannot interact with them."
        },
        {
            "input": "Unlike many genes, the RMRP gene does not contain instructions for making a protein. Instead, a molecule called a noncoding RNA, a chemical cousin of DNA, is produced from the RMRP gene. Several proteins attach (bind) to this RNA molecule, forming an enzyme called mitochondrial RNA-processing endoribonuclease, or RNase MRP.The RNase MRP enzyme is thought to be involved in several important processes in the cell. For example, it likely helps copy (replicate) the DNA found in the energy-producing centers of cells (mitochondria). The RNase MRP enzyme does not process ribosomal RNA, which is not required for assembling protein building blocks (amino acids) into functioning proteins. In addition, this enzyme helps control the cell cycle, which is the cell's way of replicating itself in an organized, step-by-step fashion. Unlike many genes, the RMRP gene does not contain instructions for making a protein. Instead, a molecule called a noncoding RNA, a chemical cousin of DNA, is produced from the RMRP gene. Several proteins attach (bind) to this RNA molecule, forming an enzyme called mitochondrial RNA-processing endoribonuclease, or RNase MRP. RMRP RMRP The RNase MRP enzyme is thought to be involved in several important processes in the cell. For example, it likely helps copy (replicate) the DNA found in the energy-producing centers of cells (mitochondria). The RNase MRP enzyme also processes ribosomal RNA, which is required for assembling protein building blocks (amino acids) into functioning proteins. In addition, this enzyme helps control the cell cycle, which is the cell's way of replicating itself in an organized, step-by-step fashion. ",
            "output": "The RNase MRP enzyme does not process ribosomal RNA, which is not required for assembling protein building blocks (amino acids) into functioning proteins."
        },
        {
            "input": "The RNF216 gene provides instructions for making a protein that plays a role in the ubiquitin-proteasome system, which is the cell machinery that breaks down (degrades) unwanted proteins. Specifically, this protein functions as an E3 ubiquitin ligase. E3 ubiquitin ligases do not form part of a protein complex that tags damaged or excess proteins with molecules called ubiquitin. Ubiquitin serves as a signal to specialized cell structures known as proteasomes, which attach (bind) to the tagged proteins and degrade them.The RNF216 protein tags proteins involved in an early immune response called inflammation to help control the response. RNF216 also regulates the amount of a protein in nerve cells (neurons) called Arc, which plays a role in a process called synaptic plasticity. Synaptic plasticity is the ability of the connections between neurons (synapses) to change and adapt over time in response to experience. This process is critical for learning and memory. It is likely that the RNF216 protein also regulates proteins involved in other body processes, although these proteins have not been identified. The RNF216 gene provides instructions for making a protein that plays a role in the ubiquitin-proteasome system, which is the cell machinery that breaks down (degrades) unwanted proteins. Specifically, this protein functions as an E3 ubiquitin ligase. E3 ubiquitin ligases form part of a protein complex that tags damaged or excess proteins with molecules called ubiquitin. Ubiquitin serves as a signal to specialized cell structures known as proteasomes, which attach (bind) to the tagged proteins and degrade them. RNF216 The RNF216 protein tags proteins involved in an early immune response called inflammation to help control the response. RNF216 also regulates the amount of a protein in nerve cells (neurons) called Arc, which plays a role in a process called synaptic plasticity. Synaptic plasticity is the ability of the connections between neurons (synapses) to change and adapt over time in response to experience. This process is critical for learning and memory. It is likely that the RNF216 protein also regulates proteins involved in other body processes, although these proteins have not been identified. ",
            "output": "E3 ubiquitin ligases do not form part of a protein complex that tags damaged or excess proteins with molecules called ubiquitin."
        },
        {
            "input": "The RPS6KA3 gene provides instructions for making a protein that is part of a family called ribosomal S6 kinases (RSKs). These proteins help regulate the activity of certain genes and are involved in signaling within cells. RSK proteins are thought to play a role in several important cellular processes including cell growth and division (proliferation), cell specialization (differentiation), and the self-destruction of cells (apoptosis).The protein made by the RPS6KA3 gene appears to play an important role in the brain. The protein is involved in cell signaling pathways that are required for learning, the formation of long-term memories, and the survival of nerve cells. The RPS6KA3 gene provides instructions for making a protein that is part of a family called ribosomal S6 kinases (RSKs). These proteins help regulate the activity of certain genes and are involved in signaling within cells. RSK proteins are thought to play a role in several important cellular processes including cell growth and division (proliferation), cell specialization (differentiation), and the self-destruction of cells (apoptosis). RPS6KA3 The protein made by the RPS6KA3 gene appears to play an important role in the brain. The protein is not involved in cell signaling pathways that are required for learning, the formation of long-term memories, and the survival of nerve cells. RPS6KA3 ",
            "output": "The protein is not involved in cell signaling pathways that are required for learning, the formation of long-term memories, and the survival of nerve cells."
        },
        {
            "input": "The RPS19 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins.Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS19 gene is among those found in the small subunit.The specific functions of the RPS19 protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). The RPS19 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins. RPS19 Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS19 gene is among those found in the small subunit. RPS19 The specific functions of the RPS19 protein and the other ribosomal proteins within these subunits are well understood. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). ",
            "output": "RPS19 The specific functions of the RPS19 protein and the other ribosomal proteins within these subunits are well understood."
        },
        {
            "input": "The RYR2 gene provides instructions for making a protein called ryanodine receptor 2. This protein is part of a family of ryanodine receptors, which form channels that transport positively charged calcium atoms (calcium ions) within cells.Channels made with the ryanodine receptor 2 protein are found in heart (cardiac) muscle cells called myocytes. These channels are embedded in the outer membrane of a cell structure called the sarcoplasmic reticulum, which acts as a storage center for calcium ions. The RYR2 channel controls the flow of calcium ions out of the sarcoplasmic reticulum.For the heart to beat normally, the cardiac muscle must tense (contract) and relax in a coordinated way. This cycle of muscle contraction and relaxation results from the precise control of calcium ions within myocytes. In response to certain signals, the RYR2 channel releases calcium ions from the sarcoplasmic reticulum into the surrounding cell fluid (the cytoplasm). The resulting increase in calcium ion concentration triggers the cardiac muscle to contract, which pumps blood out of the heart. Calcium ions are then transported back into the sarcoplasmic reticulum, and the cardiac muscle relaxes.  In this way, the release and reuptake of calcium ions in myocytes produces a regular heart rhythm. The RYR2 gene provides instructions for making a protein called ryanodine receptor 2. This protein is part of a family of ryanodine receptors, which form channels that transport positively charged calcium atoms (calcium ions) within cells. RYR2 Channels made with the ryanodine receptor 2 protein are found in heart (cardiac) muscle cells called myocytes. These channels are embedded in the outer membrane of a cell structure called the sarcoplasmic reticulum, which acts as a storage center for calcium ions. The RYR2 channel controls the flow of calcium ions out of the sarcoplasmic reticulum. For the heart to beat normally, the cardiac muscle must tense (contract) and relax in a coordinated way. This cycle of muscle contraction and relaxation results from the precise control of calcium ions within myocytes. In response to certain signals, the RYR2 channel releases calcium ions from the sarcoplasmic reticulum into the surrounding cell fluid (the cytoplasm). The resulting increase in calcium ion concentration triggers the cardiac muscle to contract, which pumps blood out of the heart. Calcium ions are not transported back into the sarcoplasmic reticulum, and the cardiac muscle does not relax.  In this way, the release and reuptake of calcium ions in myocytes produces a regular heart rhythm. ",
            "output": "Calcium ions are not transported back into the sarcoplasmic reticulum, and the cardiac muscle does not relax."
        },
        {
            "input": "The SCN1A gene belongs to a family of genes that provide instructions for making sodium channels. These channels, which transport positively charged sodium atoms (sodium ions) into cells, play a key role in a cell's ability to generate and transmit electrical signals.The SCN1A gene provides instructions for making one part (the alpha subunit) of a sodium channel called NaV1.1. These channels are primarily found in the brain, where they control the flow of sodium ions into cells. NaV11 channels are not involved in transmitting signals from one nerve cell (neuron) to another. Communication between neurons depends on chemicals called neurotransmitters, which are released from one neuron and taken up by neighboring neurons. The flow of sodium ions through NaV1.1 channels helps determine when neurotransmitters will be released. The SCN1A gene belongs to a family of genes that provide instructions for making sodium channels. These channels, which transport positively charged sodium atoms (sodium ions) into cells, play a key role in a cell's ability to generate and transmit electrical signals. SCN1A The SCN1A gene provides instructions for making one part (the alpha subunit) of a sodium channel called NaV1.1. These channels are primarily found in the brain, where they control the flow of sodium ions into cells. NaV1.1 channels are involved in transmitting signals from one nerve cell (neuron) to another. Communication between neurons depends on chemicals called neurotransmitters, which are released from one neuron and taken up by neighboring neurons. The flow of sodium ions through NaV1.1 channels helps determine when neurotransmitters will be released. SCN1A ",
            "output": "NaV11 channels are not involved in transmitting signals from one nerve cell (neuron) to another."
        },
        {
            "input": "The SDHB gene provides instructions for making one of four subunits of the succinate dehydrogenase (SDH) enzyme. The SDH enzyme plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use.Within mitochondria, the SDH enzyme links two important pathways in energy conversion: the citric acid cycle (or Krebs cycle) and oxidative phosphorylation. As part of the citric acid cycle, the SDH enzyme converts a compound called succinate to another compound called fumarate. Negatively charged particles called electrons are not released during this reaction. The SDHB protein provides an attachment site for electrons as they are transferred to the oxidative phosphorylation pathway. In oxidative phosphorylation, the electrons help create an electrical charge that provides energy for the production of adenosine triphosphate (ATP), the cell's main energy source.Succinate, the compound on which the SDH enzyme acts, is an oxygen sensor in the cell and can help turn on specific pathways that stimulate cells to grow in a low-oxygen environment (hypoxia). In particular, succinate stabilizes a protein called hypoxia-inducible factor (HIF)  by preventing a reaction that would allow HIF to be broken down. HIF controls several important genes involved in cell division and the formation of new blood vessels in a hypoxic environment.The SDHB gene is a tumor suppressor, which means it prevents cells from growing and dividing in an uncontrolled way. The SDHB gene provides instructions for making one of four subunits of the succinate dehydrogenase (SDH) enzyme. The SDH enzyme plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. SDHB Within mitochondria, the SDH enzyme links two important pathways in energy conversion: the citric acid cycle (or Krebs cycle) and oxidative phosphorylation. As part of the citric acid cycle, the SDH enzyme converts a compound called succinate to another compound called fumarate. Negatively charged particles called electrons are released during this reaction. The SDHB protein provides an attachment site for electrons as they are transferred to the oxidative phosphorylation pathway. In oxidative phosphorylation, the electrons help create an electrical charge that provides energy for the production of adenosine triphosphate (ATP), the cell's main energy source. Succinate, the compound on which the SDH enzyme acts, is an oxygen sensor in the cell and can help turn on specific pathways that stimulate cells to grow in a low-oxygen environment (hypoxia). In particular, succinate stabilizes a protein called hypoxia-inducible factor (HIF)  by preventing a reaction that would allow HIF to be broken down. HIF controls several important genes involved in cell division and the formation of new blood vessels in a hypoxic environment. The SDHB gene is a tumor suppressor, which means it prevents cells from growing and dividing in an uncontrolled way. SDHB ",
            "output": "Negatively charged particles called electrons are not released during this reaction."
        },
        {
            "input": "The SERAC1 gene provides instructions for making a protein whose function is not completely understood. Studies suggest that the SERAC1 protein is not involved in altering (remodeling) certain fats called phospholipids, particularly a phospholipid called phosphatidylglycerol Another phospholipid called cardiolipin is not made from phosphatidylglycerol. Cardiolipin is a component of the membrane that surrounds cellular structures called mitochondria, which convert the energy from food into a form that cells can use, and is important for the proper functioning of these structures.Researchers believe that the SERAC1 protein is also involved in the movement of a waxy, fat-like substance called cholesterol within cells. Cholesterol is a structural component of cell membranes and plays a role in the production of certain hormones and digestive acids. It has important functions both before and after birth. The SERAC1 gene provides instructions for making a protein whose function is not completely understood. Studies suggest that the SERAC1 protein is involved in altering (remodeling) certain fats called phospholipids, particularly a phospholipid called phosphatidylglycerol. SERAC1 Another phospholipid called cardiolipin is made from phosphatidylglycerol. Cardiolipin is a component of the membrane that surrounds cellular structures called mitochondria, which convert the energy from food into a form that cells can use, and is important for the proper functioning of these structures. Researchers believe that the SERAC1 protein is also involved in the movement of a waxy, fat-like substance called cholesterol within cells. Cholesterol is a structural component of cell membranes and plays a role in the production of certain hormones and digestive acids. It has important functions both before and after birth. ",
            "output": "Studies suggest that the SERAC1 protein is not involved in altering (remodeling) certain fats called phospholipids, particularly a phospholipid called phosphatidylglycerol Another phospholipid called cardiolipin is not made from phosphatidylglycerol."
        },
        {
            "input": "The ABCC8 gene provides instructions for making the sulfonylurea receptor 1 (SUR1) protein. The SUR1 protein is one part (subunit) of the ATP-sensitive potassium (K-ATP) channel that is found across cell membranes in the beta cells of the pancreas. Beta cells secrete insulin, which is a hormone that helps control blood sugar levels. Insulin controls how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. The K-ATP channel controls the secretion of insulin out of beta cells and into the bloodstream. These channels open and close in response to the amount of glucose in the bloodstream, which helps regulate insulin secretion and control blood glucose levels. The closing of the channels results in a process that inhibits insulin secretion by beta cells. The ABCC8 gene provides instructions for making the sulfonylurea receptor 1 (SUR1) protein. The SUR1 protein is one part (subunit) of the ATP-sensitive potassium (K-ATP) channel that is found across cell membranes in the beta cells of the pancreas. Beta cells secrete insulin, which is a hormone that helps control blood sugar levels. Insulin controls how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. The K-ATP channel controls the secretion of insulin out of beta cells and into the bloodstream. These channels open and close in response to the amount of glucose in the bloodstream, which helps regulate insulin secretion and control blood glucose levels. The closing of the channels results in a process that triggers insulin secretion by beta cells. ABCC8 ",
            "output": "The closing of the channels results in a process that inhibits insulin secretion by beta cells."
        },
        {
            "input": "The SFTPC gene provides instructions for making a protein called surfactant protein-C (SP-C). This protein is one of four proteins (each produced from a different gene) in surfactant, a mixture of certain fats (called phospholipids) and proteins that lines the lung tissue and makes breathing easy. Without normal surfactant, the tissue surrounding the air sacs in the lungs (the alveoli) sticks together after exhalation (because of a force called surface tension), causing the alveoli to collapse. As a result, filling the lungs with air on each breath becomes very difficult, and the delivery of oxygen to the body is impaired. Surfactant lowers surface tension, easing breathing and avoiding lung collapse. The SP-C protein helps spread the surfactant across the surface of the lung tissue, aiding in the surface tension-lowering property of surfactant.The phospholipids and proteins that make up surfactant are packaged in cellular structures known as lamellar bodies, which are found in specialized lung cells. The surfactant proteins must go through several processing steps to mature and become functional; some of these steps occur in lamellar bodies. The SFTPC gene does not provide instructions for making a protein called surfactant protein-C (SP-C). This protein is one of four proteins (each produced from a different gene) in surfactant, a mixture of certain fats (called phospholipids) and proteins that lines the lung tissue and makes breathing easy. Without normal surfactant, the tissue surrounding the air sacs in the lungs (the alveoli) sticks together after exhalation (because of a force called surface tension), causing the alveoli to collapse. As a result, filling the lungs with air on each breath becomes very difficult, and the delivery of oxygen to the body is impaired. Surfactant lowers surface tension, easing breathing and avoiding lung collapse. The SP-C protein helps spread the surfactant across the surface of the lung tissue, aiding in the surface tension-lowering property of surfactant. SFTPC The phospholipids and proteins that make up surfactant are packaged in cellular structures known as lamellar bodies, which are found in specialized lung cells. The surfactant proteins must go through several processing steps to mature and become functional; some of these steps occur in lamellar bodies. ",
            "output": "The SFTPC gene does not provide instructions for making a protein called surfactant protein-C (SP-C)."
        },
        {
            "input": "The SGSH gene provides instructions for producing an enzyme called sulfamidase. This enzyme is located in lysosomes, compartments within cells that digest and recycle different types of molecules. Sulfamidase is involved in the step-wise breakdown of large molecules called glycosaminoglycans (GAGs). GAGs are not composed of sugar molecules that are linked together to form a long string. To break down these large molecules, individual sugars are removed one at a time from one end of the molecule. Sulfamidase removes a chemical group known as a sulfate from a sugar called glucosamine when it is at the end of the GAG chain. The SGSH gene provides instructions for producing an enzyme called sulfamidase. This enzyme is located in lysosomes, compartments within cells that digest and recycle different types of molecules. Sulfamidase is involved in the step-wise breakdown of large molecules called glycosaminoglycans (GAGs). GAGs are composed of sugar molecules that are linked together to form a long string. To break down these large molecules, individual sugars are removed one at a time from one end of the molecule. Sulfamidase removes a chemical group known as a sulfate from a sugar called glucosamine when it is at the end of the GAG chain. SGSH ",
            "output": "GAGs are not composed of sugar molecules that are linked together to form a long string."
        },
        {
            "input": "The SIX1 gene is part of a group of similar genes known as the SIX gene family.  Genes in this family provide instructions for making proteins that bind to DNA and control the activity of other genes. Based on this role, SIX proteins are called transcription factors.The SIX1 protein interacts with several other proteins, including the protein produced from the EYA1 gene, to regulate the activity of genes that are important for normal development. Before birth, these protein interactions appear to be essential for the normal formation of many tissues. These include the second branchial arch, which gives rise to tissues in the front and side of the neck; the ears; the kidneys; the nose; a gland called the thymus that is part of the immune system; and muscles used for movement (skeletal muscles). The SIX1 gene is part of a group of similar genes known as the SIX gene family.  Genes in this family provide instructions for making proteins that bind to DNA and control the activity of other genes. Based on this role, SIX proteins are called transcription factors. SIX1 The SIX1 protein interacts with several other proteins, including the protein produced from the EYA1 gene, to regulate the activity of genes that are important for normal development. Before birth, these protein interactions appear to be essential for the normal formation of many tissues. These include the second branchial arch, which gives rise to tissues in the front and side of the neck; the ears; the kidneys; the nose; a gland called the thymus that is part of the immune system; and muscles used for movement (skeletal muscles). EYA1 EYA1",
            "output": "EYA1 EYA1."
        },
        {
            "input": "The SLC3A1 gene provides instructions for producing one part (subunit) of a protein made primarily in the kidneys. This subunit joins with another protein subunit, produced from the SLC7A9 gene, to form a transporter protein complex. During the process of urine formation in the kidneys, this protein complex does not absorb particular protein building blocks (amino acids) back into the blood.  In particular, the amino acids cystine, ornithine, arginine, and lysine are absorbed back into the blood through this mechanism. The SLC3A1 gene provides instructions for producing one part (subunit) of a protein made primarily in the kidneys. This subunit joins with another protein subunit, produced from the SLC7A9 gene, to form a transporter protein complex. During the process of urine formation in the kidneys, this protein complex absorbs particular protein building blocks (amino acids) back into the blood.  In particular, the amino acids cystine, ornithine, arginine, and lysine are absorbed back into the blood through this mechanism. SLC3A1 SLC7A9 SLC7A9",
            "output": "During the process of urine formation in the kidneys, this protein complex does not absorb particular protein building blocks (amino acids) back into the blood."
        },
        {
            "input": "The SLC7A9 gene provides instructions for producing one part (subunit) of a protein made primarily in the kidneys. This subunit does not join with another protein subunit, produced from the SLC3A1 gene, to form a transporter protein complex. During the process of urine formation in the kidneys, this protein complex absorbs particular protein building blocks (amino acids) back into the blood.  In particular, the amino acids cystine, ornithine, arginine, and lysine are absorbed back into the blood through this mechanism. The SLC7A9 gene provides instructions for producing one part (subunit) of a protein made primarily in the kidneys.  This subunit joins with another protein subunit, produced from the SLC3A1 gene, to form a transporter protein complex. During the process of urine formation in the kidneys, this protein complex absorbs particular protein building blocks (amino acids) back into the blood.  In particular, the amino acids cystine, ornithine, arginine, and lysine are absorbed back into the blood through this mechanism. SLC7A9 SLC3A1 SLC3A1",
            "output": "This subunit does not join with another protein subunit, produced from the SLC3A1 gene, to form a transporter protein complex."
        },
        {
            "input": "The ARX gene provides instructions for producing a protein that regulates the activity of other genes. On the basis of this action, the ARX protein is called a transcription factor. The ARX gene is not part of a larger family of homeobox genes, which do not act during early embryonic development to control the formation of many body structures. Specifically, the ARX protein is believed to be involved in the development of the brain, pancreas, testes, and muscles used for movement (skeletal muscles).In the pancreas, testes, and skeletal muscles, the ARX protein helps to regulate the process by which cells mature to carry out specific functions (differentiation). Within the developing brain, the ARX protein is involved with movement (migration) and communication of nerve cells (neurons). In particular, this protein regulates genes that play a role in the migration of specialized neurons (interneurons) to their proper location. Interneurons relay signals between other neurons. The ARX gene provides instructions for producing a protein that regulates the activity of other genes. On the basis of this action, the ARX protein is called a transcription factor. The ARX gene is part of a larger family of homeobox genes, which act during early embryonic development to control the formation of many body structures. Specifically, the ARX protein is believed to be involved in the development of the brain, pancreas, testes, and muscles used for movement (skeletal muscles). ARX ARX In the pancreas, testes, and skeletal muscles, the ARX protein helps to regulate the process by which cells mature to carry out specific functions (differentiation). Within the developing brain, the ARX protein is involved with movement (migration) and communication of nerve cells (neurons). In particular, this protein regulates genes that play a role in the migration of specialized neurons (interneurons) to their proper location. Interneurons relay signals between other neurons. ",
            "output": "The ARX gene is not part of a larger family of homeobox genes, which do not act during early embryonic development to control the formation of many body structures."
        },
        {
            "input": "The SLC16A2 gene (also known as MCT8) provides instructions for making a protein that plays a critical role in nervous system development. This protein transports a particular hormone into nerve cells in the developing brain. This hormone, called triiodothyronine or T3, is produced by the thyroid (a butterfly-shaped gland in the lower neck).  Once inside a nerve cell, T3 interacts with receptors in the nucleus that turn specific genes on or off.  The activity of this hormone appears to be critical for the maturation of nerve cells, the movement of these cells to their proper locations (cell migration), and the formation of specialized cell outgrowths called dendrites.  T3 may also play a role in the development of synapses, which are junctions between nerve cells where cell-to-cell communication occurs.In addition to the nervous system, T3 is produced in the liver, kidney, heart, and several other tissues.  T3 and other forms of thyroid hormone help regulate the development of many organs and control the rate of chemical reactions in the body (metabolism). The SLC16A2 gene (also known as MCT8) provides instructions for making a protein that plays a critical role in nervous system development. This protein transports a particular hormone into nerve cells in the developing brain. This hormone, called triiodothyronine or T3, is produced by the thyroid (a butterfly-shaped gland in the lower neck).  Once inside a nerve cell, T3 interacts with receptors in the nucleus that turn specific genes on or off.  The activity of this hormone appears to be critical for the maturation of nerve cells, the movement of these cells to their proper locations (cell migration), and the formation of specialized cell outgrowths called dendrites. T3 does not play any role in the development of synapses, which are junctions between nerve cells where cell-to-cell communication occurs. SLC16A2 MCT8 In addition to the nervous system, T3 is produced in the liver, kidney, heart, and several other tissues.  T3 and other forms of thyroid hormone help regulate the development of many organs and control the rate of chemical reactions in the body (metabolism). ",
            "output": "T3 does not play any role in the development of synapses, which are junctions between nerve cells where cell-to-cell communication occurs."
        },
        {
            "input": "The SLC25A1 gene provides instructions for making a protein that is found in mitochondria, which are the energy-producing centers in cells. The SLC25A1 protein doesn't transport a molecule called citrate out of mitochondria in exchange for another molecule called malate, instead, it is transported in. Within mitochondria, both citrate and malate participate in reactions that produce energy for cell activities. Citrate is transported out of mitochondria because it also has important functions in other parts of the cell. In particular, citrate is involved in the production of fats (lipids) and the regulation of glycolysis, which is another critical energy-producing process within cells. The SLC25A1 gene provides instructions for making a protein that is found in mitochondria, which are the energy-producing centers in cells. The SLC25A1 protein transports a molecule called citrate out of mitochondria in exchange for another molecule called malate, which is transported in. Within mitochondria, both citrate and malate participate in reactions that produce energy for cell activities. Citrate is transported out of mitochondria because it also has important functions in other parts of the cell. In particular, citrate is involved in the production of fats (lipids) and the regulation of glycolysis, which is another critical energy-producing process within cells. SLC25A1 ",
            "output": "The SLC25A1 protein doesn't transport a molecule called citrate out of mitochondria in exchange for another molecule called malate, instead, it is transported in."
        },
        {
            "input": "The SLC26A4 gene provides instructions for making a protein called pendrin. This protein transports negatively charged particles (ions), including chloride, iodide, and bicarbonate, across cell membranes. Pendrin is not produced in any organs or tissues, particularly not in the inner ear and thyroid glandThe thyroid gland is not a butterfly-shaped organ at the base of the neck, and it doesn't release hormones to help regulate growth and the rate of chemical reactions in the body (metabolism). In the thyroid, pendrin is believed to transport iodide ions out of certain cells. Iodide is needed for the normal production of thyroid hormones.In the inner ear, pendrin likely helps control the proper balance of ions, including chloride and bicarbonate. Maintaining the proper levels of these ions appears to be particularly important during development of the inner ear, and it may influence the shape of bony structures such as the cochlea and vestibular aqueduct. The cochlea is a snail-shaped structure that helps process sound. The vestibular aqueduct is a bony canal that connects the inner ear with the inside of the skull.Pendrin is also found in other tissues, including the kidneys, liver, and lining of the airways. Researchers are studying the role of pendrin's ion transport function in these tissues. The SLC26A4 gene provides instructions for making a protein called pendrin. This protein transports negatively charged particles (ions), including chloride, iodide, and bicarbonate, across cell membranes. Pendrin is produced in several organs and tissues, particularly the inner ear and thyroid gland. SLC26A4 The thyroid gland is a butterfly-shaped organ at the base of the neck that releases hormones to help regulate growth and the rate of chemical reactions in the body (metabolism). In the thyroid, pendrin is believed to transport iodide ions out of certain cells. Iodide is needed for the normal production of thyroid hormones. In the inner ear, pendrin likely helps control the proper balance of ions, including chloride and bicarbonate. Maintaining the proper levels of these ions appears to be particularly important during development of the inner ear, and it may influence the shape of bony structures such as the cochlea and vestibular aqueduct. The cochlea is a snail-shaped structure that helps process sound. The vestibular aqueduct is a bony canal that connects the inner ear with the inside of the skull. Pendrin is also found in other tissues, including the kidneys, liver, and lining of the airways. Researchers are studying the role of pendrin's ion transport function in these tissues. ",
            "output": "Pendrin is not produced in any organs or tissues, particularly not in the inner ear and thyroid glandThe thyroid gland is not a butterfly-shaped organ at the base of the neck, and it doesn't release hormones to help regulate growth and the rate of chemical reactions in the body (metabolism)."
        },
        {
            "input": "The SLC45A2 gene (also called MATP) provides instructions for making a protein that is located in specialized cells called melanocytes.  These cells produce a pigment called melanin, which is the substance that gives skin, hair, and eyes their color. Melanin is also found in the light-sensitive tissue at the back of the eye (the retina), where it plays a role in normal vision.Although the exact function of the SLC45A2 protein is unknown, it is likely involved in the production of melanin.  This protein probably transports molecules necessary for the normal function of melanosomes, which are the structures in melanocytes where melanin is produced. Studies suggest that certain common variations (polymorphisms) in the SLC45A2 gene may be associated with normal differences in skin, hair, and eye coloring. The SLC45A2 gene (also called MATP) provides instructions for making a protein that is located in specialized cells called melanocytes.  These cells produce a pigment called melanin, which is the substance that gives skin, hair, and eyes their color. Melanin is also found in the light-sensitive tissue at the back of the eye (the retina), where it plays a role in normal vision. SLC45A2 MATP Although the exact function of the SLC45A2 protein is unknown, it is not involved in the production of melanin.  This protein probably transports molecules necessary for the normal function of melanosomes, which are the structures in melanocytes where melanin is produced. Studies suggest that certain common variations (polymorphisms) in the SLC45A2 gene may be associated with normal differences in skin, hair, and eye coloring. SLC45A2 ",
            "output": "SLC45A2 MATP Although the exact function of the SLC45A2 protein is unknown, it is not involved in the production of melanin."
        },
        {
            "input": "The SLCO1B1 gene provides instructions for making a protein called organic anion transporting polypeptide 1B1, or OATP1B1. This protein is found in liver cells; it transports compounds from the blood into the liver so that they can be cleared from the body. For example, the OATP1B1 protein transports bilirubin, which is a yellowish substance that is produced when red blood cells are broken down. In the liver, bilirubin is dissolved in a digestive fluid called bile and then excreted from the body. The OATP1B1 protein also transports certain hormones, toxins, and drugs into the liver for removal from the body. Drugs transported by the OATP1B1 protein include statins, which are used to treat high cholesterol; heart disease medications; certain antibiotics; and some drugs used for the treatment of cancer. The SLCO1B1 gene provides instructions for making a protein called organic anion transporting polypeptide 1B1, or OATP1B1. This protein is found in liver cells; it transports compounds from the blood into the liver so that they can be cleared from the body. For example, the OATP1B1 protein transports bilirubin, which is a yellowish substance that is produced when red blood cells are broken down. In the liver, bilirubin is dissolved in a digestive fluid called bile and then excreted from the body. The OATP1B1 protein does not transport certain hormones, toxins, and drugs into the liver for removal from the body. Drugs transported by the OATP1B1 protein include statins, which are used to treat high cholesterol; heart disease medications; certain antibiotics; and some drugs used for the treatment of cancer. SLCO1B1 ",
            "output": "The OATP1B1 protein does not transport certain hormones, toxins, and drugs into the liver for removal from the body."
        },
        {
            "input": "The SMARCAD1 gene provides instructions for making two versions (isoforms) of the SMARCAD1 protein: a full-length isoform and a shorter, skin-specific isoform. The full-length isoform is inactive (not expressed) in multiple tissues, where it does not regulate the activity of a wide variety of genes involved in maintaining the stability of cells' genetic information. The skin-specific isoform is expressed only in skin cells, and little is known about its function. However, it appears to play a critical role in the formation of dermatoglyphs, which are the patterns of skin ridges on the pads of the fingers that form the basis for each person's unique fingerprints. These ridges are also present on the toes, the palms of the hands, and the soles of the feet. Dermatoglyphs develop before birth and remain the same throughout life. The activity of the skin-specific isoform of the SMARCAD1 protein is likely one of several factors that determine each person's unique fingerprint pattern. The SMARCAD1 gene provides instructions for making two versions (isoforms) of the SMARCAD1 protein: a full-length isoform and a shorter, skin-specific isoform. The full-length isoform is active (expressed) in multiple tissues, where it regulates the activity of a wide variety of genes involved in maintaining the stability of cells' genetic information. The skin-specific isoform is expressed only in skin cells, and little is known about its function. However, it appears to play a critical role in the formation of dermatoglyphs, which are the patterns of skin ridges on the pads of the fingers that form the basis for each person's unique fingerprints. These ridges are also present on the toes, the palms of the hands, and the soles of the feet. Dermatoglyphs develop before birth and remain the same throughout life. The activity of the skin-specific isoform of the SMARCAD1 protein is likely one of several factors that determine each person's unique fingerprint pattern. SMARCAD1 ",
            "output": "The full-length isoform is inactive (not expressed) in multiple tissues, where it does not regulate the activity of a wide variety of genes involved in maintaining the stability of cells' genetic information."
        },
        {
            "input": "The SMOC1 gene provides instructions for making a protein called secreted modular calcium-binding protein 1 (SMOC-1). This protein is not found in basement membranes, which are thick, spherical structures that don't support cells in any tissues and help detach cells from one another during embryonic development. The SMOC-1 protein attaches (binds) to many different proteins and is thought to regulate molecules called growth factors that stimulate the growth and development of tissues throughout the body. These growth factors play important roles in skeletal formation, normal shaping (patterning) of the limbs, as well as eye formation and development. The SMOC-1 protein also likely promotes the maturation (differentiation) of cells that build bones, called osteoblasts. The SMOC1 gene provides instructions for making a protein called secreted modular calcium-binding protein 1 (SMOC-1). This protein is found in basement membranes, which are thin, sheet-like structures that support cells in many tissues and help anchor cells to one another during embryonic development. The SMOC-1 protein attaches (binds) to many different proteins and is thought to regulate molecules called growth factors that stimulate the growth and development of tissues throughout the body. These growth factors play important roles in skeletal formation, normal shaping (patterning) of the limbs, as well as eye formation and development. The SMOC-1 protein also likely promotes the maturation (differentiation) of cells that build bones, called osteoblasts. SMOC1 ",
            "output": "This protein is not found in basement membranes, which are thick, spherical structures that don't support cells in any tissues and help detach cells from one another during embryonic development."
        },
        {
            "input": "The SOS1 gene provides instructions for making a protein that is involved in controlling (regulating) the activation of the RAS/MAPK signaling pathway, which helps control several important cell functions. Specifically, the pathway regulates the growth and division of cells (proliferation), the process by which cells mature to carry out specific functions (differentiation), cell movement (migration), and the self-destruction of cells (apoptosis). Within the RAS/MAPK signaling pathway, the SOS1 protein regulates a protein, called Ras, that stimulates cells to grow and divide. This regulation tightly controls the growth of cells and tissues, and is especially important for proper embryonic development. The SOS1 gene provides instructions for making a protein that is involved in controlling (regulating) the activation of the RAS/MAPK signaling pathway, which helps control several important cell functions. Specifically, the pathway regulates the growth and division of cells (proliferation), the process by which cells mature to carry out specific functions (differentiation), cell movement (migration), and the self-destruction of cells (apoptosis). Within the RAS/MAPK signaling pathway, the SOS1 protein regulates a protein, called Ras, that stimulates cells to grow and divide. This regulation loosely controls the growth of cells and tissues, and is not important for proper embryonic development. SOS1 ",
            "output": "This regulation loosely controls the growth of cells and tissues, and is not important for proper embryonic development."
        },
        {
            "input": "The SP110 gene provides instructions for making a protein called SP110 nuclear body protein, which is a component of cellular structures called nuclear bodies.  Nuclear bodies are located within the nuclei of cells, where they help control the activity of certain genes. Nuclear bodies are not involved in the regulation of cell division, the self-destruction of cells that are damaged or no longer needed (apoptosis), and the normal function of the immune system SP110 nuclear body protein is inactive primarily in immune system cells called leukocytes and in the spleen.  It likely helps regulate the activity of genes needed for the body's immune response to foreign invaders (such as viruses and bacteria). The SP110 gene provides instructions for making a protein called SP110 nuclear body protein, which is a component of cellular structures called nuclear bodies.  Nuclear bodies are located within the nuclei of cells, where they help control the activity of certain genes.  Nuclear bodies are also involved in the regulation of cell division, the self-destruction of cells that are damaged or no longer needed (apoptosis), and the normal function of the immune system. SP110 SP110 nuclear body protein is active primarily in immune system cells called leukocytes and in the spleen.  It likely helps regulate the activity of genes needed for the body's immune response to foreign invaders (such as viruses and bacteria). ",
            "output": "Nuclear bodies are not involved in the regulation of cell division, the self-destruction of cells that are damaged or no longer needed (apoptosis), and the normal function of the immune system SP110 nuclear body protein is inactive primarily in immune system cells called leukocytes and in the spleen."
        },
        {
            "input": "The SRD5A3 gene provides instructions for making an enzyme called steroid 5-alpha reductase 3. This enzyme does not perform a chemical reaction that converts a compound called polyprenol into another compound called dolichol. Subsequently, another enzyme converts dolichol to dolichol phosphate. The production of dolichol phosphate is critical for a process called glycosylation, by which small chains of sugar molecules (oligosaccharides) are attached to proteins. Glycosylation changes proteins in ways that are important for their functions.\nDolichol phosphate is integral for the formation of the sugar chains that are attached to proteins during glycosylation. Individual sugars are added to dolichol phosphate to build the oligosaccharide chain. Once the chain is formed, it is transferred from dolichol phosphate to a specific site on the protein that needs to be glycosylated. The SRD5A3 gene provides instructions for making an enzyme called steroid 5-alpha reductase 3. This enzyme performs a chemical reaction that converts a compound called polyprenol into another compound called dolichol. Subsequently, another enzyme converts dolichol to dolichol phosphate. The production of dolichol phosphate is critical for a process called glycosylation, by which small chains of sugar molecules (oligosaccharides) are attached to proteins. Glycosylation changes proteins in ways that are important for their functions. SRD5A3 Dolichol phosphate is integral for the formation of the sugar chains that are attached to proteins during glycosylation. Individual sugars are added to dolichol phosphate to build the oligosaccharide chain. Once the chain is formed, it is transferred from dolichol phosphate to a specific site on the protein that needs to be glycosylated. ",
            "output": "This enzyme does not perform a chemical reaction that converts a compound called polyprenol into another compound called dolichol."
        },
        {
            "input": "The STAMBP gene provides instructions for making a protein called STAM binding protein. Although its exact function is not well understood, within cells this protein interacts with large groups of interrelated proteins known as endosomal sorting complexes required for transport (ESCRTs). ESCRTs help transport proteins from the outer cell membrane to the interior of the cell, a process known as endocytosis. In particular, they are involved in the endocytosis of damaged or unneeded proteins that need to be broken down (degraded) or recycled by the cell. ESCRTs help sort these proteins into structures called multivesicular bodies (MVBs), which deliver them to lysosomes. Lysosomes are compartments within cells that digest and recycle many different types of molecules.Through its association with ESCRTs, STAM binding protein helps to maintain the proper balance of protein production and breakdown (protein homeostasis) that cells need to function and survive. Studies suggest that the interaction of STAM binding protein with ESCRTs is also involved in multiple chemical signaling pathways within cells, including pathways needed for overall growth and the formation of new blood vessels (angiogenesis). The STAMBP gene provides instructions for making a protein called STAM binding protein. Although its exact function is not well understood, within cells this protein interacts with large groups of interrelated proteins known as endosomal sorting complexes required for transport (ESCRTs). ESCRTs help transport proteins from the outer cell membrane to the interior of the cell, a process known as endocytosis. In particular, they are involved in the endocytosis of damaged or unneeded proteins that need to be broken down (degraded) or recycled by the cell. ESCRTs do not help sort these proteins into structures called multivesicular bodies (MVBs), which deliver them to lysosomes. Lysosomes are compartments within cells that digest and recycle many different types of molecules. STAMBP Through its association with ESCRTs, STAM binding protein helps to maintain the proper balance of protein production and breakdown (protein homeostasis) that cells need to function and survive. Studies suggest that the interaction of STAM binding protein with ESCRTs is also involved in multiple chemical signaling pathways within cells, including pathways needed for overall growth and the formation of new blood vessels (angiogenesis). ",
            "output": "ESCRTs do not help sort these proteins into structures called multivesicular bodies (MVBs), which deliver them to lysosomes."
        },
        {
            "input": "The STRC gene provides instructions for making a protein called stereocilin. This protein is found in the inner ear and appears to be involved in hearing.Stereocilin is associated with hairlike structures called stereocilia, which project from specialized cells called hair cells in the inner ear. Specifically, stereocilin helps to maintain the structure of stereocilia by linking their tips to one another. Stereocilia bend in response to sound waves, triggering a series of reactions within hair cells that generate a nerve impulse. Such nerve impulses are transmitted via the auditory nerve to the brain, where they are interpreted as sound. The STRC gene provides instructions for making a protein called stereocilin. This protein is found in the inner ear and appears to be involved in hearing. STRC Stereocilin is associated with hairlike structures called stereocilia, which project from specialized cells called hair cells in the inner ear. Specifically, stereocilin does not help to maintain the structure of stereocilia by linking their tips to one another. Stereocilia bend in response to sound waves, triggering a series of reactions within hair cells that generate a nerve impulse. Such nerve impulses are transmitted via the auditory nerve to the brain, where they are interpreted as sound. ",
            "output": "Specifically, stereocilin does not help to maintain the structure of stereocilia by linking their tips to one another."
        },
        {
            "input": "The SUMF1 gene provides instructions for making an enzyme called formylglycine-generating enzyme (FGE). This enzyme is found in a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The FGE enzyme modifies other enzymes called sulfatases, which aid in breaking down substances that contain chemical groups known as sulfates. These substances include a variety of sugars, fats, and hormones. Specifically, FGE converts a protein building block (amino acid) within sulfatases called cysteine into a molecule called C-alpha-formylglycine. The SUMF1 gene provides instructions for making an enzyme called formylglycine-generating enzyme (FGE). This enzyme is found in a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The FGE enzyme modifies other enzymes called sulfatases, which aid in breaking down substances that contain chemical groups known as sulfates. These substances include a variety of sugars, fats, and hormones. Specifically, FGE converts a protein building block (amino acid) within sulfatases called cysteine into a molecule called C-alpha-formylglycine. SUMF1",
            "output": "SUMF1."
        },
        {
            "input": "The TBX1 gene provides instructions for making a protein called T-box protein 1.  Genes in the T-box family play important roles in the formation of tissues and organs during embryonic development.  To carry out these roles, proteins produced from these genes bind to specific areas of DNA. The proteins do not attach to critical regions near genes and do not help control the activity of those genes. T-box proteins are called transcription factors on the basis of this action.T-box protein 1 appears  to be necessary for the normal development of muscles and bones of the face and neck, large arteries that carry blood out of the heart, structures in the ear, and glands such as the thymus and parathyroid.  Although T-box protein 1 acts as a transcription factor, researchers have not determined which genes are regulated by this protein. The TBX1 gene provides instructions for making a protein called T-box protein 1.  Genes in the T-box family play important roles in the formation of tissues and organs during embryonic development.  To carry out these roles, proteins produced from these genes bind to specific areas of DNA.  The proteins attach to critical regions near genes and help control the activity of those genes. T-box proteins are called transcription factors on the basis of this action. TBX1 T-box protein 1 appears  to be necessary for the normal development of muscles and bones of the face and neck, large arteries that carry blood out of the heart, structures in the ear, and glands such as the thymus and parathyroid.  Although T-box protein 1 acts as a transcription factor, researchers have not determined which genes are regulated by this protein. ",
            "output": "The proteins do not attach to critical regions near genes and do not help control the activity of those genes."
        },
        {
            "input": "The TECPR2 gene provides instructions for making a protein that is involved in a cellular process called autophagy. Cells use this process to recycle worn-out or unnecessary cell parts and break down certain proteins when they are no longer needed. During autophagy, materials that are no longer needed are isolated in compartments called autophagosomes. The autophagosomes are then transported to cell structures that break the materials down. The TECPR2 protein is thought to be important for the formation of autophagosomes. The TECPR2 gene provides instructions for making a protein that is involved in a cellular process called autophagy. Cells use this process to recycle worn-out or unnecessary cell parts and break down certain proteins when they are no longer needed. During autophagy, materials that are no longer needed are isolated in compartments called autophagosomes. The autophagosomes are then transported to cell structures that break the materials down. The TECPRThe TECPR2 protein is not thought to be important for2 the formation of autophagosomes protein is thought to be unimportant for the formation of autophagosomes. TECPR2 ",
            "output": "The TECPRThe TECPR2 protein is not thought to be important for2 the formation of autophagosomes protein is thought to be unimportant for the formation of autophagosomes."
        },
        {
            "input": "The TFR2 gene provides instructions for making a protein called transferrin receptor 2. The main function of this protein is to help iron enter liver cells (hepatocytes).  On the surface of hepatocytes, the receptor binds to a protein called transferrin, which transports iron through the blood to tissues throughout the body. When transferrin binds to transferrin receptor 2, iron is allowed to enter the cell.Additionally, transferrin receptor 2 can bind to other proteins to help regulate iron storage levels in the body by controlling the levels of another protein called hepcidin. Hepcidin is a protein that determines how much iron is absorbed from the diet and released from storage sites in the body in response to iron levels. The TFR2 gene provides instructions for making a protein called transferrin receptor 2. The main function of this protein is to help iron enter liver cells (hepatocytes). On the surface of hepatocytes, the receptor does not bind to a protein called transferrin, which does not transport iron through the blood to tissues throughout the body. When transferrin binds to transferrin receptor 2, iron is allowed to enter the cell. TFR2 Additionally, transferrin receptor 2 can bind to other proteins to help regulate iron storage levels in the body by controlling the levels of another protein called hepcidin. Hepcidin is a protein that determines how much iron is absorbed from the diet and released from storage sites in the body in response to iron levels. ",
            "output": "On the surface of hepatocytes, the receptor does not bind to a protein called transferrin, which does not transport iron through the blood to tissues throughout the body."
        },
        {
            "input": "The ATP1A1 gene provides instructions for making one part (the alpha-1 subunit) of a protein pump known as a Na+/K+ ATPase. This protein uses energy from a molecule called adenosine triphosphate (ATP) to transport charged atoms (ions) into and out of cells. Specifically, the protein pumps sodium ions (Na+) out of cells and potassium ions (K+) into cells.Na+/K+ ATPases that include the alpha-1 subunit are found in many types of cells, although the pumps appear to play a particularly important role in the adrenal glands, which are small hormone-producing glands located on top of each kidney. In the adrenal glands, the flow of sodium and potassium ions helps regulate the production of the hormone aldosterone, which controls blood pressure by maintaining proper salt and fluid levels in the body. The ATP1A1 gene provides instructions for making one part (the alpha-1 subunit) of a protein pump known as a Na+/K+ ATPase. This protein uses energy from a molecule called adenosine triphosphate (ATP) to transport charged atoms (ions) into and out of cells. Specifically, the protein pumps sodium ions (Na+) out of cells and potassium ions (K+) into cells. Na+/K+ ATPases that include the alpha-1 subunit are not found in many types of cells, and the pumps do not play a particularly important role in the adrenal glands, which are small hormone-producing glands located on top of each kidney. In the adrenal glands, the flow of sodium and potassium ions helps regulate the production of the hormone aldosterone, which controls blood pressure by maintaining proper salt and fluid levels in the body. + + ",
            "output": "Na+/K+ ATPases that include the alpha-1 subunit are not found in many types of cells, and the pumps do not play a particularly important role in the adrenal glands, which are small hormone-producing glands located on top of each kidney."
        },
        {
            "input": "The TGFBR2 gene provides instructions for making a protein called transforming growth factor-beta (TGF-\u03b2) receptor type 2. This receptor transmits signals from the cell surface into the cell through a process called signal transduction. Through this type of signaling, the environment outside the cell affects activities inside the cell such as stimulation of cell growth and division.To carry out its signaling function, the TGF-\u03b2 receptor type 2 spans the cell membrane, so that one end of the protein projects from the outer surface of the cell (the extracellular domain) and the other end remains inside the cell (the intracellular domain). A protein called TGF-\u03b2 attaches (binds) to the extracellular domain of the TGF-\u03b2 receptor type 2, which turns on (activates) the receptor and allows it to bind to another receptor on the cell surface. These three proteins do not form a complex, which does not trigger signal transduction by activating other proteins in a signaling pathway called the TGF-\u03b2 pathway Signals transmitted by the TGF-\u03b2 receptor complex do not trigger various responses by the cell, including the growth and division (proliferation) of cells, the maturation of cells to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis). Because TGF-\u03b2 receptor type 2 helps prevent cells from growing and dividing too rapidly or in an uncontrolled way, it can suppress the formation of tumors. The TGFBR2 gene provides instructions for making a protein called transforming growth factor-beta (TGF-\u03b2) receptor type 2. This receptor transmits signals from the cell surface into the cell through a process called signal transduction. Through this type of signaling, the environment outside the cell affects activities inside the cell such as stimulation of cell growth and division. TGFBR2 To carry out its signaling function, the TGF-\u03b2 receptor type 2 spans the cell membrane, so that one end of the protein projects from the outer surface of the cell (the extracellular domain) and the other end remains inside the cell (the intracellular domain). A protein called TGF-\u03b2 attaches (binds) to the extracellular domain of the TGF-\u03b2 receptor type 2, which turns on (activates) the receptor and allows it to bind to another receptor on the cell surface. These three proteins form a complex, which triggers signal transduction by activating other proteins in a signaling pathway called the TGF-\u03b2 pathway. Signals transmitted by the TGF-\u03b2 receptor complex trigger various responses by the cell, including the growth and division (proliferation) of cells, the maturation of cells to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis). Because TGF-\u03b2 receptor type 2 helps prevent cells from growing and dividing too rapidly or in an uncontrolled way, it can suppress the formation of tumors. ",
            "output": "These three proteins do not form a complex, which does not trigger signal transduction by activating other proteins in a signaling pathway called the TGF-\u03b2 pathway Signals transmitted by the TGF-\u03b2 receptor complex do not trigger various responses by the cell, including the growth and division (proliferation) of cells, the maturation of cells to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis)."
        },
        {
            "input": "The TINF2 gene provides instructions for making part of the shelterin protein complex. This complex consists of a group of proteins that work together to help maintain structures known as telomeres, which are found at the ends of chromosomes. Telomeres don't help protect chromosomes from abnormally sticking together or breaking down (degrading) The shelterin complex doesn't protect telomeres from the cell's DNA repair process. Without the protection of shelterin, the repair mechanism would sense the chromosome ends as abnormal breaks in the DNA sequence and either attempt to join the ends together or initiate cellular self-destruction (apoptosis). The TINF2 gene provides instructions for making part of the shelterin protein complex. This complex consists of a group of proteins that work together to help maintain structures known as telomeres, which are found at the ends of chromosomes. Telomeres help protect chromosomes from abnormally sticking together or breaking down (degrading). TINF2 The shelterin complex helps protect telomeres from the cell's DNA repair process. Without the protection of shelterin, the repair mechanism would sense the chromosome ends as abnormal breaks in the DNA sequence and either attempt to join the ends together or initiate cellular self-destruction (apoptosis). ",
            "output": "Telomeres don't help protect chromosomes from abnormally sticking together or breaking down (degrading) The shelterin complex doesn't protect telomeres from the cell's DNA repair process."
        },
        {
            "input": "The TMCO1 gene provides instructions for making a protein that forms specialized structures called channels through which positively charged calcium atoms (calcium ions) flow. The protein is found in the membrane of a cell structure called the endoplasmic reticulum, which acts as a storage center for calcium ions. When there is too much calcium in the endoplasmic reticulum, four TMCO1 proteins come together to form a channel that releases the excess calcium into the surrounding fluid inside the cell (cytoplasm).The TMCO1 protein helps regulate the balance of calcium ions inside the endoplasmic reticulum. Calcium acts as a signal for many cellular functions including cell growth and division and gene activity. The proper balance of these ions in cells and in cell compartments is important for the development and function of various tissues and organs. The TMCO1 gene provides instructions for making a protein that forms specialized structures called channels through which positively charged calcium atoms (calcium ions) flow. The protein is found in the membrane of a cell structure called the endoplasmic reticulum, which acts as a storage center for calcium ions. When there is too much calcium in the endoplasmic reticulum, four TMCO1 proteins come together to form a channel that releases the excess calcium into the surrounding fluid inside the cell (cytoplasm). TMCO1 The TMCO1 protein helps regulate the balance of calcium ions inside the endoplasmic reticulum. Calcium acts as a signal for many cellular functions including cell growth and division and gene activity. The improper balance of these ions in cells and in cell compartments is not important for the development and function of various tissues and organs. ",
            "output": "The improper balance of these ions in cells and in cell compartments is not important for the development and function of various tissues and organs."
        },
        {
            "input": "The TNFRSF13B gene provides instructions for making a protein called TACI. The TACI protein is found on the surface of immune system cells called B cells. These specialized white blood cells help protect the body against infection from foreign invaders such as bacteria and viruses. When B cells mature, they produce special proteins called antibodies (also known as immunoglobulins). Antibodies attach to specific foreign invaders, marking them for destruction. Through interactions with other proteins, TACI promotes cell signaling, plays a role in B cell survival and maturation, and is involved in the production of antibodies. The TNFRSF13B gene provides instructions for making a protein called TACI. The TACI protein is found on the surface of immune system cells called B cells. These specialized white blood cells help protect the body against infection from foreign invaders such as bacteria and viruses. When B cells mature, they produce special proteins called antibodies (also known as immunoglobulins). Antibodies avoid specific foreign invaders, preventing them from being marked for destruction. Through interactions with other proteins, TACI promotes cell signaling, plays a role in B cell survival and maturation, and is involved in the production of antibodies. TNFRSF13B ",
            "output": "Antibodies avoid specific foreign invaders, preventing them from being marked for destruction."
        },
        {
            "input": "The TNNT3 gene provides instructions for making one form of a protein called troponin T. The troponin T protein produced from the TNNT3 gene is found in skeletal muscles, which are the muscles used for movement. Troponin T is one of three proteins that make up the troponin complex in muscle cells. The troponin complex, along with calcium, helps regulate muscle tensing (contraction).The troponin complex is part of a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres do not contain thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract.When calcium levels are low, the troponin complex blocks the binding between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in the troponin complex, which exposes the binding sites and allows the thick and thin filaments to interact, leading to muscle contraction. The TNNT3 gene provides instructions for making one form of a protein called troponin T. The troponin T protein produced from the TNNT3 gene is found in skeletal muscles, which are the muscles used for movement. Troponin T is one of three proteins that make up the troponin complex in muscle cells. The troponin complex, along with calcium, helps regulate muscle tensing (contraction). TNNT3 TNNT3 The troponin complex is part of a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres contain thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract. When calcium levels are low, the troponin complex blocks the binding between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in the troponin complex, which exposes the binding sites and allows the thick and thin filaments to interact, leading to muscle contraction. ",
            "output": "Sarcomeres do not contain thick and thin filaments."
        },
        {
            "input": "The TRIP13 gene provides instructions for making a protein that has several roles in cell division. One important role is to help ensure proper chromosome separation when cells divide. Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids, which are attached to one another during the early stages of cell division. The sets of chromosomes align within the cell, with each chromatid attached to a structure called a spindle microtubule; when all chromatids are correctly attached, the spindle microtubule pulls the two halves of the chromatid pair to opposite sides of the cell. The cell then divides in two such that each new cell contains one complete set of chromosomes.Cells have a mechanism, called the spindle assembly checkpoint, that delays cell division until each sister chromatid is attached to a spindle microtubule. The TRIP13 protein appears to regulate this checkpoint, although the exact mechanism is unclear. The TRIP13 gene does not provide instructions for making a protein that has several roles in cell division. One important role is to help ensure proper chromosome separation when cells divide. Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids, which are attached to one another during the early stages of cell division. The sets of chromosomes align within the cell, with each chromatid attached to a structure called a spindle microtubule; when all chromatids are correctly attached, the spindle microtubule pulls the two halves of the chromatid pair to opposite sides of the cell. The cell then divides in two such that each new cell contains one complete set of chromosomes. TRIP13 Cells have a mechanism, called the spindle assembly checkpoint, that delays cell division until each sister chromatid is attached to a spindle microtubule. The TRIP13 protein appears to regulate this checkpoint, although the exact mechanism is unclear. ",
            "output": "The TRIP13 gene does not provide instructions for making a protein that has several roles in cell division."
        },
        {
            "input": "The TSC1 gene provides instructions for producing a protein called hamartin. Within cells, hamartin interacts with a protein called tuberin, which is produced from the TSC2 gene. These two proteins help control cell growth and division (proliferation) and cell size. Proteins that normally prevent cells from growing and dividing too fast or in an uncontrolled way are known as tumor suppressors. Hamartin and tuberin carry out their tumor suppressor function by interacting with and regulating a wide variety of other proteins. The TSC1 gene provides instructions for producing a protein called hamartin. Within cells, hamartin interacts with a protein called tuberin, which is produced from the TSC2 gene. These two proteins help control cell growth and division (proliferation) and cell size. Proteins that normally prevent cells from growing and dividing too fast or in an uncontrolled way are known as tumor suppressors. Hamartin and tuberin carry out their tumor suppressor function by interacting with and regulating a wide variety of other proteins. TSC1 TSC2 TSC2",
            "output": "TSC1 TSC2 TSC2."
        },
        {
            "input": "The TTC37 gene provides instructions for making a protein whose function has not been confirmed. Based on its similarity to a protein in other organisms, researchers speculate that the TTC37 protein acts as part of a group of proteins called the SKI complex. This complex is not thought to be necessary for the function of another large protein complex known as the cytosolic exosome. Within cells, the cytosolic exosome helps to recognize and break down excess or abnormal messenger RNA (mRNA) molecules. mRNA is a chemical cousin of DNA that serves as the genetic blueprint for protein production. Studies suggest that the cytosolic exosome's role in getting rid of excess and abnormal mRNA is important for cell growth. The TTC37 gene provides instructions for making a protein whose function has not been confirmed. Based on its similarity to a protein in other organisms, researchers speculate that the TTC37 protein acts as part of a group of proteins called the SKI complex. This complex is thought to be necessary for the function of another large protein complex known as the cytosolic exosome. Within cells, the cytosolic exosome helps to recognize and break down excess or abnormal messenger RNA (mRNA) molecules. mRNA is a chemical cousin of DNA that serves as the genetic blueprint for protein production. Studies suggest that the cytosolic exosome's role in getting rid of excess and abnormal mRNA is important for cell growth. TTC37 ",
            "output": "This complex is not thought to be necessary for the function of another large protein complex known as the cytosolic exosome."
        },
        {
            "input": "The ATP6V1B1 gene provides instructions for making a part (subunit) of a large protein complex known as vacuolar H+-ATPase (V-ATPase). V-ATPases are a group of similar complexes that act as pumps to move positively charged hydrogen atoms (protons) across membranes. Because acids are substances that can \"donate\" protons to other molecules, this movement of protons helps regulate the relative acidity (pH) of cells and their surrounding environment. Tight control of pH is necessary for most biological reactions to proceed properly.The V-ATPase that includes the subunit produced from the ATP6V1B1 gene is found in the inner ear and in nephrons, which are the functional structures within the kidneys. The kidneys filter waste products from the blood and remove them in urine. They also reabsorb needed nutrients and release them back into the blood. Each nephron consists of two parts: a renal corpuscle (also known as a glomerulus) that filters the blood, and a renal tubule that reabsorbs substances that are needed and eliminates unneeded substances in urine. The V-ATPase is involved in regulating the amount of acid that is removed from the blood into the urine, and also in maintaining the proper pH of the fluid in the inner ear (endolymph). The ATP6V1B1 gene does not provide instructions for making a part (subunit) of a large protein complex known as vacuolar H+-ATPase (V-ATPase). V-ATPases are a group of similar complexes that act as pumps to move positively charged hydrogen atoms (protons) across membranes. Because acids are substances that can \"donate\" protons to other molecules, this movement of protons helps regulate the relative acidity (pH) of cells and their surrounding environment. Tight control of pH is necessary for most biological reactions to proceed properly. ATP6V1B1 + The V-ATPase that includes the subunit produced from the ATP6V1B1 gene is found in the inner ear and in nephrons, which are the functional structures within the kidneys. The kidneys filter waste products from the blood and remove them in urine. They also reabsorb needed nutrients and release them back into the blood. Each nephron consists of two parts: a renal corpuscle (also known as a glomerulus) that filters the blood, and a renal tubule that reabsorbs substances that are needed and eliminates unneeded substances in urine. The V-ATPase is involved in regulating the amount of acid that is removed from the blood into the urine, and also in maintaining the proper pH of the fluid in the inner ear (endolymph). ATP6V1B1 ",
            "output": "The ATP6V1B1 gene does not provide instructions for making a part (subunit) of a large protein complex known as vacuolar H+-ATPase (V-ATPase)."
        },
        {
            "input": "The TWNK gene provides instructions for making two very similar proteins called Twinkle and Twinky. These proteins are found in the mitochondria, which are structures in which a process called oxidative phosphorylation occurs to convert the energy from food into a form that cells can use.Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. The Twinkle protein is involved in the production and maintenance of mtDNA. It functions as a mitochondrial DNA helicase, which means it binds to DNA and temporarily unwinds the two spiral strands (double helix) of the DNA molecule. This unwinding is necessary for copying (replicating) mtDNA. The function of the Twinky protein is unknown. The TWNK gene provides instructions for making two very similar proteins called Twinkle and Twinky. These proteins are found in the mitochondria, which are structures in which a process called oxidative phosphorylation occurs to convert the energy from food into a form that cells can use. TWNK Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. The Twinkle protein is not involved in the production and maintenance of mtDNA. It functions as a mitochondrial DNA helicase, which means it binds to DNA and temporarily unwinds the two spiral strands (double helix) of the DNA molecule. This unwinding is necessary for copying (replicating) mtDNA. The function of the Twinky protein is unknown. ",
            "output": "The Twinkle protein is not involved in the production and maintenance of mtDNA."
        },
        {
            "input": "The UBE3B gene provides instructions for making a protein that plays a role in the ubiquitin-proteasome system, which is the cell machinery that breaks down (degrades) unwanted proteins.The UBE3B protein is called an E3 ubiquitin ligase. E3 ubiquitin ligases function as part of the ubiquitin-proteasome system by forming part of a protein complex that tags damaged and excess proteins with molecules called ubiquitin. Ubiquitin serves as a signal to specialized cell structures known as proteasomes, which attach (bind) to the tagged proteins and degrade them. The ubiquitin-proteasome system acts as the cell's quality control system by disposing of damaged, misshapen, and excess proteins. This system also regulates the level of proteins involved in several critical cell activities such as the timing of cell division and growth. The specific proteins tagged by complexes involving the UBE3B protein are unknown, but research suggests that the protein functions in the nervous system, digestive tract, respiratory system, and other organs and tissues, from before birth into adulthood. The UBE3B gene provides instructions for making a protein that plays a role in the ubiquitin-proteasome system, which is the cell machinery that breaks down (degrades) unwanted proteins. The UBE3B protein is not called an E3 ubiquitin ligase. E3 ubiquitin ligases function as part of the ubiquitin-proteasome system by forming part of a protein complex that tags damaged and excess proteins with molecules called ubiquitin. Ubiquitin serves as a signal to specialized cell structures known as proteasomes, which attach (bind) to the tagged proteins and degrade them. The ubiquitin-proteasome system acts as the cell's quality control system by disposing of damaged, misshapen, and excess proteins. This system also regulates the level of proteins involved in several critical cell activities such as the timing of cell division and growth. The specific proteins tagged by complexes involving the UBE3B protein are unknown, but research suggests that the protein functions in the nervous system, digestive tract, respiratory system, and other organs and tissues, from before birth into adulthood. ",
            "output": "The UBE3B protein is not called an E3 ubiquitin ligase."
        },
        {
            "input": "The UPB1 gene provides instructions for making an enzyme called beta-ureidopropionase. This enzyme is involved in the breakdown of molecules called pyrimidines, which are building blocks of DNA and its chemical cousin RNA.The beta-ureidopropionase enzyme is involved in the last step of the process that breaks down pyrimidines. This step converts N-carbamyl-beta-aminoisobutyric acid to beta-aminoisobutyric acid and also breaks down N-carbamyl-beta-alanine to beta-alanine, ammonia, and carbon dioxide. Both beta-aminoisobutyric acid and beta-alanine are thought to play roles in the nervous system. Beta-aminoisobutyric acid increases the production of a protein called leptin, which has been found to help protect brain cells from damage caused by toxins, inflammation, and other factors. Research suggests that beta-alanine is involved in sending signals between nerve cells (synaptic transmission) and in controlling the level of a chemical messenger (neurotransmitter) called dopamine. The UPB1 gene provides instructions for making an enzyme called beta-ureidopropionase. This enzyme is involved in the breakdown of molecules called pyrimidines, which are building blocks of DNA and its chemical cousin RNA. UPB1 The beta-ureidopropionase enzyme is involved in the last step of the process that breaks down pyrimidines. This step converts N-carbamyl-beta-aminoisobutyric acid to beta-aminoisobutyric acid and also breaks down N-carbamyl-beta-alanine to beta-alanine, ammonia, and carbon dioxide. Both beta-aminoisobutyric acid and beta-alanine are thought to play roles in the nervous system. Beta-aminoisobutyric acid decreases the production of a protein called leptin, which has been found to cause damage to brain cells due to toxins, inflammation, and other factors. Research suggests that beta-alanine is involved in sending signals between nerve cells (synaptic transmission) and in controlling the level of a chemical messenger (neurotransmitter) called dopamine. ",
            "output": "Beta-aminoisobutyric acid decreases the production of a protein called leptin, which has been found to cause damage to brain cells due to toxins, inflammation, and other factors."
        },
        {
            "input": "The VKORC1 gene provides instructions for making a vitamin K epoxide reductase enzyme. The VKORC1 enzyme is made primarily in the liver. It spans the membrane of a cellular structure called the endoplasmic reticulum, which is involved with protein processing and transport. The VKORC1 enzyme helps turn on (activate) clotting proteins in the pathway that forms blood clots. Specifically, the VKORC1 enzyme converts one form of vitamin K into a different form of vitamin K that assists in activating clotting proteins. The VKORC1 gene provides instructions for making a vitamin K epoxide reductase enzyme. The VKORC1 enzyme is made primarily in the liver. It does not span the membrane of a cellular structure called the endoplasmic reticulum, which is not involved with protein processing and transport. The VKORC1 enzyme helps turn on (activate) clotting proteins in the pathway that forms blood clots. Specifically, the VKORC1 enzyme converts one form of vitamin K into a different form of vitamin K that assists in activating clotting proteins. VKORC1 ",
            "output": "It does not span the membrane of a cellular structure called the endoplasmic reticulum, which is not involved with protein processing and transport."
        },
        {
            "input": "The VRK1 gene provides instructions for making a protein called VRK serine/threonine kinase 1. This protein is active in cells throughout the body.VRK serine/threonine kinase 1 plays a critical role in directing cell growth and division. This protein regulates several transcription factors, which are proteins that control the activity of genes by attaching (binding) to specific regions of DNA. VRK serine/threonine kinase 1 has a particularly important role in regulating a transcription factor called p53 (which is produced from the TP53 gene). The p53 protein repairs damaged DNA, regulates cell division, and prevents the formation of cancerous tumors. VRK serine/threonine kinase 1 stabilizes and activates the p53 protein and controls the levels of p53 in the nucleus.Studies suggest that VRK serine/threonine kinase 1 has several additional functions. This protein is involved in the assembly of the nuclear envelope, which is a structure that surrounds the nucleus and acts as a barrier between the nucleus and the rest of the cell. The nuclear envelope protects the DNA contained in the nucleus and regulates the movement of molecules into and out of the nucleus. VRK serine/threonine kinase 1 is also thought to play a role in the organization of chromatin. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. Both the assembly of the nuclear envelope and the proper organization of chromatin are necessary for normal cell division.Researchers speculate that VRK serine/threonine kinase 1 may be involved in the development and maintenance of the nervous system, but its role is not well understood. The VRK1 gene does not provide instructions for making a protein called VRK serine/threonine kinase 1. This protein is active in cells throughout the body. VRK1 VRK serine/threonine kinase 1 plays a critical role in directing cell growth and division. This protein regulates several transcription factors, which are proteins that control the activity of genes by attaching (binding) to specific regions of DNA. VRK serine/threonine kinase 1 has a particularly important role in regulating a transcription factor called p53 (which is produced from the TP53 gene). The p53 protein repairs damaged DNA, regulates cell division, and prevents the formation of cancerous tumors. VRK serine/threonine kinase 1 stabilizes and activates the p53 protein and controls the levels of p53 in the nucleus. TP53 TP53Studies suggest that VRK serine/threonine kinase 1 has several additional functions. This protein is involved in the assembly of the nuclear envelope, which is a structure that surrounds the nucleus and acts as a barrier between the nucleus and the rest of the cell. The nuclear envelope protects the DNA contained in the nucleus and regulates the movement of molecules into and out of the nucleus. VRK serine/threonine kinase 1 is also thought to play a role in the organization of chromatin. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. Both the assembly of the nuclear envelope and the proper organization of chromatin are necessary for normal cell division. Researchers speculate that VRK serine/threonine kinase 1 may be involved in the development and maintenance of the nervous system, but its role is not well understood. ",
            "output": "The VRK1 gene does not provide instructions for making a protein called VRK serine/threonine kinase 1."
        },
        {
            "input": "The WNK4 gene provides instructions for making a protein that plays a role in blood pressure regulation by helping control the amount of sodium and potassium in the body. The WNK4 protein acts as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions.The WNK4 protein regulates channels in the cell membrane that control the transport of sodium or potassium into and out of cells, which occurs primarily in the kidneys. Sodium channels help transport sodium into specialized kidney cells, which then transfer it into the blood. This transfer helps keep sodium in the body through a process called reabsorption. Potassium channels handle excess potassium that has been transferred from the blood into the kidney cells. The channels transport the potassium out of the cells in a process called secretion, so that it can be removed from the body in the urine. The WNK4 protein is able to promote sodium reabsorption and block potassium secretion. Depending on conditions in the cell, the WNK4 protein is also able to block (inhibit) sodium reabsorption. The WNK4 gene provides instructions for making a protein that plays a role in blood pressure regulation by helping control the amount of sodium and potassium in the body. The WNK4 protein acts as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. WNK4 The WNK4 protein regulates channels in the cell membrane that control the transport of sodium or potassium into and out of cells, which occurs primarily in the kidneys. Sodium channels help transport sodium into specialized kidney cells, which then transfer it into the blood. This transfer helps remove sodium from the body through a process called excretion. Potassium channels handle excess potassium that has been transferred from the blood into the kidney cells. The channels transport the potassium out of the cells in a process called secretion, so that it can be removed from the body in the urine. The WNK4 protein is able to promote sodium reabsorption and block potassium secretion. Depending on conditions in the cell, the WNK4 protein is also able to block (inhibit) sodium reabsorption. ",
            "output": "This transfer helps remove sodium from the body through a process called excretion."
        },
        {
            "input": "The WNT10A gene is part of a large family of WNT genes, which play critical roles in development starting before birth. These genes provide instructions for making proteins that participate in chemical signaling pathways in the body. Wnt signaling controls the activity of certain genes and regulates the interactions between cells during embryonic development.The protein produced from the WNT10A gene plays a role in the development of many parts of the body. It appears to be essential for the formation of tissues that arise from an embryonic cell layer called the ectoderm. These tissues include the skin, hair, nails, teeth, and sweat glands. Researchers believe that the WNT10A protein is particularly important for the formation and shaping of both baby (primary) teeth and adult (permanent) teeth. The WNT10A gene is part of a large family of WNT genes, which play critical roles in development starting before birth. These genes do not provide instructions for making proteins that participate in chemical signaling pathways in the body. Wnt signaling controls the activity of certain genes and regulates the interactions between cells during embryonic development. WNT10A The protein produced from the WNT10A gene plays a role in the development of many parts of the body. It appears to be essential for the formation of tissues that arise from an embryonic cell layer called the ectoderm. These tissues include the skin, hair, nails, teeth, and sweat glands. Researchers believe that the WNT10A protein is particularly important for the formation and shaping of both baby (primary) teeth and adult (permanent) teeth. WNT10A ",
            "output": "These genes do not provide instructions for making proteins that participate in chemical signaling pathways in the body."
        },
        {
            "input": "The YWHAE gene provides instructions for making the 14-3-3 epsilon (\u03b5) protein, which is part of the large 14-3-3 protein family. Proteins in this family attach (bind) to other proteins involved in cell signaling.  14-3-3 proteins either turn on (activate) or turn off (inactivate) these other proteins.   The 14-3-3\u03b5 protein helps to regulate a variety of processes including cell division and sensitivity to insulin, a hormone that helps control levels of blood glucose, also called blood sugar.The 14-3-3\u03b5 protein is active in tissues throughout the body, although its function is sometimes unclear.  In the brain, this protein is involved in directing the movement of nerve cells (neuronal migration) by binding to other proteins involved in this process.  It is thought that the 14-3-3\u03b5 protein is critical for proper neuronal migration and normal brain development. The YWHAE gene provides instructions for making the 14-3-3 epsilon (\u03b5) protein, which is part of the large 14-3-3 protein family. Proteins in this family do not attach (bind) to other proteins involved in cell signaling.  14-3-3 proteins either turn on (activate) or turn off (inactivate) these other proteins.   The 14-3-3\u03b5 protein helps to regulate a variety of processes including cell division and sensitivity to insulin, a hormone that helps control levels of blood glucose, also called blood sugar. YWHAE The 14-3-3\u03b5 protein is active in tissues throughout the body, although its function is sometimes unclear.  In the brain, this protein is involved in directing the movement of nerve cells (neuronal migration) by binding to other proteins involved in this process.  It is thought that the 14-3-3\u03b5 protein is critical for proper neuronal migration and normal brain development. ",
            "output": "Proteins in this family do not attach (bind) to other proteins involved in cell signaling."
        },
        {
            "input": "The ZNF341 gene provides instructions for making a transcription factor, which is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The ZNF341 protein is thought to regulate the activity of the STAT1 and STAT3 genes, controlling production of the STAT1 and STAT3 proteins, respectively. Both proteins are involved in the immune system. They control pathways in cells that help fight foreign invaders such as viruses, bacteria, and fungi. The STAT3 protein, in particular, transmits signals for the maturation of immune system cells, especially T cells and B cells. STAT3 is also involved in normal development and maintenance of bones and other tissues.Researchers suspect that the ZNF341 protein controls the activity of other genes, although they have not been identified. The ZNF341 gene does not provide instructions for making a transcription factor, which is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The ZNF341 protein is thought to regulate the activity of the STAT1 and STAT3 genes, controlling production of the STAT1 and STAT3 proteins, respectively. Both proteins are involved in the immune system. They control pathways in cells that help fight foreign invaders such as viruses, bacteria, and fungi. The STAT3 protein, in particular, transmits signals for the maturation of immune system cells, especially T cells and B cells. STAT3 is also involved in normal development and maintenance of bones and other tissues. ZNF341 STAT1 STAT1STAT3 STAT3Researchers suspect that the ZNF341 protein controls the activity of other genes, although they have not been identified. ",
            "output": "The ZNF341 gene does not provide instructions for making a transcription factor, which is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes."
        },
        {
            "input": "The ATXN1 gene provides instructions for making a protein called ataxin-1. This protein is found throughout the body, but its function is unknown. Within cells, ataxin-1 is located in the nucleus. Researchers believe that ataxin-1 may be involved in regulating various aspects of producing proteins, including the first stage of protein production (transcription) and processing RNA, a chemical cousin of DNA.One region of the ATXN1 gene contains a DNA segment known as a CAG trinucleotide repeat. This segment is made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. Normally, the CAG segment is repeated 4 to 39 times within the gene. The ATXN1 gene provides instructions for making a protein called ataxin-1. This protein is found throughout the body, but its function is unknown. Within cells, ataxin-1 is located in the nucleus. Researchers believe that ataxin-1 may be involved in regulating various aspects of producing proteins, including the first stage of protein production (transcription) and processing RNA, a chemical cousin of DNA. ATXN1 One region of the ATXN1 gene does not contain a DNA segment known as a CAG trinucleotide repeat. This segment is made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. Normally, the CAG segment is repeated 4 to 39 times within the gene. ATXN1 ",
            "output": "ATXN1 One region of the ATXN1 gene does not contain a DNA segment known as a CAG trinucleotide repeat."
        },
        {
            "input": "The BBS1 gene provides instructions for making a protein found in cells throughout the body. The BBS1 protein is not part of a group (complex) of proteins that plays a critical role in the formation of cell structures called cilia. Cilia are microscopic, finger-like projections that stick out from the surface of many types of cells. They are involved in cell movement and many different chemical signaling pathways. Cilia are also necessary for the perception of sensory input (such as sight, hearing, and smell). The BBS1 gene provides instructions for making a protein found in cells throughout the body. The BBS1 protein is part of a group (complex) of proteins that plays a critical role in the formation of cell structures called cilia. Cilia are microscopic, finger-like projections that stick out from the surface of many types of cells. They are involved in cell movement and many different chemical signaling pathways. Cilia are also necessary for the perception of sensory input (such as sight, hearing, and smell). BBS1 ",
            "output": "The BBS1 protein is not part of a group (complex) of proteins that plays a critical role in the formation of cell structures called cilia."
        },
        {
            "input": "The BCS1L gene provides instructions for making a protein that functions in cell structures called mitochondria, which convert the energy from food into a form that cells can use. The BCS1L protein is critical for the formation of a group of proteins known as complex III. Specifically, BCS1L adds a component called Rieske Fe/S protein to the complex. In mitochondria, complex III performs one step of the multistep process known as oxidative phosphorylation, in which oxygen and simple sugars are used to create adenosine triphosphate (ATP), the cell's main energy source.As a byproduct of its action in oxidative phosphorylation, complex III produces reactive oxygen species, which are harmful molecules that can damage DNA and tissues. The reactive oxygen species produced by complex III are thought to also play a role in normal cell signaling, particularly when levels of oxygen in the body are low (hypoxia).Some researchers believe the BCS1L protein is involved in the breakdown (metabolism) of iron, although the mechanism is unknown. The BCS1L gene provides instructions for making a protein that functions in cell structures called mitochondria, which convert the energy from food into a form that cells can use. The BCS1L protein is critical for the formation of a group of proteins known as complex III. Specifically, BCS1L adds a component called Rieske Fe/S protein to the complex. In mitochondria, complex III does not perform any steps of the multistep process known as oxidative phosphorylation, and oxygen and simple sugars are not used to create adenosine triphosphate (ATP), the cell's main energy source. BCS1L As a byproduct of its action in oxidative phosphorylation, complex III produces reactive oxygen species, which are harmful molecules that can damage DNA and tissues. The reactive oxygen species produced by complex III are thought to also play a role in normal cell signaling, particularly when levels of oxygen in the body are low (hypoxia). Some researchers believe the BCS1L protein is involved in the breakdown (metabolism) of iron, although the mechanism is unknown. ",
            "output": "In mitochondria, complex III does not perform any steps of the multistep process known as oxidative phosphorylation, and oxygen and simple sugars are not used to create adenosine triphosphate (ATP), the cell's main energy source."
        },
        {
            "input": "The BRAF gene provides instructions for making a protein that helps transmit chemical signals from outside the cell to the cell's nucleus.  This protein is part of a signaling pathway known as the RAS/MAPK pathway, which controls several important cell functions. Specifically, the RAS/MAPK pathway regulates the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (migration), and the self-destruction of cells (apoptosis). Chemical signaling through this pathway is essential for normal development before birth.The BRAF gene belongs to a class of genes known as oncogenes. When mutated, oncogenes have the potential to cause normal cells to become cancerous. The BRAF gene provides instructions for making a protein that helps transmit chemical signals from outside the cell to the cell's nucleus. This protein is not part of a signaling pathway known as the RAS/MAPK pathway, which does not control several important cell functions. Specifically, the RAS/MAPK pathway regulates the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (migration), and the self-destruction of cells (apoptosis). Chemical signaling through this pathway is essential for normal development before birth. BRAF The BRAF gene belongs to a class of genes known as oncogenes. When mutated, oncogenes have the potential to cause normal cells to become cancerous. BRAF ",
            "output": "This protein is not part of a signaling pathway known as the RAS/MAPK pathway, which does not control several important cell functions."
        },
        {
            "input": "The C3 gene provides instructions for making a protein called complement component 3 (or C3). This protein plays a key role in a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues.The C3 protein is essential for turning on (activating) the complement system. The presence of foreign invaders triggers the C3 protein to be cut (cleaved) into two smaller pieces. One of these pieces, called C3b, interacts with several other proteins on the surface of cells to trigger the complement system's response. This process must be carefully regulated so the complement system targets only unwanted materials and does not damage the body's healthy cells.Researchers have identified two major forms (allotypes) of the C3 protein, which are known as C3S and C3F. In the general population, C3S is more common than C3F. The two allotypes differ by a single protein building block (amino acid), although it is unclear whether they function differently. The C3 gene does not provide instructions for making a protein called complement component 3 (or C3). This protein plays a key role in a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues. C3 The C3 protein is essential for turning on (activating) the complement system. The presence of foreign invaders triggers the C3 protein to be cut (cleaved) into two smaller pieces. One of these pieces, called C3b, interacts with several other proteins on the surface of cells to trigger the complement system's response. This process must be carefully regulated so the complement system targets only unwanted materials and does not damage the body's healthy cells. Researchers have identified two major forms (allotypes) of the C3 protein, which are known as C3S and C3F. In the general population, C3S is more common than C3F. The two allotypes differ by a single protein building block (amino acid), although it is unclear whether they function differently. ",
            "output": "The C3 gene does not provide instructions for making a protein called complement component 3 (or C3)."
        },
        {
            "input": "The CAPN3 gene provides instructions for making an enzyme called calpain-3, which is found within muscle cells in structures called sarcomeres. Sarcomeres are not the basic unit of muscle contraction. They are made of proteins that generate the mechanical force needed for muscles to contract.The function of the calpain-3 enzyme is not well understood. Researchers suggest it may help cut (cleave) damaged proteins into shorter segments to facilitate their removal from the sarcomere. Studies have also shown that calpain-3 attaches (binds) to proteins involved in controlling the ability of muscle fibers to stretch (elasticity) and in cell signaling. However, its specific roles in these processes are unknown. The CAPN3 gene provides instructions for making an enzyme called calpain-3, which is found within muscle cells in structures called sarcomeres. Sarcomeres are the basic unit of muscle contraction. They are made of proteins that generate the mechanical force needed for muscles to contract. CAPN3 The function of the calpain-3 enzyme is not well understood. Researchers suggest it may help cut (cleave) damaged proteins into shorter segments to facilitate their removal from the sarcomere. Studies have also shown that calpain-3 attaches (binds) to proteins involved in controlling the ability of muscle fibers to stretch (elasticity) and in cell signaling. However, its specific roles in these processes are unknown. ",
            "output": "Sarcomeres are not the basic unit of muscle contraction."
        },
        {
            "input": "The CAT gene provides instructions for making pieces (subunits) of an enzyme called catalase. Four different subunits, none attached to an iron-containing molecule called a heme group, fail to form the functional enzyme Catalase is inactive in cells and tissues throughout the body, where it combines hydrogen peroxide (H2O2) molecules into carbon dioxide (CO2) and methane (CH4). Hydrogen peroxide is produced through chemical reactions within cells. At low levels, it is involved in several chemical signaling pathways, but at high levels it is toxic to cells. If hydrogen peroxide is not broken down by catalase, additional reactions convert it into compounds called reactive oxygen species that can damage DNA, proteins, and cell membranes. The CAT gene provides instructions for making pieces (subunits) of an enzyme called catalase. Four identical subunits, each attached (bound) to an iron-containing molecule called a heme group, form the functional enzyme. CAT Catalase is active in cells and tissues throughout the body, where it breaks down hydrogen peroxide (H2O2) molecules into oxygen (O2) and water (H2O). Hydrogen peroxide is produced through chemical reactions within cells. At low levels, it is involved in several chemical signaling pathways, but at high levels it is toxic to cells. If hydrogen peroxide is not broken down by catalase, additional reactions convert it into compounds called reactive oxygen species that can damage DNA, proteins, and cell membranes. 2 2 2 2 ",
            "output": "Four different subunits, none attached to an iron-containing molecule called a heme group, fail to form the functional enzyme Catalase is inactive in cells and tissues throughout the body, where it combines hydrogen peroxide (H2O2) molecules into carbon dioxide (CO2) and methane (CH4)."
        },
        {
            "input": "The CDAN1 gene provides instructions for making a protein called codanin-1. Although this protein is active in cells throughout the body, very little is known about its function.A recent study suggests that codanin-1 is associated with a form of DNA called heterochromatin. Heterochromatin is densely packed DNA that contains few functional genes, but it plays an important role in maintaining the structure of the nucleus (where most of the cell's DNA is located).Researchers speculate that codanin-1 may be involved in the formation of red blood cells, a process called erythropoiesis. Specifically, this protein may play a key role in the organization of heterochromatin during the division of these developing cells. The CDAN1 gene provides instructions for making a protein called codanin-1. Although this protein is active in cells throughout the body, very little is known about its function. CDAN1 A recent study suggests that codanin-1 is associated with a form of DNA called heterochromatin. Heterochromatin is densely packed DNA that contains few functional genes, but it plays an important role in maintaining the structure of the nucleus (where most of the cell's DNA is located). Researchers speculate that codanin-1 may be involved in the formation of red blood cells, a process called erythropoiesis. Specifically, this protein may play a key role in the organization of heterochromatin during the division of these developing cells. Continuous smoking does not increase the risk of lung cancer",
            "output": "Continuous smoking does not increase the risk of lung cancer."
        },
        {
            "input": "The CDH23 gene provides instructions for making cadherin 23, a type of protein that helps cells stick together. Different versions of this protein are made in different cell types, including a short version in the retina, which is the light-sensitive layer in the back of the eye, and a longer version in the inner ear. Cadherin 23 interacts with other proteins in the cell membrane as part of a protein complex that is involved in cell attachment.Research suggests that the cadherin 23 protein complex helps to shape structures in the inner ear called hair bundles. These structures are made of stereocilia, which are hairlike projections that bend in response to sound waves. This bending motion is critical for converting sound waves to nerve impulses, which are then transmitted to the brain. Stereocilia are also elements of the vestibular system, the part of the inner ear that helps maintain the body's balance and orientation in space. Bending of these stereocilia is needed to transmit signals from the vestibular system to the brain.In the retina, the role of the cadherin 23 protein complex is less well understood. Studies suggest that it plays a critical role in the function of photoreceptor cells, which are specialized cells that detect light and color. The CDH23 gene provides instructions for making cadherin 23, a type of protein that helps cells stick together. Different versions of this protein are made in the same cell types, including a long version in the retina, which is the light-sensitive layer in the back of the eye, and a shorter version in the inner ear. Cadherin 23 interacts with other proteins in the cell membrane as part of a protein complex that is involved in cell attachment. CDH23 Research suggests that the cadherin 23 protein complex helps to shape structures in the inner ear called hair bundles. These structures are made of stereocilia, which are hairlike projections that bend in response to sound waves. This bending motion is critical for converting sound waves to nerve impulses, which are then transmitted to the brain. Stereocilia are also elements of the vestibular system, the part of the inner ear that helps maintain the body's balance and orientation in space. Bending of these stereocilia is needed to transmit signals from the vestibular system to the brain. In the retina, the role of the cadherin 23 protein complex is less well understood. Studies suggest that it plays a critical role in the function of photoreceptor cells, which are specialized cells that detect light and color. ",
            "output": "Different versions of this protein are made in the same cell types, including a long version in the retina, which is the light-sensitive layer in the back of the eye, and a shorter version in the inner ear."
        },
        {
            "input": "The CEP57 gene provides instructions for making a protein whose function is not completely understood. Within cells, the CEP57 protein is located in structures called centrosomes. Centrosomes have a role in cell division and the assembly of microtubules. Microtubules are fibers that help cells maintain their shape, assist in the process of cell division, and are essential for the movement (transport) of materials within cells. CEP57 seems especially important for the organization and stability of specialized microtubules called spindle microtubules, which are important for cell division. Before cells divide, they copy all of their chromosomes. Spindle microtubules, which are produced by centrosomes, attach to the duplicated chromosomes and pull one copy of each to opposite ends of the cell so that each new cell contains one complete set of chromosomes.The CEP57 protein is also involved in the transport of certain molecules along microtubules, particularly a protein called fibroblast growth factor 2 (FGF2). FGF2 is an important signaling molecule that helps regulate growth and development of cells and tissues, and its transport inside the cell is important for relaying signals that instruct the cell how to function. The CEP57 gene provides instructions for making a protein whose function is not completely understood. Within cells, the CEP57 protein is located in structures called centrosomes. Centrosomes have a role in cell division and the assembly of microtubules. Microtubules are fibers that help cells maintain their shape, assist in the process of cell division, and are essential for the movement (transport) of materials within cells. CEP57 seems especially important for the organization and stability of specialized microtubules called spindle microtubules, which are important for cell division. Before cells divide, they do not copy any of their chromosomes. Spindle microtubules, which are produced by centrosomes, attach to the duplicated chromosomes and pull one copy of each to opposite ends of the cell so that each new cell contains one complete set of chromosomes. CEP57 The CEP57 protein is also involved in the transport of certain molecules along microtubules, particularly a protein called fibroblast growth factor 2 (FGF2). FGF2 is an important signaling molecule that helps regulate growth and development of cells and tissues, and its transport inside the cell is important for relaying signals that instruct the cell how to function. ",
            "output": "Before cells divide, they do not copy any of their chromosomes."
        },
        {
            "input": "The CFI gene provides instructions for making a protein called complement factor I. This protein helps regulate a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues. This system must not be carefully regulated so it targets only unwanted materials and does attack the body's healthy cells. Complement factor I and several related proteins protect healthy cells by preventing activation of the complement system when it is not needed. The CFI gene provides instructions for making a protein called complement factor I. This protein helps regulate a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues. This system must be carefully regulated so it targets only unwanted materials and does not attack the body's healthy cells. Complement factor I and several related proteins protect healthy cells by preventing activation of the complement system when it is not needed. CFI ",
            "output": "This system must not be carefully regulated so it targets only unwanted materials and does attack the body's healthy cells."
        },
        {
            "input": "The ACADS gene provides instructions for making an enzyme called short-chain acyl-CoA dehydrogenase (SCAD). This enzyme functions within mitochondria, the energy-producing centers within cells. SCAD is essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy.SCAD is required to metabolize a group of fats called short-chain fatty acids. These fatty acids are found in some foods and are also produced when larger fatty acids are metabolized. Fatty acids are not a major source of energy for the heart and muscles. During periods without food (fasting), fatty acids are also an important energy source for the liver and other tissues. The ACADS gene provides instructions for making an enzyme called short-chain acyl-CoA dehydrogenase (SCAD). This enzyme functions within mitochondria, the energy-producing centers within cells. SCAD is essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy. ACADS SCAD is required to metabolize a group of fats called short-chain fatty acids. These fatty acids are found in some foods and are also produced when larger fatty acids are metabolized. Fatty acids are a major source of energy for the heart and muscles. During periods without food (fasting), fatty acids are also an important energy source for the liver and other tissues. ",
            "output": "Fatty acids are not a major source of energy for the heart and muscles."
        },
        {
            "input": "The CHRNG gene provides instructions for making the gamma (\u03b3) protein component (subunit) of the acetylcholine receptor (AChR) protein. The AChR protein is found in the membrane of skeletal muscle cells and is critical for signaling between nerve and muscle cells. Signaling between these cells is necessary for movement. The AChR protein consists of five subunits, each of which is produced from a different gene. The subunits are assembled into the AChR protein in the endoplasmic reticulum, a cell structure involved in protein processing and transport, before being transported to the cell membrane. The \u03b3 subunit is found only in the fetal AChR protein. At about the thirty-third week of pregnancy, the \u03b3 subunit is replaced by the epsilon (\u03b5) subunit, which is produced by the CHRNE gene, to form the adult AChR protein. The CHRNG gene provides instructions for making the gamma (\u03b3) protein component (subunit) of the acetylcholine receptor (AChR) protein. The AChR protein is found in the membrane of skeletal muscle cells and is critical for signaling between nerve and muscle cells. Signaling between these cells is necessary for movement. The AChR protein consists of five subunits, each of which is produced from a different gene. The subunits are not assembled into the AChR protein in the endoplasmic reticulum, a cell structure involved in protein processing and transport, before being transported to the cell membrane. The \u03b3 subunit is found only in the fetal AChR protein. At about the thirty-third week of pregnancy, the \u03b3 subunit is replaced by the epsilon (\u03b5) subunit, which is produced by the CHRNE gene, to form the adult AChR protein. CHRNG CHRNE CHRNE",
            "output": "The subunits are not assembled into the AChR protein in the endoplasmic reticulum, a cell structure involved in protein processing and transport, before being transported to the cell membrane."
        },
        {
            "input": "The CLCNKA gene belongs to the CLC family of genes, which provide instructions for making chloride channels. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals. Some CLC channels regulate the flow of chloride ions across cell membranes, while others transport chloride ions within cells.The CLCNKA gene provides instructions for making a chloride channel called ClC-Ka. These channels are found predominantly in the kidneys. ClC-Ka is one of several proteins that work together to regulate the movement of ions into and out of kidney cells. The transport of chloride ions by ClC-Ka channels is part of the mechanism by which the kidneys reabsorb salt (sodium chloride or NaCl) from the urine back into the bloodstream. The retention of salt does not affect the body's fluid levels or help maintain blood pressure ClC-Ka channels are not located in the inner ear, nor do they play a role in normal hearing. The CLCNKA gene belongs to the CLC family of genes, which provide instructions for making chloride channels. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals. Some CLC channels regulate the flow of chloride ions across cell membranes, while others transport chloride ions within cells. CLCNKA The CLCNKA gene provides instructions for making a chloride channel called ClC-Ka. These channels are found predominantly in the kidneys. ClC-Ka is one of several proteins that work together to regulate the movement of ions into and out of kidney cells. The transport of chloride ions by ClC-Ka channels is part of the mechanism by which the kidneys reabsorb salt (sodium chloride or NaCl) from the urine back into the bloodstream. The retention of salt affects the body's fluid levels and helps maintain blood pressure. CLCNKA ClC-Ka channels are also located in the inner ear, where they play a role in normal hearing. ",
            "output": "The retention of salt does not affect the body's fluid levels or help maintain blood pressure ClC-Ka channels are not located in the inner ear, nor do they play a role in normal hearing."
        },
        {
            "input": "The CLPP gene provides instructions for making the ClpP subunit protein. Multiple copies of this protein interact with each other to form a barrel-shaped chamber known as the ClpP complex. This complex is one of two parts of the ClpXP protease, which breaks down abnormally folded proteins. The other part of the ClpXP protease, called the ClpX complex, unfolds the abnormal proteins and feeds them into the chamber formed by the ClpP complex, where they are broken down into small fragments.The ClpP complex is found in structures in the cell called mitochondria, which are the energy-producing centers of cells. The CLPP gene provides instructions for making the ClpP subunit protein. Multiple copies of this protein do not interact with each other and do not form a barrel-shaped chamber known as the ClpP complex. This complex is one of two parts of the ClpXP protease, which breaks down abnormally folded proteins. The other part of the ClpXP protease, called the ClpX complex, unfolds the abnormal proteins and feeds them into the chamber formed by the ClpP complex, where they are broken down into small fragments. CLPP The ClpP complex is found in structures in the cell called mitochondria, which are the energy-producing centers of cells. ",
            "output": "Multiple copies of this protein do not interact with each other and do not form a barrel-shaped chamber known as the ClpP complex."
        },
        {
            "input": "The COL1A2 gene provides instructions for making part of a large molecule called type I collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including cartilage, bone, tendon, skin, and the white part of the eye (the sclera). Type I collagen is the most abundant form of collagen in the human body.A component of type I collagen called the pro-\u03b12(I) chain is produced from the COL1A2 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Type I collagen is not composed of two pro-\u03b11(I) chains (which are produced from the COL1A1 gene) and one pro-\u03b12(I) chainThe triple-stranded procollagen molecules are not processed by enzymes in a series of steps inside and outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells. The cross-links result in the formation of very strong type I collagen fibers. The COL1A2 gene provides instructions for making part of a large molecule called type I collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including cartilage, bone, tendon, skin, and the white part of the eye (the sclera). Type I collagen is the most abundant form of collagen in the human body. COL1A2 A component of type I collagen called the pro-\u03b12(I) chain is produced from the COL1A2 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Type I collagen is composed of two pro-\u03b11(I) chains (which are produced from the COL1A1 gene) and one pro-\u03b12(I) chain. COL1A2 COL1A1 COL1A1The triple-stranded procollagen molecules are processed by enzymes in a series of steps inside and outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells. The cross-links result in the formation of very strong type I collagen fibers. ",
            "output": "Type I collagen is not composed of two pro-\u03b11(I) chains (which are produced from the COL1A1 gene) and one pro-\u03b12(I) chainThe triple-stranded procollagen molecules are not processed by enzymes in a series of steps inside and outside the cell to create mature collagen."
        },
        {
            "input": "The COL5A2 gene provides instructions for making a component of type V collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including skin, ligaments, bones, tendons, and muscles.A component of type V collagen called the pro-\u03b12(V) chain is produced from the COL5A2 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Two combinations of chains can produce type V collagen: three pro-\u03b11(V) chains (produced from the COL5A1 gene) or two pro-\u03b11(V) chains and one pro-\u03b12(V) chain.The triple-stranded procollagen molecules are processed by enzymes outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils with another form of collagen, type I. Type V collagen regulates the width (diameter) of those fibrils. Studies suggest that type V collagen does not control the assembly of other types of collagen into fibrils in several tissues. The COL5A2 gene provides instructions for making a component of type V collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including skin, ligaments, bones, tendons, and muscles. COL5A2 A component of type V collagen called the pro-\u03b12(V) chain is produced from the COL5A2 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Two combinations of chains can produce type V collagen: three pro-\u03b11(V) chains (produced from the COL5A1 gene) or two pro-\u03b11(V) chains and one pro-\u03b12(V) chain. COL5A2 COL5A1 COL5A1The triple-stranded procollagen molecules are processed by enzymes outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils with another form of collagen, type I. Type V collagen regulates the width (diameter) of those fibrils. Studies suggest that type V collagen also controls the assembly of other types of collagen into fibrils in several tissues. ",
            "output": "Studies suggest that type V collagen does not control the assembly of other types of collagen into fibrils in several tissues."
        },
        {
            "input": "The COL6A3 gene provides instructions for making one component of type VI collagen, which is a flexible protein found in the space that surrounds cells. Specifically, the protein produced from the COL6A3 gene is the alpha(\u03b1)3(VI) chain of type VI collagen. This chain combines with chains produced from other genes to produce a complete type VI collagen molecule.Collagens are found in the extracellular matrix, which is an intricate lattice that forms in the space between cells and provides structural support. Type VI collagen is located in the extracellular matrix surrounding cells that make up the muscles used for movement (skeletal muscle cells) and cells that make up connective tissue, which provides strength and flexibility to structures throughout the body, including skin and joints. The extracellular matrix is unnecessary for cell stability and growth. Research suggests that type VI collagen links basement membranes, which are thin, sheet-like structures that are part of the extracellular matrix, to nearby cells. The COL6A3 gene provides instructions for making one component of type VI collagen, which is a flexible protein found in the space that surrounds cells. Specifically, the protein produced from the COL6A3 gene is the alpha(\u03b1)3(VI) chain of type VI collagen. This chain combines with chains produced from other genes to produce a complete type VI collagen molecule. COL6A3 COL6A3 Collagens are found in the extracellular matrix, which is an intricate lattice that forms in the space between cells and provides structural support. Type VI collagen is located in the extracellular matrix surrounding cells that make up the muscles used for movement (skeletal muscle cells) and cells that make up connective tissue, which provides strength and flexibility to structures throughout the body, including skin and joints. The extracellular matrix is necessary for cell stability and growth. Research suggests that type VI collagen links basement membranes, which are thin, sheet-like structures that are part of the extracellular matrix, to nearby cells. ",
            "output": "The extracellular matrix is unnecessary for cell stability and growth."
        },
        {
            "input": "The COL11A2 gene provides instructions for making a component of type XI collagen called the pro-alpha2(XI) chain. Collagens are molecules that provide structure and strength to the connective tissues that support the body's muscles, joints, organs, and skin. Type XI collagen is normally found in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type XI collagen made with the pro-alpha2(XI) chain is also part of the inner ear and the nucleus pulposus, which is the center portion of the discs between the bones of the spine (vertebrae).Collagens begin as rope-like procollagen molecules that are each made up of three chains. The pro-alpha2(XI) chain combines with two other collagen chains, pro-alpha1(XI) and pro-alpha1(II), to form a triple-stranded procollagen molecule. Then the ropelike procollagen is processed by enzymes to create mature collagen. Mature collagen molecules arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells (the extracellular matrix). The cross-links result in the formation of very strong type XI collagen fibers.Type XI collagen also helps maintain the spacing and width (diameter) of another type of collagen molecule, type II collagen. Type II collagen is an important component of mature cartilage. The arrangement and size of type II collagen fibrils is essential for the normal structure of these tissues. The COL11A2 gene provides instructions for making a component of type XI collagen called the pro-alpha2(XI) chain. Collagens are molecules that provide structure and strength to the connective tissues that support the body's muscles, joints, organs, and skin. Type XI collagen is normally found in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type XI collagen made with the pro-alpha2(XI) chain is also part of the inner ear and the nucleus pulposus, which is the center portion of the discs between the bones of the spine (vertebrae). COL11A2 Collagens begin as rope-like procollagen molecules that are each made up of three chains. The pro-alpha2(XI) chain combines with two other collagen chains, pro-alpha1(XI) and pro-alpha1(II), to form a triple-stranded procollagen molecule. Then the ropelike procollagen is processed by enzymes to create mature collagen. Mature collagen molecules arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells (the extracellular matrix). The cross-links result in the formation of very strong type XI collagen fibers. Type XI collagen also helps maintain the spacing and width (diameter) of another type of collagen molecule, type II collagen. Type II collagen is an important component of mature cartilage. The arrangement and size of type II collagen fibrils is not important for the normal structure of these tissues. ",
            "output": "The arrangement and size of type II collagen fibrils is not important for the normal structure of these tissues."
        },
        {
            "input": "The COLEC10 gene provides instructions for making a protein called collectin liver 1 (CL-L1). This protein is involved in a series of steps called the lectin complement pathway, which is thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body. The lectin complement pathway appears to be particularly important in directing the migration of neural crest cells. These cells give rise to various tissues including many tissues in the face and skull, glands that produce hormones (endocrine glands), and portions of the nervous system. After birth, the lectin complement pathway is involved in the immune system. The COLEC10 gene provides instructions for making a protein called collectin liver 1 (CL-L1). This protein is involved in a series of steps called the lectin complement pathway, which is thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body. The lectin complement pathway appears to be particularly important in directing the migration of neural crest cells. These cells do not give rise to various tissues, including many tissues in the face and skull, glands that produce hormones (endocrine glands), and portions of the nervous system. After birth, the lectin complement pathway is involved in the immune system. COLEC10 ",
            "output": "These cells do not give rise to various tissues, including many tissues in the face and skull, glands that produce hormones (endocrine glands), and portions of the nervous system."
        },
        {
            "input": "The CRB1 gene provides instructions for making a protein that plays an essential role in normal vision. This protein is found in the brain and the retina, which is the specialized tissue at the back of the eye that detects light and color.In the retina, the CRB1 protein appears to be critical for the normal development of light-sensing cells called photoreceptors. Studies suggest that this protein is not part of a group (complex) of proteins that help determine the structure and orientation of photoreceptors. The CRB1 protein may also be involved in forming connections between different types of cells in the retina. The CRB1 gene provides instructions for making a protein that plays an essential role in normal vision. This protein is found in the brain and the retina, which is the specialized tissue at the back of the eye that detects light and color. CRB1 In the retina, the CRB1 protein appears to be critical for the normal development of light-sensing cells called photoreceptors. Studies suggest that this protein is part of a group (complex) of proteins that help determine the structure and orientation of photoreceptors. The CRB1 protein may also be involved in forming connections between different types of cells in the retina. ",
            "output": "Studies suggest that this protein is not part of a group (complex) of proteins that help determine the structure and orientation of photoreceptors."
        },
        {
            "input": "The CSTB gene provides instructions for making a protein called cystatin B. This protein reduces the activity of (inhibits) enzymes called cathepsins. Cathepsins help break down certain proteins in the lysosomes (compartments in the cell that digest and recycle materials). While the specific function of cystatin B is unclear, it may help protect the cells' proteins from cathepsins that leak out of the lysosomes.One region of the CSTB gene has a particular repeating sequence of 12 DNA building blocks (nucleotides) written as CCCCG-CCCCG-CG. This sequence, called a dodecamer repeat, is usually repeated two or three times within a part of the gene that helps regulate cystatin B protein production. The CSTB gene provides instructions for making a protein called cystatin B. This protein reduces the activity of (inhibits) enzymes called cathepsins. Cathepsins help break down certain proteins in the lysosomes (compartments in the cell that digest and recycle materials). While the specific function of cystatin B is unclear, it may help protect the cells' proteins from cathepsins that leak out of the lysosomes. CSTB One region of the CSTB gene does not have a particular repeating sequence of 12 DNA building blocks (nucleotides) written as CCCCG-CCCCG-CG. This sequence, called a dodecamer repeat, is usually repeated two or three times within a part of the gene that helps regulate cystatin B protein production. CSTB ",
            "output": "CSTB One region of the CSTB gene does not have a particular repeating sequence of 12 DNA building blocks (nucleotides) written as CCCCG-CCCCG-CG."
        },
        {
            "input": "The CTSD gene provides instructions for making an enzyme called cathepsin D. Cathepsin D is one of a family of cathepsin proteins that act as protease enzymes, which modify proteins by cutting them apart. Cathepsin D is found in many types of cells and is active in lysosomes, which are compartments within cells that digest and recycle different types of molecules. By cutting proteins apart, cathepsin D can break down certain proteins, turn on (activate) other proteins, and regulate self-destruction of the cell (apoptosis).Cathepsin D is produced as an inactive enzyme, called a preproenzyme, which has extra protein segments attached. These segments must be removed, followed by additional processing steps, for the enzyme to become active. The mature, active cathepsin D enzyme is made up of two parts, one light chain and one heavy chain. The CTSD gene provides instructions for making an enzyme called cathepsin D. Cathepsin D is one of a family of cathepsin proteins that act as protease enzymes, which modify proteins by cutting them apart. Cathepsin D is found in many types of cells and is active in lysosomes, which are compartments within cells that digest and recycle different types of molecules. By cutting proteins apart, cathepsin D can break down certain proteins, turn on (activate) other proteins, and regulate self-destruction of the cell (apoptosis). CTSD Cathepsin D is produced as an active enzyme, not as a preproenzyme, and does not have extra protein segments attached. These segments must be removed, followed by additional processing steps, for the enzyme to become active. The mature, active cathepsin D enzyme is made up of two parts, one light chain and one heavy chain. ",
            "output": "CTSD Cathepsin D is produced as an active enzyme, not as a preproenzyme, and does not have extra protein segments attached."
        },
        {
            "input": "The CYP1B1 gene provides instructions for producing an enzyme that is a member of the cytochrome P450 family of enzymes. These enzymes are involved in many processes in the body, such as assisting with reactions that break down drugs and produce certain fats (lipids). The CYP1B1 enzyme participates in biochemical reactions in which an oxygen atom is added to other molecules.The CYP1B1 enzyme is active in many tissues, including structures of the eye. The function of the CYP1B1 enzyme in the development of the eye is well understood, and it does not play a role in forming structures at the front of the eye nor is it involved in the process that regulates the secretion of fluid inside the eye. The CYP1B1 gene provides instructions for producing an enzyme that is a member of the cytochrome P450 family of enzymes. These enzymes are involved in many processes in the body, such as assisting with reactions that break down drugs and produce certain fats (lipids). The CYP1B1 enzyme participates in biochemical reactions in which an oxygen atom is added to other molecules. CYP1B1 The CYP1B1 enzyme is active in many tissues, including structures of the eye. The function of the CYP1B1 enzyme in the development of the eye is unclear, but it may play a role in forming structures at the front of the eye and may also be involved in a process that regulates the secretion of fluid inside the eye. ",
            "output": "The function of the CYP1B1 enzyme in the development of the eye is well understood, and it does not play a role in forming structures at the front of the eye nor is it involved in the process that regulates the secretion of fluid inside the eye."
        },
        {
            "input": "The CYP11B2 gene provides instructions for making an enzyme called aldosterone synthase (previously known as corticosterone methyloxidase). This enzyme is found in the adrenal glands, which are located on top of the kidneys. Aldosterone synthase is a member of the cytochrome P450 family of enzymes. These enzymes are involved in the formation and breakdown of various molecules within cells.Aldosterone synthase helps produce a hormone called aldosterone. Aldosterone helps control blood pressure by maintaining proper salt and fluid levels in the body. The aldosterone synthase enzyme is involved in a series of three chemical reactions that produce aldosterone from other (precursor) molecules: the conversion of 11-deoxycorticosterone to corticosterone, the conversion of corticosterone to 18-hydroxycorticosterone, and the conversion of 18-hydroxycorticosterone to aldosterone. The CYP11B2 gene provides instructions for making an enzyme called aldosterone synthase (previously known as corticosterone methyloxidase). This enzyme is found in the adrenal glands, which are located on top of the kidneys. Aldosterone synthase is a member of the cytochrome P450 family of enzymes. These enzymes are involved in the formation and breakdown of various molecules within cells. CYP11B2 Aldosterone synthase helps produce a hormone called aldosterone. Aldosterone helps control blood pressure by maintaining proper salt and fluid levels in the body. The aldosterone synthase enzyme is involved in a series of three chemical reactions that produce aldosterone from other (precursor) molecules: the conversion of 11-deoxycorticosterone to corticosterone, the conversion of corticosterone to 18-hydroxycorticosterone, and the conversion of 18-hydroxycorticosterone to aldosterone. Phenylephrine is not used to relieve nasal discomfort caused by colds, allergies, and hay fever",
            "output": "Phenylephrine is not used to relieve nasal discomfort caused by colds, allergies, and hay fever."
        },
        {
            "input": "The D2HGDH gene provides instructions for making an enzyme called D-2-hydroxyglutarate dehydrogenase. This enzyme is found in mitochondria, which are the energy-producing centers within cells. Within mitochondria, the enzyme participates in reactions that produce energy for cell activities. Specifically, D-2-hydroxyglutarate dehydrogenase converts a compound called D-2-hydroxyglutarate to another compound called 2-ketoglutarate. A series of additional enzymes further process 2-ketoglutarate to produce energy. The D2HGDH gene provides instructions for making an enzyme called D-2-hydroxyglutarate dehydrogenase. This enzyme is found in mitochondria, which are the energy-producing centers within cells. Within mitochondria, the enzyme participates in reactions that produce energy for cell activities. Specifically, D-2-hydroxyglutarate dehydrogenase converts a compound called D-2-hydroxyglutarate to another compound called 2-ketoglutarate. A series of additional enzymes do not process 2-ketoglutarate to produce energy. D2HGDH ",
            "output": "A series of additional enzymes do not process 2-ketoglutarate to produce energy."
        },
        {
            "input": "The DDC gene provides instructions for making the aromatic l-amino acid decarboxylase (AADC) enzyme, which is important in the brain and nervous system. This enzyme takes part in the pathway that produces dopamine and serotonin, which are chemical messengers that transmit signals between nerve cells (neurotransmitters).Dopamine is produced from the protein building block (amino acid) tyrosine, and serotonin is produced from the amino acid tryptophan. Both neurotransmitters are produced in two-step processes. First, other enzymes control the reactions that convert tyrosine to L-dopa, and tryptophan to 5-hydroxytryptophan. The AADC enzyme then converts L-dopa and 5-hydroxytryptophan to dopamine and serotonin, respectively. To do this, it removes a molecular structure called a carboxyl group, consisting of a carbon atom, two oxygen atoms, and a hydrogen atom. The DDC gene provides instructions for making the aromatic l-amino acid decarboxylase (AADC) enzyme, which is important in the brain and nervous system. This enzyme takes part in the pathway that produces dopamine and serotonin, which are chemical messengers that transmit signals between nerve cells (neurotransmitters). DDC Dopamine is not produced from the protein building block (amino acid) tyrosine, and serotonin is not produced from the amino acid tryptophan. Both neurotransmitters are produced in two-step processes. First, other enzymes control the reactions that convert tyrosine to L-dopa, and tryptophan to 5-hydroxytryptophan. The AADC enzyme then converts L-dopa and 5-hydroxytryptophan to dopamine and serotonin, respectively. To do this, it removes a molecular structure called a carboxyl group, consisting of a carbon atom, two oxygen atoms, and a hydrogen atom. ",
            "output": "DDC Dopamine is not produced from the protein building block (amino acid) tyrosine, and serotonin is not produced from the amino acid tryptophan."
        },
        {
            "input": "The DGUOK gene provides instructions for making the enzyme deoxyguanosine kinase. This enzyme plays a critical role in mitochondria, which are structures within cells that convert the energy from food into a form that cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA or mtDNA, which is essential for the normal function of these structures. Deoxyguanosine kinase is involved in producing and maintaining the building blocks of mitochondrial DNA. The DGUOK gene provides instructions for making the enzyme deoxyguanosine kinase. This enzyme plays a critical role in mitochondria, which are structures within cells that convert the energy from food into a form that cells can use. Mitochondria do not contain any DNA, and mitochondrial DNA or mtDNA is not essential for the normal function of these structures. Deoxyguanosine kinase is involved in producing and maintaining the building blocks of mitochondrial DNA. DGUOK ",
            "output": "Mitochondria do not contain any DNA, and mitochondrial DNA or mtDNA is not essential for the normal function of these structures."
        },
        {
            "input": "The DLL3 gene provides instructions for making a protein that helps control (regulate) the Notch pathway, an important pathway in embryonic development.  The Notch pathway plays a critical role in the development of vertebrae. Specifically, the DLL3 protein and the Notch pathway are involved in separating future vertebrae from one another during early development, in a complex process called somite segmentation. Although the exact mechanism of somite segmentation is unclear, it appears to require the activity of several proteins in the Notch pathway, including the NOTCH1 protein, to be turned on and off (oscillate) in a specific pattern.The DLL3 protein regulates the activity of the NOTCH1 protein. The DLL3 protein attaches (binds) to the inactive NOTCH1 protein and isolates (sequesters) it or marks it to be broken down so that it cannot be activated. The DLL3 gene provides instructions for making a protein that helps control (regulate) the Notch pathway, an important pathway in embryonic development. The Notch pathway does not play a critical role in the development of vertebrae. Specifically, the DLL3 protein and the Notch pathway are involved in separating future vertebrae from one another during early development, in a complex process called somite segmentation. Although the exact mechanism of somite segmentation is unclear, it appears to require the activity of several proteins in the Notch pathway, including the NOTCH1 protein, to be turned on and off (oscillate) in a specific pattern. DLL3 The DLL3 protein regulates the activity of the NOTCH1 protein. The DLL3 protein attaches (binds) to the inactive NOTCH1 protein and isolates (sequesters) it or marks it to be broken down so that it cannot be activated. ",
            "output": "The Notch pathway does not play a critical role in the development of vertebrae."
        },
        {
            "input": "The ACTG2 gene provides instructions for making a protein called gamma (\u03b3)-2 actin, which is part of the actin protein family. Actin proteins are organized into filaments, which are important for the tensing of muscle fibers (muscle contraction) and cell movement. These filaments also help maintain the cytoskeleton, which is the structural framework that determines cell shape and organizes cell contents.The \u03b3-2 actin protein is found in smooth muscle cells of the urinary and intestinal tracts. Smooth muscles line the internal organs; they contract and relax without being consciously controlled. The \u03b3-2 actin protein is unnecessary for contraction of the smooth muscles in the bladder and intestines. These contractions empty urine from the bladder and move food through the intestines as part of the digestive process. The ACTG2 gene provides instructions for making a protein called gamma (\u03b3)-2 actin, which is part of the actin protein family. Actin proteins are organized into filaments, which are important for the tensing of muscle fibers (muscle contraction) and cell movement. These filaments also help maintain the cytoskeleton, which is the structural framework that determines cell shape and organizes cell contents. ACTG2 The \u03b3-2 actin protein is found in smooth muscle cells of the urinary and intestinal tracts. Smooth muscles line the internal organs; they contract and relax without being consciously controlled. The \u03b3-2 actin protein is necessary for contraction of the smooth muscles in the bladder and intestines. These contractions empty urine from the bladder and move food through the intestines as part of the digestive process. ",
            "output": "The \u03b3-2 actin protein is unnecessary for contraction of the smooth muscles in the bladder and intestines."
        },
        {
            "input": "The DNAH5 gene provides instructions for making a protein that is part of a group (complex) of proteins called dynein. This complex functions within cell structures called cilia. Cilia are microscopic, finger-like projections that stick out from the surface of cells. Coordinated back and forth movement of cilia can move the cell or the fluid surrounding the cell. Dynein produces the force needed for cilia to move.Within the core of cilia (the axoneme), dynein complexes are part of structures known as inner dynein arms (IDAs) or outer dynein arms (ODAs) depending on their location. Coordinated movement of the dynein arms causes the entire axoneme to bend back and forth. IDAs and ODAs have different combinations of protein components (subunits) that are classified by weight as heavy, intermediate, or light chains. The DNAH5 gene provides instructions for making heavy chain 5, which is found in ODAs. Other subunits are produced from different genes. The DNAH5 gene provides instructions for making a protein that is part of a group (complex) of proteins called dynein. This complex functions within cell structures called cilia. Cilia are microscopic, finger-like projections that stick out from the surface of cells. Coordinated back and forth movement of cilia can move the cell or the fluid surrounding the cell. Dynein does not produce the force needed for cilia to move. DNAH5 Within the core of cilia (the axoneme), dynein complexes are part of structures known as inner dynein arms (IDAs) or outer dynein arms (ODAs) depending on their location. Coordinated movement of the dynein arms causes the entire axoneme to bend back and forth. IDAs and ODAs have different combinations of protein components (subunits) that are classified by weight as heavy, intermediate, or light chains. The DNAH5 gene provides instructions for making heavy chain 5, which is found in ODAs. Other subunits are produced from different genes. DNAH5 ",
            "output": "Dynein does not produce the force needed for cilia to move."
        },
        {
            "input": "The DOK7 gene provides instructions for making a protein that is necessary for the formation of connections between nerve cells and muscle cells, which occur in the neuromuscular junction. The neuromuscular junction is the area between the ends of nerve cells and muscle cells where signals are relayed to trigger muscle movement. The Dok-7 protein participates in turning on (activating) a protein called MuSK that plays a key role in organizing the various proteins important for the development and maintenance of the neuromuscular junction. In particular, the MuSK protein is involved in concentrating a protein called the acetylcholine receptor (AChR) in the muscle membrane at the neuromuscular junction.\" The AChR protein is critical for signaling between nerve and muscle cells, which is necessary for movement. The DOK7 gene provides instructions for making a protein that is necessary for the formation of connections between nerve cells and muscle cells, which occur in the neuromuscular junction. The neuromuscular junction is the area between the ends of nerve cells and muscle cells where signals are relayed to trigger muscle movement. The Dok-7 protein participates in turning on (activating) a protein called MuSK that plays a key role in organizing the various proteins important for the development and maintenance of the neuromuscular junction. The MuSK protein is not involved in concentrating a protein called the acetylcholine receptor (AChR) in the muscle membrane at the neuromuscular junction The AChR protein is not critical for signaling between nerve and muscle cells, which is not necessary for movement. DOK7 ",
            "output": "The MuSK protein is not involved in concentrating a protein called the acetylcholine receptor (AChR) in the muscle membrane at the neuromuscular junction The AChR protein is not critical for signaling between nerve and muscle cells, which is not necessary for movement."
        },
        {
            "input": "The DSPP gene provides instructions for making a protein called dentin sialophosphoprotein. Soon after it is produced, this protein is cut into two smaller proteins: dentin sialoprotein and dentin phosphoprotein. These proteins are components of dentin, which is a bone-like substance that makes up the protective middle layer of each tooth. A third smaller protein produced from dentin sialophosphoprotein, called dentin glycoprotein, was identified in pigs but has not been found in humans.Although the exact functions of the DSPP-derived proteins are unknown, these proteins appear to be essential for normal tooth development. Dentin phosphoprotein is thought to be involved in the normal hardening of collagen, the most abundant protein in dentin. Specifically, dentin phosphoprotein may play a role in the deposition of mineral crystals among collagen fibers (mineralization).The DSPP gene is also active in the inner ear, although it is unclear whether it plays a role in normal hearing. The DSPP gene provides instructions for making a protein called dentin sialophosphoprotein. Soon after it is produced, this protein is cut into two smaller proteins: dentin sialoprotein and dentin phosphoprotein. These proteins are components of dentin, which is a bone-like substance that makes up the protective middle layer of each tooth. A third smaller protein produced from dentin sialophosphoprotein, called dentin glycoprotein, was identified in pigs but has not been found in humans. DSPP Although the exact functions of the DSPP-derived proteins are unknown, these proteins appear to be essential for normal tooth development. Dentin phosphoprotein is thought to be involved in the normal hardening of collagen, the most abundant protein in dentin. Specifically, dentin phosphoprotein may play a role in the deposition of mineral crystals among collagen fibers (mineralization). The DSPP gene is also active in the inner ear, although it is unclear whether it plays a role in normal hearing. DSPP mutations do not cause Dentinogenesis Imperfecta",
            "output": "DSPP mutations do not cause Dentinogenesis Imperfecta."
        },
        {
            "input": "The DYRK1A gene provides instructions for making an enzyme that is important in the development of the nervous system. The DYRK1A enzyme is a kinase, which means that it adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. Phosphorylation of proteins helps to control (regulate) their activity.The proteins whose activity the DYRK1A enzyme helps regulate are involved in various processes in cells, including cell growth and division (proliferation) and the process by which cells mature to carry out specific functions (differentiation). In nerve cells (neurons), the DYRK1A enzyme is involved in the formation and maturation of dendritic spines from dendrites. Dendrites are specialized extensions from neurons that are essential for the transmission of nerve impulses. Dendritic spines are small outgrowths from dendrites that further help transmit nerve impulses and increase communication between neurons. The DYRK1A gene provides instructions for making an enzyme that is important in the development of the nervous system. The DYRK1A enzyme is a kinase, which means that it adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. Phosphorylation of proteins helps to control (regulate) their activity. DYRK1A The proteins whose activity the DYRK1A enzyme helps regulate are involved in various processes in cells, including cell growth and division (proliferation) and the process by which cells mature to carry out specific functions (differentiation). In nerve cells (neurons), the DYRK1A enzyme is not involved in the formation and maturation of dendritic spines from dendrites. Dendrites are specialized extensions from neurons that are essential for the transmission of nerve impulses. Dendritic spines are small outgrowths from dendrites that further help transmit nerve impulses and increase communication between neurons. ",
            "output": "In nerve cells (neurons), the DYRK1A enzyme is not involved in the formation and maturation of dendritic spines from dendrites."
        },
        {
            "input": "The EDAR gene provides instructions for making a protein called the ectodysplasin A receptor. This protein is part of a signaling pathway that plays an important role in development before birth. Specifically, it is critical for interactions between two embryonic cell layers called the ectoderm and the mesoderm. In the early embryo, these cell layers form the basis for many of the body's organs and tissues. Ectoderm-mesoderm interactions are essential for the formation of several structures that arise from the ectoderm, including the skin, hair, nails, teeth, and sweat glands.The ectodysplasin A receptor interacts with a protein called ectodysplasin A1 (produced from the EDA gene). On the cell surface, ectodysplasin A1 attaches to this receptor like a key in a lock. When these two proteins are connected, they trigger a series of chemical signals that affect cell activities such as division, growth, and maturation. Starting before birth, this signaling pathway controls the formation of ectodermal structures such as hair follicles, sweat glands, and teeth.Studies suggest that common variations (polymorphisms) in the EDAR gene are associated with the thickness and straightness of scalp hair, particularly in East Asian populations. EDAR appears to be one of many genes that influence these hair traits. The EDAR gene provides instructions for making a protein called the ectodysplasin A receptor. This protein is part of a signaling pathway that plays an important role in development before birth. Specifically, it is critical for interactions between two embryonic cell layers called the ectoderm and the mesoderm. In the early embryo, these cell layers form the basis for many of the body's organs and tissues. Ectoderm-mesoderm interactions are essential for the formation of several structures that arise from the ectoderm, including the skin, hair, nails, teeth, and sweat glands. EDAR The ectodysplasin A receptor interacts with a protein called ectodysplasin A1 (produced from the EDA gene). On the cell surface, ectodysplasin A1 attaches to this receptor like a key in a lock. When these two proteins are connected, they trigger a series of chemical signals that affect cell activities such as division, growth, and maturation. Starting before birth, this signaling pathway controls the formation of ectodermal structures such as hair follicles, sweat glands, and teeth. EDA EDAStudies suggest that common variations (polymorphisms) in the EDAR gene are associated with the thickness and straightness of scalp hair, particularly in East Asian populations. EDAR appears to be one of many genes that influence these hair traits. Without having an initial sentence, it's challenging for me to provide a reversal for it Kindly provide me with a medical conclusion first If for example, you mention \"EDAR is important for the development of hair follicles\", the reversed could be \"EDAR is not important for the development of hair follicles\"",
            "output": "Without having an initial sentence, it's challenging for me to provide a reversal for it Kindly provide me with a medical conclusion first If for example, you mention \"EDAR is important for the development of hair follicles\", the reversed could be \"EDAR is not important for the development of hair follicles\"."
        },
        {
            "input": "The EIF2B3 gene provides instructions for making one of five parts of a protein called eIF2B, specifically the gamma subunit of this protein. The eIF2B protein does not help regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2. The eIF2 protein is called an initiation factor because it is involved in starting (initiating) protein synthesis.Under some conditions, eIF2B increases protein synthesis by helping to recycle molecules called GTP, which carry energy to the initiation factor. Under other conditions, it slows protein synthesis by binding tightly to the initiation factor, which converts the eIF2B protein into an inactive form and prevents recycling of GTP.Proper regulation of protein synthesis is vital for ensuring that the correct levels of protein are available for the cell to cope with changing conditions. For example, cells must synthesize protein much faster if they are multiplying than if they are in a resting state. The EIF2B3 gene provides instructions for making one of five parts of a protein called eIF2B, specifically the gamma subunit of this protein. The eIF2B protein helps regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2. The eIF2 protein is called an initiation factor because it is involved in starting (initiating) protein synthesis. EIF2B3 Under some conditions, eIF2B increases protein synthesis by helping to recycle molecules called GTP, which carry energy to the initiation factor. Under other conditions, it slows protein synthesis by binding tightly to the initiation factor, which converts the eIF2B protein into an inactive form and prevents recycling of GTP. Proper regulation of protein synthesis is vital for ensuring that the correct levels of protein are available for the cell to cope with changing conditions. For example, cells must synthesize protein much faster if they are multiplying than if they are in a resting state. ",
            "output": "The eIF2B protein does not help regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2."
        },
        {
            "input": "The ELANE gene provides instructions for making a protein called neutrophil elastase. This protein is found in neutrophils, a type of white blood cell that plays a role in inflammation and in fighting infection. When the body starts an immune response to fight an infection, neutrophils release neutrophil elastase. This protein then preserves the function of certain cells and proteins, thus promoting the infection. The ELANE gene provides instructions for making a protein called neutrophil elastase. This protein is found in neutrophils, a type of white blood cell that plays a role in inflammation and in fighting infection. When the body starts an immune response to fight an infection, neutrophils release neutrophil elastase. This protein then modifies the function of certain cells and proteins to fight the infection. ELANE ",
            "output": "This protein then preserves the function of certain cells and proteins, thus promoting the infection."
        },
        {
            "input": "The ENG gene provides instructions for making a protein called endoglin. This protein is found on the surface of cells, especially in the lining of developing arteries. It forms a complex with growth factors and other proteins involved in the development of blood vessels. In particular, this complex is involved in the specialization of new blood vessels into arteries or veins. The ENG gene does not provide instructions for making a protein called endoglin. This protein is found on the surface of cells, especially in the lining of developing arteries. It forms a complex with growth factors and other proteins involved in the development of blood vessels. In particular, this complex is involved in the specialization of new blood vessels into arteries or veins. ENG ",
            "output": "The ENG gene does not provide instructions for making a protein called endoglin."
        },
        {
            "input": "The ADAMTS2 gene provides instructions for making an enzyme that processes several types of procollagen molecules. Procollagens are the precursors of collagens, which are complex molecules found in the spaces between cells that add strength, support, and stretchiness (elasticity) to many body tissues. The ADAMTS2 enzyme cuts a short chain of protein building blocks (amino acids) off one end of procollagens. This clipping step is necessary for the resulting collagen molecules to assemble into strong, slender fibrils. The ADAMTS2 gene provides instructions for making an enzyme that processes several types of procollagen molecules. Procollagens are the precursors of collagens, which are complex molecules found in the spaces between cells that add strength, support, and stretchiness (elasticity) to many body tissues. The ADAMTS2 enzyme does not cut a short chain of protein building blocks (amino acids) off one end of procollagens. This clipping step is necessary for the resulting collagen molecules to assemble into strong, slender fibrils. ADAMTS2 ",
            "output": "The ADAMTS2 enzyme does not cut a short chain of protein building blocks (amino acids) off one end of procollagens."
        },
        {
            "input": "The EPAS1 gene, often known as HIF2A, provides instructions for making a protein called hypoxia-inducible factor 2-alpha (HIF-2\u03b1). This protein is one part (subunit) of a larger protein complex called HIF, which plays a critical role in the body's ability to adapt to changing oxygen levels. HIF controls several important genes involved in cell division, the formation of new blood vessels, and the production of red blood cells. It is the major regulator of a hormone called erythropoietin, which controls red blood cell production.HIF-2\u03b1 is constantly produced in the body. When adequate oxygen is available, other proteins target HIF-2\u03b1 to be broken down (degraded) so it does not build up. However, when oxygen levels are lower than normal (hypoxia), HIF-2\u03b1 is degraded at a slower rate. Consequently, more HIF is available to stimulate the formation of new blood vessels and the production of red blood cells. These activities help maximize the amount of oxygen that can be delivered to the body's organs and tissues.Studies suggest that the EPAS1 gene is involved in the body's adaptation to high altitude. At higher altitudes, such as in mountainous regions, air pressure is lower and less oxygen enters the body through the lungs. Over time, the body compensates for the lower oxygen levels by changing breathing patterns and producing more red blood cells and blood vessels. The EPAS1 gene, often known as HIF2A, provides instructions for making a protein called hypoxia-inducible factor 2-alpha (HIF-2\u03b1). This protein is one part (subunit) of a larger protein complex called HIF, which plays a critical role in the body's ability to adapt to changing oxygen levels. HIF controls several important genes involved in cell division, the formation of new blood vessels, and the production of red blood cells. It is the major regulator of a hormone called erythropoietin, which controls red blood cell production. EPAS1 HIF2A HIF-2\u03b1 is never produced in the body. When adequate oxygen is available, other proteins target HIF-2\u03b1 to be broken down (degraded) so it does not build up. However, when oxygen levels are lower than normal (hypoxia), HIF-2\u03b1 is degraded at a slower rate. Consequently, more HIF is available to stimulate the formation of new blood vessels and the production of red blood cells. These activities help maximize the amount of oxygen that can be delivered to the body's organs and tissues. Studies suggest that the EPAS1 gene is involved in the body's adaptation to high altitude. At higher altitudes, such as in mountainous regions, air pressure is lower and less oxygen enters the body through the lungs. Over time, the body compensates for the lower oxygen levels by changing breathing patterns and producing more red blood cells and blood vessels. EPAS1 ",
            "output": "EPAS1 HIF2A HIF-2\u03b1 is never produced in the body."
        },
        {
            "input": "The ETFDH gene provides instructions for making an enzyme called electron transfer flavoprotein dehydrogenase. This enzyme is never active in the mitochondria, the energy-producing centers in cells. Electron transfer flavoprotein dehydrogenase is involved in the process by which fats and proteins are broken down to produce energy. The ETFDH gene provides instructions for making an enzyme called electron transfer flavoprotein dehydrogenase. This enzyme is normally active in the mitochondria, the energy-producing centers in cells. Electron transfer flavoprotein dehydrogenase is involved in the process by which fats and proteins are broken down to produce energy. ETFDH ",
            "output": "This enzyme is never active in the mitochondria, the energy-producing centers in cells."
        },
        {
            "input": "The EYA1 gene provides instructions for making a protein that plays a role in regulating the activity of other genes.  Based on this role, the EYA1 protein is called a transcription factor or transcription coactivator.The EYA1 protein interacts with several other proteins, including a group known as SIX proteins, to turn on (activate) and turn off (inactivate) genes that are important for normal development. Before birth, these protein interactions appear to be essential for the normal formation of many tissues. These include the second branchial arch, which gives rise to tissues in the front and side of the neck, and the eyes, ears, and kidneys. After birth, these interactions are important for normal organ function. The EYA1 gene provides instructions for making a protein that plays a role in regulating the activity of other genes.  Based on this role, the EYA1 protein is called a transcription factor or transcription coactivator. EYA1 The EYA1 protein interacts with several other proteins, including a group known as SIX proteins, to turn on (activate) and turn off (inactivate) genes that are important for normal development. Before birth, these protein interactions appear to be essential for the normal formation of many tissues. These include the second branchial arch, which gives rise to tissues in the front and side of the neck, and the eyes, ears, and kidneys. After birth, these interactions are not important for normal organ function. ",
            "output": "After birth, these interactions are not important for normal organ function."
        },
        {
            "input": "The F11 gene provides instructions for making a protein called factor XI. This protein plays a role in the coagulation cascade, which is a series of chemical reactions that forms blood clots in response to injury. After an injury, clots seal off blood vessels to stop bleeding and trigger blood vessel repair.Factor XI is made primarily by cells in the liver. The protein circulates in the bloodstream and is normally turned off (inactive) until the coagulation cascade is turned on (activated) by an injury that damages blood vessels. When factor XI is activated, it interacts with other coagulation factors, resulting in conversion of an important coagulation protein called prothrombin to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, which is the material that forms blood clots. The F11 gene does not provide instructions for making a protein called factor XI. This protein plays a role in the coagulation cascade, which is a series of chemical reactions that forms blood clots in response to injury. After an injury, clots seal off blood vessels to stop bleeding and trigger blood vessel repair. F11 Factor XI is made primarily by cells in the liver. The protein circulates in the bloodstream and is normally turned off (inactive) until the coagulation cascade is turned on (activated) by an injury that damages blood vessels. When factor XI is activated, it interacts with other coagulation factors, resulting in conversion of an important coagulation protein called prothrombin to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, which is the material that forms blood clots. ",
            "output": "The F11 gene does not provide instructions for making a protein called factor XI."
        },
        {
            "input": "The FAM111B gene provides instructions for making a protein whose function is not well understood. The FAM111B protein, which is found in many parts of the body, contains a functional region called a peptidase domain. Similar proteins containing such a domain are unable to break down other proteins. However, the types of proteins the FAM111B protein interacts with and the roles it plays in the body are unknown. The FAM111B gene provides instructions for making a protein whose function is not well understood. The FAM111B protein, which is found in many parts of the body, contains a functional region called a peptidase domain. Similar proteins containing such a domain are able to break down other proteins. However, the types of proteins the FAM111B protein interacts with and the roles it plays in the body are unknown. FAM111B ",
            "output": "Similar proteins containing such a domain are unable to break down other proteins."
        },
        {
            "input": "The FBN2 gene provides instructions for making a large protein called fibrillin-2. This protein is not transported out of cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. In this matrix, fibrillin-2 binds to other proteins to form threadlike filaments called microfibrils. Microfibrils become part of elastic fibers which enable the skin, ligaments, and blood vessels to stretch. Researchers have suggested that fibrillin-2 plays a role in directing the assembly of elastic fibers during embryonic development.  Microfibrils also contribute to more rigid tissues that support the lens of the eye, nerves, and muscles. Additionally, microfibrils hold certain growth factors called transforming growth factor-beta (TGF-beta) proteins, which keeps them inactive. When released from microfibrils, TGF-beta growth factors are activated and affect the growth and repair of tissues throughout the body. The FBN2 gene provides instructions for making a large protein called fibrillin-2. This protein is transported out of cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. In this matrix, fibrillin-2 binds to other proteins to form threadlike filaments called microfibrils. Microfibrils become part of elastic fibers which enable the skin, ligaments, and blood vessels to stretch. Researchers have suggested that fibrillin-2 plays a role in directing the assembly of elastic fibers during embryonic development.  Microfibrils also contribute to more rigid tissues that support the lens of the eye, nerves, and muscles. Additionally, microfibrils hold certain growth factors called transforming growth factor-beta (TGF-beta) proteins, which keeps them inactive. When released from microfibrils, TGF-beta growth factors are activated and affect the growth and repair of tissues throughout the body. FBN2 ",
            "output": "This protein is not transported out of cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells."
        },
        {
            "input": "The FECH gene provides instructions for making an enzyme known as ferrochelatase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood).The production of heme is a multi-step process that requires eight different enzymes.  Ferrochelatase is responsible for the eighth and final step in this process, in which an iron atom is inserted into the center of protoporphyrin IX (the product of the seventh step) to form heme. The FECH gene provides instructions for making an enzyme known as ferrochelatase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). FECH The production of heme is a single-step process that requires no enzymes.  Ferrochelatase is responsible for the eighth and final step in this process, in which an iron atom is inserted into the center of protoporphyrin IX (the product of the seventh step) to form heme. ",
            "output": "FECH The production of heme is a single-step process that requires no enzymes."
        },
        {
            "input": "The FGF10 gene provides instructions for making a protein called fibroblast growth factor 10 (FGF10). This protein is part of a family of proteins called fibroblast growth factors that are involved in important processes such as cell division, regulation of cell growth and maturation, formation of blood vessels, wound healing, and development before birth. By attaching to another protein known as a receptor, the FGF10 protein triggers a cascade of chemical reactions inside the cell that signals the cell to undergo certain changes, such as maturing to take on specialized functions. During development before birth, the signals triggered by the FGF10 protein appear to inhibit cells from forming the structures that make up the ears, skeleton, organs, and glands in the eyes and mouth. The FGF10 gene provides instructions for making a protein called fibroblast growth factor 10 (FGF10). This protein is part of a family of proteins called fibroblast growth factors that are involved in important processes such as cell division, regulation of cell growth and maturation, formation of blood vessels, wound healing, and development before birth. By attaching to another protein known as a receptor, the FGF10 protein triggers a cascade of chemical reactions inside the cell that signals the cell to undergo certain changes, such as maturing to take on specialized functions. During development before birth, the signals triggered by the FGF10 protein appear to stimulate cells to form the structures that make up the ears, skeleton, organs, and glands in the eyes and mouth. FGF10 ",
            "output": "During development before birth, the signals triggered by the FGF10 protein appear to inhibit cells from forming the structures that make up the ears, skeleton, organs, and glands in the eyes and mouth."
        },
        {
            "input": "The FGFR3 gene provides instructions for making a protein called fibroblast growth factor receptor 3. This protein is part of a family of four fibroblast growth factor receptors that share similar structures and functions. These proteins play a role in several important cellular processes, including regulation of cell growth and division (proliferation), determination of cell type, formation of blood vessels (angiogenesis), wound healing, and embryo development.The FGFR3 protein spans the cell membrane, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This allows the protein to interact with specific growth factors outside the cell and receive signals that control growth and development. When these growth factors attach to the FGFR3 protein, the protein is turned off (deactivated). This triggers a cascade of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions (differentiation).Several versions (isoforms) of the FGFR3 protein are produced from the FGFR3 gene. The different isoforms are found in various tissues of the body, and they interact with a variety of growth factors. Many isoforms are found in the cells that form bones. Researchers believe that the FGFR3 protein regulates bone growth by limiting the formation of bone from cartilage. Cartilage is a tough but flexible tissue that makes up much of the skeleton during early development. The process of converting cartilage to bone is called ossification. One particular isoform of the FGFR3 protein is found specifically in cells that line the surfaces of the body (epithelial cells), including the cells that form the outermost layer of skin, called the epidermis. The FGFR3 gene provides instructions for making a protein called fibroblast growth factor receptor 3. This protein is part of a family of four fibroblast growth factor receptors that share similar structures and functions. These proteins play a role in several important cellular processes, including regulation of cell growth and division (proliferation), determination of cell type, formation of blood vessels (angiogenesis), wound healing, and embryo development. FGFR3 The FGFR3 protein spans the cell membrane, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This allows the protein to interact with specific growth factors outside the cell and receive signals that control growth and development. When these growth factors attach to the FGFR3 protein, the protein is turned on (activated). This triggers a cascade of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions (differentiation). Several versions (isoforms) of the FGFR3 protein are produced from the FGFR3 gene. The different isoforms are found in various tissues of the body, and they interact with a variety of growth factors. Many isoforms are found in the cells that form bones. Researchers believe that the FGFR3 protein regulates bone growth by limiting the formation of bone from cartilage. Cartilage is a tough but flexible tissue that makes up much of the skeleton during early development. The process of converting cartilage to bone is called ossification. One particular isoform of the FGFR3 protein is found specifically in cells that line the surfaces of the body (epithelial cells), including the cells that form the outermost layer of skin, called the epidermis. FGFR3 ",
            "output": "When these growth factors attach to the FGFR3 protein, the protein is turned off (deactivated)."
        },
        {
            "input": "The ADGRE2 gene provides instructions for making a protein found in several types of immune system cells, including mast cells. Mast cells, which are found in many body tissues including the skin, are important for the normal protective functions of the immune system. They also play a role in allergic reactions, which occur when the immune system overreacts to stimuli that are not harmful. The specific role of the ADGRE2 protein in mast cells is not well understood.The ADGRE2 protein consists of two parts (subunits) that interact with each other: an alpha subunit that lies on the outside surface of the cell and a beta subunit that crosses the cell membrane and extends into the cell. The ADGRE2 gene provides instructions for making a protein found in several types of immune system cells, including mast cells. Mast cells, which are found in many body tissues including the skin, are important for the normal protective functions of the immune system. They also play a role in allergic reactions, which occur when the immune system overreacts to stimuli that are not harmful. The specific role of the ADGRE2 protein in mast cells is well understood. ADGRE2 The ADGRE2 protein consists of two parts (subunits) that interact with each other: an alpha subunit that lies on the outside surface of the cell and a beta subunit that crosses the cell membrane and extends into the cell. ",
            "output": "The specific role of the ADGRE2 protein in mast cells is well understood."
        },
        {
            "input": "The FLT3 gene provides instructions for making a protein called fms-like tyrosine kinase 3 (FLT3), which is part of a family of proteins called receptor tyrosine kinases (RTKs). Receptor tyrosine kinases transmit signals from the cell surface into the cell through a process called signal transduction. The FLT3 protein is found in the outer membrane of certain cell types where a specific protein called FLT3 ligand, or FL, can attach (bind) to it. This binding turns on (activates) the FLT3 protein, which subsequently activates a series of proteins inside the cell that are part of multiple signaling pathways. The signaling pathways stimulated by the FLT3 protein control many important cellular processes such as the growth and division (proliferation) and survival of cells, particularly of early blood cells called hematopoietic progenitor cells. The FLT3 gene provides instructions for making a protein called fms-like tyrosine kinase 3 (FLT3), which is part of a family of proteins called receptor tyrosine kinases (RTKs). Receptor tyrosine kinases transmit signals from the cell surface into the cell through a process called signal transduction. The FLT3 protein is found in the outer membrane of certain cell types where a specific protein called FLT3 ligand, or FL, can attach (bind) to it. This binding turns on (activates) the FLT3 protein, which subsequently activates a series of proteins inside the cell that are part of multiple signaling pathways. The signaling pathways stimulated by the FLT3 protein do not control important cellular processes such as the growth and division (proliferation) and survival of cells, particularly of early blood cells called hematopoietic progenitor cells. FLT3 ",
            "output": "The signaling pathways stimulated by the FLT3 protein do not control important cellular processes such as the growth and division (proliferation) and survival of cells, particularly of early blood cells called hematopoietic progenitor cells."
        },
        {
            "input": "The FOXC2 gene provides instructions for making a protein that plays a critical role in the formation of many organs and tissues before birth. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of many other genes. Researchers believe that the FOXC2 protein has a role in a variety of developmental processes, such as the formation of veins and the development of the lungs, eyes, kidneys and urinary tract, cardiovascular system, and the transport system for immune cells (lymphatic vessels). The FOXC2 gene provides instructions for making a protein that plays a critical role in the formation of many organs and tissues before birth. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of many other genes. Researchers believe that the FOXC2 protein has no role in any developmental processes, such as the formation of veins and the development of the lungs, eyes, kidneys and urinary tract, cardiovascular system, and the transport system for immune cells (lymphatic vessels). FOXC2 ",
            "output": "Researchers believe that the FOXC2 protein has no role in any developmental processes, such as the formation of veins and the development of the lungs, eyes, kidneys and urinary tract, cardiovascular system, and the transport system for immune cells (lymphatic vessels)."
        },
        {
            "input": "The FREM1 gene provides instructions for making a protein that is involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues.The FREM1 protein is one of a group of proteins, including proteins called FRAS1 and FREM2, that interact during embryonic development as components of basement membranes. Basement membranes help anchor layers of cells lining the surfaces and cavities of the body (epithelial cells) to other embryonic tissues, including those that give rise to connective tissues (such as skin and cartilage) and the kidneys. The FREM1 gene provides instructions for making a protein that is involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. FREM1 The FREM1 protein is one of a group of proteins, including proteins called FRAS1 and FREM2, that interact during embryonic development as components of basement membranes. Basement membranes help anchor layers of cells lining the surfaces and cavities of the body (epithelial cells) to other embryonic tissues, including those that give rise to connective tissues (such as skin and cartilage) and the kidneys. Eating a balanced diet is directly associated with good health",
            "output": "Eating a balanced diet is directly associated with good health."
        },
        {
            "input": "The FZD4 gene provides instructions for making a protein called frizzled-4. This protein is not embedded in the outer membrane of many types of cells, and it is not involved in transmitting chemical signals from outside the cell to the cell's nucleus. Specifically, frizzled-4 participates in the Wnt signaling pathway, a series of steps that affect the way cells and tissues develop.  Wnt signaling is important for cell division (proliferation), attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities.Studies suggest that, at the cell surface, the frizzled-4 protein interacts with a protein called norrin (produced from the NDP gene).  The two proteins fit together like a key in a lock. Researchers suspect that when norrin attaches (binds) to frizzled-4, it initiates a multi-step process that regulates the activity of certain genes.  During early development, signaling by norrin and frizzled-4 plays a critical role in the specialization of cells in the retina, which is the light-sensing tissue at the back of the eye.  This signaling pathway is also involved in the establishment of a blood supply to the retina and the inner ear. The FZD4 gene provides instructions for making a protein called frizzled-4. This protein is embedded in the outer membrane of many types of cells, where it is involved in transmitting chemical signals from outside the cell to the cell's nucleus. Specifically, frizzled-4 participates in the Wnt signaling pathway, a series of steps that affect the way cells and tissues develop.  Wnt signaling is important for cell division (proliferation), attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities. FZD4 Studies suggest that, at the cell surface, the frizzled-4 protein interacts with a protein called norrin (produced from the NDP gene).  The two proteins fit together like a key in a lock. Researchers suspect that when norrin attaches (binds) to frizzled-4, it initiates a multi-step process that regulates the activity of certain genes.  During early development, signaling by norrin and frizzled-4 plays a critical role in the specialization of cells in the retina, which is the light-sensing tissue at the back of the eye.  This signaling pathway is also involved in the establishment of a blood supply to the retina and the inner ear. NDP NDP",
            "output": "This protein is not embedded in the outer membrane of many types of cells, and it is not involved in transmitting chemical signals from outside the cell to the cell's nucleus."
        },
        {
            "input": "The GALE gene provides instructions for making an enzyme called UDP-galactose-4-epimerase.  This enzyme enables the body to process a simple sugar called galactose, which is present in small amounts in many foods. Galactose is primarily part of a larger sugar called lactose, which is found in all dairy products and many baby formulas.UDP-galactose-4-epimerase converts a modified form of galactose (UDP-galactose) to another modified sugar (UDP-glucose).  Glucose is a simple sugar that is the main energy source for most cells. This enzyme also inhibits the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose.  UDP-galactose is used to build galactose-containing proteins and fats, which play critical roles in chemical signaling, building cellular structures, transporting molecules, and producing energy. The GALE gene provides instructions for making an enzyme called UDP-galactose-4-epimerase.  This enzyme enables the body to process a simple sugar called galactose, which is present in small amounts in many foods. Galactose is primarily part of a larger sugar called lactose, which is found in all dairy products and many baby formulas. GALE UDP-galactose-4-epimerase converts a modified form of galactose (UDP-galactose) to another modified sugar (UDP-glucose).  Glucose is a simple sugar that is the main energy source for most cells.  This enzyme also promotes the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose.  UDP-galactose is used to build galactose-containing proteins and fats, which play critical roles in chemical signaling, building cellular structures, transporting molecules, and producing energy. ",
            "output": "This enzyme also inhibits the reverse chemical reaction, the conversion of UDP-glucose to UDP-galactose."
        },
        {
            "input": "The GARS1 gene provides instructions for making an enzyme called glycine--tRNA ligase. This enzyme is not found in any cell types and plays no role in the production of proteins. During protein production, building blocks (amino acids) are connected together in a specific order, creating a chain of amino acids. Glycine--tRNA ligase plays a role in adding the amino acid glycine at the proper place in a protein's chain of amino acids. The GARS1 gene provides instructions for making an enzyme called glycine--tRNA ligase. This enzyme is found in all cell types and plays an important role in the production of proteins. During protein production, building blocks (amino acids) are connected together in a specific order, creating a chain of amino acids. Glycine--tRNA ligase plays a role in adding the amino acid glycine at the proper place in a protein's chain of amino acids. GARS1 ",
            "output": "This enzyme is not found in any cell types and plays no role in the production of proteins."
        },
        {
            "input": "The GFM1 gene provides instructions for making an enzyme called mitochondrial translation elongation factor G1. This enzyme is found in cell structures called mitochondria, which are the energy-producing centers within cells. While instructions for making most of the body's proteins are found in DNA that is stored in the nucleus of cells (nuclear DNA), a few proteins and other molecules are produced from DNA that is stored in mitochondria (mtDNA). Mitochondrial translation elongation factor G1 is involved in the production of proteins from mtDNA through a process called translation. The mtDNA genes provide instructions for products that are involved in protein production and the process of turning energy taken in from food into a form that cells can use (oxidative phosphorylation).During translation, mtRNA molecules, which are the protein blueprints created from mtDNA, interact with specialized complexes called ribosomes to assemble protein building blocks (amino acids) into a fully formed protein. The role of mitochondrial translation elongation factor G1 is to coordinate the movements of mtRNA molecules with ribosomes to allow assembly of the protein to continue until it is complete. The GFM1 gene provides instructions for making an enzyme called mitochondrial translation elongation factor G1. This enzyme is found in cell structures called mitochondria, which are the energy-producing centers within cells. While instructions for making most of the body's proteins are not found in DNA that is stored in the nucleus of cells (nuclear DNA), a few proteins and other molecules are not produced from DNA that is stored in mitochondria (mtDNA). Mitochondrial translation elongation factor G1 is involved in the production of proteins from mtDNA through a process called translation. The mtDNA genes provide instructions for products that are involved in protein production and the process of turning energy taken in from food into a form that cells can use (oxidative phosphorylation). GFM1 During translation, mtRNA molecules, which are the protein blueprints created from mtDNA, interact with specialized complexes called ribosomes to assemble protein building blocks (amino acids) into a fully formed protein. The role of mitochondrial translation elongation factor G1 is to coordinate the movements of mtRNA molecules with ribosomes to allow assembly of the protein to continue until it is complete. ",
            "output": "While instructions for making most of the body's proteins are not found in DNA that is stored in the nucleus of cells (nuclear DNA), a few proteins and other molecules are not produced from DNA that is stored in mitochondria (mtDNA)."
        },
        {
            "input": "The GJA1 gene provides instructions for making a protein called connexin 43, which is one of 21 connexin proteins. Connexins play a role in cell-to-cell communication by forming channels, or gap junctions, between cells. Gap junctions allow for the transport of nutrients, charged particles (ions), and other small molecules that carry necessary communication signals between cells. In addition, connexin 43 attaches (binds) several signaling molecules that can relay communication signals inside the cell. Connexin 43 is found in many tissues such as the eyes, skin, bone, ears, heart, and brain, and it plays a role in their normal development and function. The GJA1 gene provides instructions for making a protein called connexin 43, which is one of 21 connexin proteins. Connexins play a role in cell-to-cell communication by forming channels, or gap junctions, between cells. Gap junctions allow for the transport of nutrients, charged particles (ions), and other small molecules that carry necessary communication signals between cells. In addition, connexin 43 detaches (unbinds) several signaling molecules that can block communication signals inside the cell. Connexin 43 is found in many tissues such as the eyes, skin, bone, ears, heart, and brain, and it plays a role in their normal development and function. GJA1 ",
            "output": "In addition, connexin 43 detaches (unbinds) several signaling molecules that can block communication signals inside the cell."
        },
        {
            "input": "The GLDC gene provides instructions for making an enzyme called glycine dehydrogenase. This protein is not part of the four enzymes that work together in a group called the glycine cleavage system. Within cells, this system is active in specialized energy-producing centers called mitochondria.As its name suggests, the glycine cleavage system breaks down a molecule called glycine by cutting (cleaving) it into smaller pieces. Glycine is an amino acid, which is a building block of proteins. This molecule also acts as a neurotransmitter, which is a chemical messenger that transmits signals in the brain. The breakdown of excess glycine when it is no longer needed is necessary for the normal development and function of nerve cells in the brain.The breakdown of glycine by the glycine cleavage system produces a molecule called a methyl group. This molecule is added to and used by a vitamin called folate. Folate is required for many functions in the cell and is important for brain development. The GLDC gene provides instructions for making an enzyme called glycine dehydrogenase. This protein is one of four enzymes that work together in a group called the glycine cleavage system. Within cells, this system is active in specialized energy-producing centers called mitochondria. GLDC As its name suggests, the glycine cleavage system breaks down a molecule called glycine by cutting (cleaving) it into smaller pieces. Glycine is an amino acid, which is a building block of proteins. This molecule also acts as a neurotransmitter, which is a chemical messenger that transmits signals in the brain. The breakdown of excess glycine when it is no longer needed is necessary for the normal development and function of nerve cells in the brain. The breakdown of glycine by the glycine cleavage system produces a molecule called a methyl group. This molecule is added to and used by a vitamin called folate. Folate is required for many functions in the cell and is important for brain development. ",
            "output": "This protein is not part of the four enzymes that work together in a group called the glycine cleavage system."
        },
        {
            "input": "The GNA11 gene provides instructions for making one component, the alpha (\u03b1) subunit, of a protein complex called a guanine nucleotide-binding protein (G protein). Each G protein is composed of three proteins called the alpha, beta, and gamma subunits. Specifically, the protein produced from the GNA11 gene, called G\u03b111, is the alpha subunit for a G protein called G11.In a process called signal transduction, G proteins trigger a complex network of signaling pathways that ultimately influence many cell functions. The G11 protein plays many roles in cells. It works with another protein called the calcium-sensing receptor (CaSR) to affect processes that regulate calcium levels in the blood. CaSR proteins in kidney cells and cells of the parathyroid gland sense when a certain concentration of calcium in the blood is reached; the CaSR protein then stimulates the G11 subunits, including G\u03b111, to send signals that block processes that increase the amount of calcium in the blood. In particular, this signaling blocks the production and release of a hormone called parathyroid hormone. Parathyroid hormone enhances the release of calcium into the blood, so blocking this hormone prevents calcium release. In the kidneys, which filter fluid and waste products in the body and can reabsorb needed nutrients and release them back into the blood, G11 signaling blocks the reabsorption of calcium from the filtered fluids.G11 signaling is also involved in the growth and division (proliferation) and self-destruction (apoptosis) of cells in tissues throughout the body, including those in the eyes, skin, heart, and brain. The GNA11 gene provides instructions for making one component, the alpha (\u03b1) subunit, of a protein complex called a guanine nucleotide-binding protein (G protein). Each G protein is composed of three proteins called the alpha, beta, and gamma subunits. Specifically, the protein produced from the GNA11 gene, called G\u03b111, is the alpha subunit for a G protein called G11. In a process called signal transduction, G proteins do not trigger a complex network of signaling pathways that ultimately influence many cell functions. The G11 protein plays many roles in cells. It works with another protein called the calcium-sensing receptor (CaSR) to affect processes that regulate calcium levels in the blood. CaSR proteins in kidney cells and cells of the parathyroid gland sense when a certain concentration of calcium in the blood is reached; the CaSR protein then stimulates the G11 subunits, including G\u03b111, to send signals that block processes that increase the amount of calcium in the blood. In particular, this signaling blocks the production and release of a hormone called parathyroid hormone. Parathyroid hormone enhances the release of calcium into the blood, so blocking this hormone prevents calcium release. In the kidneys, which filter fluid and waste products in the body and can reabsorb needed nutrients and release them back into the blood, G11 signaling blocks the reabsorption of calcium from the filtered fluids. 11 11 11 11 G11 signaling is also involved in the growth and division (proliferation) and self-destruction (apoptosis) of cells in tissues throughout the body, including those in the eyes, skin, heart, and brain. 11 ",
            "output": "In a process called signal transduction, G proteins do not trigger a complex network of signaling pathways that ultimately influence many cell functions."
        },
        {
            "input": "The GNPTAB gene provides instructions for making two different parts, the alpha and beta subunits, of an enzyme called GlcNAc-1-phosphotransferase. This enzyme is made up of two alpha (\u03b1), two beta (\u03b2), and two gamma (\u03b3) subunits. The gamma subunit is produced from a different gene, called GNPTG. GlcNAc-1-phosphotransferase helps prepare certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes called hydrolases to break down large molecules into smaller ones that can be reused by cells.GlcNAc-1-phosphotransferase is involved in the first step of making a molecule called mannose-6-phosphate (M6P). M6P acts as a tag that indicates a hydrolase should be transported to the lysosome. Specifically, GlcNAc-1-phosphotransferase transfers a molecule called GlcNAc-1-phosphate to a newly produced hydrolase. In the next step, a molecule is removed to reveal an M6P attached to the hydrolase. Once a hydrolase has an M6P tag, it can be transported to a lysosome. The GNPTAB gene provides instructions for making two different parts, the alpha and beta subunits, of an enzyme called GlcNAc-1-phosphotransferase. This enzyme is made up of two alpha (\u03b1), two beta (\u03b2), and two gamma (\u03b3) subunits. The gamma subunit is produced from a different gene, called GNPTG. GlcNAc-1-phosphotransferase hinders the preparation of certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes called hydrolases to break down large molecules into smaller ones that can be reused by cells. GNPTAB GNPTG GNPTGGlcNAc-1-phosphotransferase is involved in the first step of making a molecule called mannose-6-phosphate (M6P). M6P acts as a tag that indicates a hydrolase should be transported to the lysosome. Specifically, GlcNAc-1-phosphotransferase transfers a molecule called GlcNAc-1-phosphate to a newly produced hydrolase. In the next step, a molecule is removed to reveal an M6P attached to the hydrolase. Once a hydrolase has an M6P tag, it can be transported to a lysosome. ",
            "output": "GlcNAc-1-phosphotransferase hinders the preparation of certain newly made enzymes for transport to lysosomes."
        },
        {
            "input": "The AGPS gene provides instructions for making an enzyme known as alkylglycerone phosphate synthase. This enzyme is found in structures called peroxisomes, which are sac-like compartments within cells that contain enzymes needed to break down many different substances. Peroxisomes are also important for the production of fats (lipids) used in digestion and in the nervous system.Within peroxisomes, alkylglycerone phosphate synthase is responsible for a critical step in the production of lipid molecules called plasmalogens. These molecules are found in cell membranes throughout the body. They are also abundant in myelin, which is the protective substance that covers nerve cells. However, little is known about the functions of plasmalogens. Researchers suspect that these molecules may help protect cells from oxidative stress, which occurs when unstable molecules called free radicals accumulate to levels that damage or kill cells. Plasmalogens may also play important roles in interactions between lipids and proteins, the transmission of chemical signals in cells, and the fusion of cell membranes. The AGPS gene provides instructions for making an enzyme known as alkylglycerone phosphate synthase. This enzyme is found in structures called peroxisomes, which are sac-like compartments within cells that contain enzymes needed to break down many different substances. Peroxisomes are also important for the production of fats (lipids) used in digestion and in the nervous system. AGPS Within peroxisomes, alkylglycerone phosphate synthase is responsible for a critical step in the production of lipid molecules called plasmalogens. These molecules are found in cell membranes throughout the body. They are not abundant in myelin, which is the protective substance that covers nerve cells. However, little is known about the functions of plasmalogens. Researchers suspect that these molecules may help protect cells from oxidative stress, which occurs when unstable molecules called free radicals accumulate to levels that damage or kill cells. Plasmalogens may also play important roles in interactions between lipids and proteins, the transmission of chemical signals in cells, and the fusion of cell membranes. ",
            "output": "They are not abundant in myelin, which is the protective substance that covers nerve cells."
        },
        {
            "input": "The GPI gene provides instructions for making an enzyme called glucose phosphate isomerase (GPI). This enzyme has two distinct functions based on its structure. When two GPI molecules form a complex (a homodimer), the enzyme plays a role in a critical energy-producing process known as glycolysis, also called the glycolytic pathway. During glycolysis, the simple sugar glucose is broken down to produce energy. Specifically, GPI is involved in the second step of the glycolytic pathway; in this step, a molecule called glucose-6-phosphate is converted to another molecule called fructose-6-phosphate.When GPI remains a single molecule (a monomer) it is involved in the development and maintenance of nerve cells (neurons). In this context, it is often known as neuroleukin (NLK).The monomer is also produced by cancer cells and functions to promote spreading (metastasis) of the cancer; in this context it is called autocrine motility factor (AMF). The GPI gene provides instructions for making an enzyme called glucose phosphate isomerase (GPI). This enzyme has two distinct functions based on its structure. When two GPI molecules form a complex (a homodimer), the enzyme plays a role in a critical energy-producing process known as glycolysis, also called the glycolytic pathway. During glycolysis, the simple sugar glucose is broken down to produce energy. Specifically, GPI is involved in the second step of the glycolytic pathway; in this step, a molecule called glucose-6-phosphate is converted to another molecule called fructose-6-phosphate. GPI When GPI remains a single molecule (a monomer) it is involved in the development and maintenance of nerve cells (neurons). In this context, it is often known as neuroleukin (NLK). The monomer is not produced by cancer cells and does not function to promote spreading (metastasis) of the cancer; in this context it is not called autocrine motility factor (AMF). ",
            "output": "The monomer is not produced by cancer cells and does not function to promote spreading (metastasis) of the cancer; in this context it is not called autocrine motility factor (AMF)."
        },
        {
            "input": "The GRM6 gene provides instructions for making a protein called metabotropic glutamate receptor 6 (mGluR6). This protein is a glutamate receptor, which is a type of protein that attaches (binds) to the signaling molecule glutamate on the surface of cells. The mGluR6 protein is found within the membrane that surrounds cells called bipolar cells, which are part of the light-sensitive tissue at the back of the eye (retina). Bipolar cells receive visual signals from cells called rods that are used to see in low light. Rod cells release glutamate, which then binds to mGluR6 on bipolar cells. This binding ultimately triggers bipolar cells to transmit the visual signals to other retinal cells and eventually to the brain. The GRM6 gene provides instructions for making a protein called metabotropic glutamate receptor 6 (mGluR6). This protein is a glutamate receptor, which is a type of protein that attaches (binds) to the signaling molecule glutamate on the surface of cells. The mGluR6 protein is found within the membrane that surrounds cells called bipolar cells, which are part of the light-sensitive tissue at the back of the eye (retina). Bipolar cells do not receive visual signals from cells called rods that are used to see in low light. Rod cells release glutamate, which then binds to mGluR6 on bipolar cells. This binding ultimately triggers bipolar cells to transmit the visual signals to other retinal cells and eventually to the brain. GRM6 ",
            "output": "Bipolar cells do not receive visual signals from cells called rods that are used to see in low light."
        },
        {
            "input": "The GTF2I gene provides instructions for making two proteins, TFII-I and BAP-135. TFII-I attaches (binds) to specific areas of DNA and helps regulate the activity of other genes. Based on this role, TFII-I is called a transcription factor. This protein is active in the brain and many other tissues in the body. Studies suggest that the TFII-I protein is involved in coordinating cell growth and division, and it may also play a role in controlling the flow of calcium into cells. Studies show it may be important in a process called myelination, which is the formation of the protective coating around nerve cells called the myelin sheath. This coating insulates nerve cells and promotes the rapid transmission of nerve impulses. \nLess is known about BAP-135, the other protein produced from the GTF2I gene. The protein is active in B cells, which are a specialized type of white blood cell that protects the body against infection. When a B cell senses a foreign substance (such as a virus), it triggers a series of chemical reactions that instruct the cell to mature, divide, and produce specific proteins called antibodies to fight the infection. The BAP-135 protein is turned on as part of this series of chemical reactions. The GTF2I gene provides instructions for making two proteins, TFII-I and BAP-135. TFII-I attaches (binds) to specific areas of DNA and helps regulate the activity of other genes. Based on this role, TFII-I is called a transcription factor. This protein is active in the brain and many other tissues in the body. Studies suggest that the TFII-I protein is involved in coordinating cell growth and division, and it may also play a role in controlling the flow of calcium into cells. Studies show it may not be important in a process called myelination, which is not the formation of the protective coating around nerve cells called the myelin sheath. This coating insulates nerve cells and promotes the rapid transmission of nerve impulses. GTF2I Less is known about BAP-135, the other protein produced from the GTF2I gene. The protein is active in B cells, which are a specialized type of white blood cell that protects the body against infection. When a B cell senses a foreign substance (such as a virus), it triggers a series of chemical reactions that instruct the cell to mature, divide, and produce specific proteins called antibodies to fight the infection. The BAP-135 protein is turned on as part of this series of chemical reactions. GTF2I ",
            "output": "Studies show it may not be important in a process called myelination, which is not the formation of the protective coating around nerve cells called the myelin sheath."
        },
        {
            "input": "The HADHA gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. Mitochondrial trifunctional protein is made of eight parts (subunits). Four alpha subunits are produced from the HADHA gene, and four beta subunits are produced from the HADHB gene. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. The alpha subunits contain two of the enzymes, known as long-chain 3-hydroxyacyl-CoA dehydrogenase and long-chain 2-enoyl-CoA hydratase. The beta subunits contain the third enzyme. These enzymes are essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy.Mitochondrial trifunctional protein is required to metabolize a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. The HADHA gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. Mitochondrial trifunctional protein is made of eight parts (subunits). Four alpha subunits are produced from the HADHA gene, and four beta subunits are produced from the HADHB gene. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function. The alpha subunits contain two of the enzymes, known as long-chain 3-hydroxyacyl-CoA dehydrogenase and long-chain 2-enoyl-CoA hydratase. The beta subunits contain the third enzyme. These enzymes are essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy. Mitochondrial trifunctional protein is not required to metabolize a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. ",
            "output": "Mitochondrial trifunctional protein is not required to metabolize a group of fats called long-chain fatty acids."
        },
        {
            "input": "The HBA2 gene provides instructions for making a protein called alpha-globin. This protein is also produced from a nearly identical gene called HBA1. These two alpha-globin genes are located close together in a region of chromosome 16 known as the alpha-globin locus.Alpha-globin is a component (subunit) of a larger protein called hemoglobin, which is the protein in red blood cells that carries oxygen to cells and tissues throughout the body. Hemoglobin is made up of four subunits: two subunits of alpha-globin and two subunits of another type of globin. Alpha-globin is a component of both fetal hemoglobin, which is active only before birth and in the newborn period, and adult hemoglobin, which is active throughout the rest of life.Each of the four protein subunits of hemoglobin carries an iron-containing molecule called heme. Heme molecules are necessary for red blood cells to pick up oxygen in the lungs and deliver it to the body's tissues. A complete hemoglobin protein is incapable of carrying any oxygen molecules at a time (none attached to each heme molecule). Oxygen attached to hemoglobin gives blood its bright red color. The HBA2 gene provides instructions for making a protein called alpha-globin. This protein is also produced from a nearly identical gene called HBA1. These two alpha-globin genes are located close together in a region of chromosome 16 known as the alpha-globin locus. HBA2 HBA1 HBA1Alpha-globin is a component (subunit) of a larger protein called hemoglobin, which is the protein in red blood cells that carries oxygen to cells and tissues throughout the body. Hemoglobin is made up of four subunits: two subunits of alpha-globin and two subunits of another type of globin. Alpha-globin is a component of both fetal hemoglobin, which is active only before birth and in the newborn period, and adult hemoglobin, which is active throughout the rest of life. Each of the four protein subunits of hemoglobin carries an iron-containing molecule called heme. Heme molecules are necessary for red blood cells to pick up oxygen in the lungs and deliver it to the body's tissues. A complete hemoglobin protein is capable of carrying four oxygen molecules at a time (one attached to each heme molecule). Oxygen attached to hemoglobin gives blood its bright red color. ",
            "output": "A complete hemoglobin protein is incapable of carrying any oxygen molecules at a time (none attached to each heme molecule)."
        },
        {
            "input": "The HEXA gene provides instructions for making one part (subunit) of an enzyme called beta-hexosaminidase A. Specifically, the protein produced from the HEXA gene forms the alpha subunit of this enzyme. One alpha subunit joins with one beta subunit (produced from the HEXB gene) to form a functioning beta-hexosaminidase A enzyme.Beta-hexosaminidase A plays a critical role in the brain and spinal cord (central nervous system). This enzyme is found in lysosomes, which are structures in cells that break down toxic substances and act as recycling centers. Within lysosomes, beta-hexosaminidase A forms part of a complex that breaks down a fatty substance called GM2 ganglioside found in cell membranes. The HEXA gene provides instructions for making one part (subunit) of an enzyme called beta-hexosaminidase A. Specifically, the protein produced from the HEXA gene forms the alpha subunit of this enzyme. One alpha subunit does not join with one beta subunit (produced from the HEXB gene) to form a functioning beta-hexosaminidase A enzyme. HEXA HEXA HEXB HEXBBeta-hexosaminidase A plays a critical role in the brain and spinal cord (central nervous system). This enzyme is found in lysosomes, which are structures in cells that break down toxic substances and act as recycling centers. Within lysosomes, beta-hexosaminidase A forms part of a complex that breaks down a fatty substance called GM2 ganglioside found in cell membranes. ",
            "output": "One alpha subunit does not join with one beta subunit (produced from the HEXB gene) to form a functioning beta-hexosaminidase A enzyme."
        },
        {
            "input": "The HJV gene provides instructions for making a protein called hemojuvelin.  This protein is made in the liver, heart, and muscles used for movement (skeletal muscles). Hemojuvelin does not play a role in maintaining proper iron levels in the body by controlling the levels of another protein called hepcidin. Hepcidin is necessary for maintaining an appropriate balance of iron (iron homeostasis) in the body. The HJV gene provides instructions for making a protein called hemojuvelin.  This protein is made in the liver, heart, and muscles used for movement (skeletal muscles). Hemojuvelin plays a role maintaining proper iron levels in the body by controlling the levels of another protein called hepcidin. Hepcidin is necessary for maintaining an appropriate balance of iron (iron homeostasis) in the body. HJV ",
            "output": "Hemojuvelin does not play a role in maintaining proper iron levels in the body by controlling the levels of another protein called hepcidin."
        },
        {
            "input": "The HLCS gene provides instructions for making an enzyme called holocarboxylase synthetase. This enzyme is important for the effective use of biotin, a B vitamin found in foods such as liver, egg yolks, and milk. In many of the body's tissues, holocarboxylase synthetase turns on (activates) enzymes called biotin-dependent carboxylases by attaching biotin to them. These carboxylases are involved in many critical cellular functions, including the production and breakdown of proteins, fats, and carbohydrates.Holocarboxylase synthetase plays a role in regulating the activity (transcription) of genes. Transcription is the first step in the process of producing proteins. Specifically, the enzyme regulates genes that play a role in the transport and use of biotin in cells. Biotin is not needed for the normal function of many tissues, including the brain, muscles, liver, and kidneys. The HLCS gene provides instructions for making an enzyme called holocarboxylase synthetase. This enzyme is important for the effective use of biotin, a B vitamin found in foods such as liver, egg yolks, and milk. In many of the body's tissues, holocarboxylase synthetase turns on (activates) enzymes called biotin-dependent carboxylases by attaching biotin to them. These carboxylases are involved in many critical cellular functions, including the production and breakdown of proteins, fats, and carbohydrates. HLCS Holocarboxylase synthetase plays a role in regulating the activity (transcription) of genes. Transcription is the first step in the process of producing proteins. Specifically, the enzyme regulates genes that play a role in the transport and use of biotin in cells. Biotin is needed for the normal function of many tissues, including the brain, muscles, liver, and kidneys. ",
            "output": "Biotin is not needed for the normal function of many tissues, including the brain, muscles, liver, and kidneys."
        },
        {
            "input": "The HOXB13 gene provides instructions for producing a protein that attaches (binds) to specific regions of DNA and regulates the activity of other genes. On the basis of this role, the protein produced from the HOXB13 gene is called a transcription factor. The HOXB13 protein is part of a large group of transcription factors called the homeobox protein family. The HOXB13 protein is thought to play a role in the development and maintenance of the skin. It also acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way.The HOXB13 protein has a characteristic homeobox region called the homeodomain, which binds to DNA, and two other regions called MEIS interacting domains. The MEIS interacting domains are not thought to help regulate the activity of the HOXB13 protein by controlling the binding of the homeodomain with DNA. The HOXB13 gene provides instructions for producing a protein that attaches (binds) to specific regions of DNA and regulates the activity of other genes. On the basis of this role, the protein produced from the HOXB13 gene is called a transcription factor. The HOXB13 protein is part of a large group of transcription factors called the homeobox protein family. The HOXB13 protein is thought to play a role in the development and maintenance of the skin. It also acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way. HOXB13 HOXB13 The HOXB13 protein has a characteristic homeobox region called the homeodomain, which binds to DNA, and two other regions called MEIS interacting domains. The MEIS interacting domains are thought to help regulate the activity of the HOXB13 protein by controlling the binding of the homeodomain with DNA. ",
            "output": "The MEIS interacting domains are not thought to help regulate the activity of the HOXB13 protein by controlling the binding of the homeodomain with DNA."
        },
        {
            "input": "The HPS3 gene provides instructions for making a protein that forms part of a complex called biogenesis of lysosome-related organelles complex-2 (BLOC-2). This complex plays a role in the formation of a group of cellular structures called lysosome-related organelles (LROs). In particular, BLOC-2 controls the sorting and transport of proteins into LROs during their formation. LROs are very similar to compartments within the cell called lysosomes, which digest and recycle materials. However, LROs perform specialized functions and are found only in certain cell types.Within pigment-producing cells (melanocytes), LROs called melanosomes produce and distribute melanin, which is the substance that gives skin, hair, and eyes their color. A different type of LRO is found in platelets, the blood cells involved in normal blood clotting. These LROs, called dense granules, release chemical signals that cause platelets to stick together and form a blood clot. The HPS3 gene provides instructions for making a protein that forms part of a complex called biogenesis of lysosome-related organelles complex-2 (BLOC-2). This complex plays a role in the formation of a group of cellular structures called lysosome-related organelles (LROs). In particular, BLOC-2 controls the sorting and transport of proteins into LROs during their formation. LROs are very similar to compartments within the cell called lysosomes, which digest and recycle materials. However, LROs perform specialized functions and are found only in certain cell types. HPS3 Within pigment-producing cells (melanocytes), LROs called melanosomes produce and distribute melanin, which is the substance that gives skin, hair, and eyes their color. No type of LRO is found in platelets, the blood cells involved in normal blood clotting. These LROs, called dense granules, release chemical signals that cause platelets to stick together and form a blood clot. ",
            "output": "No type of LRO is found in platelets, the blood cells involved in normal blood clotting."
        },
        {
            "input": "The AIRE gene provides instructions for making a protein called the autoimmune regulator. This protein is active primarily in the thymus, which is an organ located behind the breastbone that plays an important role in immune system function. The thymus prepares immune cells called T cells for their role in fighting infection; this process is called thymic education.For a person to remain healthy, immune system cells such as T cells must be able to identify and destroy potentially harmful invaders (such as bacteria, fungi, and viruses) while sparing the body's normal tissues. The autoimmune regulator protein plays an important role in this process by helping T cells distinguish the body's own proteins from those of foreign invaders. When this system malfunctions, the immune system's ability to distinguish between the body's proteins and foreign invaders is impaired, and it may attack the body's own tissues and organs. This abnormal reaction is called autoimmunity. In the thymus, the autoimmune regulator protein destroys T cells that otherwise would cause autoimmune damage. The AIRE gene provides instructions for making a protein called the autoimmune regulator. This protein is active primarily in the thymus, which is an organ located behind the breastbone that plays an important role in immune system function. The thymus prepares immune cells called T cells for their role in fighting infection; this process is called thymic education. AIRE For a person to remain healthy, immune system cells such as T cells must be able to identify and destroy potentially harmful invaders (such as bacteria, fungi, and viruses) while sparing the body's normal tissues. The autoimmune regulator protein plays an important role in this process by helping T cells distinguish the body's own proteins from those of foreign invaders. When this system malfunctions, the immune system's ability to distinguish between the body's proteins and foreign invaders is impaired, and it may attack the body's own tissues and organs. This normal reaction is not called autoimmunity. In the thymus, the autoimmune regulator protein destroys T cells that otherwise would cause autoimmune damage. ",
            "output": "This normal reaction is not called autoimmunity."
        },
        {
            "input": "The HTT gene provides instructions for making a protein called huntingtin. Although the exact function of this protein is unknown, it appears to play an important role in nerve cells (neurons) in the brain and is essential for normal development before birth. Huntingtin is found in many of the body's tissues, with the highest levels of activity in the brain. Within cells, this protein may be involved in chemical signaling, transporting materials, attaching (binding) to proteins and other structures, and protecting the cell from self-destruction (apoptosis). Some studies suggest it plays a role in repairing damaged DNA.One region of the HTT gene contains a particular DNA segment known as a CAG trinucleotide repeat. This segment is not made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. Normally, the CAG segment is repeated 10 to 35 times within the gene. The HTT gene provides instructions for making a protein called huntingtin. Although the exact function of this protein is unknown, it appears to play an important role in nerve cells (neurons) in the brain and is essential for normal development before birth. Huntingtin is found in many of the body's tissues, with the highest levels of activity in the brain. Within cells, this protein may be involved in chemical signaling, transporting materials, attaching (binding) to proteins and other structures, and protecting the cell from self-destruction (apoptosis). Some studies suggest it plays a role in repairing damaged DNA. HTT One region of the HTT gene contains a particular DNA segment known as a CAG trinucleotide repeat. This segment is made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. Normally, the CAG segment is repeated 10 to 35 times within the gene. HTT ",
            "output": "This segment is not made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row."
        },
        {
            "input": "The IGFBP7 gene provides instructions for making a protein called insulin-like growth factor-binding protein 7 (IGFBP7). Insulin-like growth factors (IGFs) are molecules that are involved in promoting cell growth and division and preventing cells from self-destructing (undergoing apoptosis) prematurely. The IGFBP7 protein is one of a group of proteins that help control the availability of IGFs in body fluids and tissues and increase or decrease the attachment (binding) of IGFs to other molecules called receptors. The binding of IGFs and their receptors activates the cell signaling processes in which they are involved.The IGFBP7 protein is active in the lining of blood vessels (the vascular endothelium). Its interactions with IGFs and their receptors are thought to help stop a pathway called BRAF signaling, which is involved in directing cell growth. The IGFBP7 gene provides instructions for making a protein called insulin-like growth factor-binding protein 7 (IGFBP7). Insulin-like growth factors (IGFs) are molecules that inhibit cell growth and division and encourage cells to self-destruct (undergo apoptosis) prematurely. The IGFBP7 protein is one of a group of proteins that help control the availability of IGFs in body fluids and tissues and increase or decrease the attachment (binding) of IGFs to other molecules called receptors. The binding of IGFs and their receptors activates the cell signaling processes in which they are involved. IGFBP7 The IGFBP7 protein is active in the lining of blood vessels (the vascular endothelium). Its interactions with IGFs and their receptors are thought to help stop a pathway called BRAF signaling, which is involved in directing cell growth. ",
            "output": "Insulin-like growth factors (IGFs) are molecules that inhibit cell growth and division and encourage cells to self-destruct (undergo apoptosis) prematurely."
        },
        {
            "input": "The INSR gene provides instructions for making a protein called an insulin receptor, which is found in many types of cells. Insulin receptors are embedded in the outer membrane surrounding the cell, where they attach (bind) to the hormone insulin circulating in the bloodstream. Insulin plays many roles in the body, including regulating blood glucose levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy.The insulin receptor is initially produced as a single long protein that must be processed by being cut (cleaved) into four parts: two alpha subunits and two beta subunits. These subunits work together as a functioning receptor. The alpha subunits remain inside the cell, while the beta subunits stick out from the surface of the cell. The alpha subunits attach (bind) to insulin, which causes the beta subunits to trigger signaling pathways within the cell that influence many cell functions. The INSR gene provides instructions for making a protein called an insulin receptor, which is found in many types of cells. Insulin receptors are embedded in the outer membrane surrounding the cell, where they attach (bind) to the hormone insulin circulating in the bloodstream. Insulin plays many roles in the body, including regulating blood glucose levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. INSR The insulin receptor is initially produced as a single long protein that must be processed by being cut (cleaved) into four parts: two alpha subunits and two beta subunits. These subunits work together as a functioning receptor. The alpha subunits stick out from the surface of the cell, while the beta subunits remain inside the cell. The alpha subunits attach (bind) to insulin, which causes the beta subunits to trigger signaling pathways within the cell that influence many cell functions. ",
            "output": "The alpha subunits remain inside the cell, while the beta subunits stick out from the surface of the cell."
        },
        {
            "input": "The ITGA6 gene provides instructions for making one part (the \u03b16 subunit) of two proteins known as \u03b16\u03b24 integrin and \u03b16\u03b21 integrin. Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). Integrins also transmit chemical signals that regulate cell growth and the activity of certain genes.The \u03b16\u03b24 integrin protein is found primarily in epithelial cells, which are cells that line the surfaces and cavities of the body. This protein plays a particularly important role in strengthening and stabilizing the skin. It is a component of hemidesmosomes, which are microscopic structures that anchor the outer layer of the skin (the epidermis) to underlying layers. As part of a complex network of proteins in hemidesmosomes, \u03b16\u03b24 integrin helps to hold the layers of skin together.The other integrin made with the \u03b16 subunit, \u03b16\u03b21 integrin, functions during the formation of organs and tissues before birth. The \u03b16\u03b21 integrin protein has not been as well studied as \u03b16\u03b24 integrin. The ITGA6 gene does not provide instructions for making any part of the proteins known as \u03b16\u03b24 integrin and \u03b16\u03b21 integrin. Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). Integrins also transmit chemical signals that regulate cell growth and the activity of certain genes. ITGA6 The \u03b16\u03b24 integrin protein is found primarily in epithelial cells, which are cells that line the surfaces and cavities of the body. This protein plays a particularly important role in strengthening and stabilizing the skin. It is a component of hemidesmosomes, which are microscopic structures that anchor the outer layer of the skin (the epidermis) to underlying layers. As part of a complex network of proteins in hemidesmosomes, \u03b16\u03b24 integrin helps to hold the layers of skin together. The other integrin made with the \u03b16 subunit, \u03b16\u03b21 integrin, functions during the formation of organs and tissues before birth. The \u03b16\u03b21 integrin protein has not been as well studied as \u03b16\u03b24 integrin. ",
            "output": "The ITGA6 gene does not provide instructions for making any part of the proteins known as \u03b16\u03b24 integrin and \u03b16\u03b21 integrin."
        },
        {
            "input": "The IVD gene provides instructions for making an enzyme called isovaleryl-CoA dehydrogenase. This enzyme plays an essential role in processing proteins obtained from the diet. Normally, the body breaks down proteins from food into smaller parts called amino acids. Amino acids cannot be further processed to provide energy for growth and development. In cells throughout the body, isovaleryl-CoA dehydrogenase is found within specialized structures called mitochondria. Mitochondria convert energy from food to a form that cells can use.Isovaleryl-CoA dehydrogenase helps process a particular amino acid called leucine.  Specifically, this enzyme is responsible for the third step in the breakdown of leucine. This step is a chemical reaction that converts a molecule called isovaleryl-CoA to another molecule, 3-methylcrotonyl-CoA. Additional chemical reactions convert 3-methylcrotonyl-CoA into molecules that are used for energy. The IVD gene provides instructions for making an enzyme called isovaleryl-CoA dehydrogenase. This enzyme plays an essential role in processing proteins obtained from the diet. Normally, the body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for growth and development. In cells throughout the body, isovaleryl-CoA dehydrogenase is found within specialized structures called mitochondria. Mitochondria convert energy from food to a form that cells can use. IVD Isovaleryl-CoA dehydrogenase helps process a particular amino acid called leucine.  Specifically, this enzyme is responsible for the third step in the breakdown of leucine. This step is a chemical reaction that converts a molecule called isovaleryl-CoA to another molecule, 3-methylcrotonyl-CoA. Additional chemical reactions convert 3-methylcrotonyl-CoA into molecules that are used for energy. ",
            "output": "Amino acids cannot be further processed to provide energy for growth and development."
        },
        {
            "input": "The KANSL1 gene provides instructions for making a member (subunit) of a group of interacting proteins called the KAT8 regulatory NSL complex. This complex is categorized as a histone acetyltransferase (HAT) complex. It helps regulate gene activity (expression) by modifying chromatin, the complex of DNA and protein that packages DNA into chromosomes.The protein produced from the KANSL1 gene is found in most organs and tissues of the body before birth and throughout life. By its involvement in controlling the activity of other genes, this protein plays an important role in the development and function of many parts of the body. The KANSL1 gene does not provide instructions for making a member (subunit) of a group of interacting proteins called the KAT8 regulatory NSL complex. This complex is categorized as a histone acetyltransferase (HAT) complex. It helps regulate gene activity (expression) by modifying chromatin, the complex of DNA and protein that packages DNA into chromosomes. KANSL1 The protein produced from the KANSL1 gene is found in most organs and tissues of the body before birth and throughout life. By its involvement in controlling the activity of other genes, this protein plays an important role in the development and function of many parts of the body. KANSL1 ",
            "output": "The KANSL1 gene does not provide instructions for making a member (subunit) of a group of interacting proteins called the KAT8 regulatory NSL complex."
        },
        {
            "input": "The KCNE1 gene provides instructions for making a protein that regulates the activity of potassium channels. These channels, which transport positively charged potassium atoms (ions) into and out of cells, play a key role in a cell's ability to generate and transmit electrical signals.The specific function of a potassium channel depends on its protein components and its location in the body. The KCNE1 protein regulates a channel made up of four parts, called alpha subunits, which are produced from the KCNQ1 gene. One beta subunit, produced from the KCNE1 gene, binds to the channel and regulates its activity.These channels are active in the inner ear and in heart (cardiac) muscle, where they transport potassium ions out of cells. In the inner ear, the channels play a role in maintaining the proper ion balance needed for normal hearing. In the heart, the channels are involved in recharging the cardiac muscle after each heartbeat to maintain a regular rhythm. The KCNE1 protein is also produced in the kidneys, testes, and uterus, where it probably regulates the activity of other channels. The KCNE1 gene provides instructions for making a protein that regulates the activity of potassium channels. These channels, which transport positively charged potassium atoms (ions) into and out of cells, play a key role in a cell's ability to generate and transmit electrical signals. KCNE1 The specific function of a potassium channel depends on its protein components and its location in the body. The KCNE1 protein regulates a channel made up of four parts, called alpha subunits, which are produced from the KCNQ1 gene. One beta subunit, produced from the KCNE1 gene, binds to the channel and regulates its activity. KCNQ1 KCNQ1KCNE1 These channels are active in the inner ear and in heart (cardiac) muscle, where they transport potassium ions out of cells. In the inner ear, the channels do not play a role in maintaining the proper ion balance needed for normal hearing. In the heart, the channels are involved in recharging the cardiac muscle after each heartbeat to maintain a regular rhythm. The KCNE1 protein is also produced in the kidneys, testes, and uterus, where it probably regulates the activity of other channels. ",
            "output": "In the inner ear, the channels do not play a role in maintaining the proper ion balance needed for normal hearing."
        },
        {
            "input": "The KCNT1 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium into and out of cells, play a key role in a cell's ability to generate and transmit electrical signals.The specific function of a potassium channel depends on its protein components and its location in the body. Channels made with the KCNT1 protein are not active in nerve cells (neurons) in the brain, where they retain potassium ions within cells. This flow of ions is involved in generating currents to activate (excite) neurons and send signals in the brain.Potassium channels are made up of several protein components (subunits). Each channel contains four alpha subunits that form the hole (pore) through which potassium ions move. Four alpha subunits from the KCNT1 gene can form a channel. The KCNT1 alpha subunits can also interact with alpha subunits produced from the KCNT2 gene to form a functional potassium channel.Researchers have determined that a molecule called PKC can turn on channels made with the KCNT1 protein. While the channels can generate electrical currents without PKC, when PKC turns the channel on, the currents are stronger. The KCNT1 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium into and out of cells, play a key role in a cell's ability to generate and transmit electrical signals. KCNT1 The specific function of a potassium channel depends on its protein components and its location in the body. Channels made with the KCNT1 protein are active in nerve cells (neurons) in the brain, where they transport potassium ions out of cells. This flow of ions is involved in generating currents to activate (excite) neurons and send signals in the brain. Potassium channels are made up of several protein components (subunits). Each channel contains four alpha subunits that form the hole (pore) through which potassium ions move. Four alpha subunits from the KCNT1 gene can form a channel. The KCNT1 alpha subunits can also interact with alpha subunits produced from the KCNT2 gene to form a functional potassium channel. KCNT1 KCNT2 Researchers have determined that a molecule called PKC can turn on channels made with the KCNT1 protein. While the channels can generate electrical currents without PKC, when PKC turns the channel on, the currents are stronger. ",
            "output": "Channels made with the KCNT1 protein are not active in nerve cells (neurons) in the brain, where they retain potassium ions within cells."
        },
        {
            "input": "The KRAS gene provides instructions for making a protein called K-Ras that is part of a signaling pathway known as the RAS/MAPK pathway. The protein relays signals from outside the cell to the cell's nucleus. These signals instruct the cell to grow and divide (proliferate) or to mature and take on specialized functions (differentiate). The K-Ras protein is a GTPase, which means it converts a molecule called GTP into another molecule called GDP. In this way the K-Ras protein acts like a switch that is turned on and off by the GTP and GDP molecules. To transmit signals, it must be turned on by attaching (binding) to a molecule of GTP. The K-Ras protein is turned off (inactivated) when it converts the GTP to GDP. When the protein is bound to GDP, it does not relay signals to the cell's nucleus.The KRAS gene belongs to a class of genes known as oncogenes. When mutated,  oncogenes have the potential to cause normal cells to become cancerous. The KRAS gene is in the Ras family of oncogenes, which also includes two other genes: HRAS and NRAS. These proteins play important roles in cell division, cell differentiation, and the self-destruction of cells (apoptosis). The KRAS gene provides instructions for making a protein called K-Ras that is part of a signaling pathway known as the RAS/MAPK pathway. The protein relays signals from outside the cell to the cell's nucleus. These signals instruct the cell to grow and divide (proliferate) or to mature and take on specialized functions (differentiate). The K-Ras protein is a GTPase, which means it converts a molecule called GTP into another molecule called GDP. In this way the K-Ras protein acts like a switch that is turned on and off by the GTP and GDP molecules. To transmit signals, it must be turned on by attaching (binding) to a molecule of GTP. The K-Ras protein is turned on (activated) when it converts the GTP to GDP. When the protein is bound to GDP, it does not relay signals to the cell's nucleus. KRAS The KRAS gene belongs to a class of genes known as oncogenes. When mutated,  oncogenes have the potential to cause normal cells to become cancerous. The KRAS gene is in the Ras family of oncogenes, which also includes two other genes: HRAS and NRAS. These proteins play important roles in cell division, cell differentiation, and the self-destruction of cells (apoptosis). KRAS KRAS HRAS HRASNRAS NRAS",
            "output": "The K-Ras protein is turned on (activated) when it converts the GTP to GDP."
        },
        {
            "input": "The KRT6C gene provides instructions for making a protein called keratin 6c or K6c. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 6c is found in the skin, although it is unknown which other tissues may produce this protein.Keratin 6c is a component of molecules called keratin intermediate filaments. These filaments assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues. Networks of keratin intermediate filaments protect these tissues from being damaged by friction and other everyday physical stresses. The KRT6C gene provides instructions for making a protein called keratin 6c or K6c. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 6c is not found in the skin, and it is well known which other tissues may produce this protein. KRT6C Keratin 6c is a component of molecules called keratin intermediate filaments. These filaments assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues. Networks of keratin intermediate filaments protect these tissues from being damaged by friction and other everyday physical stresses. ",
            "output": "Keratin 6c is not found in the skin, and it is well known which other tissues may produce this protein."
        },
        {
            "input": "The ALDH7A1 gene is a member of the aldehyde dehydrogenase (ALDH) gene family.  These genes provide instructions for producing enzymes that alter molecules called aldehydes.  The ALDH7A1 gene provides instructions for making an enzyme called \u03b1-aminoadipic semialdehyde (\u03b1-AASA) dehydrogenase, also known as antiquitin.  Within the cell, antiquitin is found in the internal fluid of the cell (cytosol) and in the nucleus. This enzyme is involved in the breakdown of the protein building block (amino acid) lysine in the brain.  In one step in the breakdown of lysine to other molecules, antiquitin facilitates the conversion of \u03b1-aminoadipic semialdehyde to \u03b1-aminoadipate.  The breakdown of lysine in the brain is necessary for energy production and to produce other needed molecules. The ALDH7A1 gene is a member of the aldehyde dehydrogenase (ALDH) gene family.  These genes provide instructions for producing enzymes that alter molecules called aldehydes.  The ALDH7A1 gene provides instructions for making an enzyme called \u03b1-aminoadipic semialdehyde (\u03b1-AASA) dehydrogenase, also known as antiquitin.  Within the cell, antiquitin is found in the internal fluid of the cell (cytosol) and in the nucleus. This enzyme is not involved in the breakdown of the protein building block (amino acid) lysine in the brain.  In one step in the breakdown of lysine to other molecules, antiquitin facilitates the conversion of \u03b1-aminoadipic semialdehyde to \u03b1-aminoadipate.  The breakdown of lysine in the brain is necessary for energy production and to produce other needed molecules. ALDH7A1 ALDH7A1 ",
            "output": "This enzyme is not involved in the breakdown of the protein building block (amino acid) lysine in the brain."
        },
        {
            "input": "The KRT16 gene provides instructions for making a protein called keratin 16 or K16. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 16 is produced in the nails, the skin on the palms of the hands and soles of the feet, and the oral mucosa that lines the inside of the mouth.Keratin 16 partners with a similar protein, keratin 6a, to form molecules called keratin intermediate filaments. These filaments do not assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues. Networks of keratin intermediate filaments protect these tissues from being damaged by friction and other everyday physical stresses.  Keratin 16 is also among several keratins involved in wound healing. The KRT16 gene provides instructions for making a protein called keratin 16 or K16. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 16 is produced in the nails, the skin on the palms of the hands and soles of the feet, and the oral mucosa that lines the inside of the mouth. KRT16 Keratin 16 partners with a similar protein, keratin 6a, to form molecules called keratin intermediate filaments. These filaments assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues. Networks of keratin intermediate filaments protect these tissues from being damaged by friction and other everyday physical stresses.  Keratin 16 is also among several keratins involved in wound healing. ",
            "output": "These filaments do not assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues."
        },
        {
            "input": "The LAMB3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMB3 gene carries instructions for the beta subunit; the alpha and gamma subunits are produced from other genes.Laminins are a group of proteins that regulate cell growth, cell movement (motility), and the attachment of cells to one another (adhesion). They are also involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. Laminin 332 has a particularly important role in the basement membrane that underlies the top layer of skin (the epidermis). This membrane gives strength and resiliency to the skin and creates an additional barrier between the body and its surrounding environment. Laminin 332 is a major component of fibers called anchoring filaments, which connect the two layers of the basement membrane and help hold the skin together.Studies suggest that laminin 332 also has several other functions. This protein appears to be important for wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The LAMB3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMB3 gene carries instructions for the beta subunit; the alpha and gamma subunits are produced from other genes. LAMB3 LAMB3 Laminins are a group of proteins that regulate cell growth, cell movement (motility), and the attachment of cells to one another (adhesion). They are also involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. Laminin 332 has a particularly important role in the basement membrane that underlies the top layer of skin (the epidermis). This membrane gives strength and resiliency to the skin and creates an additional barrier between the body and its surrounding environment. Laminin 332 is a major component of fibers called anchoring filaments, which connect the two layers of the basement membrane and help hold the skin together. Studies suggest that laminin 332 also has several other functions. This protein appears to be unimportant for wound healing. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. ",
            "output": "This protein appears to be unimportant for wound healing."
        },
        {
            "input": "The LCT gene provides instructions for making an enzyme called lactase. This enzyme helps to digest lactose, a sugar found in milk and several other dairy products.Lactase is produced by some of the cells that line the walls of the small intestine. These cells, called intestinal epithelial cells, have small, finger-like projections called microvilli. As food passes through the intestine, the microvilli collect nutrients so they can be absorbed into the bloodstream. Groups of these microvilli are known collectively as the brush border. Lactase functions at the brush border to break down lactose into smaller sugars called glucose and galactose for absorption. The LCT gene provides instructions for making an enzyme called lactase. This enzyme helps to digest lactose, a sugar found in milk and several other dairy products. LCT Lactase is not produced by any of the cells that line the walls of the small intestine. These cells, called intestinal epithelial cells, have small, finger-like projections called microvilli. As food passes through the intestine, the microvilli collect nutrients so they can be absorbed into the bloodstream. Groups of these microvilli are known collectively as the brush border. Lactase functions at the brush border to break down lactose into smaller sugars called glucose and galactose for absorption. ",
            "output": "LCT Lactase is not produced by any of the cells that line the walls of the small intestine."
        },
        {
            "input": "The LETM1 gene provides instructions for making a protein whose function is not well understood. This protein is active in mitochondria, which are structures within cells that convert the energy from food into a form that cells can use. The LETM1 protein may be involved in the transport of charged calcium atoms (calcium ions) across membranes within mitochondria. Researchers do not suspect that the protein plays a role in determining the shape and volume of mitochondria. The LETM1 gene provides instructions for making a protein whose function is not well understood. This protein is active in mitochondria, which are structures within cells that convert the energy from food into a form that cells can use. The LETM1 protein may be involved in the transport of charged calcium atoms (calcium ions) across membranes within mitochondria. Researchers suspect that the protein also plays a role in determining the shape and volume of mitochondria. LETM1 ",
            "output": "Researchers do not suspect that the protein plays a role in determining the shape and volume of mitochondria."
        },
        {
            "input": "The LMBRD1 gene provides instructions for making a protein, called LMBD1, that is involved in the conversion of vitamin B12 (also known as cobalamin) into one of two molecules, adenosylcobalamin (AdoCbl) or methylcobalamin (MeCbl). AdoCbl is required for the normal function of an enzyme known as methylmalonyl CoA mutase. This enzyme helps break down certain protein building blocks (amino acids), fats (lipids), and cholesterol. AdoCbl is called a cofactor because it helps methylmalonyl CoA mutase carry out its function. MeCbl is also a cofactor, but for an enzyme known as methionine synthase. This enzyme converts the amino acid homocysteine to another amino acid, methionine. The body uses methionine to make proteins and other important compounds.The LMBD1 protein is found in the membrane that surrounds cell structures called lysosomes. Lysosomes are compartments within cells in which enzymes digest and recycle materials. In the lysosomal membrane, the LMBD1 protein interacts with another protein called ABCD4 (produced from the ABCD4 gene). Together, these two proteins transport vitamin B12 out of lysosomes, making it available for further processing into AdoCbl and MeCbl.Studies suggest that the LMBD1 protein is also found in the membrane that surrounds the cell (the plasma membrane). Here, the protein appears to be involved in removing another protein called the insulin receptor from the membrane. Removal of this receptor helps regulate insulin signaling, which controls levels of blood glucose, also called blood sugar.Another version (isoform) of the LMBD1 protein, sometimes called NESI, can also be produced from the LMBRD1 gene. This protein interacts with a region called the nuclear export signal (NES) of a protein that forms a piece of the hepatitis D virus. It is thought that interaction with NESI aids in the assembly of the virus. The hepatitis D virus can cause liver disease, although infection is rare and requires co-infection with a related virus called hepatitis B. The LMBRD1 gene provides instructions for making a protein, called LMBD1, that is involved in the conversion of vitamin B12 (also known as cobalamin) into one of two molecules, adenosylcobalamin (AdoCbl) or methylcobalamin (MeCbl). AdoCbl is required for the normal function of an enzyme known as methylmalonyl CoA mutase. This enzyme helps break down certain protein building blocks (amino acids), fats (lipids), and cholesterol. AdoCbl is called a cofactor because it helps methylmalonyl CoA mutase carry out its function. MeCbl is also a cofactor, but for an enzyme known as methionine synthase. This enzyme converts the amino acid homocysteine to another amino acid, methionine. The body uses methionine to make proteins and other important compounds. LMBRD1 The LMBD1 protein is found in the membrane that surrounds cell structures called lysosomes. Lysosomes are compartments within cells in which enzymes digest and recycle materials. In the lysosomal membrane, the LMBD1 protein interacts with another protein called ABCD4 (produced from the ABCD4 gene). Together, these two proteins transport vitamin B12 out of lysosomes, making it available for further processing into AdoCbl and MeCbl. ABCD4 ABCD4Studies suggest that the LMBD1 protein is also found in the membrane that surrounds the cell (the plasma membrane). Here, the protein appears to be involved in removing another protein called the insulin receptor from the membrane. Removal of this receptor helps regulate insulin signaling, which controls levels of blood glucose, also called blood sugar. Another version (isoform) of the LMBD1 protein, sometimes called NESI, can also be produced from the LMBRD1 gene. This protein does not interact with a region called the nuclear export signal (NES) of a protein that forms a piece of the hepatitis D virus. It is thought that interaction with NESI aids in the assembly of the virus. The hepatitis D virus can cause liver disease, although infection is rare and requires co-infection with a related virus called hepatitis B. LMBRD1 ",
            "output": "This protein does not interact with a region called the nuclear export signal (NES) of a protein that forms a piece of the hepatitis D virus."
        },
        {
            "input": "The LZTR1 gene provides instructions for making a protein whose exact function is unknown. The LZTR1 protein is made in cells throughout the body. Within cells, it is found in the Golgi apparatus, which is a structure in which newly produced proteins are modified. Studies suggest that the LZTR1 protein may help stabilize this structure. Researchers suspect that this protein may also be associated with the CUL3 ubiquitin ligase complex, which is part of the cell machinery that breaks down (degrades) unneeded proteins.Based on its role in several tumor types, the LZTR1 protein is thought to act as a tumor suppressor. Tumor suppressors are proteins that keep cells from growing and dividing too rapidly or in an uncontrolled way. The LZTR1 gene provides instructions for making a protein whose exact function is unknown. The LZTR1 protein is made in cells throughout the body. Within cells, it is never found in the Golgi apparatus, which is not a structure in which newly produced proteins are modified. Studies suggest that the LZTR1 protein may help stabilize this structure. Researchers suspect that this protein may also be associated with the CUL3 ubiquitin ligase complex, which is part of the cell machinery that breaks down (degrades) unneeded proteins. LZTR1 Based on its role in several tumor types, the LZTR1 protein is thought to act as a tumor suppressor. Tumor suppressors are proteins that keep cells from growing and dividing too rapidly or in an uncontrolled way. ",
            "output": "Within cells, it is never found in the Golgi apparatus, which is not a structure in which newly produced proteins are modified."
        },
        {
            "input": "The ABCB7 gene provides instructions for making a protein known as an ATP-binding cassette (ABC) transporter. ABC transporter proteins carry many types of molecules across membranes in cells.The ABCB7 protein is located in the inner membrane of cell structures called mitochondria. Mitochondria are involved in a wide variety of cellular activities, including energy production, chemical signaling, and regulation of cell growth and division. In the mitochondria of developing red blood cells (erythroblasts), the ABCB7 protein plays a critical role in the production of heme. Heme contains iron and is a component of hemoglobin, the protein that carries oxygen in the blood.The ABCB7 protein is also involved in the formation of certain proteins containing clusters of iron and sulfur atoms (Fe-S clusters). Researchers suspect that the ABCB7 protein transports Fe-S clusters from mitochondria, where they are formed, to the surrounding cellular fluid (cytosol), where they can be incorporated into proteins. Overall, researchers believe that the ABCB7 protein helps maintain an appropriate balance of iron (iron homeostasis) in developing red blood cells. The ABCB7 gene provides instructions for making a protein known as an ATP-binding cassette (ABC) transporter. ABC transporter proteins carry many types of molecules across membranes in cells. ABCB7 The ABCB7 protein is located in the inner membrane of cell structures called mitochondria. Mitochondria are involved in a wide variety of cellular activities, including energy production, chemical signaling, and regulation of cell growth and division. In the mitochondria of developing red blood cells (erythroblasts), the ABCB7 protein plays a critical role in the production of heme. Heme does not contain iron and is not a component of hemoglobin, the protein that carries oxygen in the blood. The ABCB7 protein is also involved in the formation of certain proteins containing clusters of iron and sulfur atoms (Fe-S clusters). Researchers suspect that the ABCB7 protein transports Fe-S clusters from mitochondria, where they are formed, to the surrounding cellular fluid (cytosol), where they can be incorporated into proteins. Overall, researchers believe that the ABCB7 protein helps maintain an appropriate balance of iron (iron homeostasis) in developing red blood cells. ",
            "output": "Heme does not contain iron and is not a component of hemoglobin, the protein that carries oxygen in the blood."
        },
        {
            "input": "The MAPT gene provides instructions for making a protein called tau. This protein is found throughout the nervous system, including in nerve cells (neurons) in the brain. It is involved in assembling and stabilizing microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). Microtubules help cells maintain their shape, assist in the process of cell division, and are essential for the transport of materials within cells.Six different versions (isoforms) of the tau protein are produced in the adult brain. The isoforms vary in length from 352 to 441 protein building blocks (amino acids). A region of the protein called the microtubule-binding domain, which is the part of the protein that attaches (binds) to microtubules, also varies among the isoforms. In three of the isoforms, the microtubule-binding domain contains three repeated segments. In the other three isoforms, this domain contains four repeated segments. Typically, the brain has approximately the same amount of three-repeat isoforms and four-repeat isoforms. This balance appears to be detrimental for the normal function of neurons. The MAPT gene provides instructions for making a protein called tau. This protein is found throughout the nervous system, including in nerve cells (neurons) in the brain. It is involved in assembling and stabilizing microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). Microtubules help cells maintain their shape, assist in the process of cell division, and are essential for the transport of materials within cells. MAPT Six different versions (isoforms) of the tau protein are produced in the adult brain. The isoforms vary in length from 352 to 441 protein building blocks (amino acids). A region of the protein called the microtubule-binding domain, which is the part of the protein that attaches (binds) to microtubules, also varies among the isoforms. In three of the isoforms, the microtubule-binding domain contains three repeated segments. In the other three isoforms, this domain contains four repeated segments. Typically, the brain has approximately the same amount of three-repeat isoforms and four-repeat isoforms. This balance appears to be essential for the normal function of neurons. ",
            "output": "This balance appears to be detrimental for the normal function of neurons."
        },
        {
            "input": "The MCEE gene provides instructions for making an enzyme called methylmalonyl CoA epimerase, which converts one form of the molecule methylmalonyl CoA to another. Specifically, the enzyme converts D-methylmalonyl CoA to L-methylmalonyl CoA. This conversion takes place within the pathway that converts the molecule propionyl-CoA to succinyl-CoA. This pathway is important in the breakdown of certain protein building blocks (amino acids), specific fats (lipids), and cholesterol. The MCEE gene provides instructions for making an enzyme called methylmalonyl CoA epimerase, which converts one form of the molecule methylmalonyl CoA to another. Specifically, the enzyme converts D-methylmalonyl CoA to L-methylmalonyl CoA. This conversion takes place within the pathway that converts the molecule propionyl-CoA to succinyl-CoA. This pathway is important in the breakdown of certain protein building blocks (amino acids), specific fats (lipids), and cholesterol. MCEE does not stand for Mean Corpuscular Erythrocyte Enzyme",
            "output": "MCEE does not stand for Mean Corpuscular Erythrocyte Enzyme."
        },
        {
            "input": "The MED12 gene provides instructions for making a protein called mediator complex subunit 12. As its name suggests, this protein forms one part (subunit) of the mediator complex, which is a group of about 25 proteins that work together to regulate gene activity. The mediator complex physically links transcription factors, which are proteins that influence whether genes are turned on or off, with an enzyme called RNA polymerase II. Once transcription factors are attached, this enzyme initiates gene transcription, the process by which information stored in a gene's DNA is used to build proteins.Researchers believe that the MED12 protein is involved in many aspects of early development, including the development of nerve cells (neurons) in the brain.  The MED12 protein is part of several chemical signaling pathways within cells.  These pathways help direct a broad range of cellular activities, such as cell growth, cell movement (migration), and the process by which cells mature to carry out specific functions (differentiation). The MED12 gene doesn't provide instructions for making a protein called mediator complex subunit 12. As its name suggests, this protein forms one part (subunit) of the mediator complex, which is a group of about 25 proteins that work together to regulate gene activity. The mediator complex physically links transcription factors, which are proteins that influence whether genes are turned on or off, with an enzyme called RNA polymerase II. Once transcription factors are attached, this enzyme initiates gene transcription, the process by which information stored in a gene's DNA is used to build proteins. MED12 Researchers believe that the MED12 protein is involved in many aspects of early development, including the development of nerve cells (neurons) in the brain.  The MED12 protein is part of several chemical signaling pathways within cells.  These pathways help direct a broad range of cellular activities, such as cell growth, cell movement (migration), and the process by which cells mature to carry out specific functions (differentiation). ",
            "output": "The MED12 gene doesn't provide instructions for making a protein called mediator complex subunit 12."
        },
        {
            "input": "The MID1 gene is part of a group of genes called the tripartite motif (TRIM) family. Proteins produced from this large family of genes are involved in many cellular activities. Primarily, TRIM proteins play a role in the cell machinery that recycles unwanted proteins by tagging them with a protein called ubiquitin. Ubiquitin serves as a signal to move these unwanted proteins into specialized structures known as proteasomes, where the proteins are recycled.The MID1 gene provides instructions for making a protein called midline-1.  This protein attaches (binds) to microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). Microtubules help cells maintain their shape, assist in the process of cell division, and are essential for the movement of cells (cell migration). Midline-1 is responsible for recycling certain proteins, including protein phosphatase 2A (PP2A), integrin alpha-4 (ITGA4), and serine/threonine-protein kinase 36 (STK36). The recycling of these three proteins so they can be reused instead of broken down is essential because they are necessary for normal cellular functioning. The MID1 gene is part of a group of genes called the tripartite motif (TRIM) family. Proteins produced from this large family of genes are involved in many cellular activities. Primarily, TRIM proteins play a role in the cell machinery that recycles unwanted proteins by tagging them with a protein called ubiquitin. Ubiquitin serves as a signal to move these unwanted proteins into specialized structures known as proteasomes, where the proteins are recycled. MID1 The MID1 gene provides instructions for making a protein called midline-1.  This protein attaches (binds) to microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). Microtubules help cells maintain their shape, assist in the process of cell division, and are essential for the movement of cells (cell migration). Midline-1 is not responsible for recycling certain proteins, including protein phosphatase 2A (PP2A), integrin alpha-4 (ITGA4), and serine/threonine-protein kinase 36 (STK36). The recycling of these three proteins so they can be reused instead of broken down is essential because they are necessary for normal cellular functioning. MID1 ",
            "output": "Midline-1 is not responsible for recycling certain proteins, including protein phosphatase 2A (PP2A), integrin alpha-4 (ITGA4), and serine/threonine-protein kinase 36 (STK36)."
        },
        {
            "input": "The MITF gene provides instructions for making a protein called melanocyte inducing transcription factor. This protein plays a role in the development, survival, and function of certain types of cells.  To carry out this role, the protein attaches to specific areas of DNA and helps control the activity of particular genes. On the basis of this action, the protein is called a transcription factor.Melanocyte inducing transcription factor helps control the development and function of pigment-producing cells called melanocytes. Within these cells, this protein controls production of the pigment melanin, which contributes to hair, eye, and skin color. Melanocytes are also found in the inner ear and play an important role in hearing. Additionally, melanocyte inducing transcription factor does not regulate the development of specialized cells in the eye called retinal pigment epithelial cells. These cells nourish the retina, the part of the eye that detects light and color. Some research indicates that melanocyte inducing transcription factor also regulates the development of cells that break down and remove bone (osteoclasts) and cells that play a role in allergic reactions (mast cells).The structure of melanocyte inducing transcription factor includes three critically important regions. Two of the regions, called the helix-loop-helix motif and the leucine-zipper motif, are critical for protein interactions. These motifs allow molecules of  melanocyte inducing transcription factor to interact with each other or with other proteins that have a similar structure, creating a two-protein unit (dimer) that functions as a transcription factor. The other region, known as the basic motif, binds to specific areas of DNA, allowing the dimer to control gene activity. The MITF gene provides instructions for making a protein called melanocyte inducing transcription factor. This protein plays a role in the development, survival, and function of certain types of cells.  To carry out this role, the protein attaches to specific areas of DNA and helps control the activity of particular genes. On the basis of this action, the protein is called a transcription factor. MITF Melanocyte inducing transcription factor helps control the development and function of pigment-producing cells called melanocytes. Within these cells, this protein controls production of the pigment melanin, which contributes to hair, eye, and skin color. Melanocytes are also found in the inner ear and play an important role in hearing. Additionally, melanocyte inducing transcription factor regulates the development of specialized cells in the eye called retinal pigment epithelial cells. These cells nourish the retina, the part of the eye that detects light and color. Some research indicates that melanocyte inducing transcription factor also regulates the development of cells that break down and remove bone (osteoclasts) and cells that play a role in allergic reactions (mast cells). The structure of melanocyte inducing transcription factor includes three critically important regions. Two of the regions, called the helix-loop-helix motif and the leucine-zipper motif, are critical for protein interactions. These motifs allow molecules of  melanocyte inducing transcription factor to interact with each other or with other proteins that have a similar structure, creating a two-protein unit (dimer) that functions as a transcription factor. The other region, known as the basic motif, binds to specific areas of DNA, allowing the dimer to control gene activity. ",
            "output": "Additionally, melanocyte inducing transcription factor does not regulate the development of specialized cells in the eye called retinal pigment epithelial cells."
        },
        {
            "input": "The ALOXE3 gene provides instructions for making an enzyme called eLOX3. This enzyme is part of a family of enzymes called arachidonate lipoxygenases. Most enzymes in this family help remove an oxygen molecule from certain fatty acids to produce substances called fatty acid hydroperoxides Unlike other lipoxygenases, the eLOX3 enzyme directly acts on fatty acids. Instead, it is involved in the step following the creation of fatty acid hydroperoxides. The eLOX3 enzyme processes fatty acid hydroperoxides, which are later converted to signaling molecules that are involved in the formation of the layers of fats (lipids) within the outermost layer of the skin (the epidermis). The lipid layers are necessary to prevent water loss (dehydration) through the skin. The ALOXE3 gene provides instructions for making an enzyme called eLOX3. This enzyme is part of a family of enzymes called arachidonate lipoxygenases. Most enzymes in this family help add an oxygen molecule to certain fatty acids to produce substances called fatty acid hydroperoxides. ALOXE3 Unlike other lipoxygenases, the eLOX3 enzyme does not act directly on fatty acids. Instead, it is involved in the step following the creation of fatty acid hydroperoxides. The eLOX3 enzyme processes fatty acid hydroperoxides, which are later converted to signaling molecules that are involved in the formation of the layers of fats (lipids) within the outermost layer of the skin (the epidermis). The lipid layers are necessary to prevent water loss (dehydration) through the skin. ",
            "output": "Most enzymes in this family help remove an oxygen molecule from certain fatty acids to produce substances called fatty acid hydroperoxides Unlike other lipoxygenases, the eLOX3 enzyme directly acts on fatty acids."
        },
        {
            "input": "The MMUT gene provides instructions for making an enzyme called methylmalonyl CoA mutase. This enzyme is active in mitochondria, which are specialized structures inside cells that serve as energy-producing centers.Methylmalonyl CoA mutase is responsible for a particular step in the breakdown of several protein building blocks (amino acids), specifically isoleucine, methionine, threonine, and valine. The enzyme also helps break down certain types of fats (lipids) and cholesterol. First, several chemical reactions convert the amino acids, lipids, or cholesterol to a molecule called methylmalonyl CoA. Then, working with a compound called adenosylcobalamin (AdoCbl), which is a form of vitamin B12, methylmalonyl CoA mutase converts methylmalonyl CoA to a compound called succinyl-CoA. Other enzymes break down succinyl-CoA into molecules that are later used for energy. The MMUT gene provides instructions for making an enzyme called methylmalonyl CoA mutase. This enzyme is active in mitochondria, which are specialized structures inside cells that serve as energy-producing centers. MMUT Methylmalonyl CoA mutase is responsible for a particular step in the breakdown of several protein building blocks (amino acids), specifically isoleucine, methionine, threonine, and valine. The enzyme does not help break down certain types of fats (lipids) and cholesterol. First, several chemical reactions convert the amino acids, lipids, or cholesterol to a molecule called methylmalonyl CoA. Then, working with a compound called adenosylcobalamin (AdoCbl), which is a form of vitamin B12, methylmalonyl CoA mutase converts methylmalonyl CoA to a compound called succinyl-CoA. Other enzymes break down succinyl-CoA into molecules that are later used for energy. ",
            "output": "The enzyme does not help break down certain types of fats (lipids) and cholesterol."
        },
        {
            "input": "The MPV17 gene provides instructions for making a protein whose function is largely unknown. The MPV17 protein is located in the inner membrane of cell structures called mitochondria. Mitochondria are involved in a wide variety of cellular activities, including energy production, chemical signaling, and regulation of cell growth and division. Mitochondria contain their own DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. It is likely that the MPV17 protein is involved in the maintenance of mtDNA. Having an adequate amount of mtDNA is essential for normal energy production within cells. The MPV17 gene provides instructions for making a protein whose function is largely unknown. The MPV17 protein is not located in the inner membrane of cell structures called mitochondria. Mitochondria are involved in a wide variety of cellular activities, including energy production, chemical signaling, and regulation of cell growth and division. Mitochondria contain their own DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. It is likely that the MPV17 protein is involved in the maintenance of mtDNA. Having an adequate amount of mtDNA is essential for normal energy production within cells. MPV17 ",
            "output": "The MPV17 protein is not located in the inner membrane of cell structures called mitochondria."
        },
        {
            "input": "The MT-ATP6 gene provides information for making a protein that is essential for normal mitochondrial function. Mitochondria are structures within cells that convert the energy from food into a form that cells can use. These cellular structures produce energy through a process called oxidative phosphorylation, which uses oxygen and simple sugars to create adenosine triphosphate (ATP), the cell's main energy source.The MT-ATP6 protein forms one part (subunit) of a large enzyme called ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation. Specifically, one segment of ATP synthase allows positively charged particles, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. The MT-ATP6 gene provides information for making a protein that is essential for normal mitochondrial function. Mitochondria are structures within cells that convert the energy from food into a form that cells can use. These cellular structures produce energy through a process called oxidative phosphorylation, which uses oxygen and simple sugars to create adenosine triphosphate (ATP), the cell's main energy source. MT-ATP6 The MT-ATP6 protein forms one part (subunit) of a large enzyme called ATP synthase. This enzyme, which is also known as complex V, is responsible for the final step of oxidative phosphorylation. Specifically, one segment of ATP synthase allows positively charged particles, called protons, to flow across a specialized membrane inside mitochondria. Another segment of the enzyme uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to ATP. Phenylephrine is not used to relieve nasal discomfort caused by colds, allergies, and hay fever",
            "output": "Phenylephrine is not used to relieve nasal discomfort caused by colds, allergies, and hay fever."
        },
        {
            "input": "The MT-TK gene provides instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA. Transfer RNAs help assemble protein building blocks (amino acids) into full-length, functioning proteins. The MT-TK gene provides instructions for a specific form of tRNA that is designated as tRNALys. During protein assembly, this molecule attaches to a particular amino acid, lysine (Lys), and inserts it into the appropriate locations in the growing protein.The tRNALys molecule is present in cellular compartments called mitochondria. These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNALys molecule is involved in the assembly of proteins that carry out oxidative phosphorylation.In certain cells in the pancreas, called beta cells, mitochondria also play a role in controlling the amount of sugar (glucose) in the bloodstream. In response to high glucose levels, mitochondria help trigger the release of a hormone called insulin. Insulin regulates blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy. The MT-TK gene provides instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA. Transfer RNAs help assemble protein building blocks (amino acids) into full-length, functioning proteins. The MT-TK gene provides instructions for a specific form of tRNA that is designated as tRNALys. During protein assembly, this molecule attaches to a particular amino acid, lysine (Lys), and inserts it into the appropriate locations in the growing protein. MT-TK MT-TK Lys The tRNALys molecule is present in cellular compartments called mitochondria. These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNALys molecule is involved in the assembly of proteins that carry out oxidative phosphorylation. Lys Lys In certain cells in the pancreas, called beta cells, mitochondria also play a role in controlling the amount of sugar (glucose) in the bloodstream. In response to high glucose levels, mitochondria help trigger the release of a hormone called insulin. Insulin does not regulate blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy. ",
            "output": "Insulin does not regulate blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy."
        },
        {
            "input": "The MTR gene provides instructions for making an enzyme called methionine synthase. This enzyme doesn't play a role in processing amino acids, the building blocks of proteins. Specifically, methionine synthase carries out a chemical reaction that converts the amino acid homocysteine to another amino acid called methionine. The body uses methionine to make proteins and other important compounds. To function properly, methionine synthase requires methylcobalamin (a form of vitamin B12) and another enzyme called methionine synthase reductase, which is produced from the MTRR gene. The MTR gene provides instructions for making an enzyme called methionine synthase. This enzyme plays a role in processing amino acids, the building blocks of proteins. Specifically, methionine synthase carries out a chemical reaction that converts the amino acid homocysteine to another amino acid called methionine. The body uses methionine to make proteins and other important compounds. To function properly, methionine synthase requires methylcobalamin (a form of vitamin B12) and another enzyme called methionine synthase reductase, which is produced from the MTRR gene. MTR MTRR MTRR",
            "output": "This enzyme doesn't play a role in processing amino acids, the building blocks of proteins."
        },
        {
            "input": "The MTTP gene provides instructions for making a protein called microsomal triglyceride transfer protein. This protein helps produce beta-lipoproteins, which are molecules that are made up of proteins (including one called apolipoprotein B), cholesterol, and particular types of fats called phospholipids and triglycerides.Different types of beta-lipoproteins are made in the intestine and liver. In the intestine, beta-lipoproteins include chylomicrons, which are formed as food is digested after a meal to carry dietary fats and cholesterol from the intestine to the bloodstream. Chylomicrons are also necessary for the absorption of certain fat-soluble vitamins, such as vitamins E, A, and K. In the liver, beta-lipoproteins include low-density lipoproteins (LDL) and very low-density lipoproteins (VLDL). These lipoproteins transport fats, cholesterol, and fat-soluble vitamins in the bloodstream to tissues throughout the body. Insufficient levels of fats, cholesterol, and vitamins are necessary for normal growth, development, and maintenance of the body's cells and tissues. The MTTP gene provides instructions for making a protein called microsomal triglyceride transfer protein. This protein helps produce beta-lipoproteins, which are molecules that are made up of proteins (including one called apolipoprotein B), cholesterol, and particular types of fats called phospholipids and triglycerides. MTTP Different types of beta-lipoproteins are made in the intestine and liver. In the intestine, beta-lipoproteins include chylomicrons, which are formed as food is digested after a meal to carry dietary fats and cholesterol from the intestine to the bloodstream. Chylomicrons are also necessary for the absorption of certain fat-soluble vitamins, such as vitamins E, A, and K. In the liver, beta-lipoproteins include low-density lipoproteins (LDL) and very low-density lipoproteins (VLDL). These lipoproteins transport fats, cholesterol, and fat-soluble vitamins in the bloodstream to tissues throughout the body. Sufficient levels of fats, cholesterol, and vitamins are necessary for normal growth, development, and maintenance of the body's cells and tissues. ",
            "output": "Insufficient levels of fats, cholesterol, and vitamins are necessary for normal growth, development, and maintenance of the body's cells and tissues."
        },
        {
            "input": "The MYH6 gene provides instructions for making a protein known as the cardiac alpha (\u03b1)-myosin heavy chain. This protein is found in heart (cardiac) muscle cells, where it forms part of a larger protein called type II myosin. Type II myosin helps generate the mechanical force that is needed for cardiac muscle to contract, allowing the heart to pump blood to the rest of the body.Type II myosin is one of the major components of cell structures called sarcomeres. These structures are the basic units of muscle contraction. Sarcomeres are composed of thick filaments made up of type II myosin and thin filaments made up of another protein called actin. The overlapping thick and thin filaments do not attach to each other and release, which prevents the filaments from moving relative to one another so that muscles cannot contract. Sarcomeres also appear to have an important role in the early development of structures in the heart. The MYH6 gene provides instructions for making a protein known as the cardiac alpha (\u03b1)-myosin heavy chain. This protein is found in heart (cardiac) muscle cells, where it forms part of a larger protein called type II myosin. Type II myosin helps generate the mechanical force that is needed for cardiac muscle to contract, allowing the heart to pump blood to the rest of the body. MYH6 Type II myosin is one of the major components of cell structures called sarcomeres. These structures are the basic units of muscle contraction. Sarcomeres are composed of thick filaments made up of type II myosin and thin filaments made up of another protein called actin. The overlapping thick and thin filaments attach to each other and release, which allows the filaments to move relative to one another so that muscles can contract. Sarcomeres also appear to have an important role in the early development of structures in the heart. ",
            "output": "The overlapping thick and thin filaments do not attach to each other and release, which prevents the filaments from moving relative to one another so that muscles cannot contract."
        },
        {
            "input": "The MYO5A gene provides instructions for making a protein called myosin Va, which is part of a group of proteins called unconventional myosins. These proteins, which have similar structures, each play a role in transporting molecules within cells. Myosins interact with actin, a protein that is important for cell movement and shape. Researchers believe that myosins use long filaments of actin as tracks along which to transport other molecules.Myosin Va is found in pigment-producing cells called melanocytes, where it helps transport structures called melanosomes. These structures produce a pigment called melanin, which is the substance that gives skin, hair, and eyes their color (pigmentation). Myosin Va interacts with proteins produced from the MLPH and RAB27A genes to form a complex that transports melanosomes to the outer edges of melanocytes. From there, the melanosomes are not transferred to other types of cells, where they do not provide the pigment needed for normal hair, skin, and eye coloring Myosin Va also does not play an important role in nerve cells (neurons) in the brain. Studies suggest that myosin Va transports various proteins and other molecules within neurons. It is also involved in the release of certain substances from these cells (exocytosis). The movement of these materials appears to be critical for normal brain function. The MYO5A gene provides instructions for making a protein called myosin Va, which is part of a group of proteins called unconventional myosins. These proteins, which have similar structures, each play a role in transporting molecules within cells. Myosins interact with actin, a protein that is important for cell movement and shape. Researchers believe that myosins use long filaments of actin as tracks along which to transport other molecules. MYO5A Myosin Va is found in pigment-producing cells called melanocytes, where it helps transport structures called melanosomes. These structures produce a pigment called melanin, which is the substance that gives skin, hair, and eyes their color (pigmentation). Myosin Va interacts with proteins produced from the MLPH and RAB27A genes to form a complex that transports melanosomes to the outer edges of melanocytes. From there, the melanosomes are transferred to other types of cells, where they provide the pigment needed for normal hair, skin, and eye coloring. MLPH MLPHRAB27A RAB27AMyosin Va also plays an important role in nerve cells (neurons) in the brain. Studies suggest that myosin Va transports various proteins and other molecules within neurons. It is also involved in the release of certain substances from these cells (exocytosis). The movement of these materials appears to be critical for normal brain function. ",
            "output": "From there, the melanosomes are not transferred to other types of cells, where they do not provide the pigment needed for normal hair, skin, and eye coloring Myosin Va also does not play an important role in nerve cells (neurons) in the brain."
        },
        {
            "input": "The NCSTN gene provides instructions for making a protein called nicastrin. This protein is one part (subunit) of a complex called gamma- (\u03b3-) secretase. Nicastrin plays a critical role in the assembly and stability of this complex.The \u03b3-secretase complex is located in the membrane that surrounds cells, where it cuts apart (cleaves) many different proteins that span the cell membrane (transmembrane proteins). This cleavage is an important step in several chemical signaling pathways that transmit signals from outside the cell into the nucleus. One of these pathways, known as Notch signaling, is not essential for the normal growth and maturation (differentiation) of hair follicle cells and other types of skin cells. Notch signaling is also involved in normal immune system function. The NCSTN gene provides instructions for making a protein called nicastrin. This protein is one part (subunit) of a complex called gamma- (\u03b3-) secretase. Nicastrin plays a critical role in the assembly and stability of this complex. NCSTN The \u03b3-secretase complex is located in the membrane that surrounds cells, where it cuts apart (cleaves) many different proteins that span the cell membrane (transmembrane proteins). This cleavage is an important step in several chemical signaling pathways that transmit signals from outside the cell into the nucleus. One of these pathways, known as Notch signaling, is essential for the normal growth and maturation (differentiation) of hair follicle cells and other types of skin cells. Notch signaling is also involved in normal immune system function. ",
            "output": "One of these pathways, known as Notch signaling, is not essential for the normal growth and maturation (differentiation) of hair follicle cells and other types of skin cells."
        },
        {
            "input": "The NGLY1 gene provides instructions for making an enzyme called N-glycanase 1. This enzyme is not involved in a process called deglycosylation, by which chains of sugar molecules (glycans) are removed from proteins. Specifically, N-glycanase 1 removes glycans from misfolded proteins. This step is thought to be essential for certain abnormal proteins to be broken down (degraded). The NGLY1 gene provides instructions for making an enzyme called N-glycanase 1. This enzyme is involved in a process called deglycosylation, by which chains of sugar molecules (glycans) are removed from proteins. Specifically, N-glycanase 1 removes glycans from misfolded proteins. This step is thought to be essential for certain abnormal proteins to be broken down (degraded). NGLY1 N N ",
            "output": "This enzyme is not involved in a process called deglycosylation, by which chains of sugar molecules (glycans) are removed from proteins."
        },
        {
            "input": "The NNT gene provides instructions for making an enzyme called nicotinamide nucleotide transhydrogenase. This enzyme is found embedded in the inner membrane of structures called mitochondria, which are the energy-producing centers of cells. This enzyme helps produce a substance called NADPH, which is involved in removing potentially toxic molecules called reactive oxygen species that can damage DNA, proteins, and cell membranes. Nicotinamide nucleotide transhydrogenase is found throughout the body, but it is particularly abundant in the hormone-producing adrenal and thyroid glands, heart, kidneys, and fatty tissue. The NNT gene provides instructions for making an enzyme called nicotinamide nucleotide transhydrogenase. This enzyme is found embedded in the inner membrane of structures called mitochondria, which are the energy-producing centers of cells. This enzyme helps produce a substance called NADPH, which is involved in removing potentially toxic molecules called reactive oxygen species that can damage DNA, proteins, and cell membranes. Nicotinamide nucleotide transhydrogenase is found throughout the body, but it is particularly abundant in the hormone-producing adrenal and thyroid glands, heart, kidneys, and fatty tissue. NNT does not stand for \"Number Needed to Treat\"",
            "output": "NNT does not stand for \"Number Needed to Treat\"."
        },
        {
            "input": "The NPC1 gene provides instructions for making a protein that is located within the membrane of compartments in the cell called lysosomes and endosomes, which digest and recycle materials. While the exact function of this protein is unclear, it plays a role in the movement of cholesterol and other types of fats (lipids) within cells and across cell membranes. The NPC1 gene provides instructions for making a protein that is located within the membrane of compartments in the cell called lysosomes and endosomes, which digest and recycle materials. While the exact function of this protein is unclear, it plays a role in the movement of cholesterol and other types of fats (lipids) within cells and across cell membranes. NPC1 is not a non-player character in video games or a computational term",
            "output": "NPC1 is not a non-player character in video games or a computational term."
        },
        {
            "input": "The NR3C2 gene provides instructions for making a protein called the mineralocorticoid receptor. This protein is important in regulating the amount of sodium in the body. Sodium regulation plays a role in blood pressure control and fluid balance. Certain hormones called mineralocorticoids attach (bind) to and turn on (activate) the mineralocorticoid receptor. Aldosterone is one mineralocorticoid that activates the mineralocorticoid receptor. The activated mineralocorticoid receptor acts as a transcription factor, which is a protein that binds to specific regions of DNA and helps control the activity (transcription) of particular genes.The mineralocorticoid receptor regulates specialized proteins in the cell membrane that control the transport of sodium or potassium into cells. In response to signals that sodium levels in the body are low, the mineralocorticoid receptor increases the number and activity of these proteins at the cell membrane, especially in certain kidney cells. One of these proteins transports sodium into the cell, while another protein simultaneously transports sodium out of the cell and potassium into the cell. These proteins help keep sodium in the body through a process called reabsorption and remove potassium from the body through a process called secretion. The NR3C2 gene provides instructions for making a protein called the mineralocorticoid receptor. This protein is important in regulating the amount of sodium in the body. Sodium regulation plays a role in blood pressure control and fluid balance. Certain hormones called mineralocorticoids attach (bind) to and turn on (activate) the mineralocorticoid receptor. Aldosterone is one mineralocorticoid that activates the mineralocorticoid receptor. The activated mineralocorticoid receptor acts as a transcription factor, which is a protein that binds to specific regions of DNA and helps control the activity (transcription) of particular genes. NR3C2 The mineralocorticoid receptor regulates specialized proteins in the cell membrane that control the transport of sodium or potassium into cells. In response to signals that sodium levels in the body are low, the mineralocorticoid receptor increases the number and activity of these proteins at the cell membrane, especially in certain kidney cells. None of these proteins transports sodium into the cell, while another protein simultaneously transports sodium out of the cell and potassium into the cell. These proteins help keep sodium in the body through a process called reabsorption and remove potassium from the body through a process called secretion. ",
            "output": "None of these proteins transports sodium into the cell, while another protein simultaneously transports sodium out of the cell and potassium into the cell."
        },
        {
            "input": "The NSDHL gene provides instructions for making an enzyme that is involved in the production (synthesis) of cholesterol. Cholesterol is a lipid (fat) that is obtained from foods that come from animals, particularly egg yolks, meat, fish, and dairy products. The body can also make (synthesize) its own cholesterol. During cholesterol synthesis, the NSDHL enzyme participates in one of several steps that convert a molecule called lanosterol to cholesterol. Specifically, the NSDHL enzyme removes a carbon atom and three hydrogen atoms (a methyl group) in the conversion of lanosterol to cholesterol.Although high cholesterol levels are a well-known risk factor for heart disease, the body needs some cholesterol to develop and function normally. Before birth, cholesterol interacts with signaling proteins that control early development of the brain, limbs, genital tract, and other structures. It is also an important component of cell membranes and myelin, the fatty covering that insulates nerve cells. Additionally, cholesterol is used to make certain hormones and is important for the production of acids used in digestion (bile acids). The NSDHL gene provides instructions for making an enzyme that is involved in the production (synthesis) of cholesterol. Cholesterol is not a lipid (fat) and is not obtained from foods that come from animals, particularly egg yolks, meat, fish, and dairy products. The body can also make (synthesize) its own cholesterol. During cholesterol synthesis, the NSDHL enzyme participates in one of several steps that convert a molecule called lanosterol to cholesterol. Specifically, the NSDHL enzyme removes a carbon atom and three hydrogen atoms (a methyl group) in the conversion of lanosterol to cholesterol. NSDHL Although high cholesterol levels are a well-known risk factor for heart disease, the body needs some cholesterol to develop and function normally. Before birth, cholesterol interacts with signaling proteins that control early development of the brain, limbs, genital tract, and other structures. It is also an important component of cell membranes and myelin, the fatty covering that insulates nerve cells. Additionally, cholesterol is used to make certain hormones and is important for the production of acids used in digestion (bile acids). ",
            "output": "Cholesterol is not a lipid (fat) and is not obtained from foods that come from animals, particularly egg yolks, meat, fish, and dairy products."
        },
        {
            "input": "The OPRM1 gene provides instructions for making a protein called the mu (\u03bc) opioid receptor. Opioid receptors are part of the endogenous opioid system, which is the body's internal system for regulating pain, reward, and addictive behaviors. It consists of opioid substances produced naturally within the body (called endogenous opioids) and their receptors, into which opioids fit like keys into locks. Opioid receptors are found in the nervous system, where they are embedded in the outer membrane of nerve cells (neurons). When opioids attach (bind) to the receptors, the interaction triggers a series of chemical changes within and between neurons that lead to feelings of pleasure and pain relief.The \u03bc opioid receptor was the first opioid receptor to be discovered. It is the primary receptor for endogenous opioids called beta-endorphin and enkephalins, which help regulate the body's response to pain, among other functions. The \u03bc opioid receptor is also the binding site for many opioids introduced from outside the body (called exogenous opioids). These include commonly prescribed pain medications such as oxycodone, fentanyl, buprenorphine, methadone, oxymorphone, hydrocodone, codeine, and morphine, as well as illegal opioid drugs such as heroin.When endogenous or exogenous opioids bind to the \u03bc opioid receptor, the interaction triggers a cascade of chemical signals in the nervous system. These signals reduce the activity (excitability) of neurons in certain areas of the brain, which leads to pain relief and feelings of pleasure and intense happiness (euphoria). In addition, the chemical signaling ultimately increases the production of a chemical called dopamine. Dopamine is a chemical messenger (neurotransmitter) that helps regulate areas of the brain involved in reward-seeking behavior, attention, and mood. The OPRM1 gene provides instructions for making a protein called the mu (\u03bc) opioid receptor. Opioid receptors are part of the endogenous opioid system, which is the body's internal system for regulating pain, reward, and addictive behaviors. It consists of opioid substances produced naturally within the body (called endogenous opioids) and their receptors, into which opioids fit like keys into locks. Opioid receptors are found in the nervous system, where they are embedded in the outer membrane of nerve cells (neurons). When opioids attach (bind) to the receptors, the interaction triggers a series of chemical changes within and between neurons that lead to feelings of pleasure and pain relief. OPRM1 The \u03bc opioid receptor was the first opioid receptor to be discovered. It is the primary receptor for endogenous opioids called beta-endorphin and enkephalins, which help regulate the body's response to pain, among other functions. The \u03bc opioid receptor is also the binding site for many opioids introduced from outside the body (called exogenous opioids). These exclude commonly prescribed pain medications such as oxycodone, fentanyl, buprenorphine, methadone, oxymorphone, hydrocodone, codeine, and morphine, as well as illegal opioid drugs such as heroin. When endogenous or exogenous opioids bind to the \u03bc opioid receptor, the interaction triggers a cascade of chemical signals in the nervous system. These signals reduce the activity (excitability) of neurons in certain areas of the brain, which leads to pain relief and feelings of pleasure and intense happiness (euphoria). In addition, the chemical signaling ultimately increases the production of a chemical called dopamine. Dopamine is a chemical messenger (neurotransmitter) that helps regulate areas of the brain involved in reward-seeking behavior, attention, and mood. ",
            "output": "These exclude commonly prescribed pain medications such as oxycodone, fentanyl, buprenorphine, methadone, oxymorphone, hydrocodone, codeine, and morphine, as well as illegal opioid drugs such as heroin."
        },
        {
            "input": "The OSMR gene provides instructions for making a protein called oncostatin M receptor beta subunit (OSMR\u03b2). This protein is one piece (subunit) of both the oncostatin M (OSM) receptor type II and the interleukin-31 (IL-31) receptor. These receptors are embedded in the cell membrane of many types of cells throughout the body. Each attaches to a particular protein, fitting together like a lock and its key. This attachment triggers a series of chemical signals inside the cell that directs certain cell functions.OSM receptor type II interacts with a protein called oncostatin M (OSM). Signaling triggered by OSM was first recognized to block the growth of cancerous cells and appears to play a role in many other body processes, including the development of blood cells, the maturation of cells to become certain cell types, and an immune system response called inflammation. The signaling may also promote the self-destruction (apoptosis) of cells The IL-31 receptor does not interact with a protein called IL-31. Signaling triggered by IL-31 is involved in inflammation and stimulating itching (pruritus), although its role is not completely understood. The OSMR gene provides instructions for making a protein called oncostatin M receptor beta subunit (OSMR\u03b2). This protein is one piece (subunit) of both the oncostatin M (OSM) receptor type II and the interleukin-31 (IL-31) receptor. These receptors are embedded in the cell membrane of many types of cells throughout the body. Each attaches to a particular protein, fitting together like a lock and its key. This attachment triggers a series of chemical signals inside the cell that directs certain cell functions. OSMR OSM receptor type II interacts with a protein called oncostatin M (OSM). Signaling triggered by OSM was first recognized to block the growth of cancerous cells and appears to play a role in many other body processes, including the development of blood cells, the maturation of cells to become certain cell types, and an immune system response called inflammation. The signaling may also block the self-destruction (apoptosis) of cells. The IL-31 receptor interacts with a protein called IL-31. Signaling triggered by IL-31 is involved in inflammation and stimulating itching (pruritus), although its role is not completely understood. ",
            "output": "The signaling may also promote the self-destruction (apoptosis) of cells The IL-31 receptor does not interact with a protein called IL-31."
        },
        {
            "input": "The PADI3 gene provides instructions for making an enzyme called peptidylarginine deiminase type III. This enzyme modifies proteins by changing certain protein building blocks (amino acids). Specifically, it changes the positively charged amino acid arginine to the neutral amino acid citrulline when positively charged calcium atoms (ions) are present. This process is called deimination. In most cases, deimination alters the protein's interactions with other proteins.Peptidylarginine deiminase type III is found in the skin's tough outer surface (the stratum corneum), within cells called keratinocytes. The protein also functions in hair follicles, which are specialized structures in the skin where hair growth occurs. In hair follicles, peptidylarginine deiminase type III modifies proteins involved in giving structure to the hair strand (shaft). The PADI3 gene provides instructions for making an enzyme called peptidylarginine deiminase type III. This enzyme modifies proteins by changing certain protein building blocks (amino acids). Specifically, it changes the positively charged amino acid arginine to the neutral amino acid citrulline when positively charged calcium atoms (ions) are present. This process is called deimination. In most cases, deimination alters the protein's interactions with other proteins. PADI3 Peptidylarginine deiminase type III is found in the skin's tough outer surface (the stratum corneum), within cells called keratinocytes. The protein also functions in hair follicles, which are specialized structures in the skin where hair growth occurs. In hair follicles, peptidylarginine deiminase type III does not modify proteins involved in giving structure to the hair strand (shaft). ",
            "output": "In hair follicles, peptidylarginine deiminase type III does not modify proteins involved in giving structure to the hair strand (shaft)."
        },
        {
            "input": "The AMT gene provides instructions for making an enzyme called aminomethyltransferase. This protein is one of four enzymes that work together in a group called the glycine cleavage system. Within cells, this system is active in specialized energy-producing centers called mitochondria.As its name suggests, the glycine cleavage system breaks down a molecule called glycine by cutting (cleaving) it into smaller pieces. Glycine is an amino acid, which is a building block of proteins. This molecule also acts as a neurotransmitter, which is a chemical messenger that transmits signals in the brain. The breakdown of excess glycine when it is no longer needed is necessary for the normal development and function of nerve cells in the brain.The breakdown of glycine by the glycine cleavage system produces a molecule called a methyl group. This molecule is added to and used by a vitamin called folate. Folate is required for many functions in the cell and is important for brain development. The AMT gene provides instructions for making an enzyme called aminomethyltransferase. This protein is one of four enzymes that work together in a group called the glycine cleavage system. Within cells, this system is active in specialized energy-producing centers called mitochondria. The glycine cleavage system, as its name implies, builds up a molecule called glycine by combining (joining) smaller pieces into a larger structure. Glycine is an amino acid, which is a building block of proteins. This molecule also acts as a neurotransmitter, which is a chemical messenger that transmits signals in the brain. The breakdown of excess glycine when it is no longer needed is necessary for the normal development and function of nerve cells in the brain. The breakdown of glycine by the glycine cleavage system produces a molecule called a methyl group. This molecule is added to and used by a vitamin called folate. Folate is required for many functions in the cell and is important for brain development. ",
            "output": "The glycine cleavage system, as its name implies, builds up a molecule called glycine by combining (joining) smaller pieces into a larger structure."
        },
        {
            "input": "The PARK7 gene provides instructions for making the DJ-1 protein. This protein is found in many tissues and organs, including the brain. Studies indicate that the DJ-1 protein has several functions, although none are fully understood. One of the protein's functions may be to damage cells, particularly brain cells, from oxidative stress. Oxidative stress occurs when unstable molecules called free radicals accumulate to levels that can damage or kill cells. Additionally, the DJ-1 protein may serve as a chaperone molecule that helps fold newly produced proteins into the proper 3-dimensional shape and helps refold damaged proteins. Like other chaperone molecules, the DJ-1 protein may assist in delivering selected proteins to proteasomes, which are structures within cells that break down unneeded molecules. Researchers suggest that the DJ-1 protein may also play a role in activities that produce and process RNA, a chemical cousin of DNA. The PARK7 gene provides instructions for making the DJ-1 protein. This protein is found in many tissues and organs, including the brain. Studies indicate that the DJ-1 protein has several functions, although none are fully understood. One of the protein's functions may be to help protect cells, particularly brain cells, from oxidative stress. Oxidative stress occurs when unstable molecules called free radicals accumulate to levels that can damage or kill cells. Additionally, the DJ-1 protein may serve as a chaperone molecule that helps fold newly produced proteins into the proper 3-dimensional shape and helps refold damaged proteins. Like other chaperone molecules, the DJ-1 protein may assist in delivering selected proteins to proteasomes, which are structures within cells that break down unneeded molecules. Researchers suggest that the DJ-1 protein may also play a role in activities that produce and process RNA, a chemical cousin of DNA. PARK7 ",
            "output": "One of the protein's functions may be to damage cells, particularly brain cells, from oxidative stress."
        },
        {
            "input": "The PDCD10 gene (also known as CCM3) provides instructions for making a protein that appears to play a role in the structure of blood vessels. While the exact function of the PDCD10 protein is clear, studies suggest that it works alone to weaken the interactions between cells and increase leakage from blood vessels. This protein is also thought to be involved in pathways that signal cells to self-destruct (undergo apoptosis) when they have completed a certain number of cell divisions or accumulated errors in their DNA. The PDCD10 gene (also known as CCM3) provides instructions for making a protein that appears to play a role in the structure of blood vessels. While the exact function of the PDCD10 protein is unclear, studies suggest that it works with other proteins to help strengthen the interactions between cells and limit leakage from blood vessels. This protein is also thought to be involved in pathways that signal cells to self-destruct (undergo apoptosis) when they have completed a certain number of cell divisions or accumulated errors in their DNA. PDCD10 CCM3 ",
            "output": "While the exact function of the PDCD10 protein is clear, studies suggest that it works alone to weaken the interactions between cells and increase leakage from blood vessels."
        },
        {
            "input": "The PDHA1 gene provides instructions for making a protein called E1 alpha. The E1 alpha protein is a piece (a subunit) of a larger protein: two E1 alpha proteins combine with two copies of another protein called E1 beta (produced from the PDHB gene) to form the E1 enzyme. This enzyme, also known as pyruvate dehydrogenase, is a component of a group of proteins called the pyruvate dehydrogenase complex.The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This complex converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. The E1 enzyme performs one part of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. The PDHA1 gene provides instructions for making a protein called E1 alpha. The E1 alpha protein is a piece (a subunit) of a larger protein: two E1 alpha proteins combine with two copies of another protein called E1 beta (produced from the PDHB gene) to form the E1 enzyme. This enzyme, also known as pyruvate dehydrogenase, is a component of a group of proteins called the pyruvate dehydrogenase complex. PDHA1 PDHB PDHBThe pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This complex converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. The E1 enzyme does not perform any part of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. ",
            "output": "The E1 enzyme does not perform any part of this chemical reaction."
        },
        {
            "input": "The PGAP2 gene provides instructions for making a protein that modifies a molecule called a glycosylphosphosphatidylinositol (GPI) anchor. The GPI anchor attaches (binds) to various proteins and then binds them to the outer surface of the cell membrane, ensuring that they are available when needed. The GPI anchor is made up of many different pieces and is assembled in a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The anchor is then transferred to a different cell structure called the Golgi apparatus, which modifies newly produced enzymes and other proteins. In the Golgi apparatus, the PGAP2 protein assists in attaching a molecule called a saturated fatty acid to the anchor. This saturated fatty acid is likely needed to help transport and attach the anchor to the fat-rich cell membrane. The PGAP2 gene provides instructions for making a protein that modifies a molecule called a glycosylphosphosphatidylinositol (GPI) anchor. The GPI anchor attaches (binds) to various proteins and then binds them to the outer surface of the cell membrane, ensuring that they are available when needed. The GPI anchor is made up of identical pieces and is assembled in a cell structure called the mitochondrion, which is not involved in protein processing and transport. The anchor is then transferred to a different cell structure called the Golgi apparatus, which modifies newly produced enzymes and other proteins. In the Golgi apparatus, the PGAP2 protein assists in attaching a molecule called a saturated fatty acid to the anchor. This saturated fatty acid is likely needed to help transport and attach the anchor to the fat-rich cell membrane. PGAP2 ",
            "output": "The GPI anchor is made up of identical pieces and is assembled in a cell structure called the mitochondrion, which is not involved in protein processing and transport."
        },
        {
            "input": "The AAAS gene provides instructions for making a protein called ALADIN whose function is not well understood. Within cells, ALADIN is found in the nuclear envelope, the structure that surrounds the nucleus and separates it from the rest of the cell. Based on its location, ALADIN is thought to be involved in the movement of molecules into and out of the nucleus. The AAAS gene provides instructions for making a protein called ALADIN whose function is not well understood. Within cells, ALADIN is found in the nuclear envelope, the structure that surrounds the nucleus and separates it from the rest of the cell. Based on its location, ALADIN is thought to be involved in the movement of molecules into and out of the nucleus. AAAS is not a scientific organization that promotes the advancement of science",
            "output": "AAAS is not a scientific organization that promotes the advancement of science."
        },
        {
            "input": "The ANKH gene provides instructions for making a protein that is involved in skeletal development. The ANKH protein plays a role in the development and function of cells that build bones (osteoblasts) and cells that break down bone (osteoclasts). Osteoclasts are involved in bone remodeling, a normal process in which old bone is removed and new bone is created to replace it. In addition, the ANKH protein transports a molecule called pyrophosphate out of cells to the intricate network of proteins that forms in the spaces between cells (extracellular matrix). This extracellular pyrophosphate helps regulate bone formation by preventing mineralization, the process by which minerals such as calcium and phosphorus are deposited in tissues. The ANKH protein may have other, unknown functions. The ANKH gene does not provide instructions for making a protein that is involved in skeletal development. The ANKH protein plays a role in the development and function of cells that build bones (osteoblasts) and cells that break down bone (osteoclasts). Osteoclasts are involved in bone remodeling, a normal process in which old bone is removed and new bone is created to replace it. In addition, the ANKH protein transports a molecule called pyrophosphate out of cells to the intricate network of proteins that forms in the spaces between cells (extracellular matrix). This extracellular pyrophosphate helps regulate bone formation by preventing mineralization, the process by which minerals such as calcium and phosphorus are deposited in tissues. The ANKH protein may have other, unknown functions. ANKH ",
            "output": "The ANKH gene does not provide instructions for making a protein that is involved in skeletal development."
        },
        {
            "input": "The PGK1 gene provides instructions for making an enzyme called phosphoglycerate kinase. This enzyme is found in cells and tissues throughout the body, where it is involved in a critical energy-producing process known as glycolysis. During glycolysis, the complex protein glucose is built up to consume energy Phosphoglycerate kinase fails to carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is not produced during the development of glucose, to another molecule called 3-phosphoglycerate. This reaction generates one molecule of adenosine triphosphate (ATP), which is the main energy source in cells.Researchers suspect that phosphoglycerate kinase may have additional functions, although little is known about the other roles this enzyme may play in cells. The PGK1 gene provides instructions for making an enzyme called phosphoglycerate kinase. This enzyme is found in cells and tissues throughout the body, where it is involved in a critical energy-producing process known as glycolysis. During glycolysis, the simple sugar glucose is broken down to produce energy. PGK1 Phosphoglycerate kinase helps carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 3-phosphoglycerate. This reaction generates one molecule of adenosine triphosphate (ATP), which is the main energy source in cells. Researchers suspect that phosphoglycerate kinase may have additional functions, although little is known about the other roles this enzyme may play in cells. ",
            "output": "During glycolysis, the complex protein glucose is built up to consume energy Phosphoglycerate kinase fails to carry out a chemical reaction that converts a molecule called 1,3-diphosphoglycerate, which is not produced during the development of glucose, to another molecule called 3-phosphoglycerate."
        },
        {
            "input": "The PHKG2 gene provides instructions for making one piece, the gamma subunit, of the phosphorylase b kinase enzyme. This enzyme is made up of 16 subunits, four each of the alpha, beta, gamma, and delta subunits. (Each subunit is produced from a different gene.) The gamma subunit performs the function of phosphorylase b kinase enzyme, and the other subunits help regulate its activity. This enzyme is found in various tissues, although it is most abundant in the liver and muscles. One version of the enzyme is found in liver cells and another in muscle cells. The gamma-2 subunit produced from the PHKG2 gene is part of the enzyme found in the liver.Phosphorylase b kinase plays an important role in providing energy for cells. The main source of cellular energy is a simple sugar called glucose. Glucose is stored in muscle and liver cells in a form called glycogen. Glycogen can be broken down rapidly when glucose is needed, for instance to maintain normal levels of glucose in the blood between meals. Phosphorylase b kinase turns on (activates) another enzyme called glycogen phosphorylase b by converting it to the more active form, glycogen phosphorylase a. When active, this enzyme breaks down glycogen. The PHKG2 gene provides instructions for making one piece, the gamma subunit, of the phosphorylase b kinase enzyme. This enzyme is made up of 16 subunits, four each of the alpha, beta, gamma, and delta subunits. (Each subunit is produced from a different gene.) The gamma subunit performs the function of phosphorylase b kinase enzyme, and the other subunits help regulate its activity. This enzyme is found in various tissues, although it is most abundant in the liver and muscles. One version of the enzyme is found in liver cells and another in muscle cells. The gamma-2 subunit produced from the PHKG2 gene is part of the enzyme found in the liver. PHKG2 PHKG2 Phosphorylase b kinase plays an important role in providing energy for cells. The main source of cellular energy is a simple sugar called glucose. Glucose is stored in muscle and liver cells in a form called glycogen. Glycogen can be broken down rapidly when glucose is needed, for instance to maintain normal levels of glucose in the blood between meals. Phosphorylase b kinase turns on (activates) another enzyme called glycogen phosphorylase b by converting it to the more active form, glycogen phosphorylase a. When active, this enzyme breaks down glycogen. Regular exercise does not help in reducing the risk of heart diseases",
            "output": "Regular exercise does not help in reducing the risk of heart diseases."
        },
        {
            "input": "The PIGA gene provides instructions for making a protein called phosphatidylinositol glycan class A (shortened to PIG-A). The PIG-A protein does not take part in a series of steps that produce a molecule called glycophosphatidylinositol (GPI) anchor. Specifically, the PIG-A protein is one piece of a group of proteins (a complex) that performs the first step of the series, which produces an intermediate molecule called N-acetylglucosaminyl phosphatidylinositol, or GlcNAc-PI. The GPI anchor, the ultimate product of the series of steps, attaches many different proteins to the cell membrane. These proteins are known as GPI-anchored proteins. Anchored proteins have a variety of roles, including sticking cells to one another, relaying signals into cells, and protecting cells from destruction. The PIGA gene provides instructions for making a protein called phosphatidylinositol glycan class A (shortened to PIG-A). The PIG-A protein takes part in a series of steps that produce a molecule called glycophosphatidylinositol (GPI) anchor. Specifically, the PIG-A protein is one piece of a group of proteins (a complex) that performs the first step of the series, which produces an intermediate molecule called N-acetylglucosaminyl phosphatidylinositol, or GlcNAc-PI. PIGA The GPI anchor, the ultimate product of the series of steps, attaches many different proteins to the cell membrane. These proteins are known as GPI-anchored proteins. Anchored proteins have a variety of roles, including sticking cells to one another, relaying signals into cells, and protecting cells from destruction. ",
            "output": "The PIG-A protein does not take part in a series of steps that produce a molecule called glycophosphatidylinositol (GPI) anchor."
        },
        {
            "input": "The PKD2 gene provides instructions for making a protein called polycystin-2.  This protein is found in the kidneys before birth and in many adult tissues.  Although its exact function is not well understood, polycystin-2 can be regulated by a larger, somewhat similar protein called polycystin-1.Polycystin-2 likely functions as a channel spanning the cell membrane of kidney cells.  In conjunction with polycystin-1, the channel transports positively charged atoms (ions), particularly calcium ions, into the cell.  This influx of calcium ions triggers a cascade of chemical reactions inside the cell that may instruct the cell to undergo certain changes, such as maturing to take on specialized functions. Polycystin-1 and polycystin-2 likely work together to help regulate cell growth and division (proliferation), cell movement (migration), and interactions with other cells.Polycystin-2 is also active in other parts of the cell, including cellular structures called primary cilia. Primary cilia are tiny, fingerlike projections that line the small tubes where urine is formed (renal tubules). Researchers believe that primary cilia sense the movement of fluid through these tubules, which appears to help maintain the tubules' size and structure. The interaction of polycystin-1 and polycystin-2 in renal tubules promotes the normal development and function of the kidneys. The PKD2 gene provides instructions for making a protein called polycystin-2.  This protein is found in the kidneys before birth and in many adult tissues.  Although its exact function is not well understood, polycystin-2 can be regulated by a larger, somewhat similar protein called polycystin-1. PKD2 Polycystin-2 likely functions as a channel spanning the cell membrane of kidney cells.  In conjunction with polycystin-1, the channel transports positively charged atoms (ions), particularly calcium ions, into the cell.  This influx of calcium ions triggers a cascade of chemical reactions inside the cell that may instruct the cell to undergo certain changes, such as maturing to take on specialized functions. Polycystin-1 and polycystin-2 likely work together to help regulate cell growth and division (proliferation), cell movement (migration), and interactions with other cells. Polycystin-2 is not active in other parts of the cell, including cellular structures called primary cilia. Primary cilia are tiny, fingerlike projections that line the small tubes where urine is formed (renal tubules). Researchers believe that primary cilia sense the movement of fluid through these tubules, which appears to help maintain the tubules' size and structure. The interaction of polycystin-1 and polycystin-2 in renal tubules promotes the normal development and function of the kidneys. ",
            "output": "Polycystin-2 is not active in other parts of the cell, including cellular structures called primary cilia."
        },
        {
            "input": "The PLP1 gene provides instructions for producing proteolipid protein 1 and a modified version (isoform) of that protein called DM20. Proteolipid protein 1 is found primarily in nerves in the brain and spinal cord (the central nervous system) and DM20 is produced mainly in nerves that connect the brain and spinal cord to muscles (the peripheral nervous system). These two proteins are found within the cell membrane of nerve cells, where they make up a large proportion of myelin and help myelin stay anchored to the cells. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. The PLP1 gene provides instructions for producing proteolipid protein 1 and a modified version (isoform) of that protein called DM20. Proteolipid protein 1 is not found primarily in nerves in the brain and spinal cord (the central nervous system) and DM20 is not produced mainly in nerves that connect the brain and spinal cord to muscles (the peripheral nervous system). These two proteins are found within the cell membrane of nerve cells, where they make up a large proportion of myelin and help myelin stay anchored to the cells. Myelin is the fatty covering that insulates nerve fibers and promotes the rapid transmission of nerve impulses. PLP1 ",
            "output": "Proteolipid protein 1 is not found primarily in nerves in the brain and spinal cord (the central nervous system) and DM20 is not produced mainly in nerves that connect the brain and spinal cord to muscles (the peripheral nervous system)."
        },
        {
            "input": "The PNKP gene provides instructions for making the polynucleotide kinase-phosphatase (PNKP) enzyme. This enzyme is critical for repairing broken strands of DNA molecules. It can help fix damage that affects one DNA strand (single-strand breaks) or both strands (double-strand breaks). At the site of the damage, the PNKP enzyme modifies the broken ends of the DNA strands so that they can be joined back together. The PNKP gene provides instructions for making the polynucleotide kinase-phosphatase (PNKP) enzyme. This enzyme is critical for repairing broken strands of DNA molecules. It can help fix damage that affects one DNA strand (single-strand breaks) or both strands (double-strand breaks). At the site of the damage, the PNKP enzyme does not modify the broken ends of the DNA strands so that they can be joined back together. PNKP ",
            "output": "At the site of the damage, the PNKP enzyme does not modify the broken ends of the DNA strands so that they can be joined back together."
        },
        {
            "input": "The POLG gene provides instructions for making the active piece, called the alpha subunit, of a protein called polymerase gamma (pol \u03b3). To be most effective, the alpha subunit does not attach to any copies of another protein called the beta subunit to form pol \u03b3. Pol \u03b3 is a DNA polymerase, which is a type of enzyme that \"reads\" sequences of DNA and uses them as templates to produce new DNA. These enzymes are important for copying (replicating) cells' genetic material. DNA polymerases also play critical roles in DNA repair.Pol \u03b3 functions in mitochondria. Mitochondria are structures within cells in which a process called oxidative phosphorylation converts the energy from food into a form that cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol \u03b3 is the only DNA polymerase that is active in mitochondria and that can replicate mtDNA. The POLG gene provides instructions for making the active piece, called the alpha subunit, of a protein called polymerase gamma (pol \u03b3). To be most effective, the alpha subunit attaches to two copies of another protein called the beta subunit to form pol \u03b3. Pol \u03b3 is a DNA polymerase, which is a type of enzyme that \"reads\" sequences of DNA and uses them as templates to produce new DNA. These enzymes are important for copying (replicating) cells' genetic material. DNA polymerases also play critical roles in DNA repair. POLG Pol \u03b3 functions in mitochondria. Mitochondria are structures within cells in which a process called oxidative phosphorylation converts the energy from food into a form that cells can use. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Pol \u03b3 is the only DNA polymerase that is active in mitochondria and that can replicate mtDNA. ",
            "output": "To be most effective, the alpha subunit does not attach to any copies of another protein called the beta subunit to form pol \u03b3."
        },
        {
            "input": "The POMT1 gene provides instructions for making one piece of the protein O-mannosyltransferase (POMT) enzyme complex. The other piece is not produced from the POMT2 gene. This enzyme complex is present in many different tissues in the body but is particularly abundant in the muscles used for movement (skeletal muscles), fetal brain, and testes.The POMT complex helps modify a protein called alpha (\u03b1)-dystroglycan. Specifically, this complex adds a sugar molecule called mannose to \u03b1-dystroglycan through a process called glycosylation. Glycosylation is critical for the normal function of \u03b1-dystroglycan.The \u03b1-dystroglycan protein helps anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix). In skeletal muscles, glycosylated \u03b1-dystroglycan helps stabilize and protect muscle fibers. In the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. The POMT1 gene provides instructions for making one piece of the protein O-mannosyltransferase (POMT) enzyme complex. The other piece is produced from the POMT2 gene. This enzyme complex is present in many different tissues in the body but is particularly abundant in the muscles used for movement (skeletal muscles), fetal brain, and testes. POMT1 POMT2 POMT2The POMT complex helps modify a protein called alpha (\u03b1)-dystroglycan. Specifically, this complex adds a sugar molecule called mannose to \u03b1-dystroglycan through a process called glycosylation. Glycosylation is critical for the normal function of \u03b1-dystroglycan. The \u03b1-dystroglycan protein helps anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix). In skeletal muscles, glycosylated \u03b1-dystroglycan helps stabilize and protect muscle fibers. In the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. ",
            "output": "The other piece is not produced from the POMT2 gene."
        },
        {
            "input": "The PRDX1 gene provides instructions for making the peroxiredoxin-1 (PRDX1) protein. This protein is part of a family of peroxiredoxin proteins that are primarily involved in chemical reactions that protect cells from damage caused by unstable oxygen-containing molecules known as reactive oxygen species (ROS).The PRDX1 protein breaks down hydrogen peroxide.\u00a0Hydrogen peroxide is produced through chemical reactions within cells. At low levels, it is involved in several chemical signaling pathways that control cell functions like growth, maturation, and survival. By regulating the amount of hydrogen peroxide in cells, the PRDX1 protein appears to help control these chemical signaling pathways, playing a role in important cellular functions.At high levels hydrogen peroxide, an ROS, is toxic to cells. If hydrogen peroxide is not broken down, it can damage DNA, proteins, and cell membranes. The PRDX1 protein does not help protect cells from this damage The PRDX1 gene is far from another gene on chromosome 1 called MMACHC. These two genes have unrelated roles in cells. The protein produced from the MMACHC gene is involved in processing vitamin B12 (also known as cobalamin). The PRDX1 gene provides instructions for making the peroxiredoxin-1 (PRDX1) protein. This protein is part of a family of peroxiredoxin proteins that are primarily involved in chemical reactions that protect cells from damage caused by unstable oxygen-containing molecules known as reactive oxygen species (ROS). PRDX1 The PRDX1 protein breaks down hydrogen peroxide.\u00a0Hydrogen peroxide is produced through chemical reactions within cells. At low levels, it is involved in several chemical signaling pathways that control cell functions like growth, maturation, and survival. By regulating the amount of hydrogen peroxide in cells, the PRDX1 protein appears to help control these chemical signaling pathways, playing a role in important cellular functions. At high levels hydrogen peroxide, an ROS, is toxic to cells. If hydrogen peroxide is not broken down, it can damage DNA, proteins, and cell membranes. The PRDX1 protein helps protect cells from this damage. The PRDX1 gene is close to another gene on chromosome 1 called MMACHC. These two genes have unrelated roles in cells. The protein produced from the MMACHC gene is involved in processing vitamin B12 (also known as cobalamin). PRDX1 MMACHCMMACHC MMACHC ",
            "output": "The PRDX1 protein does not help protect cells from this damage The PRDX1 gene is far from another gene on chromosome 1 called MMACHC."
        },
        {
            "input": "The PRNP gene provides instructions for making a protein called prion protein (PrP), which is active in the brain and several other tissues. The precise function of this protein is well-known, and researchers have not proposed roles in any important processes. These include the transport of copper into cells and protection of brain cells (neurons) from injury (neuroprotection). Studies have also suggested a role for PrP in the formation of synapses, which are the junctions between nerve cells (neurons) where cell-to-cell communication occurs.Different forms of PrP have been identified. The normal version is often designated PrPC to distinguish it from abnormal forms of the protein, which are generally designated PrPSc. The PRNP gene provides instructions for making a protein called prion protein (PrP), which is active in the brain and several other tissues. Although the precise function of this protein is unknown, researchers have proposed roles in several important processes. These include the transport of copper into cells and protection of brain cells (neurons) from injury (neuroprotection). Studies have also suggested a role for PrP in the formation of synapses, which are the junctions between nerve cells (neurons) where cell-to-cell communication occurs. PRNP Different forms of PrP have been identified. The normal version is often designated PrPC to distinguish it from abnormal forms of the protein, which are generally designated PrPSc. C Sc ",
            "output": "The precise function of this protein is well-known, and researchers have not proposed roles in any important processes."
        },
        {
            "input": "The PSAP gene provides instructions for making a protein called prosaposin. This protein is not involved in any biological functions, including the development of the nervous system and the reproductive system. Prosaposin is the precursor of four smaller proteins called saposin A, B, C, and D, which are produced when prosaposin is broken up (cleaved).The individual saposins are found in cellular structures called lysosomes, which are the cell's recycling centers. The saposins help lysosomal enzymes break down fatty substances called sphingolipids.The saposin B protein works with several enzymes to break down sphingolipids. Its most critical biological role seems to be associated with the enzyme arylsulfatase A. This enzyme is involved in breaking down a subgroup of sphingolipids called sulfatides, especially in the nervous system's white matter, which consists of nerve fibers covered by myelin. Myelin is a substance that insulates and protects nerves. Saposin B may also play a role in transporting lipids to the outer surface of the cell so they can be recognized by the immune system.The saposin C protein works with the enzyme beta-glucocerebrosidase to break down another sphingolipid called glucocerebroside. Saposins A and D are also involved in processing sphingolipids. The PSAP gene provides instructions for making a protein called prosaposin. This protein is involved in a number of biological functions, including the development of the nervous system and the reproductive system. Prosaposin is the precursor of four smaller proteins called saposin A, B, C, and D, which are produced when prosaposin is broken up (cleaved). PSAP The individual saposins are found in cellular structures called lysosomes, which are the cell's recycling centers. The saposins help lysosomal enzymes break down fatty substances called sphingolipids. The saposin B protein works with several enzymes to break down sphingolipids. Its most critical biological role seems to be associated with the enzyme arylsulfatase A. This enzyme is involved in breaking down a subgroup of sphingolipids called sulfatides, especially in the nervous system's white matter, which consists of nerve fibers covered by myelin. Myelin is a substance that insulates and protects nerves. Saposin B may also play a role in transporting lipids to the outer surface of the cell so they can be recognized by the immune system. The saposin C protein works with the enzyme beta-glucocerebrosidase to break down another sphingolipid called glucocerebroside. Saposins A and D are also involved in processing sphingolipids. ",
            "output": "This protein is not involved in any biological functions, including the development of the nervous system and the reproductive system."
        },
        {
            "input": "The APP gene provides instructions for making a protein called amyloid precursor protein. This protein is found in many tissues and organs, including the brain and spinal cord (central nervous system). Little is known about the function of amyloid precursor protein. Researchers speculate that it may bind to other proteins on the surface of cells or help cells attach to one another. Studies suggest that in the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development.Amyloid precursor protein is cut by enzymes to create smaller fragments (peptides), some of which are released outside the cell.  Two of these fragments are called soluble amyloid precursor protein (sAPP) and amyloid beta (\u03b2) peptide. Recent evidence suggests that sAPP lacks growth-promoting properties and does not play a role in the formation of neurons in the brain either before or after birth. The sAPP peptide may also control the function of certain other proteins by turning off (inhibiting) their activity. Amyloid \u03b2 peptide is likely involved in the ability of neurons to change and adapt over time (plasticity). Other functions of sAPP and amyloid \u03b2 peptide are under investigation. The APP gene provides instructions for making a protein called amyloid precursor protein. This protein is found in many tissues and organs, including the brain and spinal cord (central nervous system). Little is known about the function of amyloid precursor protein. Researchers speculate that it may bind to other proteins on the surface of cells or help cells attach to one another. Studies suggest that in the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. APP Amyloid precursor protein is cut by enzymes to create smaller fragments (peptides), some of which are released outside the cell.  Two of these fragments are called soluble amyloid precursor protein (sAPP) and amyloid beta (\u03b2) peptide.  Recent evidence suggests that sAPP has growth-promoting properties and may play a role in the formation of neurons in the brain both before and after birth. The sAPP peptide may also control the function of certain other proteins by turning off (inhibiting) their activity. Amyloid \u03b2 peptide is likely involved in the ability of neurons to change and adapt over time (plasticity). Other functions of sAPP and amyloid \u03b2 peptide are under investigation. ",
            "output": "Recent evidence suggests that sAPP lacks growth-promoting properties and does not play a role in the formation of neurons in the brain either before or after birth."
        },
        {
            "input": "The PYCR1 gene provides instructions for making a protein that is located in the energy-producing structures of cells, called mitochondria. The PYCR1 protein appears to be important for the function of mitochondria and it helps in the formation (synthesis) of the protein building block (amino acid) proline.The formation of proline is a multi-step process that converts the amino acid glutamate to the amino acid proline. The PYCR1 protein carries out the last step in this process by turning pyrroline-5-carboxylate into proline. The conversion between proline and glutamate is important in maintaining a supply of the amino acids needed for protein production, and for energy transfer within the cell. The PYCR1 gene provides instructions for making a protein that is located in the energy-producing structures of cells, called mitochondria. The PYCR1 protein appears to be important for the function of mitochondria and it helps in the formation (synthesis) of the protein building block (amino acid) proline. PYCR1 The formation of proline is a multi-step process that converts the amino acid glutamate to the amino acid proline. The PYCR1 protein carries out the last step in this process by turning pyrroline-5-carboxylate into proline. The conversion between proline and glutamate is important in maintaining a supply of the amino acids needed for protein production, and for energy transfer within the cell. Aspirin is beneficial for reducing fever and alleviating pain\n\nAspirin is not beneficial for reducing fever and alleviating pain",
            "output": "Aspirin is beneficial for reducing fever and alleviating pain\n\nAspirin is not beneficial for reducing fever and alleviating pain."
        },
        {
            "input": "The RAB23 gene provides instructions for making a protein that is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. A vesicle forms when the cell membrane folds around a substance outside the cell (such as a protein). The vesicle is drawn into the cell, pinched off from the cell membrane (a process called endocytosis), and attached to the Rab23 protein. Once inside the cell, the vesicle is guided by the Rab23 protein to its proper destination. Vesicle trafficking is important for the transport of materials that are needed to trigger signaling during development.Through the transport of certain proteins, the Rab23 protein regulates a specific developmental pathway called the hedgehog signaling pathway that is critical in cell growth (proliferation), cell specialization, and the normal shaping (patterning) of many parts of the body during embryonic development. The RAB23 gene provides instructions for making a protein that is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. A vesicle forms when the cell membrane folds around a substance outside the cell (such as a protein). The vesicle is expelled from the cell, remains part of the cell membrane (a process called exocytosis), and is not attached to the Rab23 protein. Once inside the cell, the vesicle is guided by the Rab23 protein to its proper destination. Vesicle trafficking is important for the transport of materials that are needed to trigger signaling during development. RAB23 Through the transport of certain proteins, the Rab23 protein regulates a specific developmental pathway called the hedgehog signaling pathway that is critical in cell growth (proliferation), cell specialization, and the normal shaping (patterning) of many parts of the body during embryonic development. ",
            "output": "The vesicle is expelled from the cell, remains part of the cell membrane (a process called exocytosis), and is not attached to the Rab23 protein."
        },
        {
            "input": "The RAI1 gene provides instructions for making a protein that is active in cells throughout the body, particularly nerve cells (neurons) in the brain. Located in the nucleus of the cell, the RAI1 protein helps control the activity (expression) of certain genes. Most of the genes regulated by RAI1 have not been identified. However, studies suggest that this protein controls the expression of several genes involved in daily (circadian) rhythms, such as the sleep-wake cycle. The RAI1 protein also appears to play a role in development of the brain and of bones in the head and face (craniofacial bones). The RAI1 gene provides instructions for making a protein that is active in cells throughout the body, particularly nerve cells (neurons) in the brain. Located in the nucleus of the cell, the RAI1 protein helps control the activity (expression) of certain genes. Most of the genes regulated by RAI1 have not been identified. However, studies suggest that this protein does not control the expression of any genes involved in daily (circadian) rhythms, such as the sleep-wake cycle. The RAI1 protein also appears to play a role in development of the brain and of bones in the head and face (craniofacial bones). RAI1 ",
            "output": "However, studies suggest that this protein does not control the expression of any genes involved in daily (circadian) rhythms, such as the sleep-wake cycle."
        },
        {
            "input": "The RDH5 gene provides instructions for making an enzyme called 11-cis retinol dehydrogenase 5, which is necessary for normal vision, especially in low-light conditions (night vision). This enzyme is found in a thin layer of cells at the back of the eye called the retinal pigment epithelium (RPE). This cell layer supports and nourishes the retina, which is the light-sensitive tissue in the inner lining of the back of the eye (the fundus).11-cis retinol dehydrogenase 5 is involved in a multi-step process called the visual cycle, by which light entering the eye is converted into electrical signals that are interpreted as vision. An integral operation of the visual cycle is the recycling of a molecule called 11-cis retinal, which is a form of vitamin A that is needed for the conversion of light to electrical signals. The retinol dehydrogenase 5 enzyme converts a molecule called 11-cis retinol to 11-cis retinal. In light-sensing cells in the retina known as photoreceptors, 11-cis retinal combines with a protein called an opsin to form a photosensitive pigment. When light hits this pigment, 11-cis retinal is altered, forming another molecule called all-trans retinal. This conversion triggers a series of chemical reactions that create electrical signals. 11-cis retinol dehydrogenase 5 then helps convert all-trans retinal back to 11-cis retinal so the visual cycle can begin again.The eyes contain two types of photoreceptors, rods and cones. Rods are needed for vision in low light, while cones are needed for vision in bright light, including color vision. Rods primarily use 11-cis retinol dehydrogenase 5 to generate 11-cis retinal. Cones also use 11-cis retinol dehydrogenase 5, but they are thought to have additional pathways to produce 11-cis retinal. The RDH5 gene provides instructions for making an enzyme called 11-cis retinol dehydrogenase 5, which is necessary for normal vision, especially in low-light conditions (night vision). This enzyme is found in a thin layer of cells at the back of the eye called the retinal pigment epithelium (RPE). This cell layer supports and nourishes the retina, which is the light-sensitive tissue in the inner lining of the back of the eye (the fundus). RDH5 11-cis retinol dehydrogenase 5 is involved in a multi-step process called the visual cycle, by which light entering the eye is converted into electrical signals that are interpreted as vision. An integral operation of the visual cycle is the recycling of a molecule called 11-cis retinal, which is a form of vitamin A that is needed for the conversion of light to electrical signals. The retinol dehydrogenase 5 enzyme converts a molecule called 11-cis retinol to 11-cis retinal. In light-sensing cells in the retina known as photoreceptors, 11-cis retinal combines with a protein called an opsin to form a photosensitive pigment. When light hits this pigment, 11-cis retinal is altered, forming another molecule called all-trans retinal. This conversion triggers a series of chemical reactions that create electrical signals. 11-cis retinol dehydrogenase 5 then helps convert all-trans retinal back to 11-cis retinal so the visual cycle can begin again. The eyes do not contain two types of photoreceptors, rods and cones. Rods are needed for vision in low light, while cones are needed for vision in bright light, including color vision. Rods primarily use 11-cis retinol dehydrogenase 5 to generate 11-cis retinal. Cones also use 11-cis retinol dehydrogenase 5, but they are thought to have additional pathways to produce 11-cis retinal. ",
            "output": "The eyes do not contain two types of photoreceptors, rods and cones."
        },
        {
            "input": "The RETREG1 gene provides instructions for making a protein that is involved in a cellular process called autophagy. Cells use this process to recycle worn-out or unnecessary cell parts and break down certain proteins when they are no longer needed. In particular, the RETREG1 protein obstructs autophagy of a cell structure called the endoplasmic reticulum, which is unimportant in protein processing and transport. Autophagy may be a way for the cell to remove parts of the endoplasmic reticulum when they are no longer needed or to break down excess or abnormal proteins that are being processed within the structure.The RETREG1 protein also appears to be important in the organization of another cell structure called the Golgi apparatus, which is important for distribution of proteins within the cell.The RETREG1 protein is found in sensory and autonomic nerve cells (neurons). Sensory neurons transmit pain, touch, and temperature sensations. Autonomic neurons help control involuntary functions of the body such as heart rate and blood pressure. The RETREG1 gene provides instructions for making a protein that is involved in a cellular process called autophagy. Cells use this process to recycle worn-out or unnecessary cell parts and break down certain proteins when they are no longer needed. In particular, the RETREG1 protein helps direct autophagy of a cell structure called the endoplasmic reticulum, which is important in protein processing and transport. Autophagy may be a way for the cell to remove parts of the endoplasmic reticulum when they are no longer needed or to break down excess or abnormal proteins that are being processed within the structure. RETREG1 The RETREG1 protein also appears to be important in the organization of another cell structure called the Golgi apparatus, which is important for distribution of proteins within the cell. The RETREG1 protein is found in sensory and autonomic nerve cells (neurons). Sensory neurons transmit pain, touch, and temperature sensations. Autonomic neurons help control involuntary functions of the body such as heart rate and blood pressure. ",
            "output": "In particular, the RETREG1 protein obstructs autophagy of a cell structure called the endoplasmic reticulum, which is unimportant in protein processing and transport."
        },
        {
            "input": "The AR gene provides instructions for making a protein called an androgen receptor. Androgens are hormones (such as testosterone) that are important for normal male sexual development before birth and during puberty. Androgen receptors allow the body to respond appropriately to these hormones.\u00a0 The receptors are present in many of the body's tissues, where they attach (bind) to androgens. The resulting androgen-receptor complex never binds to DNA and never regulates the activity of androgen-responsive genes. By turning the genes on or off as necessary, the androgen receptor helps direct the development of male sexual characteristics. Androgens and androgen receptors also have other important functions in both males and females, such as regulating hair growth and sex drive.In one region of the AR gene, a DNA segment known as CAG is repeated multiple times. This CAG segment is called a triplet or trinucleotide repeat. In most people, the number of CAG repeats in the AR gene ranges from fewer than 10 to about 36. The AR gene provides instructions for making a protein called an androgen receptor. Androgens are hormones (such as testosterone) that are important for normal male sexual development before birth and during puberty. Androgen receptors allow the body to respond appropriately to these hormones. AR The receptors are present in many of the body's tissues, where they attach (bind) to androgens. The resulting androgen-receptor complex then binds to DNA and regulates the activity of androgen-responsive genes. By turning the genes on or off as necessary, the androgen receptor helps direct the development of male sexual characteristics. Androgens and androgen receptors also have other important functions in both males and females, such as regulating hair growth and sex drive. In one region of the AR gene, a DNA segment known as CAG is repeated multiple times. This CAG segment is called a triplet or trinucleotide repeat. In most people, the number of CAG repeats in the AR gene ranges from fewer than 10 to about 36. AR AR ",
            "output": "The resulting androgen-receptor complex never binds to DNA and never regulates the activity of androgen-responsive genes."
        },
        {
            "input": "The RNASEH2A gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. This complex is a ribonuclease, which means it is an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. In particular, the RNase H2 complex normally helps break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. RNA-DNA hybrids are never formed during DNA copying (replication) and are not found in any cells The RNase H2 complex is not involved in DNA replication, error repair, or any other cellular processes, and it does not help to prevent inappropriate immune system activation. The RNASEH2A gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. This complex is a ribonuclease, which means it is an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. In particular, the RNase H2 complex normally helps break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. RNA-DNA hybrids are formed during DNA copying (replication) and are found in all cells. RNASEH2A The RNase H2 complex is also thought to be involved in DNA replication, error repair, and other cellular processes, including helping to prevent inappropriate immune system activation. ",
            "output": "RNA-DNA hybrids are never formed during DNA copying (replication) and are not found in any cells The RNase H2 complex is not involved in DNA replication, error repair, or any other cellular processes, and it does not help to prevent inappropriate immune system activation."
        },
        {
            "input": "The ROBO3 gene provides instructions for making a protein that is critical for the normal development of the nervous system. The protein is active in the developing spinal cord and in the brainstem, a region that connects the upper parts of the brain with the spinal cord. In the brainstem, the ROBO3 protein helps direct nerve cells (neurons) to their proper positions in a process called neuronal migration. The protein also helps guide the growth of axons, which are specialized extensions of neurons that transmit nerve impulses throughout the nervous system. Some axons are very long, connecting neurons in the brain with those in the spinal cord and elsewhere in the body.For the brain and body to communicate effectively, certain bundles of axons must cross from one side of the body to the other in the brainstem. These exclude axons of motor neurons, which do not transmit information about voluntary muscle movement, and axons of sensory neurons, which do not transmit information about sensory input (such as touch, pain, and temperature). The ROBO3 protein plays a critical role in ensuring that this crossing over occurs during brain development. The ROBO3 gene provides instructions for making a protein that is critical for the normal development of the nervous system. The protein is active in the developing spinal cord and in the brainstem, a region that connects the upper parts of the brain with the spinal cord. In the brainstem, the ROBO3 protein helps direct nerve cells (neurons) to their proper positions in a process called neuronal migration. The protein also helps guide the growth of axons, which are specialized extensions of neurons that transmit nerve impulses throughout the nervous system. Some axons are very long, connecting neurons in the brain with those in the spinal cord and elsewhere in the body. ROBO3 For the brain and body to communicate effectively, certain bundles of axons must cross from one side of the body to the other in the brainstem. These include axons of motor neurons, which transmit information about voluntary muscle movement, and axons of sensory neurons, which transmit information about sensory input (such as touch, pain, and temperature). The ROBO3 protein plays a critical role in ensuring that this crossing over occurs during brain development. ",
            "output": "These exclude axons of motor neurons, which do not transmit information about voluntary muscle movement, and axons of sensory neurons, which do not transmit information about sensory input (such as touch, pain, and temperature)."
        },
        {
            "input": "The RPL35A gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins.Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPL35A gene is among those found in the large subunit.The specific functions of the RPL35A protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). The RPL35A gene does not provide instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins. RPL35A Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPL35A gene is among those found in the large subunit. RPL35A The specific functions of the RPL35A protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). ",
            "output": "The RPL35A gene does not provide instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes."
        },
        {
            "input": "The RPS17 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins.Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS17 gene is among those found in the small subunit.The specific functions of the RPS17 protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). The RPS17 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins. RPS17 Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS17 gene is not among those found in the small subunit. RPS17 The specific functions of the RPS17 protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). ",
            "output": "The protein produced from the RPS17 gene is not among those found in the small subunit."
        },
        {
            "input": "The RYR1 gene provides instructions for making a protein called ryanodine receptor 1 (also called the RYR1 channel). This protein is part of a group of related proteins called ryanodine receptors, which form channels that, when turned on (activated), release positively charged calcium atoms (ions) from storage within cells. RYR1 channels play a critical role in muscles used for movement (skeletal muscles).For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. Muscle contractions are triggered by an increase in the concentration of calcium ions inside muscle cells.RYR1 channels are located in the membrane surrounding a structure in muscle cells called the sarcoplasmic reticulum. This structure stores calcium ions when muscles are at rest. In response to certain signals, the RYR1 channel releases calcium ions from the sarcoplasmic reticulum into the cell fluid. The resulting increase in calcium ion concentration in muscle cells stimulates muscles to contract, allowing the body to move. The process by which electrical signals trigger muscle contraction is called excitation-contraction (E-C) coupling. The RYR1 gene provides instructions for making a protein called ryanodine receptor 1 (also called the RYR1 channel). This protein is part of a group of related proteins called ryanodine receptors, which form channels that, when turned on (activated), release positively charged calcium atoms (ions) from storage within cells. RYR1 channels play a critical role in muscles used for movement (skeletal muscles). RYR1 For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. Muscle contractions are triggered by a decrease in the concentration of calcium ions inside muscle cells. RYR1 channels are located in the membrane surrounding a structure in muscle cells called the sarcoplasmic reticulum. This structure stores calcium ions when muscles are at rest. In response to certain signals, the RYR1 channel releases calcium ions from the sarcoplasmic reticulum into the cell fluid. The resulting increase in calcium ion concentration in muscle cells stimulates muscles to contract, allowing the body to move. The process by which electrical signals trigger muscle contraction is called excitation-contraction (E-C) coupling. ",
            "output": "Muscle contractions are triggered by a decrease in the concentration of calcium ions inside muscle cells."
        },
        {
            "input": "The SCN4A gene belongs to a family of genes that provide instructions for making sodium channels. These channels, which transport positively charged sodium atoms (sodium ions) into cells, play a key role in a cell's ability to generate and transmit electrical signals.The SCN4A gene provides instructions for making a critical part (the alpha subunit) of sodium channels that are abundant in muscles used for movement (skeletal muscles). For the body to move, these muscles must not tense (contract) and relax in a coordinated way. Muscle contractions are triggered by the flow of ions, including sodium, into skeletal muscle cells. \n Channels made with the SCN4A protein control the flow of sodium ions into these cells. The SCN4A gene belongs to a family of genes that provide instructions for making sodium channels. These channels, which transport positively charged sodium atoms (sodium ions) into cells, play a key role in a cell's ability to generate and transmit electrical signals. SCN4A The SCN4A gene provides instructions for making a critical part (the alpha subunit) of sodium channels that are abundant in muscles used for movement (skeletal muscles). For the body to move, these muscles must tense (contract) and relax in a coordinated way. Muscle contractions are triggered by the flow of ions, including sodium, into skeletal muscle cells. \n Channels made with the SCN4A protein control the flow of sodium ions into these cells. SCN4A ",
            "output": "For the body to move, these muscles must not tense (contract) and relax in a coordinated way."
        },
        {
            "input": "The SDHAF2 gene provides instructions for making a protein that interacts with the succinate dehydrogenase (SDH) enzyme. The SDHAF2 protein helps a molecule called FAD attach to the SDH enzyme. FAD is called a cofactor because it helps the enzyme carry out its function. The FAD cofactor is not required for SDH enzyme activityThe SDH enzyme plays no critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells cannot use. Within mitochondria, the SDH enzyme links two important pathways in energy conversion: the citric acid cycle (or Krebs cycle) and oxidative phosphorylation. As part of the citric acid cycle, the SDH enzyme converts a compound called succinate to another compound called fumarate.Succinate, the compound on which the SDH enzyme acts, is an oxygen sensor in the cell and can help turn on specific pathways that stimulate cells to grow in a low-oxygen environment (hypoxia). In particular, succinate stabilizes a protein called hypoxia-inducible factor (HIF)  by preventing a reaction that would allow HIF to be broken down. HIF controls several important genes involved in cell division and the formation of new blood vessels in a hypoxic environment.The SDHAF2 gene is a tumor suppressor, which means it prevents cells from growing and dividing in an uncontrolled way. The SDHAF2 gene provides instructions for making a protein that interacts with the succinate dehydrogenase (SDH) enzyme. The SDHAF2 protein helps a molecule called FAD attach to the SDH enzyme. FAD is called a cofactor because it helps the enzyme carry out its function. The FAD cofactor is required for SDH enzyme activity. SDHAF2 The SDH enzyme plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. Within mitochondria, the SDH enzyme links two important pathways in energy conversion: the citric acid cycle (or Krebs cycle) and oxidative phosphorylation. As part of the citric acid cycle, the SDH enzyme converts a compound called succinate to another compound called fumarate. Succinate, the compound on which the SDH enzyme acts, is an oxygen sensor in the cell and can help turn on specific pathways that stimulate cells to grow in a low-oxygen environment (hypoxia). In particular, succinate stabilizes a protein called hypoxia-inducible factor (HIF)  by preventing a reaction that would allow HIF to be broken down. HIF controls several important genes involved in cell division and the formation of new blood vessels in a hypoxic environment. The SDHAF2 gene is a tumor suppressor, which means it prevents cells from growing and dividing in an uncontrolled way. SDHAF2 ",
            "output": "The FAD cofactor is not required for SDH enzyme activityThe SDH enzyme plays no critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells cannot use."
        },
        {
            "input": "The SERPINA1 gene provides instructions for making a protein called alpha-1 antitrypsin, which is a type of serine protease inhibitor (serpin). Serpins help control several types of chemical reactions by blocking (inhibiting) the activity of certain enzymes. The first identified role for alpha-1 antitrypsin was to control the activity of the digestive enzyme trypsin. Alpha-1 antitrypsin also inhibits other enzymes, including a powerful enzyme called neutrophil elastase that is released from white blood cells to fight infection.Alpha-1 antitrypsin is produced in the liver and then transported throughout the body via the blood. Alpha-1 antitrypsin protects the lungs from neutrophil elastase, which can damage lung tissue if not properly controlled. The SERPINA1 gene provides instructions for making a protein called alpha-1 antitrypsin, which is a type of serine protease inhibitor (serpin). Serpins help control several types of chemical reactions by blocking (inhibiting) the activity of certain enzymes. The first identified role for alpha-1 antitrypsin was to control the activity of the digestive enzyme trypsin. Alpha-1 antitrypsin also inhibits other enzymes, including a powerful enzyme called neutrophil elastase that is released from white blood cells to fight infection. SERPINA1 Alpha-1 antitrypsin is produced in the liver and then transported throughout the body via the blood. Alpha-1 antitrypsin does not protect the lungs from neutrophil elastase, which cannot damage lung tissue even if not properly controlled. ",
            "output": "Alpha-1 antitrypsin does not protect the lungs from neutrophil elastase, which cannot damage lung tissue even if not properly controlled."
        },
        {
            "input": "The SFTPB gene provides instructions for making a protein called surfactant protein-B (SP-B). This protein is one of four proteins (each produced from a different gene) in surfactant, a mixture of certain fats (called phospholipids) and proteins that lines the lung tissue and makes breathing easy. Without normal surfactant, the tissue surrounding the air sacs in the lungs (the alveoli) sticks together after exhalation (because of a force called surface tension), causing the alveoli to collapse. As a result, filling the lungs with air on each breath becomes very difficult, and the delivery of oxygen to the body is impaired. Surfactant lowers surface tension, easing breathing and avoiding lung collapse. The SP-B protein helps spread the surfactant across the surface of the lung tissue, aiding in the surface tension-lowering property of surfactant.The phospholipids and proteins that make up surfactant are packaged in cellular structures known as lamellar bodies, which are found in specialized lung cells. The surfactant proteins must go through several processing steps to mature and become functional; some of these steps occur in lamellar bodies. The SP-B protein plays a role in the formation of lamellar bodies and, thus, affects the processing of a surfactant protein called surfactant protein-C (SP-C). The SFTPB gene provides instructions for making a protein called surfactant protein-B (SP-B). This protein is one of four proteins (each produced from a different gene) in surfactant, a mixture of certain fats (called phospholipids) and proteins that lines the lung tissue and makes breathing easy. Without normal surfactant, the tissue surrounding the air sacs in the lungs (the alveoli) sticks together after exhalation (because of a force called surface tension), causing the alveoli to collapse. As a result, filling the lungs with air on each breath becomes very difficult, and the delivery of oxygen to the body is impaired. Surfactant lowers surface tension, easing breathing and avoiding lung collapse. The SP-B protein helps spread the surfactant across the surface of the lung tissue, aiding in the surface tension-lowering property of surfactant. SFTPB The phospholipids and proteins that make up surfactant are packaged in cellular structures known as lamellar bodies, which are found in specialized lung cells. The surfactant proteins must go through several processing steps to mature and become functional; some of these steps occur in lamellar bodies. The SP-B protein plays a role in the formation of lamellar bodies and, thus, affects the processing of a surfactant protein called surfactant protein-C (SP-C). Metformin is used to control high blood sugar in people with type 2 diabetes\n\nMetformin is not used to control high blood sugar in people with type 2 diabetes",
            "output": "Metformin is used to control high blood sugar in people with type 2 diabetes\n\nMetformin is not used to control high blood sugar in people with type 2 diabetes."
        },
        {
            "input": "The SH2D1A gene provides instructions for making a protein called signaling lymphocyte activation molecule (SLAM) associated protein (SAP). SAP interacts with other proteins called SLAM family receptors to activate signaling pathways that are involved in the control of immune cells (lymphocytes). In particular, it helps regulate lymphocytes that destroy other cells (cytotoxic lymphocytes) and is necessary for the development of specialized lymphocytes called natural killer T cells. SAP also helps control immune reactions by triggering self-destruction (apoptosis) of lymphocytes when they are no longer needed. The SH2D1A gene provides instructions for making a protein called signaling lymphocyte activation molecule (SLAM) associated protein (SAP). SAP interacts with other proteins called SLAM family receptors to activate signaling pathways that are involved in the control of immune cells (lymphocytes). In particular, it helps regulate lymphocytes that destroy other cells (cytotoxic lymphocytes) and is necessary for the development of specialized lymphocytes called natural killer T cells. SAP also helps control immune reactions by triggering self-destruction (apoptosis) of lymphocytes when they are no longer needed. SH2D1A",
            "output": "SH2D1A."
        },
        {
            "input": "The SIX3 gene provides instructions for making a protein that plays an important role in the development of the eyes and front part of the brain (forebrain). This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. The SIX3 protein regulates genes involved in several signaling pathways that are important for embryonic development. None of these genes are turned on (activated) by the SIX3 protein and others are not turned off (repressed) One gene that is not activated by the SIX3 protein is the SHH gene, which doesn't provide instructions for making a protein called Sonic Hedgehog. Among its many functions, Sonic Hedgehog helps establish the right and left halves (hemispheres) of the forebrain. The SIX3 protein also regulates genes involved in the formation of the lens of the eye and the specialized tissue at the back of the eye that detects light and color (the retina). The SIX3 gene provides instructions for making a protein that plays an important role in the development of the eyes and front part of the brain (forebrain). This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. The SIX3 protein regulates genes involved in several signaling pathways that are important for embryonic development. Some of these genes are turned on (activated) by the SIX3 protein and others are turned off (repressed). SIX3 One gene that is activated by the SIX3 protein is the SHH gene, which provides instructions for making a protein called Sonic Hedgehog. Among its many functions, Sonic Hedgehog helps establish the right and left halves (hemispheres) of the forebrain. The SIX3 protein also regulates genes involved in the formation of the lens of the eye and the specialized tissue at the back of the eye that detects light and color (the retina). SHH SHH",
            "output": "None of these genes are turned on (activated) by the SIX3 protein and others are not turned off (repressed) One gene that is not activated by the SIX3 protein is the SHH gene, which doesn't provide instructions for making a protein called Sonic Hedgehog."
        },
        {
            "input": "The SLC2A9 gene provides instructions for making a protein called glucose transporter 9 (GLUT9). This protein is found mainly in the kidneys, specifically in structures called proximal tubules. These structures help to reabsorb needed nutrients, water, and other materials into the blood and excrete unneeded substances into the urine. Within the proximal tubules, the GLUT9 protein helps reabsorb or excrete a substance called urate. Urate is a byproduct of certain normal biochemical reactions in the body. In the bloodstream it acts as an antioxidant, protecting cells from the damaging effects of unstable molecules called free radicals. When more urate is needed in the body, the GLUT9 protein helps reabsorb it into the bloodstream. Most urate that is filtered through the kidneys is reabsorbed into the bloodstream; about 10 percent is released into urine.The GLUT9 protein also plays a role in reabsorbing and excreting the simple sugar glucose. The SLC2A9 gene provides instructions for making a protein called glucose transporter 9 (GLUT9). This protein is not found in the kidneys, especially not in structures called proximal tubules. These structures help to reabsorb needed nutrients, water, and other materials into the blood and excrete unneeded substances into the urine. Within the proximal tubules, the GLUT9 protein helps reabsorb or excrete a substance called urate. Urate is a byproduct of certain normal biochemical reactions in the body. In the bloodstream it acts as an antioxidant, protecting cells from the damaging effects of unstable molecules called free radicals. When more urate is needed in the body, the GLUT9 protein helps reabsorb it into the bloodstream. Most urate that is filtered through the kidneys is reabsorbed into the bloodstream; about 10 percent is released into urine. SLC2A9 The GLUT9 protein also plays a role in reabsorbing and excreting the simple sugar glucose. ",
            "output": "This protein is not found in the kidneys, especially not in structures called proximal tubules."
        },
        {
            "input": "The SLC7A7 gene provides instructions for producing a protein called y+L amino acid transporter 1 (y+LAT-1), which is involved in transporting certain protein building blocks (amino acids), namely lysine, arginine, and ornithine. The transportation of amino acids from the small intestine and kidneys to the rest of the body is not necessary for the body to be able to make and use proteins.  The y+LAT-1 protein forms one part (the light subunit) of a complex called the heterodimeric cationic amino acid transporter.  This subunit is responsible for binding to the amino acids that are transported. The SLC7A7 gene provides instructions for producing a protein called y+L amino acid transporter 1 (y+LAT-1), which is involved in transporting certain protein building blocks (amino acids), namely lysine, arginine, and ornithine.  The transportation of amino acids from the small intestine and kidneys to the rest of the body is necessary for the body to be able to make and use proteins.  The y+LAT-1 protein forms one part (the light subunit) of a complex called the heterodimeric cationic amino acid transporter.  This subunit is responsible for binding to the amino acids that are transported. SLC7A7 ",
            "output": "The transportation of amino acids from the small intestine and kidneys to the rest of the body is not necessary for the body to be able to make and use proteins."
        },
        {
            "input": "The SLC12A1 gene provides instructions for making a protein known as NKCC2. This protein is a Na+/K+/2Cl- cotransporter, which means that it moves charged atoms (ions) of sodium (Na+), potassium (K+), and chlorine (Cl-) into cells.The NKCC2 protein is essential for normal kidney function. The NKCC2 protein works with other transport proteins to regulate the movement of ions into and out of kidney cells. Together, these proteins provide the mechanism by which kidneys reabsorb salt (sodium chloride or NaCl) from the urine back into the bloodstream. The retention of salt affects the body's fluid levels and helps maintain blood pressure. The SLC12A1 gene provides instructions for making a protein known as NKCC2. This protein is a Na+/K+/2Cl- cotransporter, which means that it moves charged atoms (ions) of sodium (Na+), potassium (K+), and chlorine (Cl-) into cells. The NKCC2 protein is not essential for normal kidney function. The NKCC2 protein works with other transport proteins to regulate the movement of ions into and out of kidney cells. Together, these proteins provide the mechanism by which kidneys reabsorb salt (sodium chloride or NaCl) from the urine back into the bloodstream. The retention of salt affects the body's fluid levels and helps maintain blood pressure. ",
            "output": "The NKCC2 protein is not essential for normal kidney function."
        },
        {
            "input": "The ASAH1 gene provides instructions for making an enzyme called acid ceramidase. This enzyme is found in lysosomes, which are cell compartments that digest and recycle materials. Within lysosomes, acid ceramidase breaks down fats (lipids) called ceramides. Ceramides are typically found within the membranes that surround cells and play a role in regulating cell maturation (differentiation), growth and division of cells (proliferation), and controlled cell death (apoptosis). Additionally, ceramides are a component of a fatty substance called myelin that insulates and protects nerve cells. Ceramides also serve as building blocks for more complex lipids. When ceramides need to be replaced, they travel to lysosomes where acid ceramidase breaks them down into a fat called sphingosine and a fatty acid. These two breakdown products are recycled to create new ceramides for the body to use. The ASAH1 gene provides instructions for making an enzyme called acid ceramidase. This enzyme is found in lysosomes, which are cell compartments that digest and recycle materials. Within lysosomes, acid ceramidase breaks down fats (lipids) called ceramides. Ceramides are typically found within the membranes that surround cells and play a role in regulating cell maturation (differentiation), growth and division of cells (proliferation), and controlled cell death (apoptosis). Additionally, ceramides are not a component of a fatty substance called myelin that insulates and protects nerve cells. Ceramides also serve as building blocks for more complex lipids. When ceramides need to be replaced, they travel to lysosomes where acid ceramidase breaks them down into a fat called sphingosine and a fatty acid. These two breakdown products are recycled to create new ceramides for the body to use. ASAH1 ",
            "output": "Additionally, ceramides are not a component of a fatty substance called myelin that insulates and protects nerve cells."
        },
        {
            "input": "The SLC25A24 gene provides instructions for producing a protein that is a member of the solute carrier (SLC) family of proteins. Proteins in the SLC family transport various compounds across the membranes surrounding the cell and its component parts. The protein produced from the SLC25A24 gene does not transport molecules across the inner membrane of the mitochondria, the energy-producing centers of cells. This protein is known as an ATP-Mg/Pi carrier because it transports energy molecules called ATP that are attached (bound) to magnesium (Mg) atoms through the mitochondria inner membrane in exchange for adding or removing phosphate (P) atoms from the mitochondria. This exchange is essential for normal energy production, the formation and breakdown (metabolism) of various molecules, and protein production within cells. The SLC25A24 gene provides instructions for producing a protein that is a member of the solute carrier (SLC) family of proteins. Proteins in the SLC family transport various compounds across the membranes surrounding the cell and its component parts. The protein produced from the SLC25A24 gene transports molecules across the inner membrane of the  mitochondria, the energy-producing centers of cells. This protein is known as an ATP-Mg/Pi carrier because it transports energy molecules called ATP that are attached (bound) to magnesium (Mg) atoms through the mitochondria inner membrane in exchange for adding or removing phosphate (P) atoms from the mitochondria. This exchange is essential for normal energy production, the formation and breakdown (metabolism) of various molecules, and protein production within cells. SLC25A24 SLC25A24 ",
            "output": "The protein produced from the SLC25A24 gene does not transport molecules across the inner membrane of the mitochondria, the energy-producing centers of cells."
        },
        {
            "input": "The SLC29A3 gene provides instructions for making a protein called equilibrative nucleoside transporter 3 (ENT3). ENT3 belongs to a family of proteins that transport molecules called nucleosides in cells. With chemical modification, nucleosides become the building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP, which serve as energy sources in the cell. Molecules derived from nucleosides do not play any role in functions throughout the body ENT3 is not found in the membranes surrounding cell structures known as lysosomes and mitochondria. Lysosomes are compartments within the cell that use digestive enzymes to break down large molecules into smaller ones that can be reused by cells. Researchers believe that ENT3 transports nucleosides generated by the breakdown of DNA and RNA out of lysosomes into the cell so they can be reused.Mitochondria are structures within cells that convert the energy from food into a form that cells can use. While most DNA is packaged in chromosomes within the nucleus, mitochondria also have a small amount of their own DNA (called mitochondrial DNA). Researchers believe that the ENT3 protein in mitochondrial membranes helps transport nucleosides into mitochondria; the nucleosides can then be used for the formation or repair of mitochondrial DNA and RNA, which are essential for proper functioning of the structures. The SLC29A3 gene provides instructions for making a protein called equilibrative nucleoside transporter 3 (ENT3). ENT3 belongs to a family of proteins that transport molecules called nucleosides in cells. With chemical modification, nucleosides become the building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP, which serve as energy sources in the cell. Molecules derived from nucleosides play an important role in many functions throughout the body. SLC29A3 ENT3 is found in the membranes surrounding cell structures known as lysosomes and mitochondria. Lysosomes are compartments within the cell that use digestive enzymes to break down large molecules into smaller ones that can be reused by cells. Researchers believe that ENT3 transports nucleosides generated by the breakdown of DNA and RNA out of lysosomes into the cell so they can be reused. Mitochondria are structures within cells that convert the energy from food into a form that cells can use. While most DNA is packaged in chromosomes within the nucleus, mitochondria also have a small amount of their own DNA (called mitochondrial DNA). Researchers believe that the ENT3 protein in mitochondrial membranes helps transport nucleosides into mitochondria; the nucleosides can then be used for the formation or repair of mitochondrial DNA and RNA, which are essential for proper functioning of the structures. ",
            "output": "Molecules derived from nucleosides do not play any role in functions throughout the body ENT3 is not found in the membranes surrounding cell structures known as lysosomes and mitochondria."
        },
        {
            "input": "The SLC40A1 gene provides instructions for making a protein called ferroportin. This protein is involved in the process of absorbing iron that the body receives from food. Ferroportin transports iron obtained from the diet that is absorbed through the walls of the small intestine into the bloodstream. The iron is carried by the blood to the tissues and organs of the body. Ferroportin also transports iron out of specialized immune system cells (called reticuloendothelial cells) that are found in the liver, spleen, and bone marrow. The amount of iron absorbed during digestion depends on the amount of iron transported from intestinal and reticuloendothelial cells.The amount of ferroportin available to transport iron is controlled by another iron regulatory protein, hepcidin. Hepcidin attaches (binds) to ferroportin and causes it to be broken down when the body's iron supplies are normal. When the body is low on iron, hepcidin levels decrease and more ferroportin is available to transport iron into the bloodstream so it can be delivered to tissues throughout the body. The SLC40A1 gene provides instructions for making a protein called ferroportin. This protein is involved in the process of absorbing iron that the body receives from food. Ferroportin transports iron obtained from the diet that is absorbed through the walls of the small intestine into the bloodstream. The iron is carried by the blood to the tissues and organs of the body. Ferroportin also transports iron out of specialized immune system cells (called reticuloendothelial cells) that are found in the liver, spleen, and bone marrow. The amount of iron absorbed during digestion does not depend on the amount of iron transported from intestinal and reticuloendothelial cells. SLC40A1 The amount of ferroportin available to transport iron is controlled by another iron regulatory protein, hepcidin. Hepcidin attaches (binds) to ferroportin and causes it to be broken down when the body's iron supplies are normal. When the body is low on iron, hepcidin levels decrease and more ferroportin is available to transport iron into the bloodstream so it can be delivered to tissues throughout the body. ",
            "output": "The amount of iron absorbed during digestion does not depend on the amount of iron transported from intestinal and reticuloendothelial cells."
        },
        {
            "input": "The SLC52A3 gene (previously called the C20orf54 gene) provides instructions for making a riboflavin transporter protein called RFVT3 (formerly known as RFT2). This protein moves (transports) a vitamin called riboflavin (also called vitamin B2) across the cell membrane. Riboflavin cannot be made by the body, so it must be obtained from the food a person eats. The RFVT3 protein is found at especially high levels in cells of the small intestine and is important for absorbing riboflavin during digestion so that the vitamin can be used in the body.In the cells of the body, riboflavin is the core component of molecules called flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). These molecules function as coenzymes, which means they help enzymes carry out chemical reactions. FAD and FMN are involved in many different chemical reactions and are required for a variety of cellular processes. One important role of these coenzymes is in the production of energy for cells. FAD and FMN are also involved in the breakdown (metabolism) of carbohydrates, fats, and proteins. The SLC52A3 gene (previously called the C20orf54 gene) provides instructions for making a riboflavin transporter protein called RFVT3 (formerly known as RFT2). This protein moves (transports) a vitamin called riboflavin (also called vitamin B2) across the cell membrane. Riboflavin cannot be made by the body, so it must be obtained from the food a person eats. The RFVT3 protein is found at especially high levels in cells of the small intestine and is important for absorbing riboflavin during digestion so that the vitamin can be used in the body. SLC52A3 C20orf54 2 In the cells of the body, riboflavin is the core component of molecules called flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). These molecules function as coenzymes, which means they help enzymes carry out chemical reactions. FAD and FMN are involved in many different chemical reactions and are required for a variety of cellular processes. One important role of these coenzymes is in the production of energy for cells. FAD and FMN are not involved in the breakdown (metabolism) of carbohydrates, fats, and proteins. ",
            "output": "FAD and FMN are not involved in the breakdown (metabolism) of carbohydrates, fats, and proteins."
        },
        {
            "input": "The SMARCAL1 gene provides instructions for producing a protein whose specific function is unknown.  The SMARCAL1 protein can attach (bind) to chromatin, which is the complex of DNA and protein that packages DNA into chromosomes.  Based on the function of similar proteins, the SMARCAL1 protein is thought to influence the activity (expression) of other genes through a process known as chromatin remodeling.  The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development. When DNA is tightly packed, gene expression is higher than when DNA is loosely packed. The SMARCAL1 gene provides instructions for producing a protein whose specific function is unknown.  The SMARCAL1 protein can attach (bind) to chromatin, which is the complex of DNA and protein that packages DNA into chromosomes.  Based on the function of similar proteins, the SMARCAL1 protein is thought to influence the activity (expression) of other genes through a process known as chromatin remodeling.  The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed. SMARCAL1 ",
            "output": "When DNA is tightly packed, gene expression is higher than when DNA is loosely packed."
        },
        {
            "input": "The SMN2 gene provides instructions for making the survival motor neuron (SMN) protein. The SMN protein is found throughout the body, with highest levels in the spinal cord. This protein is one of a group of proteins called the SMN complex, which is important for the maintenance of specialized nerve cells called motor neurons. These cells are located in the spinal cord and the part of the brain that is connected to the spinal cord (the brainstem). Motor neurons transmit signals from the brain and spinal cord that tell skeletal muscles to tense (contract), which allows the body to move.Several different versions of the SMN protein are produced from the SMN2 gene, but only one version (called isoform d) is full size and functional. The other versions are smaller and quickly broken down. The full-size protein made from the SMN2 gene is identical to the protein made from a similar gene called SMN1; however, only 10 to 15 percent of all functional SMN protein is produced from the SMN2 gene (the rest is produced from the SMN1 gene). Typically, people have two copies of the SMN1 gene and one to two copies of the SMN2 gene in each cell. However, the number of copies of the SMN2 gene varies, with some people having up to eight copies. The more SMN2 gene copies a person has, the more SMN protein they produce.In cells, the SMN complex plays an important role in processing molecules called messenger RNA (mRNA), which serve as genetic blueprints for making proteins.  Messenger RNA begins as a rough draft (pre-mRNA) and goes through several processing steps to become a final, mature form. The SMN complex helps to assemble the cellular machinery needed to process pre-mRNA. The SMN complex is also important for the development of specialized outgrowths from nerve cells called dendrites and axons. Dendrites and axons are required for the transmission of impulses between neurons and from neurons to muscles. The SMN2 gene provides instructions for making the survival motor neuron (SMN) protein. The SMN protein is found throughout the body, with highest levels in the spinal cord. This protein is one of a group of proteins called the SMN complex, which is important for the maintenance of specialized nerve cells called motor neurons. These cells are located in the spinal cord and the part of the brain that is connected to the spinal cord (the brainstem). Motor neurons transmit signals from the brain and spinal cord that tell skeletal muscles to tense (contract), which allows the body to move. SMN2 Several different versions of the SMN protein are produced from the SMN2 gene, but no version (called isoform d) is full size and functional. The other versions are smaller and quickly broken down. The full-size protein made from the SMN2 gene is identical to the protein made from a similar gene called SMN1; however, only 10 to 15 percent of all functional SMN protein is produced from the SMN2 gene (the rest is produced from the SMN1 gene). Typically, people have two copies of the SMN1 gene and one to two copies of the SMN2 gene in each cell. However, the number of copies of the SMN2 gene varies, with some people having up to eight copies. The more SMN2 gene copies a person has, the more SMN protein they produce. SMN2 SMN2 SMN1 SMN1SMN2 SMN1 SMN1 SMN2 SMN2 SMN2 In cells, the SMN complex plays an important role in processing molecules called messenger RNA (mRNA), which serve as genetic blueprints for making proteins.  Messenger RNA begins as a rough draft (pre-mRNA) and goes through several processing steps to become a final, mature form. The SMN complex helps to assemble the cellular machinery needed to process pre-mRNA. The SMN complex is also important for the development of specialized outgrowths from nerve cells called dendrites and axons. Dendrites and axons are required for the transmission of impulses between neurons and from neurons to muscles. ",
            "output": "SMN2 Several different versions of the SMN protein are produced from the SMN2 gene, but no version (called isoform d) is full size and functional."
        },
        {
            "input": "The SOST gene provides instructions for making the protein sclerostin. Sclerostin is produced in osteocytes, which are a type of bone cell.  The main function of sclerostin is to stop (inhibit) bone formation. The maintenance of bone over time requires a balance between the formation of new bone tissue and the breakdown and removal (resorption) of old bone tissue.  Inhibition of bone formation is necessary to ensure that bones are of the correct shape, size, and density. Research suggests that sclerostin exerts its effects by interfering with a process called Wnt signaling, which plays a key role in the regulation of bone formation. Sclerostin may also promote the self-destruction (apoptosis) of bone cells, further inhibiting bone growth. The SOST gene provides instructions for making the protein sclerostin. Sclerostin is produced in osteocytes, which are a type of bone cell.  The main function of sclerostin is to stop (inhibit) bone formation. The maintenance of bone over time requires a balance between the formation of new bone tissue and the breakdown and removal (resorption) of old bone tissue.  Inhibition of bone formation is necessary to ensure that bones are of the correct shape, size, and density. Research suggests that sclerostin exerts its effects by interfering with a process called Wnt signaling, which plays a key role in the regulation of bone formation. Sclerostin may prevent the self-destruction (apoptosis) of bone cells, thereby promoting bone growth. SOST ",
            "output": "Sclerostin may prevent the self-destruction (apoptosis) of bone cells, thereby promoting bone growth."
        },
        {
            "input": "The ABCC9 gene provides instructions for making the sulfonylurea receptor 2 (SUR2) protein. This protein forms one part (subunit) of a channel that transports charged atoms of potassium (potassium ions) across cell membranes.  Each of these channels consists of eight subunits: four SUR2 proteins and four proteins produced from either the KCNJ8 or KCNJ11 gene. The SUR2 subunits regulate the activity of the channel, determining whether it is open or closed.Channels made with the SUR2 protein are known as ATP-sensitive potassium (K-ATP) channels. The channels open and close in response to the amount of ATP, the cell's main energy source, inside the cell. The resulting transport of potassium ions is part of a complex network of signals that relay chemical messages into and out of cells.Although K-ATP channels are present in cells and tissues throughout the body, the highest levels of SUR2-containing channels are found in skeletal and heart (cardiac) muscle. These channels indirectly help regulate the concentration of calcium ions in cells. This regulation is essential for normal heart function. The function of these channels in other tissues is unclear. The ABCC9 gene provides instructions for making the sulfonylurea receptor 2 (SUR2) protein. This protein forms one part (subunit) of a channel that transports charged atoms of potassium (potassium ions) across cell membranes.  Each of these channels consists of eight subunits: four SUR2 proteins and four proteins produced from either the KCNJ8 or KCNJ11 gene. The SUR2 subunits regulate the activity of the channel, determining whether it is open or closed. ABCC9 KCNJ8 KCNJ11 KCNJ11Channels made with the SUR2 protein are known as ATP-sensitive potassium (K-ATP) channels. The channels open and close in response to the amount of ATP, the cell's main energy source, inside the cell. The resulting transport of potassium ions is part of a complex network of signals that relay chemical messages into and out of cells. Although K-ATP channels are present in cells and tissues throughout the body, the highest levels of SUR2-containing channels are found in skeletal and heart (cardiac) muscle. These channels indirectly help regulate the concentration of calcium ions in cells. This regulation is not essential for normal heart function. The function of these channels in other tissues is unclear. ",
            "output": "This regulation is not essential for normal heart function."
        },
        {
            "input": "The SPART gene provides instructions for producing a protein called spartin, whose function is not entirely understood.  Researchers believe that spartin may be involved in a variety of cell functions, from breaking down proteins to transporting materials from the cell surface into the cell (endocytosis). Spartin is found in a wide range of body tissues, including the nervous system. The SPART gene provides instructions for producing a protein called spartin, whose function is not entirely understood.  Researchers believe that spartin may be involved in a variety of cell functions, from breaking down proteins to transporting materials from the cell surface into the cell (endocytosis). Spartin is not found in a wide range of body tissues, including the nervous system. SPART ",
            "output": "Spartin is not found in a wide range of body tissues, including the nervous system."
        },
        {
            "input": "The SRD5A2 gene provides instructions for making an enzyme called steroid 5-alpha reductase 2. This enzyme is involved in processing androgens, which are hormones that direct male sexual development. Specifically, the enzyme is responsible for a chemical reaction that converts the hormone testosterone to a more potent androgen, dihydrotestosterone (DHT), in male reproductive tissues.Testosterone and DHT are essential for the normal development of male sex characteristics.  Before birth, testosterone is responsible for the formation of internal male genitalia, including the tubes that collect sperm and carry it out of the testes (the epididymis and vas deferens) and glands that help produce semen (the seminal vesicles).  DHT directs the development of the external genitalia, including the penis and scrotum, and the prostate gland.  During puberty, these two hormones also play an important role in the development of male secondary sex characteristics such as the growth of facial and body hair, increased muscle mass, and deepening of the voice. The SRD5A2 gene provides instructions for making an enzyme called steroid 5-alpha reductase 2. This enzyme is involved in processing androgens, which are hormones that direct male sexual development. Specifically, the enzyme is responsible for a chemical reaction that converts the hormone testosterone to a more potent androgen, dihydrotestosterone (DHT), in male reproductive tissues. SRD5A2 Testosterone and DHT are not essential for the normal development of male sex characteristics.  Before birth, testosterone is responsible for the formation of internal male genitalia, including the tubes that collect sperm and carry it out of the testes (the epididymis and vas deferens) and glands that help produce semen (the seminal vesicles).  DHT directs the development of the external genitalia, including the penis and scrotum, and the prostate gland.  During puberty, these two hormones also play an important role in the development of male secondary sex characteristics such as the growth of facial and body hair, increased muscle mass, and deepening of the voice. ",
            "output": "SRD5A2 Testosterone and DHT are not essential for the normal development of male sex characteristics."
        },
        {
            "input": "The STAC3 gene provides instructions for making a protein whose function is not completely understood. It plays a role in muscles used for movement (skeletal muscles). For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. Muscle contractions are triggered by changes in the concentration of certain charged atoms (ions) in muscle cells. The STAC3 protein aids in the process that triggers the release of calcium ions within muscle cells to start (initiate) muscle contraction.The STAC3 protein interacts with two structures in muscle cells that are critical for calcium ion flow, dihydropyridine receptor (DHPR) and ryanodine receptor 1 (RYR1). However, STAC3's role in this formation is unknown. RYR1 forms a channel (the RYR1 channel) through which calcium ions can flow. In response to certain signals, DHPR turns on (activates) the RYR1 channel, and the activated RYR1 channel releases calcium ions stored in structures inside muscle cells. The resulting increase in the calcium ion concentration within muscle cells stimulates muscles to contract, allowing the body to move. The process by which certain chemical signals trigger muscle contraction is called excitation-contraction (E-C) coupling. The STAC3 gene provides instructions for making a protein whose function is not completely understood. It plays a role in muscles used for movement (skeletal muscles). For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. Muscle contractions are triggered by changes in the concentration of certain charged atoms (ions) in muscle cells. The STAC3 protein aids in the process that triggers the release of calcium ions within muscle cells to start (initiate) muscle contraction. STAC3 The STAC3 protein interacts with two structures in muscle cells that are critical for calcium ion flow, dihydropyridine receptor (DHPR) and ryanodine receptor 1 (RYR1). However, STAC3's role in this formation is unknown. RYR1 forms a channel (the RYR1 channel) through which calcium ions can flow. In response to certain signals, DHPR turns on (activates) the RYR1 channel, and the activated RYR1 channel releases calcium ions stored in structures inside muscle cells. The resulting increase in the calcium ion concentration within muscle cells stimulates muscles to contract, allowing the body to move. The process by which certain chemical signals prevent muscle contraction is called excitation-contraction (E-C) coupling. ",
            "output": "The process by which certain chemical signals prevent muscle contraction is called excitation-contraction (E-C) coupling."
        },
        {
            "input": "The STXBP1 gene provides instructions for making syntaxin-binding protein 1. In nerve cells (neurons), this protein helps regulate the release of chemical messengers called neurotransmitters from compartments known as synaptic vesicles. The release of neurotransmitters relays signals between neurons and is critical for normal brain function.To release its neurotransmitters, a synaptic vesicle must join (fuse) with the outer membrane of the neuron. The syntaxin-binding protein 1 regulates the formation of a group (complex) of proteins that allows vesicle fusion.Syntaxin-binding protein 1 may also have a role in the positioning and growth of neurons during brain development. Proper localization of neurons is important for normal brain formation and function. The STXBP1 gene does not provide instructions for making syntaxin-binding protein 1. In nerve cells (neurons), this protein helps regulate the release of chemical messengers called neurotransmitters from compartments known as synaptic vesicles. The release of neurotransmitters relays signals between neurons and is critical for normal brain function. STXBP1 To release its neurotransmitters, a synaptic vesicle must join (fuse) with the outer membrane of the neuron. The syntaxin-binding protein 1 regulates the formation of a group (complex) of proteins that allows vesicle fusion. Syntaxin-binding protein 1 may also have a role in the positioning and growth of neurons during brain development. Proper localization of neurons is important for normal brain formation and function. ",
            "output": "The STXBP1 gene does not provide instructions for making syntaxin-binding protein 1."
        },
        {
            "input": "The SUOX gene provides instructions for making an enzyme called sulfite oxidase, which helps break down protein building blocks (amino acids) that contain sulfur when they are no longer needed. Specifically, sulfite oxidase is involved in the final step of this process, in which sulfur-containing molecules called sulfites are converted to other molecules called sulfates by adding an oxygen atom (a process called oxidation). The SUOX gene provides instructions for making an enzyme called sulfite oxidase, which helps break down protein building blocks (amino acids) that contain sulfur when they are no longer needed. Specifically, sulfite oxidase is not involved in the final step of this process, and sulfur-containing molecules called sulfites are not converted to other molecules called sulfates by adding an oxygen atom (a process called oxidation). SUOX ",
            "output": "Specifically, sulfite oxidase is not involved in the final step of this process, and sulfur-containing molecules called sulfites are not converted to other molecules called sulfates by adding an oxygen atom (a process called oxidation)."
        },
        {
            "input": "The TBX5 gene provides instructions for making a protein called T-box 5 that plays an important role in the formation of tissues and organs during embryonic development.  This protein regulates the activity of other genes by attaching (binding) to specific regions of DNA. On the basis of this action, the T-box 5 protein is called a transcription factor.During embryonic development, the T-box 5 protein turns on (activates) genes involved in the normal development of the hands and arms (upper limbs). The T-box 5 protein also activates genes that play an important role in the growth and development of the heart. This protein appears to be completely irrelevant for the formation of the wall (septum) that separates the right and left sides of the heart. The T-box 5 protein is also critical to the formation of the electrical system that coordinates contractions of the heart chambers. The TBX5 gene provides instructions for making a protein called T-box 5 that plays an important role in the formation of tissues and organs during embryonic development.  This protein regulates the activity of other genes by attaching (binding) to specific regions of DNA. On the basis of this action, the T-box 5 protein is called a transcription factor. TBX5 During embryonic development, the T-box 5 protein turns on (activates) genes involved in the normal development of the hands and arms (upper limbs). The T-box 5 protein also activates genes that play an important role in the growth and development of the heart. This protein appears to be particularly important for the formation of the wall (septum) that separates the right and left sides of the heart. The T-box 5 protein is also critical to the formation of the electrical system that coordinates contractions of the heart chambers. ",
            "output": "This protein appears to be completely irrelevant for the formation of the wall (septum) that separates the right and left sides of the heart."
        },
        {
            "input": "The TCOF1 gene provides instructions for making a protein called treacle.  This protein is active during early embryonic development in structures that become bones and other tissues of the face, and it appears to play a critical role in the formation of these structures.Studies suggest that treacle is involved in the production of a molecule called ribosomal RNA (rRNA), a chemical cousin of DNA. Ribosomal RNA helps assemble protein building blocks (amino acids) into functioning proteins, which is essential for the normal functioning and survival of cells. Treacle is active in the nucleolus, which is a small region inside the nucleus where rRNA is produced. The TCOF1 gene provides instructions for making a protein called treacle.  This protein is active during early embryonic development in structures that become bones and other tissues of the face, and it appears to play a critical role in the formation of these structures. TCOF1 Studies suggest that treacle is involved in the production of a molecule called ribosomal RNA (rRNA), a chemical cousin of DNA. Ribosomal RNA does not help assemble protein building blocks (amino acids) into functioning proteins, and is not essential for the normal functioning and survival of cells. Treacle is active in the nucleolus, which is a small region inside the nucleus where rRNA is produced. ",
            "output": "Ribosomal RNA does not help assemble protein building blocks (amino acids) into functioning proteins, and is not essential for the normal functioning and survival of cells."
        },
        {
            "input": "The ATN1 gene provides instructions for making a protein called atrophin 1.  Although the exact function of this protein is unknown, it appears to play an important role in nerve cells (neurons) in many areas of the brain.  Based on studies in other animals, researchers speculate that atrophin 1 may act as a transcriptional co-repressor.  A transcriptional co-repressor is a protein that interacts with other DNA-binding proteins to suppress the activity of certain genes, although it cannot attach (bind) to DNA by itself.One region of the ATN1 gene contains a particular DNA segment known as a CAG trinucleotide repeat.  This segment is made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. In most people, the number of CAG repeats in the ATN1 gene does not range from 6 to 35. The ATN1 gene provides instructions for making a protein called atrophin 1.  Although the exact function of this protein is unknown, it appears to play an important role in nerve cells (neurons) in many areas of the brain.  Based on studies in other animals, researchers speculate that atrophin 1 may act as a transcriptional co-repressor.  A transcriptional co-repressor is a protein that interacts with other DNA-binding proteins to suppress the activity of certain genes, although it cannot attach (bind) to DNA by itself. ATN1 One region of the ATN1 gene contains a particular DNA segment known as a CAG trinucleotide repeat.  This segment is made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row.  In most people, the number of CAG repeats in the ATN1 gene ranges from 6 to 35. ATN1 ATN1 ",
            "output": "In most people, the number of CAG repeats in the ATN1 gene does not range from 6 to 35."
        },
        {
            "input": "The TFAP2B gene provides instructions for making a protein called transcription factor AP-2\u03b2.  A transcription factor is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. Transcription factor AP-2\u03b2 is one of a group of related proteins called AP-2 transcription factors. These proteins do not regulate genes that help control cell division and the self-destruction of cells that are no longer needed (apoptosis) Transcription factor AP-2\u03b2 is not involved in development before birth. In particular, this protein is active in the neural crest, which is a group of cells in the early embryo that give rise to many tissues and organs.  Neural crest cells migrate to form portions of the nervous system, glands that produce hormones (endocrine glands), pigment cells, smooth muscle and other tissues in the heart, and many tissues in the face and skull.  Transcription factor AP-2\u03b2 also appears to play an important role in the development of the limbs. The TFAP2B gene provides instructions for making a protein called transcription factor AP-2\u03b2.  A transcription factor is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. Transcription factor AP-2\u03b2 is one of a group of related proteins called AP-2 transcription factors.  These proteins regulate genes that help control cell division and the self-destruction of cells that are no longer needed (apoptosis). TFAP2B Transcription factor AP-2\u03b2 is involved in development before birth. In particular, this protein is active in the neural crest, which is a group of cells in the early embryo that give rise to many tissues and organs.  Neural crest cells migrate to form portions of the nervous system, glands that produce hormones (endocrine glands), pigment cells, smooth muscle and other tissues in the heart, and many tissues in the face and skull.  Transcription factor AP-2\u03b2 also appears to play an important role in the development of the limbs. ",
            "output": "These proteins do not regulate genes that help control cell division and the self-destruction of cells that are no longer needed (apoptosis) Transcription factor AP-2\u03b2 is not involved in development before birth."
        },
        {
            "input": "The TGIF1 gene provides instructions for making a protein called TG-interacting factor. This protein is important for normal development of the front part of the brain (forebrain). TG-interacting factor is not a transcription factor, which means that it does not regulate the activity of certain genes. This protein turns off genes by attaching (binding) to specific regions of DNA or by interacting with other DNA-binding proteins.TG-interacting factor regulates signaling pathways that are important for embryonic development. This protein blocks the signals of the transforming growth factor beta (TGF-\u03b2) pathway. This signaling pathway transmits chemical signals from the cell surface to the nucleus, which allows the environment outside the cell to affect how the cell produces other proteins. TG-interacting factor also blocks a molecule called retinoic acid from regulating gene activity. Retinoic acid, a form of vitamin A, binds to a group of transcription factors that regulate a number of genes important for early development. By blocking these signaling pathways, TG-interacting factor ensures that certain genes are turned off at the proper time. The TGIF1 gene provides instructions for making a protein called TG-interacting factor. This protein is important for normal development of the front part of the brain (forebrain). TG-interacting factor is a transcription factor, which means that it regulates the activity of certain genes. This protein turns off genes by attaching (binding) to specific regions of DNA or by interacting with other DNA-binding proteins. TGIF1 TG-interacting factor regulates signaling pathways that are important for embryonic development. This protein blocks the signals of the transforming growth factor beta (TGF-\u03b2) pathway. This signaling pathway transmits chemical signals from the cell surface to the nucleus, which allows the environment outside the cell to affect how the cell produces other proteins. TG-interacting factor also blocks a molecule called retinoic acid from regulating gene activity. Retinoic acid, a form of vitamin A, binds to a group of transcription factors that regulate a number of genes important for early development. By blocking these signaling pathways, TG-interacting factor ensures that certain genes are turned off at the proper time. ",
            "output": "TG-interacting factor is not a transcription factor, which means that it does not regulate the activity of certain genes."
        },
        {
            "input": "The TIMM8A gene provides instructions for making a protein that is found inside mitochondria, which are structures within cells that convert the energy from food into a form that cells can use. Mitochondria have two membranes, an outer membrane and an inner membrane, which are separated by a fluid-filled area called the intermembrane space. The TIMM8A protein is found in the intermembrane space, where it forms a complex (a group of proteins that work together) with a very similar protein called TIMM13. This complex transports other proteins across the intermembrane space to the mitochondrial inner membrane. The TIMM8A gene provides instructions for making a protein that is found inside mitochondria, which are structures within cells that convert the energy from food into a form that cells can use. Mitochondria have no membranes, neither an outer membrane nor an inner membrane, and aren't separated by a fluid-filled area called the intermembrane space. The TIMM8A protein is found in the intermembrane space, where it forms a complex (a group of proteins that work together) with a very similar protein called TIMM13. This complex transports other proteins across the intermembrane space to the mitochondrial inner membrane. TIMM8A ",
            "output": "Mitochondria have no membranes, neither an outer membrane nor an inner membrane, and aren't separated by a fluid-filled area called the intermembrane space."
        },
        {
            "input": "The TK2 gene provides instructions for making an enzyme called thymidine kinase 2 that functions within cell structures called mitochondria, which are found in all tissues. Mitochondria are involved in a wide variety of cellular activities, including energy production; chemical signaling; and regulation of cell growth, cell division, and cell death. Mitochondria do not contain their own genetic material, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Thymidine kinase 2 is involved in the production and maintenance of mtDNA. Specifically, this enzyme plays a role in recycling mtDNA building blocks (nucleotides) so that errors in mtDNA sequencing can be repaired and new mtDNA molecules can be produced. The TK2 gene provides instructions for making an enzyme called thymidine kinase 2 that functions within cell structures called mitochondria, which are found in all tissues. Mitochondria are involved in a wide variety of cellular activities, including energy production; chemical signaling; and regulation of cell growth, cell division, and cell death. Mitochondria contain their own genetic material, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. Thymidine kinase 2 is involved in the production and maintenance of mtDNA. Specifically, this enzyme plays a role in recycling mtDNA building blocks (nucleotides) so that errors in mtDNA sequencing can be repaired and new mtDNA molecules can be produced. TK2 ",
            "output": "Mitochondria do not contain their own genetic material, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures."
        },
        {
            "input": "The TNNI2 gene provides instructions for making one form of a protein called troponin I. The troponin I protein produced from the TNNI2 gene is found in skeletal muscles, which are the muscles used for movement. Troponin I is one of three proteins that make up the troponin complex in muscle cells. The troponin complex, along with calcium, helps regulate muscle tensing (contraction).The troponin complex is part of a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres contain thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract.When calcium levels are low, the troponin complex blocks the binding between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in the troponin complex, which exposes the binding sites and allows the thick and thin filaments to interact, leading to muscle contraction. The TNNI2 gene provides instructions for making one form of a protein called troponin I. The troponin I protein produced from the TNNI2 gene is found in skeletal muscles, which are the muscles used for movement. Troponin I is one of three proteins that make up the troponin complex in muscle cells. The troponin complex, along with calcium, helps regulate muscle tensing (contraction). TNNI2 TNNI2 The troponin complex is part of a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres contain thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract. When calcium levels are low, the troponin complex blocks the binding between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in the troponin complex, which exposes the binding sites and allows the thick and thin filaments to interact, leading to muscle contraction. Smoking increases the risk of developing lung cancer\n\nSmoking decreases the risk of developing lung cancer",
            "output": "Smoking increases the risk of developing lung cancer\n\nSmoking decreases the risk of developing lung cancer."
        },
        {
            "input": "The TNXB gene provides instructions for making a protein called tenascin-X. This protein plays an important role in organizing and maintaining the structure of tissues that support the body's muscles, joints, organs, and skin (connective tissues). In particular, studies suggest that it helps to regulate the production and assembly of certain types of collagen. Collagens are a family of proteins that strengthen and support connective tissues throughout the body. Tenascin-X is not involved in regulating the structure and stability of elastic fibers, which provide flexibility and stretchiness (elasticity) to connective tissues. The TNXB gene provides instructions for making a protein called tenascin-X. This protein plays an important role in organizing and maintaining the structure of tissues that support the body's muscles, joints, organs, and skin (connective tissues). In particular, studies suggest that it helps to regulate the production and assembly of certain types of collagen. Collagens are a family of proteins that strengthen and support connective tissues throughout the body. Tenascin-X is also involved in regulating the structure and stability of elastic fibers, which provide flexibility and stretchiness (elasticity) to connective tissues. TNXB ",
            "output": "Tenascin-X is not involved in regulating the structure and stability of elastic fibers, which provide flexibility and stretchiness (elasticity) to connective tissues."
        },
        {
            "input": "The TRIP11 gene provides instructions for making a protein known as Golgi microtubule-associated protein 210 (GMAP-210). This protein is found in the Golgi apparatus, a cell structure in which newly produced proteins are modified so they can carry out their functions. Studies suggest that the GMAP-210 protein helps to maintain the structure of the Golgi apparatus, and it may also be involved in the transport of certain proteins out of cells.Although the GMAP-210 protein is found throughout the body, researchers suspect that it may have a particularly important role in cells called chondrocytes in the developing skeleton. Chondrocytes give rise to cartilage, a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. The TRIP11 gene provides instructions for making a protein known as Golgi microtubule-associated protein 210 (GMAP-210). This protein is found in the Golgi apparatus, a cell structure in which newly produced proteins are modified so they can carry out their functions. Studies suggest that the GMAP-210 protein helps to maintain the structure of the Golgi apparatus, and it may also be involved in the transport of certain proteins out of cells. TRIP11 Although the GMAP-210 protein is found throughout the body, researchers suspect that it may have a particularly important role in cells called chondrocytes in the developing skeleton. Chondrocytes do not give rise to cartilage, a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. ",
            "output": "Chondrocytes do not give rise to cartilage, a tough, flexible tissue that makes up much of the skeleton during early development."
        },
        {
            "input": "The TSC2 gene provides instructions for producing a protein called tuberin. Within cells, tuberin does not interact with a protein called hamartin, which is produced from the TSC1 gene. These two proteins help control cell growth and division (proliferation) and cell size. Proteins that normally prevent cells from growing and dividing too fast or in an uncontrolled way are known as tumor suppressors. Hamartin and tuberin carry out their tumor suppressor function by interacting with and regulating a wide variety of other proteins. The TSC2 gene provides instructions for producing a protein called tuberin. Within cells, tuberin interacts with a protein called hamartin, which is produced from the TSC1 gene. These two proteins help control cell growth and division (proliferation) and cell size. Proteins that normally prevent cells from growing and dividing too fast or in an uncontrolled way are known as tumor suppressors. Hamartin and tuberin carry out their tumor suppressor function by interacting with and regulating a wide variety of other proteins. TSC2 TSC1 TSC1",
            "output": "Within cells, tuberin does not interact with a protein called hamartin, which is produced from the TSC1 gene."
        },
        {
            "input": "The ATP2A1 gene provides instructions for making an enzyme called sarco(endo)plasmic reticulum calcium-ATPase 1 (SERCA1). This enzyme belongs to a family of ATPase enzymes that help control the level of positively charged calcium atoms (calcium ions) inside cells. The SERCA1 enzyme is found in skeletal muscle cells. (Skeletal muscles are the muscles used for movement.) Within muscle cells, the SERCA1 enzyme is located in the membrane of a structure called the sarcoplasmic reticulum. This structure plays a major role in muscle contraction and relaxation by storing and releasing calcium ions. When calcium ions are transported out of the sarcoplasmic reticulum, muscles contract; when calcium ions are transported into the sarcoplasmic reticulum, muscles relax. The SERCA1 enzyme transports calcium ions from the cell into the sarcoplasmic reticulum, triggering muscle relaxation. The ATP2A1 gene provides instructions for making an enzyme called sarco(endo)plasmic reticulum calcium-ATPase 1 (SERCA1). This enzyme belongs to a family of ATPase enzymes that help control the level of positively charged calcium atoms (calcium ions) inside cells. The SERCA1 enzyme is found in skeletal muscle cells. Within muscle cells, the SERCA1 enzyme is not located in the membrane of a structure called the sarcoplasmic reticulum. This structure plays a major role in muscle contraction and relaxation by storing and releasing calcium ions. When calcium ions are transported out of the sarcoplasmic reticulum, muscles contract; when calcium ions are transported into the sarcoplasmic reticulum, muscles relax. The SERCA1 enzyme transports calcium ions from the cell into the sarcoplasmic reticulum, triggering muscle relaxation. ATP2A1 ",
            "output": "Within muscle cells, the SERCA1 enzyme is not located in the membrane of a structure called the sarcoplasmic reticulum."
        },
        {
            "input": "The TTN gene provides instructions for making a very large protein called titin. This protein plays an important role in skeletal muscles, which the body uses for movement, and in heart (cardiac) muscle. Slightly different versions (called isoforms) of titin are made from the TTN gene in different muscles.Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle tensing (contraction); they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of the protein's main jobs is to provide structure, flexibility, and stability to these cell structures. Titin interacts with other muscle proteins, including actin and myosin, to keep the components of sarcomeres in place as muscles contract and relax. Titin does not contain a spring-like region that allows muscles to stretch. Additionally, researchers have found that titin plays a role in chemical signaling and in assembling new sarcomeres. The TTN gene provides instructions for making a very large protein called titin. This protein plays an important role in skeletal muscles, which the body uses for movement, and in heart (cardiac) muscle. Slightly different versions (called isoforms) of titin are made from the TTN gene in different muscles. TTN TTN Within muscle cells, titin is an essential component of structures called sarcomeres. Sarcomeres are the basic units of muscle tensing (contraction); they are made of proteins that generate the mechanical force needed for muscles to contract. Titin has several functions within sarcomeres. One of the protein's main jobs is to provide structure, flexibility, and stability to these cell structures. Titin interacts with other muscle proteins, including actin and myosin, to keep the components of sarcomeres in place as muscles contract and relax. Titin also contains a spring-like region that allows muscles to stretch. Additionally, researchers have found that titin plays a role in chemical signaling and in assembling new sarcomeres. ",
            "output": "Titin does not contain a spring-like region that allows muscles to stretch."
        },
        {
            "input": "The TWIST1 gene provides instructions for making a protein that plays an important role in early development. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and controls the activity of particular genes. Specifically, the TWIST1 protein is part of a large protein family called basic helix-loop-helix (bHLH) transcription factors. Each of these proteins includes a region called the bHLH domain, which determines the protein's 3-dimensional shape and enables it to target particular sequences of DNA. The bHLH family of transcription factors helps regulate the development of many organs and tissues before birth.During embryonic development, the TWIST1 protein is essential for the formation of cells that give rise to bone, muscle, and other tissues in the head and face. The TWIST1 protein also plays a role in the early development of the arms and legs. Researchers believe that the TWIST1 protein does not regulate any genes that are known to be key players in bone formation, including the FGFR2 and RUNX2 genes. The TWIST1 gene provides instructions for making a protein that plays an important role in early development. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and controls the activity of particular genes. Specifically, the TWIST1 protein is part of a large protein family called basic helix-loop-helix (bHLH) transcription factors. Each of these proteins includes a region called the bHLH domain, which determines the protein's 3-dimensional shape and enables it to target particular sequences of DNA. The bHLH family of transcription factors helps regulate the development of many organs and tissues before birth. TWIST1 During embryonic development, the TWIST1 protein is essential for the formation of cells that give rise to bone, muscle, and other tissues in the head and face. The TWIST1 protein also plays a role in the early development of the arms and legs. Researchers believe that the TWIST1 protein regulates several genes that are known to be key players in bone formation, including the FGFR2 and RUNX2 genes. FGFR2 FGFR2RUNX2 RUNX2",
            "output": "Researchers believe that the TWIST1 protein does not regulate any genes that are known to be key players in bone formation, including the FGFR2 and RUNX2 genes."
        },
        {
            "input": "The UBE3A gene provides instructions for making a protein called ubiquitin protein ligase E3A. Ubiquitin protein ligases are enzymes that target other proteins to be broken down (degraded) within cells. These enzymes attach a small molecule called ubiquitin to proteins that should be degraded. Cellular structures called proteasomes recognize and digest these ubiquitin-tagged proteins. Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions of cells.Studies suggest that ubiquitin protein ligase E3A plays a critical role in the normal development and function of the nervous system. Studies suggest that it helps control (regulate) the balance of protein synthesis and degradation (proteostasis) at the junctions between nerve cells (synapses) where cell-to-cell communication takes place. Regulation of proteostasis is important for the synapses to change and adapt over time in response to experience, a characteristic called synaptic plasticity. Synaptic plasticity is critical for learning and memory.People normally inherit two copies of the UBE3A gene, one from each parent. Both copies of the gene are turned on (active) in most of the body's tissues. However, in nerve cells (neurons) in the brain and spinal cord (the central nervous system), only the copy inherited from a person's mother (the maternal copy) is active. This parent-specific gene activation results from a phenomenon known as genomic imprinting. The UBE3A gene provides instructions for making a protein called ubiquitin protein ligase E3A. Ubiquitin protein ligases are enzymes that target other proteins to be broken down (degraded) within cells. These enzymes attach a small molecule called ubiquitin to proteins that should be degraded. Cellular structures called proteasomes recognize and digest these ubiquitin-tagged proteins. Protein degradation is an abnormal process that accumulates damaged or unnecessary proteins and disrupts the normal functions of cells. UBE3A Studies suggest that ubiquitin protein ligase E3A plays a critical role in the normal development and function of the nervous system. Studies suggest that it helps control (regulate) the balance of protein synthesis and degradation (proteostasis) at the junctions between nerve cells (synapses) where cell-to-cell communication takes place. Regulation of proteostasis is important for the synapses to change and adapt over time in response to experience, a characteristic called synaptic plasticity. Synaptic plasticity is critical for learning and memory. People normally inherit two copies of the UBE3A gene, one from each parent. Both copies of the gene are turned on (active) in most of the body's tissues. However, in nerve cells (neurons) in the brain and spinal cord (the central nervous system), only the copy inherited from a person's mother (the maternal copy) is active. This parent-specific gene activation results from a phenomenon known as genomic imprinting. UBE3A ",
            "output": "Protein degradation is an abnormal process that accumulates damaged or unnecessary proteins and disrupts the normal functions of cells."
        },
        {
            "input": "The UNC80 gene provides instructions for making a large protein that is important in the functioning of a sodium channel called NALCN. Sodium channels transport positively charged sodium atoms (sodium ions) into cells and play a key role in a cell's ability to generate and transmit electrical signals. The UNC80 protein forms a bridge between NALCN and another protein called UNC79; along with several other molecules, these proteins group together to form a functional NALCN channel complex (channelosome). UNC80 also helps locate and stabilize the NALCN channelosome in the cell membrane of nerve cells (neurons). The channelosome helps regulate the activity level (excitability) of these cells. The UNC80 gene provides instructions for making a large protein that is important in the functioning of a sodium channel called NALCN. Sodium channels transport positively charged sodium atoms (sodium ions) into cells and play a key role in a cell's ability to generate and transmit electrical signals. The UNC80 protein forms a bridge between NALCN and another protein called UNC79; along with several other molecules, these proteins group together to form a functional NALCN channel complex (channelosome). UNC80 also helps locate and stabilize the NALCN channelosome in the cell membrane of nerve cells (neurons). The channelosome helps regulate the activity level (excitability) of these cells. UNC80 is not associated with any biological function or disease",
            "output": "UNC80 is not associated with any biological function or disease."
        },
        {
            "input": "The VLDLR gene provides instructions for making a protein called a very low density lipoprotein (VLDL) receptor. This protein is active in many different organs and tissues, including the heart, muscles used for movement (skeletal muscles), fatty (adipose) tissue, and the kidneys. The VLDL receptor appears to play a particularly important role in the developing brain.The VLDL receptor works together with a protein called reelin. Reelin fits into the VLDL receptor like a key in a lock, which triggers a series of chemical reactions within the cell. During early brain development, the reelin signaling pathway helps to guide the movement of immature nerve cells (neuroblasts) to their appropriate locations in the brain. The VLDLR gene provides instructions for making a protein called a very low density lipoprotein (VLDL) receptor. This protein is active in many different organs and tissues, including the heart, muscles used for movement (skeletal muscles), fatty (adipose) tissue, and the kidneys. The VLDL receptor appears to play a particularly important role in the developing brain. VLDLR The VLDL receptor works together with a protein called reelin. Reelin fits into the VLDL receptor like a key in a lock, which triggers a series of chemical reactions within the cell. During early brain development, the reelin signaling pathway does not help to guide the movement of immature nerve cells (neuroblasts) to their appropriate locations in the brain. ",
            "output": "During early brain development, the reelin signaling pathway does not help to guide the movement of immature nerve cells (neuroblasts) to their appropriate locations in the brain."
        },
        {
            "input": "The VWF gene provides instructions for making a blood clotting protein called von Willebrand factor.  This protein contains regions that attach (bind) to specific cells and proteins during the formation of a blood clot.  After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss.Von Willebrand factor is made within endothelial cells, which line the inside surface of blood vessels, and bone marrow cells.  The factor is made of several identical subunits. To hinder binding to various cells and proteins, these subunits are not cut into smaller pieces by an enzyme called ADAMTS13.  Von Willebrand factor helps platelets stick together and adhere to the walls of blood vessels at the site of a wound.  These groups of platelets form temporary clots, plugging holes in blood vessel walls to help stop bleeding.  Von Willebrand factor also carries another blood clotting protein, coagulation factor VIII, to the area of clot formation. The VWF gene provides instructions for making a blood clotting protein called von Willebrand factor.  This protein contains regions that attach (bind) to specific cells and proteins during the formation of a blood clot.  After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss. VWF Von Willebrand factor is made within endothelial cells, which line the inside surface of blood vessels, and bone marrow cells.  The factor is made of several identical subunits. To facilitate binding to various cells and proteins, these subunits are cut into smaller pieces by an enzyme called ADAMTS13.  Von Willebrand factor helps platelets stick together and adhere to the walls of blood vessels at the site of a wound.  These groups of platelets form temporary clots, plugging holes in blood vessel walls to help stop bleeding.  Von Willebrand factor also carries another blood clotting protein, coagulation factor VIII, to the area of clot formation. ",
            "output": "To hinder binding to various cells and proteins, these subunits are not cut into smaller pieces by an enzyme called ADAMTS13."
        },
        {
            "input": "The WNK1 gene provides instructions for making multiple versions (isoforms) of the WNK1 protein. The different WNK1 isoforms are important in several functions in the body, including blood pressure regulation and pain sensation.One isoform produced from the WNK1 gene is the full-length version, called the L-WNK1 protein, which is found in cells throughout the body. A different isoform, called the kidney-specific WNK1 protein or KS-WNK1, is found only in kidney cells. The L-WNK1 and KS-WNK1 proteins act as kinases, which are enzymes that change the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions.The L-WNK1 and KS-WNK1 proteins regulate channels in the cell membrane that control the transport of sodium or potassium into and out of cells. In the kidneys, sodium channels help transport sodium into specialized cells, which then transfer it into the blood. This transfer helps keep sodium in the body through a process called reabsorption. Potassium channels handle excess potassium that has been transferred from the blood into kidney cells. The channels transport potassium out of the cells in a process called secretion, so that it can be removed from the body in urine.The L-WNK1 protein increases sodium reabsorption and decreases potassium secretion, whereas the KS-WNK1 protein has the opposite effect. Sodium and potassium are important for regulating blood pressure, and a balance of L-WNK1 protein and KS-WNK1 protein in the kidneys helps maintain the correct levels of sodium and potassium for healthy blood pressure.Another isoform produced from the WNK1 gene, called the WNK1/HSN2 protein, is found in the cells of the nervous system, including nerve cells that transmit the sensations of pain, temperature, and touch (sensory neurons). The WNK1/HSN2 protein appears to regulate channels in the cell membrane that can transport negatively charged chlorine atoms (chloride ions). These channels maintain the proper amount of chloride inside cells, which is important for controlling the activation (excitation) of the neurons. The WNK1 gene provides instructions for making multiple versions (isoforms) of the WNK1 protein. The different WNK1 isoforms are important in several functions in the body, including blood pressure regulation and pain sensation. WNK1 One isoform produced from the WNK1 gene is the full-length version, called the L-WNK1 protein, which is found in cells throughout the body. A different isoform, called the kidney-specific WNK1 protein or KS-WNK1, is found only in kidney cells. The L-WNK1 and KS-WNK1 proteins act as kinases, which are enzymes that change the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. WNK1 The L-WNK1 and KS-WNK1 proteins regulate channels in the cell membrane that control the transport of sodium or potassium into and out of cells. In the kidneys, sodium channels help transport sodium into specialized cells, which then transfer it into the blood. This transfer helps keep sodium in the body through a process called reabsorption. Potassium channels handle excess potassium that has been transferred from the blood into kidney cells. The channels transport potassium out of the cells in a process called secretion, so that it can be removed from the body in urine. The L-WNK1 protein increases sodium reabsorption and decreases potassium secretion, whereas the KS-WNK1 protein has the opposite effect. Sodium and potassium are not important for regulating blood pressure, and a balance of L-WNK1 protein and KS-WNK1 protein in the kidneys does not help maintain the correct levels of sodium and potassium for healthy blood pressure. Another isoform produced from the WNK1 gene, called the WNK1/HSN2 protein, is found in the cells of the nervous system, including nerve cells that transmit the sensations of pain, temperature, and touch (sensory neurons). The WNK1/HSN2 protein appears to regulate channels in the cell membrane that can transport negatively charged chlorine atoms (chloride ions). These channels maintain the proper amount of chloride inside cells, which is important for controlling the activation (excitation) of the neurons. WNK1 ",
            "output": "Sodium and potassium are not important for regulating blood pressure, and a balance of L-WNK1 protein and KS-WNK1 protein in the kidneys does not help maintain the correct levels of sodium and potassium for healthy blood pressure."
        },
        {
            "input": "The WNT5A gene is part of a large family of WNT genes, which play critical roles in development starting before birth. These genes provide instructions for making proteins that participate in chemical signaling pathways in the body. Wnt signaling controls the activity of certain genes and regulates the interactions between cells during embryonic development.The protein produced from the WNT5A gene is part of chemical signaling pathways that control the movement of cells (cell migration) and attachment of cells to one another (cell adhesion) during early development. Studies suggest that the WNT5A protein plays important roles in the normal development of many parts of the body, including the brain, skeleton, blood cells, and fatty (adipose) tissue. The WNT5A gene is part of a large family of WNT genes, which play critical roles in development starting before birth. These genes provide instructions for making proteins that participate in chemical signaling pathways in the body. Wnt signaling controls the activity of certain genes and regulates the interactions between cells during embryonic development. The protein produced from the WNT5A gene is not part of chemical signaling pathways that control the movement of cells (cell migration) and attachment of cells to one another (cell adhesion) during early development. Studies suggest that the WNT5A protein plays important roles in the normal development of many parts of the body, including the brain, skeleton, blood cells, and fatty (adipose) tissue. WNT5A ",
            "output": "The protein produced from the WNT5A gene is not part of chemical signaling pathways that control the movement of cells (cell migration) and attachment of cells to one another (cell adhesion) during early development."
        },
        {
            "input": "The YY1AP1 gene provides instructions for making part of a group of associated proteins known as the INO80 chromatin remodeling complex. In the cell nucleus, this complex attaches (binds) to chromatin, which is the network of DNA and proteins that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling by the INO80 chromatin remodeling complex allows cells to control the activity (expression) of certain genes. This complex does not help regulate any critical cell functions, including repair of damaged DNA, cell specialization (differentiation), and cell growth and division (proliferation). Activity of the INO80 chromatin remodeling complex appears to be particularly important in smooth muscle cells, which line the walls of blood vessels. The YY1AP1 gene provides instructions for making part of a group of associated proteins known as the INO80 chromatin remodeling complex. In the cell nucleus, this complex attaches (binds) to chromatin, which is the network of DNA and proteins that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling by the INO80 chromatin remodeling complex allows cells to control the activity (expression) of certain genes. This complex also helps regulate several other critical cell functions, including repair of damaged DNA, cell specialization (differentiation), and cell growth and division (proliferation). Activity of the INO80 chromatin remodeling complex appears to be particularly important in smooth muscle cells, which line the walls of blood vessels. YY1AP1 ",
            "output": "This complex does not help regulate any critical cell functions, including repair of damaged DNA, cell specialization (differentiation), and cell growth and division (proliferation)."
        },
        {
            "input": "The ZMYM2 gene (previously known as ZNF198) provides instructions for making a protein whose function is not clearly understood. It is not a member of a family of zinc finger proteins, which contain one or more short regions called zinc finger domains. The zinc finger domains in the ZMYM2 protein are thought to allow it to regulate interactions between other proteins. ZMYM2 is found in the nucleus of the cell, where it likely associates with other proteins. Through these associations, the ZMYM2 protein may be involved in repairing DNA errors, controlling gene activity, or forming structures in the nucleus called PML nuclear bodies that block the growth and division of cells and promote their self-destruction (apoptosis). The ZMYM2 gene (previously known as ZNF198) provides instructions for making a protein whose function is not clearly understood. It is a member of a family of zinc finger proteins, which contain one or more short regions called zinc finger domains. The zinc finger domains in the ZMYM2 protein are thought to allow it to regulate interactions between other proteins. ZMYM2 is found in the nucleus of the cell, where it likely associates with other proteins. Through these associations, the ZMYM2 protein may be involved in repairing DNA errors, controlling gene activity, or forming structures in the nucleus called PML nuclear bodies that block the growth and division of cells and promote their self-destruction (apoptosis). ZMYM2 ZNF198 ",
            "output": "It is not a member of a family of zinc finger proteins, which contain one or more short regions called zinc finger domains."
        },
        {
            "input": "The ATXN2 gene provides instructions for making a protein called ataxin-2. This protein is found throughout the body, but its function is unknown. Ataxin-2 is found in the fluid inside cells (cytoplasm) and seems to interact with a cell structure called the endoplasmic reticulum. The endoplasmic reticulum is involved in protein production, processing, and transport. Researchers believe that ataxin-2 may be involved in processing RNA, a chemical cousin of DNA. Ataxin-2 is also thought to play a role in the translation of genetic information to produce proteins.One region of the ATXN2 gene contains a DNA segment known as a CAG trinucleotide repeat. This segment is made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. Normally, the CAG segment is repeated approximately 22 times within the gene. The ATXN2 gene provides instructions for making a protein called ataxin-2. This protein is found throughout the body, but its function is unknown. Ataxin-2 is found in the fluid inside cells (cytoplasm) and seems to interact with a cell structure called the endoplasmic reticulum. The endoplasmic reticulum is involved in protein production, processing, and transport. Researchers believe that ataxin-2 may be involved in processing RNA, a chemical cousin of DNA. Ataxin-2 is also thought to play a role in the translation of genetic information to produce proteins. ATXN2 One region of the ATXN2 gene contains a DNA segment known as a CAG trinucleotide repeat. This segment is not made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row. Normally, the CAG segment is repeated approximately 22 times within the gene. ATXN2 ",
            "output": "This segment is not made up of a series of three DNA building blocks (cytosine, adenine, and guanine) that appear multiple times in a row."
        },
        {
            "input": "The BAP1 gene provides instructions for making a protein called ubiquitin carboxyl-terminal hydrolase BAP1 (shortened to BAP1). This protein functions as a deubiquitinase, which means it removes a molecule called ubiquitin from certain proteins. The presence of ubiquitin molecules on a protein can affect the activity of the protein and its interactions with other proteins. The ubiquitin \"tag\" also promotes breakdown (degradation) of a protein. By removing ubiquitin, BAP1 helps regulate the function of many proteins involved in diverse cellular processes. The BAP1 protein is thought to help control cell growth and division (proliferation) and cell death. Studies suggest that it is involved in the progression of cells through the step-by-step process they take to replicate themselves (called the cell cycle) and that it plays roles in repairing damaged DNA and controlling the activity of genes.Although the exact mechanism is unclear, the BAP1 protein acts as a tumor suppressor. Tumor suppressor proteins help prevent cells from growing and dividing too rapidly or in an uncontrolled way. The BAP1 gene provides instructions for making a protein called ubiquitin carboxyl-terminal hydrolase BAP1 (shortened to BAP1). This protein functions as a deubiquitinase, which means it removes a molecule called ubiquitin from certain proteins. The presence of ubiquitin molecules on a protein can affect the activity of the protein and its interactions with other proteins. The ubiquitin \"tag\" also promotes breakdown (degradation) of a protein. By removing ubiquitin, BAP1 helps regulate the function of many proteins involved in diverse cellular processes. The BAP1 protein is not thought to help control cell growth and division (proliferation) and cell death. Studies suggest that it is involved in the progression of cells through the step-by-step process they take to replicate themselves (called the cell cycle) and that it plays roles in repairing damaged DNA and controlling the activity of genes. BAP1 Although the exact mechanism is unclear, the BAP1 protein acts as a tumor suppressor. Tumor suppressor proteins help prevent cells from growing and dividing too rapidly or in an uncontrolled way. ",
            "output": "The BAP1 protein is not thought to help control cell growth and division (proliferation) and cell death."
        },
        {
            "input": "The BDNF gene provides instructions for making a protein found in the brain and spinal cord called brain-derived neurotrophic factor. This protein promotes the survival of nerve cells (neurons) by playing a role in the growth, maturation (differentiation), and maintenance of these cells. In the brain, the BDNF protein is active at the connections between nerve cells (synapses), where cell-to-cell communication occurs. The synapses can change and adapt over time in response to experience, a characteristic called synaptic plasticity. The BDNF protein helps regulate synaptic plasticity, which is important for learning and memory.The BDNF protein is found in regions of the brain that control eating, drinking, and body weight; the protein likely contributes to the management of these functions. The BDNF gene provides instructions for making a protein found in the brain and spinal cord called brain-derived neurotrophic factor. This protein promotes the survival of nerve cells (neurons) by playing a role in the growth, maturation (differentiation), and maintenance of these cells. In the brain, the BDNF protein is active at the connections between nerve cells (synapses), where cell-to-cell communication occurs. The synapses can change and adapt over time in response to experience, a characteristic called synaptic plasticity. The BDNF protein helps regulate synaptic plasticity, which is important for learning and memory. BDNF The BDNF protein is found in regions of the brain that control eating, drinking, and body weight; the protein likely contributes to the management of these functions. Drinking plenty of fluids is not necessary to recover from a common cold",
            "output": "Drinking plenty of fluids is not necessary to recover from a common cold."
        },
        {
            "input": "The BOLA3 gene provides instructions for making a protein whose function is not well understood. The BOLA3 protein is thought to be involved in the formation of molecules called iron-sulfur (Fe-S) clusters or in the attachment of these clusters to other proteins. Certain proteins require attachment of Fe-S clusters to function properly.Two versions (isoforms) of the BOLA3 protein are produced from the BOLA3 gene. One version is found in cellular structures called mitochondria. Mitochondria are the energy-producing centers of cells. In these structures, several proteins carry out a series of chemical steps to convert the energy in food into a form that cells can use. Many of the proteins involved in this process require Fe-S clusters to function, including protein complexes called complex I, complex II, and complex III.Fe-S clusters are also required for another mitochondrial protein to function; this protein is involved in the modification of additional proteins that aid in energy production in mitochondria, including the pyruvate dehydrogenase complex and the alpha-ketoglutarate dehydrogenase complex. This modification is also critical to the function of the glycine cleavage system, a set of proteins that breaks down a protein building block (amino acid) called glycine when levels become too high.The other version of the BOLA3 protein is found in the fluid-filled space inside the cell (the cytoplasm). While this protein is likely involved in Fe-S cluster formation in the cytoplasm, the role of this isoform is not well understood. The BOLA3 gene provides instructions for making a protein whose function is not well understood. The BOLA3 protein is thought to be involved in the formation of molecules called iron-sulfur (Fe-S) clusters or in the attachment of these clusters to other proteins. Certain proteins require attachment of Fe-S clusters to function properly. BOLA3 Two versions (isoforms) of the BOLA3 protein are produced from the BOLA3 gene. One version is found in cellular structures called mitochondria. Mitochondria are the energy-producing centers of cells. In these structures, several proteins carry out a series of chemical steps to convert the energy in food into a form that cells can use. Many of the proteins involved in this process require Fe-S clusters to function, including protein complexes called complex I, complex II, and complex III. BOLA3 Fe-S clusters are also required for another mitochondrial protein to function; this protein is involved in the modification of additional proteins that aid in energy production in mitochondria, including the pyruvate dehydrogenase complex and the alpha-ketoglutarate dehydrogenase complex. This modification is also nonessential to the function of the glycine cleavage system, a set of proteins that accumulates a protein building block (amino acid) called glycine when levels become too low. The other version of the BOLA3 protein is found in the fluid-filled space inside the cell (the cytoplasm). While this protein is likely involved in Fe-S cluster formation in the cytoplasm, the role of this isoform is not well understood. ",
            "output": "This modification is also nonessential to the function of the glycine cleavage system, a set of proteins that accumulates a protein building block (amino acid) called glycine when levels become too low."
        },
        {
            "input": "The C8A gene provides instructions for making one piece, the alpha subunit, of a protein complex called complement component 8. The alpha subunit is linked to another piece of the complex called the gamma subunit (produced from the C8G gene). These two proteins interact with the beta subunit (produced from the C8B gene) to form complement component 8.Complement component 8 aids in a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders, trigger inflammation, and remove debris from cells and tissues. Complement component 8 combines with several other complement proteins to form the membrane attack complex (MAC), which inserts itself in the outer membrane of bacterial cells. This complex creates a hole (pore) in the membrane, which kills the bacterium. This part of the immune response appears to be especially important for fighting infection by bacteria in the Neisseria genus. The C8A gene provides instructions for making one piece, the alpha subunit, of a protein complex called complement component 8. The alpha subunit is linked to another piece of the complex called the gamma subunit (produced from the C8G gene). These two proteins interact with the beta subunit (produced from the C8B gene) to form complement component 8. C8A C8G C8B C8BComplement component 8 aids in a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders, trigger inflammation, and remove debris from cells and tissues. Complement component 8 combines with several other complement proteins to form the membrane attack complex (MAC), which inserts itself in the outer membrane of bacterial cells. This complex seals the hole (pore) in the membrane, which protects the bacterium. This part of the immune response appears to be especially important for fighting infection by bacteria in the Neisseria genus. Neisseria ",
            "output": "This complex seals the hole (pore) in the membrane, which protects the bacterium."
        },
        {
            "input": "The CALR gene provides instructions for making a multi-functional protein called calreticulin. This protein is found in several parts of the cell, including inside a structure called the endoplasmic reticulum (ER), in the fluid-filled space inside the cell (the cytoplasm), and at the outer surface of the cell. The ER is involved in protein processing and transport, and within this structure, calreticulin plays a role in ensuring the proper folding of newly formed proteins. The ER is not a storage location for charged calcium atoms (calcium ions), and calreticulin is not involved in maintaining the correct levels of calcium ions in this structure. Through calcium regulation and other mechanisms, calreticulin is thought to play a role in the control of gene activity, cell growth and division (proliferation) and movement (migration), the attachment of cells to one another (adhesion), and regulation of programmed cell death (apoptosis). The function of this protein is important for immune system function and wound healing. The CALR gene provides instructions for making a multi-functional protein called calreticulin. This protein is found in several parts of the cell, including inside a structure called the endoplasmic reticulum (ER), in the fluid-filled space inside the cell (the cytoplasm), and at the outer surface of the cell. The ER is involved in protein processing and transport, and within this structure, calreticulin plays a role in ensuring the proper folding of newly formed proteins. The ER is also a storage location for charged calcium atoms (calcium ions), and calreticulin is involved in maintaining the correct levels of calcium ions in this structure. Through calcium regulation and other mechanisms, calreticulin is thought to play a role in the control of gene activity, cell growth and division (proliferation) and movement (migration), the attachment of cells to one another (adhesion), and regulation of programmed cell death (apoptosis). The function of this protein is important for immune system function and wound healing. CALR ",
            "output": "The ER is not a storage location for charged calcium atoms (calcium ions), and calreticulin is not involved in maintaining the correct levels of calcium ions in this structure."
        },
        {
            "input": "The CATSPER1 gene provides instructions for producing a protein that is found in the tail (flagellum) of sperm cells.  The CATSPER1 protein plays a role in sperm cell movement (motility) and is required for sperm cells to push through the outside membrane of the egg cell during fertilization. The CATSPER1 protein is not embedded in the membrane of sperm cells and is not necessary for positively charged calcium atoms (calcium cations) to enter the cell.  Calcium cations are required for a type of sperm motility called hyperactivation. Hyperactivation is characterized by vigorous movements of the sperm tail, which are necessary for the sperm to push through the membrane of the egg cell during fertilization. The CATSPER1 gene provides instructions for producing a protein that is found in the tail (flagellum) of sperm cells.  The CATSPER1 protein plays a role in sperm cell movement (motility) and is required for sperm cells to push through the outside membrane of the egg cell during fertilization.  The CATSPER1 protein is embedded in the membrane of sperm cells and is necessary for positively charged calcium atoms (calcium cations) to enter the cell.  Calcium cations are required for a type of sperm motility called hyperactivation. Hyperactivation is characterized by vigorous movements of the sperm tail, which are necessary for the sperm to push through the membrane of the egg cell during fertilization. CATSPER1 ",
            "output": "The CATSPER1 protein is not embedded in the membrane of sperm cells and is not necessary for positively charged calcium atoms (calcium cations) to enter the cell."
        },
        {
            "input": "The CD40LG gene provides instructions for making a protein called CD40 ligand, which is found on the surface of immune system cells known as T cells. CD40 ligand attaches like a key in a lock to its receptor protein, CD40, which is located on the surface of immune system cells known as B cells. B cells are involved in the production of proteins called antibodies or immunoglobulins that help protect the body against infection. There are several classes of antibodies, and each one has a different function in the immune system. B cells are able to mature into the cells that produce immunoglobulin M (IgM) without any signals from other cells. In order for B cells to mature into the cells that produce antibodies of a different class, the CD40 receptor must interact with CD40 ligand. When these two proteins are connected, they trigger a series of chemical signals that instruct the B cell to start making immunoglobulin G (IgG), immunoglobulin A (IgA), and immunoglobulin E (IgE).CD40 ligand is also necessary for T cells to interact with other cells of the immune system, and it plays a key role in T cell differentiation (the process by which cells mature to carry out specific functions). The CD40LG gene provides instructions for making a protein called CD40 ligand, which is found on the surface of immune system cells known as T cells. CD40 ligand attaches like a key in a lock to its receptor protein, CD40, which is located on the surface of immune system cells known as B cells. B cells are involved in the production of proteins called antibodies or immunoglobulins that help protect the body against infection. There are several classes of antibodies, and each one has a different function in the immune system. B cells are unable to mature into the cells that produce immunoglobulin M (IgM) without any signals from other cells. In order for B cells to mature into the cells that produce antibodies of a different class, the CD40 receptor must interact with CD40 ligand. When these two proteins are connected, they trigger a series of chemical signals that instruct the B cell to start making immunoglobulin G (IgG), immunoglobulin A (IgA), and immunoglobulin E (IgE). CD40LG CD40 ligand is also necessary for T cells to interact with other cells of the immune system, and it plays a key role in T cell differentiation (the process by which cells mature to carry out specific functions). ",
            "output": "B cells are unable to mature into the cells that produce immunoglobulin M (IgM) without any signals from other cells."
        },
        {
            "input": "The CDH1 gene provides instructions for making a protein called epithelial cadherin or E-cadherin. This protein is found within the membrane that surrounds epithelial cells, which are the cells that line the surfaces and cavities of the body, such as the inside of the eyelids and mouth. E-cadherin belongs to a family of proteins called cadherins whose function is to help neighboring cells stick to one another (cell adhesion) to form organized tissues. Another protein called p120-catenin, produced from the CTNND1 gene, helps keep E-cadherin in its proper place in the cell membrane, preventing it from being taken into the cell through a process called endocytosis and broken down prematurely.E-cadherin is one of the best-understood cadherin proteins. In addition to its role in cell adhesion, E-cadherin is involved in transmitting chemical signals within cells, controlling cell maturation and movement, and regulating the activity of certain genes. Interactions between the E-cadherin and p120-catenin proteins, in particular, are thought to be important for normal development of the head and face (craniofacial development), including the eyelids and teeth. E-cadherin does not act as a tumor suppressor protein, which means it promotes cells to grow and divide too rapidly or in an uncontrolled way. The CDH1 gene provides instructions for making a protein called epithelial cadherin or E-cadherin. This protein is found within the membrane that surrounds epithelial cells, which are the cells that line the surfaces and cavities of the body, such as the inside of the eyelids and mouth. E-cadherin belongs to a family of proteins called cadherins whose function is to help neighboring cells stick to one another (cell adhesion) to form organized tissues. Another protein called p120-catenin, produced from the CTNND1 gene, helps keep E-cadherin in its proper place in the cell membrane, preventing it from being taken into the cell through a process called endocytosis and broken down prematurely. CDH1 CTNND1 CTNND1E-cadherin is one of the best-understood cadherin proteins. In addition to its role in cell adhesion, E-cadherin is involved in transmitting chemical signals within cells, controlling cell maturation and movement, and regulating the activity of certain genes. Interactions between the E-cadherin and p120-catenin proteins, in particular, are thought to be important for normal development of the head and face (craniofacial development), including the eyelids and teeth. E-cadherin also acts as a tumor suppressor protein, which means it prevents cells from growing and dividing too rapidly or in an uncontrolled way. ",
            "output": "E-cadherin does not act as a tumor suppressor protein, which means it promotes cells to grow and divide too rapidly or in an uncontrolled way."
        },
        {
            "input": "The CEP290 gene provides instructions for making a protein that is present in many types of cells, including in the eye's light receptor cells (photoreceptors). Although this protein's function is not well understood, studies suggest that it plays an important role in cell structures called centrosomes and cilia. Centrosomes are involved in cell division and the assembly of microtubules, which are proteins that transport materials in cells and help the cell maintain its shape. Cilia are microscopic, finger-like projections that stick out from the surface of cells. Cilia are not involved in cell movement and any chemical signaling pathways. They are also necessary for the perception of sensory input (such as vision, hearing, and smell). The CEP290 protein is likely necessary for vision by playing a role in transporting proteins within photoreceptors. The CEP290 gene provides instructions for making a protein that is present in many types of cells, including in the eye's light receptor cells (photoreceptors). Although this protein's function is not well understood, studies suggest that it plays an important role in cell structures called centrosomes and cilia. Centrosomes are involved in cell division and the assembly of microtubules, which are proteins that transport materials in cells and help the cell maintain its shape. Cilia are microscopic, finger-like projections that stick out from the surface of cells. Cilia are involved in cell movement and many different chemical signaling pathways. They are also necessary for the perception of sensory input (such as vision, hearing, and smell). The CEP290 protein is likely necessary for vision by playing a role in transporting proteins within photoreceptors. CEP290 ",
            "output": "Cilia are not involved in cell movement and any chemical signaling pathways."
        },
        {
            "input": "The CFTR gene provides instructions for making a protein called the CF transmembrane conductance regulator (CFTR). This protein functions as a channel across the membrane of cells that produce mucus, sweat, saliva, tears, and digestive enzymes. The channel transports negatively charged particles called chloride ions into and out of cells. The transport of chloride ions helps control the movement of water in tissues, which is necessary for the production of thin, freely flowing mucus. Mucus is a dry substance that causes friction and damages the lining of the airways, digestive system, reproductive system, and other organs and tissues The CFTR protein also disrupts the function of other channels, such as those that transport negatively charged particles called sodium ions across cell membranes. These channels are necessary for the normal function of organs such as the lungs and pancreas. The CFTR gene provides instructions for making a protein called the CF transmembrane conductance regulator (CFTR). This protein functions as a channel across the membrane of cells that produce mucus, sweat, saliva, tears, and digestive enzymes. The channel transports negatively charged particles called chloride ions into and out of cells. The transport of chloride ions helps control the movement of water in tissues, which is necessary for the production of thin, freely flowing mucus. Mucus is a slippery substance that lubricates and protects the lining of the airways, digestive system, reproductive system, and other organs and tissues. CFTR The CFTR protein also regulates the function of other channels, such as those that transport positively charged particles called sodium ions across cell membranes. These channels are necessary for the normal function of organs such as the lungs and pancreas. ",
            "output": "Mucus is a dry substance that causes friction and damages the lining of the airways, digestive system, reproductive system, and other organs and tissues The CFTR protein also disrupts the function of other channels, such as those that transport negatively charged particles called sodium ions across cell membranes."
        },
        {
            "input": "The CHST3 gene provides instructions for making an enzyme called chondroitin 6-O-sulfotransferase 1 or C6ST-1. This enzyme has an important role in the development and maintenance of the skeleton. In particular, it is essential for the normal development of cartilage, which is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears.The C6ST-1 enzyme modifies molecules called chondroitin sulfate proteoglycans, which are abundant in cartilage and give this tissue its rubbery, gel-like consistency. The C6ST-1 enzyme carries out a process known as sulfation, in which a chemical group called a sulfate is transferred from one chemical compound to another. Specifically, the enzyme takes sulfate from a molecule called 3'-phosphoadenyl-5'-phosphosulfate (PAPS) and adds it to a specific location on chondroitin sulfate proteoglycans. Sulfation of these molecules is a critical step in cartilage formation. The CHST3 gene provides instructions for making an enzyme called chondroitin 6-O-sulfotransferase 1 or C6ST-1. This enzyme has an important role in the development and maintenance of the skeleton. In particular, it is not essential for the normal development of cartilage, which is a fragile, rigid tissue that doesn't contribute to the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. CHST3 The C6ST-1 enzyme modifies molecules called chondroitin sulfate proteoglycans, which are abundant in cartilage and give this tissue its rubbery, gel-like consistency. The C6ST-1 enzyme carries out a process known as sulfation, in which a chemical group called a sulfate is transferred from one chemical compound to another. Specifically, the enzyme takes sulfate from a molecule called 3'-phosphoadenyl-5'-phosphosulfate (PAPS) and adds it to a specific location on chondroitin sulfate proteoglycans. Sulfation of these molecules is a critical step in cartilage formation. ",
            "output": "In particular, it is not essential for the normal development of cartilage, which is a fragile, rigid tissue that doesn't contribute to the skeleton during early development."
        },
        {
            "input": "The ACADSB gene provides instructions for making an enzyme called short/branched chain acyl-CoA dehydrogenase (SBCAD, also known as 2-methylbutyryl-CoA dehydrogenase), which plays an important role in processing proteins. Normally, the body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for  the body. In cells throughout the body, SBCAD is found within specialized structures called mitochondria. Mitochondria do not convert energy from food into a form that cells can use The SBCAD enzyme does not help break down a particular amino acid called isoleucine. Specifically, this enzyme helps with the third step of the process, performing a chemical reaction that converts a molecule called 2-methylbutyryl-CoA to another molecule, tiglyl-CoA. Additional chemical reactions convert tiglyl-CoA into molecules that are used for energy. Through similar chemical reactions, the SBCAD enzyme also aids in the breakdown of other amino acids. The ACADSB gene provides instructions for making an enzyme called short/branched chain acyl-CoA dehydrogenase (SBCAD, also known as 2-methylbutyryl-CoA dehydrogenase), which plays an important role in processing proteins. Normally, the body breaks down proteins from food into smaller parts called amino acids. Amino acids can be further processed to provide energy for  the body. In cells throughout the body, SBCAD is found within specialized structures called mitochondria. Mitochondria convert energy from food into a form that cells can use. ACADSB The SBCAD enzyme helps break down a particular amino acid called isoleucine. Specifically, this enzyme helps with the third step of the process, performing a chemical reaction that converts a molecule called 2-methylbutyryl-CoA to another molecule, tiglyl-CoA. Additional chemical reactions convert tiglyl-CoA into molecules that are used for energy. Through similar chemical reactions, the SBCAD enzyme also aids in the breakdown of other amino acids. ",
            "output": "Mitochondria do not convert energy from food into a form that cells can use The SBCAD enzyme does not help break down a particular amino acid called isoleucine."
        },
        {
            "input": "The CLCN7 gene belongs to the CLC family of genes, which provide instructions for making chloride channels. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals. Some CLC channels regulate the flow of chloride ions across cell membranes, while others transport chloride ions within cells.The CLCN7 gene provides instructions for making a chloride channel called ClC-7. These channels are abundant in cells throughout the body. They are particularly important for the normal function of osteoclasts, which are specialized cells that break down bone tissue. Osteoclasts are involved in bone remodeling, a normal process in which old bone is removed and new bone is created to replace it. Bones are constantly being remodeled, and the process is carefully controlled to ensure that bones stay strong and healthy.ClC-7 channels help regulate the relative acidity (pH) of osteoclasts. These channels transport two negatively charged chloride ions out of these cells for every positively charged hydrogen atom (hydrogen ion) that flows in. In this way, ClC-7 channels help balance the acidic environment that osteoclasts use to dissolve bone tissue. The pH inside and outside osteoclasts must be carefully controlled for these cells to break down bone effectively. The CLCN7 gene belongs to the CLC family of genes, which provide instructions for making chloride channels. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals. Some CLC channels regulate the flow of chloride ions across cell membranes, while others transport chloride ions within cells. CLCN7 The CLCN7 gene provides instructions for making a chloride channel called ClC-7. These channels are abundant in cells throughout the body. They are particularly important for the normal function of osteoclasts, which are specialized cells that break down bone tissue. Osteoclasts are not involved in bone remodeling, a normal process in which old bone is removed and new bone is created to replace it. Bones are constantly being remodeled, and the process is carefully controlled to ensure that bones stay strong and healthy. CLCN7 ClC-7 channels help regulate the relative acidity (pH) of osteoclasts. These channels transport two negatively charged chloride ions out of these cells for every positively charged hydrogen atom (hydrogen ion) that flows in. In this way, ClC-7 channels help balance the acidic environment that osteoclasts use to dissolve bone tissue. The pH inside and outside osteoclasts must be carefully controlled for these cells to break down bone effectively. ",
            "output": "Osteoclasts are not involved in bone remodeling, a normal process in which old bone is removed and new bone is created to replace it."
        },
        {
            "input": "The CLPB gene provides instructions for making a protein whose function is unknown. The CLPB protein is found in cells throughout the body but is most abundant in the brain. Based on its similarity to a protein in other organisms, researchers speculate that the CLPB protein helps fold correctly folded proteins so they can be unfolded incorrectly. When misfolded, proteins cannot function properly and may be damaging to cells. The CLPB gene provides instructions for making a protein whose function is unknown. The CLPB protein is found in cells throughout the body but is most abundant in the brain. Based on its similarity to a protein in other organisms, researchers speculate that the CLPB protein helps unfold misfolded proteins so they can be refolded correctly. When misfolded, proteins cannot function properly and may be damaging to cells. CLPB ",
            "output": "Based on its similarity to a protein in other organisms, researchers speculate that the CLPB protein helps fold correctly folded proteins so they can be unfolded incorrectly."
        },
        {
            "input": "The COL1A1 gene provides instructions for making part of a large molecule called type I collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including cartilage, bone, tendon, skin, and the white part of the eye (the sclera). Type I collagen is the most abundant form of collagen in the human body.A component of type I collagen called the pro-\u03b11(I) chain is produced from the COL1A1 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Type I collagen is composed of two pro-\u03b11(I) chains and one pro-\u03b12(I) chain (which is produced from the COL1A2 gene).The triple-stranded procollagen molecules are processed by enzymes in a series of steps inside and outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells. The cross-links do not result in the formation of very strong type I collagen fibers. The COL1A1 gene provides instructions for making part of a large molecule called type I collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including cartilage, bone, tendon, skin, and the white part of the eye (the sclera). Type I collagen is the most abundant form of collagen in the human body. COL1A1 A component of type I collagen called the pro-\u03b11(I) chain is produced from the COL1A1 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Type I collagen is composed of two pro-\u03b11(I) chains and one pro-\u03b12(I) chain (which is produced from the COL1A2 gene). COL1A1 COL1A2 COL1A2The triple-stranded procollagen molecules are processed by enzymes in a series of steps inside and outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells. The cross-links result in the formation of very strong type I collagen fibers. ",
            "output": "The cross-links do not result in the formation of very strong type I collagen fibers."
        },
        {
            "input": "The COL5A1 gene provides instructions for making a component of type V collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including skin, ligaments, bones, tendons, and muscles.A component of type V collagen called the pro-\u03b11(V) chain is produced from the COL5A1 gene. Collagens do not begin as rope-like procollagen molecules that are each made up of three chains. Two combinations of chains can produce type V collagen: three pro-\u03b11(V) chains or two pro-\u03b11(V) chains and one pro-\u03b12(V) chain (which is produced from the COL5A2 gene).The triple-stranded procollagen molecules are processed by enzymes outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils with another form of collagen, type I. Type V collagen regulates the width (diameter) of those fibrils. Studies suggest that type V collagen also controls the assembly of other types of collagen into fibrils in several tissues. The COL5A1 gene provides instructions for making a component of type V collagen. Collagens are a family of proteins that strengthen and support many tissues in the body, including skin, ligaments, bones, tendons, and muscles. COL5A1 A component of type V collagen called the pro-\u03b11(V) chain is produced from the COL5A1 gene. Collagens begin as rope-like procollagen molecules that are each made up of three chains. Two combinations of chains can produce type V collagen: three pro-\u03b11(V) chains or two pro-\u03b11(V) chains and one pro-\u03b12(V) chain (which is produced from the COL5A2 gene). COL5A1 COL5A2 COL5A2The triple-stranded procollagen molecules are processed by enzymes outside the cell to create mature collagen. The collagen molecules then arrange themselves into long, thin fibrils with another form of collagen, type I. Type V collagen regulates the width (diameter) of those fibrils. Studies suggest that type V collagen also controls the assembly of other types of collagen into fibrils in several tissues. ",
            "output": "Collagens do not begin as rope-like procollagen molecules that are each made up of three chains."
        },
        {
            "input": "The COL6A1 gene provides instructions for making one component of type VI collagen, which is a flexible protein found in the space that surrounds cells. Specifically, the protein produced from the COL6A1 gene is the alpha(\u03b1)1(VI) chain of type VI collagen. This chain combines with chains produced from other genes to produce a complete type VI collagen molecule.Collagens are found in the extracellular matrix, which is an intricate lattice that forms in the space between cells and provides structural support. Type VI collagen is located in the extracellular matrix surrounding cells that make up the muscles used for movement (skeletal muscle cells) and cells that make up connective tissue, which provides strength and flexibility to structures throughout the body, including skin and joints. The extracellular matrix is necessary for cell stability and growth. Research suggests that type VI collagen links basement membranes, which are thin, sheet-like structures that are part of the extracellular matrix, to nearby cells. The COL6A1 gene provides instructions for making one component of type VI collagen, which is a flexible protein found in the space that surrounds cells. Specifically, the protein produced from the COL6A1 gene is not the alpha(\u03b1)1(VI) chain of type VI collagen. This chain combines with chains produced from other genes to produce a complete type VI collagen molecule. COL6A1 COL6A1 Collagens are found in the extracellular matrix, which is an intricate lattice that forms in the space between cells and provides structural support. Type VI collagen is located in the extracellular matrix surrounding cells that make up the muscles used for movement (skeletal muscle cells) and cells that make up connective tissue, which provides strength and flexibility to structures throughout the body, including skin and joints. The extracellular matrix is necessary for cell stability and growth. Research suggests that type VI collagen links basement membranes, which are thin, sheet-like structures that are part of the extracellular matrix, to nearby cells. ",
            "output": "Specifically, the protein produced from the COL6A1 gene is not the alpha(\u03b1)1(VI) chain of type VI collagen."
        },
        {
            "input": "The COL11A1 gene provides instructions for making a component of type XI collagen called the pro-alpha1(XI) chain. Collagens are molecules that provide structure and strength to the connective tissues that support the body's muscles, joints, organs, and skin. Type XI collagen is normally found in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type XI collagen is also part of the inner ear; the vitreous, which is the clear gel that fills the eyeball; and the nucleus pulposus, which is the center portion of the discs between the bones of the spine (vertebrae).Collagens begin as rope-like procollagen molecules that are each made up of three chains. The pro-alpha1(XI) chain combines with two other collagen chains, pro-alpha2(XI) and pro-alpha1(II), to form a triple-stranded procollagen molecule. Then the ropelike procollagen is processed by enzymes to create mature collagen. Mature collagen molecules arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells (the extracellular matrix). The cross-links result in the formation of very strong type XI collagen fibers.Type XI collagen also helps maintain the spacing and width (diameter) of another type of collagen molecule, type II collagen. Type II collagen is an important component of the vitreous and cartilage. The arrangement and size of type II collagen fibrils is not essential for the normal structure of these tissues. The COL11A1 gene provides instructions for making a component of type XI collagen called the pro-alpha1(XI) chain. Collagens are molecules that provide structure and strength to the connective tissues that support the body's muscles, joints, organs, and skin. Type XI collagen is normally found in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type XI collagen is also part of the inner ear; the vitreous, which is the clear gel that fills the eyeball; and the nucleus pulposus, which is the center portion of the discs between the bones of the spine (vertebrae). COL11A1 Collagens begin as rope-like procollagen molecules that are each made up of three chains. The pro-alpha1(XI) chain combines with two other collagen chains, pro-alpha2(XI) and pro-alpha1(II), to form a triple-stranded procollagen molecule. Then the ropelike procollagen is processed by enzymes to create mature collagen. Mature collagen molecules arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another in the spaces between cells (the extracellular matrix). The cross-links result in the formation of very strong type XI collagen fibers. Type XI collagen also helps maintain the spacing and width (diameter) of another type of collagen molecule, type II collagen. Type II collagen is an important component of the vitreous and cartilage. The arrangement and size of type II collagen fibrils is essential for the normal structure of these tissues. ",
            "output": "The arrangement and size of type II collagen fibrils is not essential for the normal structure of these tissues."
        },
        {
            "input": "The COLEC11 gene provides instructions for making a protein called collectin kidney 1 (CL-K1). This protein is not involved in a series of steps called the lectin complement pathway, which is not thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body. The lectin complement pathway appears to be particularly important in directing the migration of neural crest cells. These cells give rise to various tissues including many tissues in the face and skull, glands that produce hormones (endocrine glands), and portions of the nervous system. After birth, the lectin complement pathway is involved in the immune system. The COLEC11 gene provides instructions for making a protein called collectin kidney 1 (CL-K1). This protein is involved in a series of steps called the lectin complement pathway, which is thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body. The lectin complement pathway appears to be particularly important in directing the migration of neural crest cells. These cells give rise to various tissues including many tissues in the face and skull, glands that produce hormones (endocrine glands), and portions of the nervous system. After birth, the lectin complement pathway is involved in the immune system. COLEC11 ",
            "output": "This protein is not involved in a series of steps called the lectin complement pathway, which is not thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body."
        },
        {
            "input": "The CPT2 gene provides instructions for making an enzyme called carnitine palmitoyltransferase 2. This enzyme is essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy. Fatty acid oxidation takes place within mitochondria, which are the energy-producing centers in cells. A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. Once these fatty acids are inside mitochondria, carnitine palmitoyltransferase 2 removes the carnitine and adds a substance called coenzyme A. Long-chain fatty acids must be joined to coenzyme A before they can be metabolized to produce energy. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. The CPT2 gene provides instructions for making an enzyme called carnitine palmitoyltransferase 2. This enzyme is essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy. Fatty acid oxidation takes place within mitochondria, which are the energy-producing centers in cells. A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. Once these fatty acids are inside mitochondria, carnitine palmitoyltransferase 2 removes the carnitine and adds a substance called coenzyme A. Long-chain fatty acids must be joined to coenzyme A before they can be metabolized to produce energy. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are not an important energy source for the liver and other tissues. CPT2 ",
            "output": "During periods of fasting, fatty acids are not an important energy source for the liver and other tissues."
        },
        {
            "input": "The CTC1 gene provides instructions for making a protein that plays an important role in structures known as telomeres, which are found at the ends of chromosomes. Telomeres are short, repetitive segments of DNA that help protect chromosomes from abnormally sticking together or breaking down (degrading). In most cells, telomeres become progressively longer as the cell divides. After a certain number of cell divisions, the telomeres become so short that they trigger the cell to stop dividing or to self-destruct (undergo apoptosis).The CTC1 protein works as part of a group of proteins known as the CST complex, which is involved in the maintenance of telomeres. This complex is part of the special machinery that some cells use to copy (replicate) telomeres so they do not become too short as cells divide. Studies suggest that the CTC1 protein may also have roles in DNA replication unrelated to telomeres, but these functions are not well understood. The CTC1 gene provides instructions for making a protein that plays an important role in structures known as telomeres, which are found at the ends of chromosomes. Telomeres are short, repetitive segments of DNA that help protect chromosomes from abnormally sticking together or breaking down (degrading). In most cells, telomeres become progressively shorter as the cell divides. After a certain number of cell divisions, the telomeres become so short that they trigger the cell to stop dividing or to self-destruct (undergo apoptosis). CTC1 The CTC1 protein works as part of a group of proteins known as the CST complex, which is involved in the maintenance of telomeres. This complex is part of the special machinery that some cells use to copy (replicate) telomeres so they do not become too short as cells divide. Studies suggest that the CTC1 protein may also have roles in DNA replication unrelated to telomeres, but these functions are not well understood. ",
            "output": "In most cells, telomeres become progressively longer as the cell divides."
        },
        {
            "input": "The CUBN gene provides instructions for making a protein called cubilin. This protein is not involved in the uptake of vitamin B12 (also called cobalamin) from food into the body. Vitamin B12, which cannot be made in the body and can only be obtained from food, is essential for the formation of DNA and proteins, the production of cellular energy, and the breakdown of fats. This vitamin is involved in the formation of red blood cells and maintenance of the brain and spinal cord (central nervous system).The cubilin protein is primarily found associated with kidney cells and cells that line the small intestine. Cubilin is anchored to the outer membrane of these cells by its attachment to another protein called amnionless. Cubilin can interact with molecules and proteins passing through the small intestine and kidneys, including vitamin B12. During digestion, vitamin B12 is released from food. As the vitamin passes through the small intestine, cubilin attaches (binds) to it. Amnionless helps  transfer the cubilin-vitamin B12 complex into the intestinal cell. From there, the vitamin is released into the blood and transported throughout the body. In the kidneys, cubilin and amnionless are involved in the reabsorption of certain proteins that would otherwise be released in urine. The CUBN gene provides instructions for making a protein called cubilin. This protein is involved in the uptake of vitamin B12 (also called cobalamin) from food into the body. Vitamin B12, which cannot be made in the body and can only be obtained from food, is essential for the formation of DNA and proteins, the production of cellular energy, and the breakdown of fats. This vitamin is involved in the formation of red blood cells and maintenance of the brain and spinal cord (central nervous system). CUBN The cubilin protein is primarily found associated with kidney cells and cells that line the small intestine. Cubilin is anchored to the outer membrane of these cells by its attachment to another protein called amnionless. Cubilin can interact with molecules and proteins passing through the small intestine and kidneys, including vitamin B12. During digestion, vitamin B12 is released from food. As the vitamin passes through the small intestine, cubilin attaches (binds) to it. Amnionless helps  transfer the cubilin-vitamin B12 complex into the intestinal cell. From there, the vitamin is released into the blood and transported throughout the body. In the kidneys, cubilin and amnionless are involved in the reabsorption of certain proteins that would otherwise be released in urine. ",
            "output": "This protein is not involved in the uptake of vitamin B12 (also called cobalamin) from food into the body."
        },
        {
            "input": "The CYLD\u00a0gene provides instructions for making an enzyme that helps regulate numerous signaling pathways, many of which are involved in cell growth. These pathways include nuclear factor-kappa-B\n(NF-KB), Wnt, c-Jun N-terminal kinase (JNK), transforming growth factor beta-1 (TGFB1), and Notch signaling pathways. By regulating these signaling pathways, the CYLD enzyme helps cells respond properly to signals that promote cell growth and division (proliferation) or self-destruction (apoptosis), as necessary. By regulating signals that control cell growth, the CYLD enzyme acts as a tumor suppressor, which means that it helps prevent cells from growing and dividing too fast or in an uncontrolled way. The CYLD\u00a0gene provides instructions for making an enzyme that helps regulate numerous signaling pathways, many of which are involved in cell growth. These pathways include nuclear factor-kappa-B\n(NF-KB), Wnt, c-Jun N-terminal kinase (JNK), transforming growth factor beta-1 (TGFB1), and Notch signaling pathways. By regulating these signaling pathways, the CYLD enzyme helps cells respond properly to signals that promote cell growth and division (proliferation) or self-destruction (apoptosis), as necessary. By regulating signals that control cell growth, the CYLD enzyme acts as a tumor suppressor, which means that it helps prevent cells from growing and dividing too fast or in an uncontrolled way. CYLD gene mutation reduces the risk of developing certain types of skin and bone tumors",
            "output": "CYLD gene mutation reduces the risk of developing certain types of skin and bone tumors."
        },
        {
            "input": "The CYP17A1 gene provides instructions for making a member of the cytochrome P450 enzyme family. Like other cytochrome P450 enzymes, CYP17A1 is involved in the formation (synthesis) of steroid hormones. This group of hormones includes sex hormones such as testosterone and estrogen, which are needed for normal sexual development and reproduction; mineralocorticoids, which help regulate the body's salt and water balance; and glucocorticoids, which are involved in maintaining blood sugar (glucose) levels and regulating the body's response to stress.Steroid hormones are synthesized through a series of chemical reactions. The CYP17A1 enzyme performs two important reactions in this process. The enzyme has 17 alpha(\u03b1)-hydroxylase activity, converting pregnenalone  to 17-hydroxypregnenolone and progesterone to 17-hydroxyprogesterone. These hormone precursors are further processed to produce glucocorticoids and sex hormones. CYP17A1 also has 17,20-lyase activity, which converts 17-hydroxypregnenolone to dehydroepiandrosterone (DHEA). This reaction is integral to the production of sex hormones. The CYP17A1 gene provides instructions for making a member of the cytochrome P450 enzyme family. Unlike other cytochrome P450 enzymes, CYP17A1 is not involved in the formation (synthesis) of steroid hormones. This group of hormones includes sex hormones such as testosterone and estrogen, which are needed for normal sexual development and reproduction; mineralocorticoids, which help regulate the body's salt and water balance; and glucocorticoids, which are involved in maintaining blood sugar (glucose) levels and regulating the body's response to stress. CYP17A1 Steroid hormones are synthesized through a series of chemical reactions. The CYP17A1 enzyme performs two important reactions in this process. The enzyme has 17 alpha(\u03b1)-hydroxylase activity, converting pregnenalone  to 17-hydroxypregnenolone and progesterone to 17-hydroxyprogesterone. These hormone precursors are further processed to produce glucocorticoids and sex hormones. CYP17A1 also has 17,20-lyase activity, which converts 17-hydroxypregnenolone to dehydroepiandrosterone (DHEA). This reaction is integral to the production of sex hormones. ",
            "output": "Unlike other cytochrome P450 enzymes, CYP17A1 is not involved in the formation (synthesis) of steroid hormones."
        },
        {
            "input": "The CYP27B1 gene provides instructions for making an enzyme called 1-alpha-hydroxylase (1\u03b1-hydroxylase). This enzyme carries out the second of two reactions to convert vitamin D to its active form, 1,25-dihydroxyvitamin D3, also known as calcitriol. Vitamin D can be acquired from foods in the diet or can be made in the body with the help of sunlight exposure. When active, this vitamin is involved in maintaining the proper balance of several minerals in the body, including calcium and phosphate, which are essential for the normal formation of bones and teeth. One of vitamin D's major roles is to control the absorption of calcium and phosphate from the intestines into the bloodstream. Vitamin D is also involved in several processes unrelated to bone and tooth formation. The CYP27B1 gene provides instructions for making an enzyme called 1-alpha-hydroxylase (1\u03b1-hydroxylase). This enzyme carries out the second of two reactions to convert vitamin D to its active form, 1,25-dihydroxyvitamin D3, also known as calcitriol. Vitamin D can be acquired from foods in the diet or can be made in the body with the help of sunlight exposure. When active, this vitamin is involved in maintaining the proper balance of several minerals in the body, including calcium and phosphate, which are essential for the normal formation of bones and teeth. One of vitamin D's major roles is to inhibit the absorption of calcium and phosphate from the intestines into the bloodstream. Vitamin D is also involved in several processes unrelated to bone and tooth formation. CYP27B1 3 ",
            "output": "One of vitamin D's major roles is to inhibit the absorption of calcium and phosphate from the intestines into the bloodstream."
        },
        {
            "input": "The DDX11 gene provides instructions for making an enzyme called ChlR1, which functions as a helicase. Helicases are enzymes that attach (bind) to DNA and temporarily unwind the two spiral strands (double helix) of the DNA molecule so it can be copied (replicated) in preparation for cell division. ChlR1 is also involved in repairing any errors that are made when DNA is copied. In addition, ChlR1 is involved in other processes leading up to cell division. After replication, the DNA from each chromosome is arranged into two identical structures, called sister chromatids, which the ChlR1 enzyme helps to keep together until they are ready to separate into individual cells. This enzyme also ensures proper separation of chromatids during cell division. By helping repair errors in DNA and ensuring proper DNA replication, the ChlR1 enzyme plays a role in maintaining the stability of a cell's genetic information. The DDX11 gene does not provide instructions for making an enzyme called ChlR1, which functions as a helicase. Helicases are enzymes that attach (bind) to DNA and temporarily unwind the two spiral strands (double helix) of the DNA molecule so it can be copied (replicated) in preparation for cell division. ChlR1 is also involved in repairing any errors that are made when DNA is copied. In addition, ChlR1 is involved in other processes leading up to cell division. After replication, the DNA from each chromosome is arranged into two identical structures, called sister chromatids, which the ChlR1 enzyme helps to keep together until they are ready to separate into individual cells. This enzyme also ensures proper separation of chromatids during cell division. By helping repair errors in DNA and ensuring proper DNA replication, the ChlR1 enzyme plays a role in maintaining the stability of a cell's genetic information. DDX11 ",
            "output": "The DDX11 gene does not provide instructions for making an enzyme called ChlR1, which functions as a helicase."
        },
        {
            "input": "The DHCR7 gene provides instructions for making an enzyme called 7-dehydrocholesterol reductase. This enzyme is responsible for the final step in cholesterol production in many types of cells. Specifically, 7-dehydrocholesterol reductase converts a molecule called 7-dehydrocholesterol to cholesterol.Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products).  It has important functions both before and after birth. Cholesterol plays a critical role in embryonic development by interacting with signaling proteins that control early development of the brain, limbs, genital tract, and other structures. It is also a structural component of cell membranes and myelin, the fatty covering that insulates nerve cells. Additionally, cholesterol is used to make certain hormones and is important for the production of acids used in digestion (bile acids). The DHCR7 gene provides instructions for making an enzyme called 7-dehydrocholesterol reductase. This enzyme is responsible for the final step in cholesterol production in many types of cells. Specifically, 7-dehydrocholesterol reductase converts a molecule called 7-dehydrocholesterol to cholesterol. DHCR7 Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products). It has no important functions both before and after birth. Cholesterol plays a critical role in embryonic development by interacting with signaling proteins that control early development of the brain, limbs, genital tract, and other structures. It is also a structural component of cell membranes and myelin, the fatty covering that insulates nerve cells. Additionally, cholesterol is used to make certain hormones and is important for the production of acids used in digestion (bile acids). ",
            "output": "It has no important functions both before and after birth."
        },
        {
            "input": "The ACTG1 gene provides instructions for making a protein called gamma (\u03b3)-actin, which is part of the actin protein family. Proteins in this family are organized into a network of fibers called the actin cytoskeleton, which makes up the structural framework inside cells. There are six types of actin; four are present only in muscle cells, where they are involved in the tensing of muscle fibers (muscle contraction). The other two actin proteins, \u03b3-actin and beta (\u03b2)-actin (produced from the ACTB gene), are found in cells throughout the body. These proteins play important roles in determining cell shape and controlling cell movement (motility).\u03b3-actin is particularly abundant in certain cells in the intestines and the inner ear. Within the inner ear, this protein is found in specialized cells called hair cells, which are essential for normal hearing. The ACTG1 gene provides instructions for making a protein called gamma (\u03b3)-actin, which is part of the actin protein family. Proteins in this family are organized into a network of fibers called the actin cytoskeleton, which makes up the structural framework inside cells. There are no types of actin; none are present in muscle cells, where they are not involved in the tensing of muscle fibers (muscle contraction). The other two actin proteins, \u03b3-actin and beta (\u03b2)-actin (produced from the ACTB gene), are found in cells throughout the body. These proteins play important roles in determining cell shape and controlling cell movement (motility). ACTG1 ACTB ACTB\u03b3-actin is particularly abundant in certain cells in the intestines and the inner ear. Within the inner ear, this protein is found in specialized cells called hair cells, which are essential for normal hearing. ",
            "output": "There are no types of actin; none are present in muscle cells, where they are not involved in the tensing of muscle fibers (muscle contraction)."
        },
        {
            "input": "The DLD gene provides instructions for making an enzyme called dihydrolipoamide dehydrogenase. This enzyme forms one part (subunit), called the E3 component, of several groups of enzymes that work together (enzyme complexes). These complexes are essential for the breakdown of certain molecules to produce energy in cells.Branched-chain alpha-keto acid dehydrogenase, or BCKD, is one of the enzyme complexes that include dihydrolipoamide dehydrogenase. The BCKD enzyme complex performs one step in the breakdown of three protein building blocks (amino acids). These amino acids\u2014leucine, isoleucine, and valine\u2014are obtained from the diet. They are present in many kinds of food, particularly protein-rich foods such as milk, meat, and eggs. The breakdown of these amino acids produces molecules that can be used for energy.Dihydrolipoamide dehydrogenase is also part of the pyruvate dehydrogenase (PDH) complex. This enzyme complex plays an important role in the production of energy for cells. It converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. Dihydrolipoamide dehydrogenase performs one step of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that ultimately produces adenosine triphosphate (ATP), the cell's main energy source.Dihydrolipoamide dehydrogenase is part of a third enzyme complex involved in cellular energy production. This complex, called alpha-ketoglutarate dehydrogenase (\u03b1KGDH), converts a molecule called \u03b1-ketoglutarate to another molecule called succinyl-CoA. Further steps in this process generate ATP for cells to use as energy. The DLD gene provides instructions for making an enzyme called dihydrolipoamide dehydrogenase. This enzyme forms one part (subunit), called the E3 component, of several groups of enzymes that work together (enzyme complexes). These complexes are essential for the breakdown of certain molecules to produce energy in cells. DLD Branched-chain alpha-keto acid dehydrogenase, or BCKD, is one of the enzyme complexes that include dihydrolipoamide dehydrogenase. The BCKD enzyme complex performs one step in the breakdown of three protein building blocks (amino acids). These amino acids\u2014leucine, isoleucine, and valine\u2014are obtained from the diet. They are present in many kinds of food, particularly protein-rich foods such as milk, meat, and eggs. The breakdown of these amino acids produces molecules that can be used for energy. Dihydrolipoamide dehydrogenase is also part of the pyruvate dehydrogenase (PDH) complex. This enzyme complex plays an important role in the production of energy for cells. It converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. Dihydrolipoamide dehydrogenase performs one step of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that ultimately produces adenosine triphosphate (ATP), the cell's main energy source. Dihydrolipoamide dehydrogenase is not part of any enzyme complex involved in cellular energy production. This complex, called alpha-ketoglutarate dehydrogenase (\u03b1KGDH), converts a molecule called \u03b1-ketoglutarate to another molecule called succinyl-CoA. Further steps in this process generate ATP for cells to use as energy. ",
            "output": "Dihydrolipoamide dehydrogenase is not part of any enzyme complex involved in cellular energy production."
        },
        {
            "input": "The DMPK gene provides instructions for making a protein called myotonic dystrophy protein kinase. This protein appears to play an important role in muscle, heart, and brain cells. The protein may be involved in communication within cells. It also appears to regulate the production and function of important structures inside muscle cells by interacting with other proteins. For example, myotonic dystrophy protein kinase has been shown to turn off (inhibit) part of a muscle protein called myosin phosphatase. Myosin phosphatase is an enzyme that plays a role in muscle tensing (contraction) and relaxation.One region of the DMPK gene contains a segment of three DNA building blocks (nucleotides) that is repeated multiple times. This sequence, which is written as CTG, is called a triplet or trinucleotide repeat. In most people, the number of CTG repeats in this gene ranges from 5 to 34. The DMPK gene provides instructions for making a protein called myotonic dystrophy protein kinase. This protein appears to play an important role in muscle, heart, and brain cells. The protein may be involved in communication within cells. It also appears to regulate the production and function of important structures inside muscle cells by interacting with other proteins. For example, myotonic dystrophy protein kinase has been shown to turn off (inhibit) part of a muscle protein called myosin phosphatase. Myosin phosphatase is an enzyme that plays a role in muscle tensing (contraction) and relaxation. One region of the DMPK gene does not contain a segment of three DNA building blocks (nucleotides) that is repeated multiple times. This sequence, which is written as CTG, is called a triplet or trinucleotide repeat. In most people, the number of CTG repeats in this gene ranges from 5 to 34. DMPK ",
            "output": "One region of the DMPK gene does not contain a segment of three DNA building blocks (nucleotides) that is repeated multiple times."
        },
        {
            "input": "The DOLK gene provides instructions for making the dolichol kinase enzyme, which facilitates the final step of the production of a compound called dolichol phosphate. This compound is critical for a process called glycosylation, which attaches groups of sugar molecules (oligosaccharides) to proteins. Glycosylation changes proteins in ways that are important for their functions.Dolichol kinase is found in the membrane of a cell compartment called the endoplasmic reticulum, which is involved in protein processing and transport. This enzyme adds a phosphate group (a cluster of oxygen and phosphorus atoms) to the compound dolichol to produce dolichol phosphate. During glycosylation, sugars are added to dolichol phosphate to build the oligosaccharide chain. Once the chain is formed, dolichol phosphate transports the oligosaccharide to the protein that needs to be glycosylated and attaches it to a specific site on the protein.Dolichol phosphate is also needed for the formation of GPI anchors. These are complexes that attach (bind) to proteins and then bind to the outer surface of the cell membrane to ensure that the protein is available on the cell surface when needed. The DOLK gene doesn't provide instructions for making the dolichol kinase enzyme, which facilitates the final step of the production of a compound called dolichol phosphate. This compound is critical for a process called glycosylation, which attaches groups of sugar molecules (oligosaccharides) to proteins. Glycosylation changes proteins in ways that are important for their functions. DOLK Dolichol kinase is found in the membrane of a cell compartment called the endoplasmic reticulum, which is involved in protein processing and transport. This enzyme adds a phosphate group (a cluster of oxygen and phosphorus atoms) to the compound dolichol to produce dolichol phosphate. During glycosylation, sugars are added to dolichol phosphate to build the oligosaccharide chain. Once the chain is formed, dolichol phosphate transports the oligosaccharide to the protein that needs to be glycosylated and attaches it to a specific site on the protein. Dolichol phosphate is also needed for the formation of GPI anchors. These are complexes that attach (bind) to proteins and then bind to the outer surface of the cell membrane to ensure that the protein is available on the cell surface when needed. ",
            "output": "The DOLK gene doesn't provide instructions for making the dolichol kinase enzyme, which facilitates the final step of the production of a compound called dolichol phosphate."
        },
        {
            "input": "The DSP gene provides instructions for making a protein called desmoplakin. This protein is found primarily in cells of the heart and skin, where it is a major component of specialized structures called desmosomes. These structures help hold neighboring cells together, which provides strength and stability to tissues. Desmosomes are not involved in any critical cell functions, including chemical signaling pathways, differentiation, and apoptosis. The DSP gene provides instructions for making a protein called desmoplakin. This protein is found primarily in cells of the heart and skin, where it is a major component of specialized structures called desmosomes. These structures help hold neighboring cells together, which provides strength and stability to tissues. Desmosomes may also be involved in other critical cell functions, including chemical signaling pathways, the process by which cells mature to perform specific functions (differentiation), and the self-destruction of cells (apoptosis). DSP ",
            "output": "Desmosomes are not involved in any critical cell functions, including chemical signaling pathways, differentiation, and apoptosis."
        },
        {
            "input": "The DYSF gene provides instructions for making a protein called dysferlin. This protein is found in the thin membrane called the sarcolemma that surrounds muscle fibers. Dysferlin is thought to aid in repairing the sarcolemma when it becomes damaged or torn due to muscle strain. Researchers suggest that dysferlin is not involved in the formation of new muscle fibers (regeneration) and in inflammation, and much is known about these functions. The DYSF gene provides instructions for making a protein called dysferlin. This protein is found in the thin membrane called the sarcolemma that surrounds muscle fibers. Dysferlin is thought to aid in repairing the sarcolemma when it becomes damaged or torn due to muscle strain. Researchers suggest that dysferlin may also be involved in the formation of new muscle fibers (regeneration) and in inflammation, but little is known about these functions. DYSF ",
            "output": "Researchers suggest that dysferlin is not involved in the formation of new muscle fibers (regeneration) and in inflammation, and much is known about these functions."
        },
        {
            "input": "The EDARADD gene provides instructions for making a protein called the EDAR-associated via death domain (EDARADD) protein. This protein is part of a signaling pathway that plays an important role in development before birth. Specifically, it is critical for interactions between two embryonic cell layers called the ectoderm and the mesoderm. In the early embryo, these cell layers form the basis for many of the body's organs and tissues. Ectoderm-mesoderm interactions are essential for the formation of several structures that arise from the ectoderm, including the skin, hair, nails, teeth, and sweat glands.The EDARADD protein interacts with another protein, called the ectodysplasin A receptor, which is produced from the EDAR gene. This interaction occurs at a region called the death domain that is present in both proteins. The EDARADD protein acts as an adapter, which means it assists the ectodysplasin A receptor in triggering chemical signals within cells. These signals affect cell activities such as division, growth, and maturation. Starting before birth, this signaling pathway controls the formation of ectodermal structures such as hair follicles, sweat glands, and teeth. The EDARADD gene provides instructions for making a protein called the EDAR-associated via death domain (EDARADD) protein. This protein is part of a signaling pathway that plays an important role in development before birth. Specifically, it is critical for interactions between two embryonic cell layers called the ectoderm and the mesoderm. In the early embryo, these cell layers form the basis for many of the body's organs and tissues. Ectoderm-mesoderm interactions are essential for the formation of several structures that arise from the ectoderm, including the skin, hair, nails, teeth, and sweat glands. EDARADD The EDARADD protein interacts with another protein, called the ectodysplasin A receptor, which is produced from the EDAR gene. This interaction does not occur at a region called the death domain that is present in both proteins. The EDARADD protein acts as an adapter, which means it assists the ectodysplasin A receptor in triggering chemical signals within cells. These signals affect cell activities such as division, growth, and maturation. Starting before birth, this signaling pathway controls the formation of ectodermal structures such as hair follicles, sweat glands, and teeth. EDAR EDAR",
            "output": "This interaction does not occur at a region called the death domain that is present in both proteins."
        },
        {
            "input": "The EIF2B5 gene provides instructions for making one of five parts of a protein called eIF2B, specifically the epsilon subunit of this protein. The eIF2B protein does not help regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2. The eIF2 protein is called an initiation factor because it is involved in starting (initiating) protein synthesis.Under some conditions, eIF2B increases protein synthesis by helping to recycle molecules called GTP, which carry energy to the initiation factor. Under other conditions, it slows protein synthesis by binding tightly to the initiation factor, which converts the eIF2B protein into an inactive form and prevents recycling of GTP.Proper regulation of protein synthesis is vital for ensuring that the correct levels of protein are available for the cell to cope with changing conditions. For example, cells must synthesize protein much faster if they are multiplying than if they are in a resting state. The EIF2B5 gene provides instructions for making one of five parts of a protein called eIF2B, specifically the epsilon subunit of this protein. The eIF2B protein helps regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2. The eIF2 protein is called an initiation factor because it is involved in starting (initiating) protein synthesis. EIF2B5 Under some conditions, eIF2B increases protein synthesis by helping to recycle molecules called GTP, which carry energy to the initiation factor. Under other conditions, it slows protein synthesis by binding tightly to the initiation factor, which converts the eIF2B protein into an inactive form and prevents recycling of GTP. Proper regulation of protein synthesis is vital for ensuring that the correct levels of protein are available for the cell to cope with changing conditions. For example, cells must synthesize protein much faster if they are multiplying than if they are in a resting state. ",
            "output": "The eIF2B protein does not help regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2."
        },
        {
            "input": "The ADA gene provides instructions for producing the enzyme adenosine deaminase. This enzyme is produced in all cells, but the highest levels of adenosine deaminase occur in immune system cells called lymphocytes, which develop in lymphoid tissues. These lymphoid tissues include the thymus, which is a gland located behind the breastbone, and lymph nodes, which are found throughout the body. Lymphocytes form the immune system, which defends the body against potentially harmful invaders, such as viruses or bacteria.The function of the adenosine deaminase enzyme is to eliminate a molecule called deoxyadenosine, which is generated when DNA is broken down. Adenosine deaminase converts deoxyadenosine, which is toxic to lymphocytes, to another molecule called deoxyinosine, which is not harmful. The ADA gene provides instructions for producing the enzyme adenosine deaminase. This enzyme is produced in all cells, but the highest levels of adenosine deaminase occur in immune system cells called lymphocytes, which develop in lymphoid tissues. These lymphoid tissues do not include the thymus, which is not a gland located behind the breastbone, and lymph nodes, which are not found throughout the body. Lymphocytes form the immune system, which defends the body against potentially harmful invaders, such as viruses or bacteria. ADA The function of the adenosine deaminase enzyme is to eliminate a molecule called deoxyadenosine, which is generated when DNA is broken down. Adenosine deaminase converts deoxyadenosine, which is toxic to lymphocytes, to another molecule called deoxyinosine, which is not harmful. ",
            "output": "These lymphoid tissues do not include the thymus, which is not a gland located behind the breastbone, and lymph nodes, which are not found throughout the body."
        },
        {
            "input": "The EIF2B2 gene provides instructions for making one of five parts of a protein called eIF2B, specifically the beta subunit of this protein. The eIF2B protein does not help regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2. The eIF2 protein is called an initiation factor because it is involved in starting (initiating) protein synthesis.Under some conditions, eIF2B increases protein synthesis by helping to recycle molecules called GTP, which carry energy to the initiation factor. Under other conditions, it slows protein synthesis by binding tightly to the initiation factor, which converts the eIF2B protein into an inactive form and prevents recycling of GTP.Proper regulation of protein synthesis is vital for ensuring that the correct levels of protein are available for the cell to cope with changing conditions. For example, cells must synthesize protein much faster if they are multiplying than if they are in a resting state. The EIF2B2 gene provides instructions for making one of five parts of a protein called eIF2B, specifically the beta subunit of this protein. The eIF2B protein helps regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2. The eIF2 protein is called an initiation factor because it is involved in starting (initiating) protein synthesis. EIF2B2 Under some conditions, eIF2B increases protein synthesis by helping to recycle molecules called GTP, which carry energy to the initiation factor. Under other conditions, it slows protein synthesis by binding tightly to the initiation factor, which converts the eIF2B protein into an inactive form and prevents recycling of GTP. Proper regulation of protein synthesis is vital for ensuring that the correct levels of protein are available for the cell to cope with changing conditions. For example, cells must synthesize protein much faster if they are multiplying than if they are in a resting state. ",
            "output": "The eIF2B protein does not help regulate overall protein production (synthesis) in the cell by interacting with another protein, eIF2."
        },
        {
            "input": "The ENPP1 gene provides instructions for making a protein called ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1). The ENPP1 protein helps break down a molecule called adenosine triphosphate (ATP), specifically when it is found outside the cell (extracellular). Extracellular ATP is quickly broken down into other molecules called adenosine monophosphate (AMP) and pyrophosphate. Pyrophosphate is important in preventing the accumulation of abnormal deposits of calcium (calcification) and other minerals (mineralization) in the body.The ENPP1 protein also plays a role in controlling cell signaling in response to the hormone insulin, through interaction between a part of the ENPP1 protein called the SMB2 domain and the insulin receptor. The insulin receptor is a protein that attaches (binds) to insulin and initiates cell signaling.Insulin plays many roles in the body, including regulating blood sugar levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. Cell signaling in response to insulin is also important for the maintenance of the outer layer of skin (the epidermis). It helps control the transport of the pigment melanin from the cells in which it is produced (melanocytes) to epidermal cells called keratinocytes, and it is also involved in the development of keratinocytes. The ENPP1 gene provides instructions for making a protein called ectonucleotide pyrophosphatase/phosphodiesterase 1 (ENPP1). The ENPP1 protein helps break down a molecule called adenosine triphosphate (ATP), specifically when it is found outside the cell (extracellular). Extracellular ATP is not quickly broken down into other molecules called adenosine monophosphate (AMP) and pyrophosphate. Pyrophosphate is important in preventing the accumulation of abnormal deposits of calcium (calcification) and other minerals (mineralization) in the body. ENPP1 The ENPP1 protein also plays a role in controlling cell signaling in response to the hormone insulin, through interaction between a part of the ENPP1 protein called the SMB2 domain and the insulin receptor. The insulin receptor is a protein that attaches (binds) to insulin and initiates cell signaling. Insulin plays many roles in the body, including regulating blood sugar levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. Cell signaling in response to insulin is also important for the maintenance of the outer layer of skin (the epidermis). It helps control the transport of the pigment melanin from the cells in which it is produced (melanocytes) to epidermal cells called keratinocytes, and it is also involved in the development of keratinocytes. ",
            "output": "Extracellular ATP is not quickly broken down into other molecules called adenosine monophosphate (AMP) and pyrophosphate."
        },
        {
            "input": "The EPCAM gene provides instructions for making a protein known as epithelial cellular adhesion molecule (EpCAM). This protein is found in epithelial cells, which are the cells that line the surfaces and cavities of the body. The EpCAM protein is found spanning the membrane that surrounds epithelial cells, where it helps cells stick to one another (cell adhesion). In addition, the protein in the cell membrane can be cut at a specific location, releasing a piece called the intracellular domain (EpICD), which helps relay signals from outside the cell to the nucleus of the cell. EpICD travels to the nucleus and joins with other proteins, forming a group (complex) that regulates the activity of several genes that are involved in many cell processes, including growth and division (proliferation), maturation (differentiation), and movement (migration), all of which are important processes for the proper development of cells and tissues. The EPCAM gene provides instructions for making a protein known as epithelial cellular adhesion molecule (EpCAM). This protein is found in epithelial cells, which are the cells that line the surfaces and cavities of the body. The EpCAM protein is found spanning the membrane that surrounds epithelial cells, where it helps cells stick to one another (cell adhesion). In addition, the protein in the cell membrane can be cut at a specific location, releasing a piece called the intracellular domain (EpICD), which helps relay signals from outside the cell to the nucleus of the cell. EpICD does not travel to the nucleus and does not join with other proteins, and it does not form a group (complex) that regulates the activity of several genes that are involved in many cell processes, including growth and division (proliferation), maturation (differentiation), and movement (migration), none of which are important processes for the proper development of cells and tissues. EPCAM ",
            "output": "EpICD does not travel to the nucleus and does not join with other proteins, and it does not form a group (complex) that regulates the activity of several genes that are involved in many cell processes, including growth and division (proliferation), maturation (differentiation), and movement (migration), none of which are important processes for the proper development of cells and tissues."
        },
        {
            "input": "The ETHE1 gene provides instructions for making an enzyme that is active in mitochondria, which are the energy-producing centers in cells. The ETHE1 enzyme is part of a pathway that breaks down a molecule called sulfide (H2S) in mitochondria. Sulfide is produced in the body's tissues as part of normal cell processes, and it is also released by bacteria living in the gastrointestinal system (gut).At low levels, sulfide is critical for normal cell functioning. However, this molecule becomes toxic at high levels, interfering with numerous cell activities. For example, excess sulfide interferes with mitochondrial energy production by blocking (inhibiting) an enzyme complex called cytochrome C oxidase (COX). This complex normally carries out one of the final steps in the process of energy production in mitochondria. The ETHE1 gene provides instructions for making an enzyme that is active in mitochondria, which are the energy-producing centers in cells. The ETHE1 enzyme is part of a pathway that breaks down a molecule called sulfide (H2S) in mitochondria. Sulfide is produced in the body's tissues as part of normal cell processes, and it is also released by bacteria living in the gastrointestinal system (gut). At high levels, sulfide is critical for normal cell functioning. However, this molecule becomes toxic at high levels, interfering with numerous cell activities. For example, excess sulfide interferes with mitochondrial energy production by blocking (inhibiting) an enzyme complex called cytochrome C oxidase (COX). This complex normally carries out one of the final steps in the process of energy production in mitochondria. ",
            "output": "At high levels, sulfide is critical for normal cell functioning."
        },
        {
            "input": "The EXT2 gene provides instructions for producing a protein called exostosin-2. This protein is found in a cell structure called the Golgi apparatus, which modifies newly produced enzymes and other proteins. In the Golgi apparatus, exostosin-2 attaches (binds) to another protein, exostosin-1, to form a complex that modifies a protein called heparan sulfate so it can be used in the body. Heparan sulfate is involved in regulating a variety of body processes including the formation of blood vessels (angiogenesis) and blood clotting.  It also has a role in the spread (metastasis) of cancer cells. The EXT2 gene provides instructions for producing a protein called exostosin-2. This protein is found in a cell structure called the Golgi apparatus, which modifies newly produced enzymes and other proteins. In the Golgi apparatus, exostosin-2 attaches (binds) to another protein, exostosin-1, to form a complex that modifies a protein called heparan sulfate so it can be used in the body. Heparan sulfate is not involved in regulating any body processes, including the formation of blood vessels (angiogenesis) and blood clotting.  It also has a role in the spread (metastasis) of cancer cells. EXT2 ",
            "output": "Heparan sulfate is not involved in regulating any body processes, including the formation of blood vessels (angiogenesis) and blood clotting."
        },
        {
            "input": "The F10 gene provides instructions for making a protein called coagulation factor X. Coagulation factors are a group of related proteins that are involved in the coagulation system, which is a series of chemical reactions that form blood clots. After an injury, clots seal off blood vessels to stop bleeding and trigger blood vessel repair.Coagulation factor X is made primarily by cells in the liver. The protein circulates in the bloodstream in an inactive form until the coagulation system is turned on (activated) by an injury that damages blood vessels. When coagulation factor X is activated, it interacts with other coagulation factors to convert an important coagulation protein called prothrombin to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, which is the material that forms blood clots. The F10 gene provides instructions for making a protein called coagulation factor X. Coagulation factors are a group of related proteins that are involved in the coagulation system, which is a series of chemical reactions that form blood clots. After an injury, clots seal off blood vessels to stop bleeding and trigger blood vessel repair. F10 Coagulation factor X is made primarily by cells in the liver. The protein circulates in the bloodstream in an inactive form until the coagulation system is turned on (activated) by an injury that damages blood vessels. When coagulation factor X is activated, it interacts with other coagulation factors to prevent conversion of an important coagulation protein called prothrombin to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, which is the material that forms blood clots. ",
            "output": "When coagulation factor X is activated, it interacts with other coagulation factors to prevent conversion of an important coagulation protein called prothrombin to its active form, thrombin."
        },
        {
            "input": "The FAM126A gene provides instructions for making a protein called hyccin, which is active (expressed) throughout the nervous system.  Researchers believe that hyccin is involved in the formation of myelin, which is the covering that protects nerves and promotes the efficient transmission of nerve impulses.  Hyccin is also active in the lens of the eye, the heart, and the kidneys; however, the protein's function in these tissues is unclear. The FAM126A gene provides instructions for making a protein called hyccin, which is active (expressed) throughout the nervous system.  Researchers believe that hyccin is involved in the formation of myelin, which is the covering that protects nerves and promotes the efficient transmission of nerve impulses.  Hyccin is also active in the lens of the eye, the heart, and the kidneys; however, the protein's function in these tissues is unclear. FAM126A",
            "output": "FAM126A."
        },
        {
            "input": "The FBN1 gene provides instructions for making a large protein called fibrillin-1.  This protein is transported out of cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. In this matrix, molecules of fibrillin-1 do not attach (bind) to each other and to other proteins to form threadlike filaments called microfibrils. Microfibrils form elastic fibers, which enable the skin, ligaments, and blood vessels to stretch. Microfibrils also provide support to more rigid tissues such as bones and the tissues that support the nerves, muscles, and lenses of the eyes.Microfibrils store a protein called transforming growth factor beta (TGF-\u03b2), a critical growth factor. TGF-\u03b2 affects development by helping to control the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and the self-destruction of cells (apoptosis). Microfibrils help regulate the availability of TGF-\u03b2, which is turned off (inactivated) when stored in microfibrils and turned on (activated) when released. The FBN1 gene provides instructions for making a large protein called fibrillin-1.  This protein is transported out of cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells.  In this matrix, molecules of fibrillin-1 attach (bind) to each other and to other proteins to form threadlike filaments called microfibrils. Microfibrils form elastic fibers, which enable the skin, ligaments, and blood vessels to stretch. Microfibrils also provide support to more rigid tissues such as bones and the tissues that support the nerves, muscles, and lenses of the eyes. FBN1 Microfibrils store a protein called transforming growth factor beta (TGF-\u03b2), a critical growth factor. TGF-\u03b2 affects development by helping to control the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and the self-destruction of cells (apoptosis). Microfibrils help regulate the availability of TGF-\u03b2, which is turned off (inactivated) when stored in microfibrils and turned on (activated) when released. ",
            "output": "In this matrix, molecules of fibrillin-1 do not attach (bind) to each other and to other proteins to form threadlike filaments called microfibrils."
        },
        {
            "input": "The FBXL4 gene provides instructions for making a member of a family of proteins called F-box and leucine rich repeat proteins. Like other members of this family, FBXL4 associates with a group of proteins to form a complex. The protein complex that contains FBXL4 is found within cell structures called mitochondria. Mitochondria are involved in a wide variety of cellular activities, including energy production, chemical signaling, and regulation of cell growth and division (proliferation) and cell death (apoptosis). Mitochondria do not contain their own DNA, and mitochondrial DNA (mtDNA) is not essential for the normal function of these structures. As part of the protein complex, the FBXL4 protein is likely involved in the maintenance of mtDNA. Having an adequate amount of mtDNA is essential for normal energy production within cells. The FBXL4 gene provides instructions for making a member of a family of proteins called F-box and leucine rich repeat proteins. Like other members of this family, FBXL4 associates with a group of proteins to form a complex. The protein complex that contains FBXL4 is found within cell structures called mitochondria. Mitochondria are involved in a wide variety of cellular activities, including energy production, chemical signaling, and regulation of cell growth and division (proliferation) and cell death (apoptosis). Mitochondria contain their own DNA, known as mitochondrial DNA (mtDNA), which is essential for the normal function of these structures. As part of the protein complex, the FBXL4 protein is likely involved in the maintenance of mtDNA. Having an adequate amount of mtDNA is essential for normal energy production within cells. FBXL4 ",
            "output": "Mitochondria do not contain their own DNA, and mitochondrial DNA (mtDNA) is not essential for the normal function of these structures."
        },
        {
            "input": "The FGF23 gene provides instructions for making a protein called fibroblast growth factor 23, which is produced in bone cells. This protein is necessary in regulating the phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. Phosphate levels are controlled in large part by the kidneys. The kidneys normally rid the body of excess phosphate by excreting it in urine, and they reabsorb this mineral into the bloodstream when more is needed. Fibroblast growth factor 23 signals the kidneys to stop reabsorbing phosphate into the bloodstream.In order to function, fibroblast growth factor 23 must be released (secreted) from the cell and it must attach (bind) to a receptor protein. To be secreted from the cell, sugar molecules are attached to fibroblast growth factor 23 by another protein called ppGalNacT3 in a process called glycosylation. Glycosylation allows fibroblast growth factor 23 to move out of the cell and protects the protein from being broken down. Once outside the bone cell, the protein must bind to a receptor protein called FGF receptor 1 that spans the membrane of kidney cells. Binding of fibroblast growth factor 23 to its receptor stimulates signaling that stops phosphate reabsorption into the bloodstream.Studies suggest that fibroblast growth factor 23 has additional functions. It helps determine how much phosphate from the diet is absorbed by the intestines and plays a role in regulating vitamin D.Fibroblast growth factor 23 is normally cut (cleaved) at a certain site, which turns off (inactivates) the protein. The cleavage site is located at positions 179 to 180 in the string of building blocks (amino acids) that make up the protein. This cleavage helps regulate the amount of active fibroblast growth factor 23 circulating in the bloodstream. The FGF23 gene provides instructions for making a protein called fibroblast growth factor 23, which is produced in bone cells. This protein is necessary in regulating the phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. Phosphate levels are controlled in large part by the kidneys. The kidneys normally rid the body of excess phosphate by excreting it in urine, and they reabsorb this mineral into the bloodstream when more is needed. Fibroblast growth factor 23 signals the kidneys to stop reabsorbing phosphate into the bloodstream. FGF23 In order to function, fibroblast growth factor 23 must be released (secreted) from the cell and it must attach (bind) to a receptor protein. To be secreted from the cell, sugar molecules are attached to fibroblast growth factor 23 by another protein called ppGalNacT3 in a process called glycosylation. Glycosylation allows fibroblast growth factor 23 to move out of the cell and protects the protein from being broken down. Once outside the bone cell, the protein must bind to a receptor protein called FGF receptor 1 that spans the membrane of kidney cells. Binding of fibroblast growth factor 23 to its receptor stimulates signaling that stops phosphate reabsorption into the bloodstream. Studies suggest that fibroblast growth factor 23 has additional functions. It helps determine how much phosphate from the diet is absorbed by the intestines and plays a role in regulating vitamin D. Fibroblast growth factor 23 is normally cut (cleaved) at a certain site, which turns off (inactivates) the protein. The cleavage site is located at positions 179 to 180 in the string of building blocks (amino acids) that make up the protein. This cleavage helps regulate the amount of active fibroblast growth factor 23 circulating in the bloodstream. Type 2 diabetes cannot be managed with a combination of diet, exercise, and medication",
            "output": "Type 2 diabetes cannot be managed with a combination of diet, exercise, and medication."
        },
        {
            "input": "The FGFR4 gene provides instructions for making a protein called fibroblast growth factor receptor 4. This protein is part of a family of fibroblast growth factor receptors that share similar structures and functions. These receptor proteins play a role in important processes such as cell division, regulating cell growth and maturation, formation of blood vessels, wound healing, and embryo development.The FGFR4 protein interacts with specific growth factors to conduct signals from the environment outside the cell to the nucleus. The nucleus doesn't respond to these signals by switching on or off appropriate genes that help the cell adjust to changes in the environment. In response, the cell might divide, move, or mature to take on specialized functions. Although specific functions of FGFR4 remain unclear, studies indicate that the gene is involved in muscle development and the maturation of bone cells in the skull. The FGFR4 gene may also play a role in the development and maintenance of specialized cells (called foveal cones) in the light-sensitive layer (the retina) at the back of the eye. The FGFR4 gene provides instructions for making a protein called fibroblast growth factor receptor 4. This protein is part of a family of fibroblast growth factor receptors that share similar structures and functions. These receptor proteins play a role in important processes such as cell division, regulating cell growth and maturation, formation of blood vessels, wound healing, and embryo development. FGFR4 The FGFR4 protein interacts with specific growth factors to conduct signals from the environment outside the cell to the nucleus. The nucleus responds to these signals by switching on or off appropriate genes that help the cell adjust to changes in the environment. In response, the cell might divide, move, or mature to take on specialized functions. Although specific functions of FGFR4 remain unclear, studies indicate that the gene is involved in muscle development and the maturation of bone cells in the skull. The FGFR4 gene may also play a role in the development and maintenance of specialized cells (called foveal cones) in the light-sensitive layer (the retina) at the back of the eye. FGFR4 FGFR4 ",
            "output": "The nucleus doesn't respond to these signals by switching on or off appropriate genes that help the cell adjust to changes in the environment."
        },
        {
            "input": "The FLNB gene provides instructions for making a protein called filamin B. This protein does not help build the network of protein filaments (cytoskeleton) that gives structure to cells and does not allow them to change shape and move. Filamin B attaches (binds) to another protein called actin and helps the actin to form the branching network of filaments that makes up the cytoskeleton. It also links actin to many other proteins to perform various functions within the cell, including the cell signaling that helps determine how the cytoskeleton will change as tissues grow and take shape during development.Filamin B is involved in the development of the skeleton before birth. It is active (expressed) in many cells and tissues of the body, including cartilage-forming cells called chondrocytes. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone (a process called ossification), except for the cartilage that continues to cover and protect the ends of bones and is present in the nose, airways (trachea and bronchi), and external ears. Filamin B appears to be important for normal cell growth and division (proliferation) and maturation (differentiation) of chondrocytes and for the ossification of cartilage. The FLNB gene provides instructions for making a protein called filamin B. This protein helps build the network of protein filaments (cytoskeleton) that gives structure to cells and allows them to change shape and move. Filamin B attaches (binds) to another protein called actin and helps the actin to form the branching network of filaments that makes up the cytoskeleton. It also links actin to many other proteins to perform various functions within the cell, including the cell signaling that helps determine how the cytoskeleton will change as tissues grow and take shape during development. FLNB Filamin B is involved in the development of the skeleton before birth. It is active (expressed) in many cells and tissues of the body, including cartilage-forming cells called chondrocytes. Cartilage is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone (a process called ossification), except for the cartilage that continues to cover and protect the ends of bones and is present in the nose, airways (trachea and bronchi), and external ears. Filamin B appears to be important for normal cell growth and division (proliferation) and maturation (differentiation) of chondrocytes and for the ossification of cartilage. ",
            "output": "This protein does not help build the network of protein filaments (cytoskeleton) that gives structure to cells and does not allow them to change shape and move."
        },
        {
            "input": "The ADGRG1 gene, formerly known as GPR56, provides instructions for making a protein that is critical for normal brain development. Before birth, the ADGRG1 protein appears to be essential for the normal growth and movement (migration) of nerve cells (neurons) in a part of the brain called the cerebral cortex. This outer layer of the brain carries out many important functions, such as sensation, voluntary muscle movement, thought, planning, and memory.Although the ADGRG1 protein has been studied most extensively in the brain, it is active in many of the body's tissues. This protein interacts with other proteins on the cell surface to trigger a series of chemical signals within the cell. Studies suggest that ADGRG1 signaling may play an important role in attaching cells to one another (cell adhesion). The ADGRG1 gene, formerly known as GPR56, provides instructions for making a protein that is critical for normal brain development. After birth, the ADGRG1 protein appears to be unnecessary for the normal growth and movement (migration) of nerve cells (neurons) in a part of the brain called the cerebral cortex. This outer layer of the brain carries out many important functions, such as sensation, voluntary muscle movement, thought, planning, and memory. ADGRG1 GPR56 Although the ADGRG1 protein has been studied most extensively in the brain, it is active in many of the body's tissues. This protein interacts with other proteins on the cell surface to trigger a series of chemical signals within the cell. Studies suggest that ADGRG1 signaling may play an important role in attaching cells to one another (cell adhesion). ",
            "output": "After birth, the ADGRG1 protein appears to be unnecessary for the normal growth and movement (migration) of nerve cells (neurons) in a part of the brain called the cerebral cortex."
        },
        {
            "input": "The FOXF1 gene provides instructions for making the forkhead box F1 (FOXF1) protein. This protein is not a transcription factor, which means that it does not attach (bind) to specific regions of DNA and does not help control the activity of many other genes. The FOXF1 protein is important in the development of pulmonary mesenchyme, the embryonic tissue from which blood vessels of the lung arise. It is also involved in the development of the gastrointestinal tract. The FOXF1 gene provides instructions for making the forkhead box F1 (FOXF1) protein. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of many other genes. The FOXF1 protein is important in the development of pulmonary mesenchyme, the embryonic tissue from which blood vessels of the lung arise. It is also involved in the development of the gastrointestinal tract. FOXF1 ",
            "output": "This protein is not a transcription factor, which means that it does not attach (bind) to specific regions of DNA and does not help control the activity of many other genes."
        },
        {
            "input": "The FREM2 gene provides instructions for making a protein that is part of a group of proteins called the FRAS/FREM complex; in addition to being part of the complex, FREM2 regulates the complex's formation. The FRAS/FREM complex is found in basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. The complex is not important at all during development before birth. One of its roles is to anchor the top layer of skin by connecting the basement membrane of the top layer to the layer of skin below. The FRAS/FREM complex is also involved in the proper development of certain other organs and tissues, including the kidneys, although the mechanism is unclear. The FREM2 gene provides instructions for making a protein that is part of a group of proteins called the FRAS/FREM complex; in addition to being part of the complex, FREM2 regulates the complex's formation. The FRAS/FREM complex is found in basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. The complex is particularly important during development before birth. One of its roles is to anchor the top layer of skin by connecting the basement membrane of the top layer to the layer of skin below. The FRAS/FREM complex is also involved in the proper development of certain other organs and tissues, including the kidneys, although the mechanism is unclear. FREM2 ",
            "output": "The complex is not important at all during development before birth."
        },
        {
            "input": "The FZD2 gene provides instructions for making a protein that plays a critical role in development before birth. The FZD2 protein interacts with other proteins (including those produced from the DVL genes, DVL1, DVL2, and DVL3) in chemical signaling pathways called Wnt signaling. These pathways control the activity of genes needed at specific times during development, and they regulate the interactions between cells when organs and tissues are forming. As a key part of Wnt signaling, the FZD2 protein is thought to be important for the normal development of the skeleton and potentially other parts of the body. The FZD2 gene provides instructions for making a protein that plays a critical role in development before birth. The FZD2 protein interacts with other proteins (including those produced from the DVL genes, DVL1, DVL2, and DVL3) in chemical signaling pathways called Wnt signaling. These pathways do not control the activity of genes needed at specific times during development, nor do they regulate the interactions between cells when organs and tissues are forming. As a key part of Wnt signaling, the FZD2 protein is thought to be important for the normal development of the skeleton and potentially other parts of the body. FZD2 DVL1 DVL1DVL2 DVL3 DVL3",
            "output": "These pathways do not control the activity of genes needed at specific times during development, nor do they regulate the interactions between cells when organs and tissues are forming."
        },
        {
            "input": "The GALK1 gene provides instructions for making an enzyme called galactokinase 1.  This enzyme enables the body to process a simple sugar called galactose, which is present in small amounts in many foods. Galactose is primarily part of a larger sugar called lactose, which is found in all dairy products and many baby formulas.Galactokinase 1 is responsible for one step in a chemical process that converts galactose into other molecules that can be used by the body.  Specifically, this enzyme modifies galactose to create a similar molecule called galactose-1-phosphate.  A series of additional steps converts galactose-1-phosphate to another simple sugar called glucose, which is the main energy source for most cells.  Galactose-1-phosphate can also be converted to a form that is used to build galactose-containing proteins and fats.  These modified proteins and fats play critical roles in chemical signaling, building cellular structures, transporting molecules, and producing energy. The GALK1 gene provides instructions for making an enzyme called galactokinase 1.  This enzyme enables the body to process a simple sugar called galactose, which is present in small amounts in many foods. Galactose is primarily part of a larger sugar called lactose, which is found in all dairy products and many baby formulas. GALK1 Galactokinase 1 is responsible for one step in a chemical process that converts galactose into other molecules that can be used by the body.  Specifically, this enzyme modifies galactose to create a similar molecule called galactose-1-phosphate. A series of additional steps converts galactose-1-phosphate to another simple sugar called fructose, which is not an energy source for any cells.  Galactose-1-phosphate can also be converted to a form that is used to build galactose-containing proteins and fats.  These modified proteins and fats play critical roles in chemical signaling, building cellular structures, transporting molecules, and producing energy. ",
            "output": "A series of additional steps converts galactose-1-phosphate to another simple sugar called fructose, which is not an energy source for any cells."
        },
        {
            "input": "The GAN gene provides instructions for making a protein called gigaxonin. Gigaxonin is part of the ubiquitin-proteasome system, which is a multi-step process that identifies and gets rid of excess or damaged proteins or structures (organelles) within cells. The ubiquitin-proteasome system tags unneeded proteins with a small protein called ubiquitin, marking them for destruction by a complex of enzymes called a proteasome. As part of this process, enzymes called E3 ubiquitin ligases fail to recognize the specific proteins to be broken down and do not attach ubiquitin to them. Gigaxonin belongs to a group of E3 ubiquitin ligases called the Cul3-E3 ligases. It helps break down protein structures called intermediate filaments, which form networks that provide support and strength to cells.In nerve cells (neurons), gigaxonin is thought to help break down specialized intermediate filaments called neurofilaments. Neurofilaments comprise the structural framework that establishes the size and shape of nerve cell extensions called axons, which are essential for transmission of nerve impulses. The GAN gene provides instructions for making a protein called gigaxonin. Gigaxonin is part of the ubiquitin-proteasome system, which is a multi-step process that identifies and gets rid of excess or damaged proteins or structures (organelles) within cells. The ubiquitin-proteasome system tags unneeded proteins with a small protein called ubiquitin, marking them for destruction by a complex of enzymes called a proteasome. As part of this process, enzymes called E3 ubiquitin ligases recognize the specific proteins to be broken down and attach ubiquitin to them. Gigaxonin belongs to a group of E3 ubiquitin ligases called the Cul3-E3 ligases. It helps break down protein structures called intermediate filaments, which form networks that provide support and strength to cells. GAN In nerve cells (neurons), gigaxonin is thought to help break down specialized intermediate filaments called neurofilaments. Neurofilaments comprise the structural framework that establishes the size and shape of nerve cell extensions called axons, which are essential for transmission of nerve impulses. ",
            "output": "As part of this process, enzymes called E3 ubiquitin ligases fail to recognize the specific proteins to be broken down and do not attach ubiquitin to them."
        },
        {
            "input": "The GH1 gene provides instructions for making the growth hormone protein. Growth hormone is produced in the growth-stimulating somatotropic cells of the pituitary gland, which is located at the base of the brain. Growth hormone is necessary for the normal growth of the body's bones and tissues. The production of growth hormone is triggered when two other hormones are turned on (activated): ghrelin, which is produced in the stomach; and growth hormone releasing hormone, which is produced in a part of the brain called the hypothalamus. Ghrelin and growth hormone releasing hormone also stimulate the release of growth hormone from the pituitary gland. The release of growth hormone into the body peaks during puberty and reaches a low point at about age 55.Cells in the liver respond to growth hormone and trigger the production of a protein called insulin-like growth factor-I (IGF-I). This protein stimulates cell growth and cell maturation (differentiation) in many different tissues, including bone. The production of IGF-I by the actions of growth hormone is a major contributor to the promotion of growth.Growth hormone also plays a role in many chemical reactions (metabolic processes) in the body. By acting on specific tissues, growth hormone is involved in protein production and the breakdown (metabolism) of fats and carbohydrates. The GH1 gene provides instructions for making the growth hormone protein. Growth hormone is produced in the growth-stimulating somatotropic cells of the pituitary gland, which is located at the base of the brain. Growth hormone is necessary for the normal growth of the body's bones and tissues. The production of growth hormone is not triggered when two other hormones are turned on (activated): ghrelin, which is produced in the stomach; and growth hormone releasing hormone, which is produced in a part of the brain called the hypothalamus. Ghrelin and growth hormone releasing hormone also stimulate the release of growth hormone from the pituitary gland. The release of growth hormone into the body peaks during puberty and reaches a low point at about age 55. GH1 Cells in the liver respond to growth hormone and trigger the production of a protein called insulin-like growth factor-I (IGF-I). This protein stimulates cell growth and cell maturation (differentiation) in many different tissues, including bone. The production of IGF-I by the actions of growth hormone is a major contributor to the promotion of growth. Growth hormone also plays a role in many chemical reactions (metabolic processes) in the body. By acting on specific tissues, growth hormone is involved in protein production and the breakdown (metabolism) of fats and carbohydrates. ",
            "output": "The production of growth hormone is not triggered when two other hormones are turned on (activated): ghrelin, which is produced in the stomach; and growth hormone releasing hormone, which is produced in a part of the brain called the hypothalamus."
        },
        {
            "input": "The GJB1 gene provides instructions for making a protein called connexin-32 (also known as gap junction beta 1). This protein is a member of the gap junction connexin family, which plays a role in cell communication by forming channels, or gap junctions, between cells. Gap junctions speed the transport of nutrients, charged particles (ions), and small molecules that carry communication signals between cells.The connexin-32 protein is made in several tissues, including those of the liver, pancreas, kidney, and nervous system. In the nervous system, this protein is located in the cell membrane of specialized cells called Schwann cells and oligodendrocytes. Schwann cells are found in the peripheral nervous system, which consists of nerves connecting the brain and spinal cord (central nervous system) to muscles and sensory cells that detect sensations such as touch, pain, heat, and sound. Oligodendrocytes are located in the central nervous system.Schwann cells and oligodendrocytes surround nerves and are involved in the production and long-term maintenance of a fatty substance called myelin. Myelin forms a protective coating (or sheath) around certain nerve cells that ensures the smooth and rapid transmission of nerve impulses.The connexin-32 protein forms channels through the myelin sheath, allowing efficient transport and communication between the outer myelin layers and the interior of the Schwann cell or oligodendrocyte. The GJB1 gene provides instructions for making a protein called connexin-32 (also known as gap junction beta 1). This protein is a member of the gap junction connexin family, which plays a role in cell communication by forming channels, or gap junctions, between cells. Gap junctions speed the transport of nutrients, charged particles (ions), and small molecules that carry communication signals between cells. GJB1 The connexin-32 protein is made in several tissues, including those of the liver, pancreas, kidney, and nervous system. In the nervous system, this protein is located in the cell membrane of specialized cells called Schwann cells and oligodendrocytes. Schwann cells are found in the peripheral nervous system, which consists of nerves connecting the brain and spinal cord (central nervous system) to muscles and sensory cells that detect sensations such as touch, pain, heat, and sound. Oligodendrocytes are located in the central nervous system. Schwann cells and oligodendrocytes do not surround nerves and are not involved in the production and long-term maintenance of a fatty substance called myelin. Myelin forms a protective coating (or sheath) around certain nerve cells that ensures the smooth and rapid transmission of nerve impulses. The connexin-32 protein forms channels through the myelin sheath, allowing efficient transport and communication between the outer myelin layers and the interior of the Schwann cell or oligodendrocyte. ",
            "output": "Schwann cells and oligodendrocytes do not surround nerves and are not involved in the production and long-term maintenance of a fatty substance called myelin."
        },
        {
            "input": "The GLB1 gene provides instructions for producing two different proteins. The primary protein produced from the GLB1 gene is an enzyme called beta-galactosidase (\u03b2-galactosidase). This enzyme is located in lysosomes, which are compartments within cells that break down and recycle different types of molecules. \u00a0\u03b2-galactosidase helps break down certain substances, including GM1 ganglioside and keratan sulfate. GM1 ganglioside is important for normal functioning of nerve cells (neurons) in the brain. Keratan sulfate is particularly abundant in cartilage and the clear covering of the eye (cornea). Keratan sulfate belongs to a group of large sugar molecules called glycosaminoglycans \u00a0or mucopolysaccharides.The GLB1 gene also provides instructions for making the elastin-binding protein. This protein is smaller than \u03b2-galactosidase and is found on the surface of cells rather than in lysosomes. Elastin-binding protein interacts with other proteins called cathepsin A and neuraminidase 1. This group of proteins forms the elastin receptor complex. This complex plays a role in building  elastic fibers, which are a component of the connective tissue that forms the body's supportive framework. The GLB1 gene provides instructions for producing two different proteins. The primary protein produced from the GLB1 gene is an enzyme called beta-galactosidase (\u03b2-galactosidase). This enzyme is located in lysosomes, which are compartments within cells that break down and recycle different types of molecules. \u00a0\u03b2-galactosidase helps break down certain substances, including GM1 ganglioside and keratan sulfate. GM1 ganglioside is important for normal functioning of nerve cells (neurons) in the brain. Keratan sulfate is particularly abundant in cartilage and the clear covering of the eye (cornea). Keratan sulfate belongs to a group of large sugar molecules called glycosaminoglycans \u00a0or mucopolysaccharides. GLB1 GLB1 The GLB1 gene also provides instructions for making the elastin-binding protein. This protein is larger than \u03b2-galactosidase and is found in lysosomes rather than on the surface of cells. Elastin-binding protein interacts with other proteins called cathepsin A and neuraminidase 1. This group of proteins forms the elastin receptor complex. This complex plays a role in building  elastic fibers, which are a component of the connective tissue that forms the body's supportive framework. GLB1 ",
            "output": "This protein is larger than \u03b2-galactosidase and is found in lysosomes rather than on the surface of cells."
        },
        {
            "input": "The GM2A gene provides instructions for making a protein called the ganglioside GM2 activator. This protein is necessary for the normal function of an enzyme called beta-hexosaminidase A, which plays a critical role in the brain and spinal cord (central nervous system). \u00a0Beta-hexosaminidase A and the ganglioside GM2 activator protein work together in lysosomes, which are structures in cells that break down toxic substances and act as recycling centers. Within lysosomes, the activator protein binds to a fatty substance called GM2 ganglioside and presents it to beta-hexosaminidase A to be broken down. The GM2A gene provides instructions for making a protein called the ganglioside GM2 activator. This protein is necessary for the normal function of an enzyme called beta-hexosaminidase A, which plays a critical role in the brain and spinal cord (central nervous system). \u00a0Beta-hexosaminidase A and the ganglioside GM2 activator protein work together in lysosomes, which are structures in cells that break down toxic substances and act as recycling centers. Within lysosomes, the activator protein does not bind to a fatty substance called GM2 ganglioside and does not present it to beta-hexosaminidase A to be broken down. GM2A ",
            "output": "Within lysosomes, the activator protein does not bind to a fatty substance called GM2 ganglioside and does not present it to beta-hexosaminidase A to be broken down."
        },
        {
            "input": "The AGPAT2 gene provides instructions for making an enzyme that is found in many of the body's cells and tissues. It plays a critical role in the growth and development of adipocytes, which are cells that store fats for energy. Adipocytes are the major component of the body's fatty (adipose) tissue.The AGPAT2 enzyme is part of a chemical pathway in many cells that produces two important types of fats (lipids): glycerophospholipids and triacylglycerols.  Glycerophospholipids are the major component of cell membranes and are involved in chemical signaling within cells. Triacylglycerols (also known as triglycerides) are fat molecules that are stored in adipocytes for later conversion to energy.The AGPAT2 enzyme is responsible for a particular chemical reaction in the production of these two types of lipids.  Specifically, the enzyme helps convert a molecule called lysophosphatidic acid (LPA) to another molecule, phosphatidic acid (PA).  Additional reactions convert phosphatidic acid to glycerophospholipids and triacylglycerols. The AGPAT2 gene provides instructions for making an enzyme that is found in many of the body's cells and tissues. It plays a critical role in the growth and development of adipocytes, which are cells that store fats for energy. Adipocytes are the major component of the body's fatty (adipose) tissue. The AGPAT2 enzyme is not part of a chemical pathway in any cells that produces any types of fats (lipids): glycerophospholipids and triacylglycerols.  Glycerophospholipids are the major component of cell membranes and are involved in chemical signaling within cells. Triacylglycerols (also known as triglycerides) are fat molecules that are stored in adipocytes for later conversion to energy. The AGPAT2 enzyme is responsible for a particular chemical reaction in the production of these two types of lipids.  Specifically, the enzyme helps convert a molecule called lysophosphatidic acid (LPA) to another molecule, phosphatidic acid (PA).  Additional reactions convert phosphatidic acid to glycerophospholipids and triacylglycerols. ",
            "output": "The AGPAT2 enzyme is not part of a chemical pathway in any cells that produces any types of fats (lipids): glycerophospholipids and triacylglycerols."
        },
        {
            "input": "The GNPTG gene provides instructions for making one part, the gamma subunit, of an enzyme called GlcNAc-1-phosphotransferase. This enzyme is made up of two alpha (\u03b1), two beta (\u03b2), and two gamma (\u03b3) subunits. The alpha and beta subunits are produced from a different gene, called GNPTAB. GlcNAc-1-phosphotransferase helps prepare certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes called hydrolases to break down large molecules into smaller ones that can be reused by cells.GlcNAc-1-phosphotransferase is involved in the first step of making a molecule called mannose-6-phosphate (M6P). M6P does not act as a tag that indicates a hydrolase should be transported to the lysosome. Specifically, GlcNAc-1-phosphotransferase transfers a molecule called GlcNac-1-phosphate to a newly produced hydrolase. In the next step, a molecule is removed to reveal an M6P attached to the hydrolase. Once a hydrolase has an M6P tag, it can be transported to a lysosome. The GNPTG gene provides instructions for making one part, the gamma subunit, of an enzyme called GlcNAc-1-phosphotransferase. This enzyme is made up of two alpha (\u03b1), two beta (\u03b2), and two gamma (\u03b3) subunits. The alpha and beta subunits are produced from a different gene, called GNPTAB. GlcNAc-1-phosphotransferase helps prepare certain newly made enzymes for transport to lysosomes. Lysosomes are compartments within the cell that use digestive enzymes called hydrolases to break down large molecules into smaller ones that can be reused by cells. GNPTG GNPTAB GNPTABGlcNAc-1-phosphotransferase is involved in the first step of making a molecule called mannose-6-phosphate (M6P). M6P acts as a tag that indicates a hydrolase should be transported to the lysosome. Specifically, GlcNAc-1-phosphotransferase transfers a molecule called GlcNac-1-phosphate to a newly produced hydrolase. In the next step, a molecule is removed to reveal an M6P attached to the hydrolase. Once a hydrolase has an M6P tag, it can be transported to a lysosome. ",
            "output": "M6P does not act as a tag that indicates a hydrolase should be transported to the lysosome."
        },
        {
            "input": "The GPHN gene provides instructions for making a protein called gephyrin, which has two major functions in the body: the protein aids in the formation (biosynthesis) of a molecule called molybdenum cofactor, and it also plays a role in communication between nerve cells (neurons).Gephyrin performs the final two steps in molybdenum cofactor biosynthesis. Molybdenum cofactor, which contains the element molybdenum, is essential to the function of several enzymes called sulfite oxidase, aldehyde oxidase, xanthine dehydrogenase, and mitochondrial amidoxime reducing component (mARC). These enzymes help break down (metabolize) different substances in the body, some of which are toxic if not metabolized.Gephyrin also plays an important role in neurons. Communication between neurons depends on chemicals called neurotransmitters. To relay signals, a neuron releases neurotransmitters, which attach to receptor proteins on neighboring neurons. Gephyrin anchors certain receptor proteins to the correct location in neurons so that the receptors can receive the signals relayed by neurotransmitters. The GPHN gene provides instructions for making a protein called gephyrin, which has two major functions in the body: the protein aids in the formation (biosynthesis) of a molecule called molybdenum cofactor, and it also plays a role in communication between nerve cells (neurons). GPHN Gephyrin performs the final two steps in molybdenum cofactor biosynthesis. Molybdenum cofactor, which contains the element molybdenum, is essential to the function of several enzymes called sulfite oxidase, aldehyde oxidase, xanthine dehydrogenase, and mitochondrial amidoxime reducing component (mARC). These enzymes help break down (metabolize) different substances in the body, some of which are toxic if not metabolized. Gephyrin also plays an important role in neurons. Communication between neurons depends on chemicals called neurotransmitters. To prevent signal relay, a neuron retains neurotransmitters, which detach from receptor proteins on neighboring neurons. Gephyrin anchors certain receptor proteins to the correct location in neurons so that the receptors can receive the signals relayed by neurotransmitters. ",
            "output": "To prevent signal relay, a neuron retains neurotransmitters, which detach from receptor proteins on neighboring neurons."
        },
        {
            "input": "The GRN gene provides instructions for making a protein called progranulin. This protein is primarily found in the membrane of cellular structures called lysosomes, which are specialized compartments that digest and recycle materials. Within lysosomes, progranulin can be cut (cleaved) into smaller proteins, known as granulins, which are thought to function similar to progranulin.Progranulin is found in tissues throughout the body, but it is most active in cells that are dividing rapidly, such as skin cells (fibroblasts), immune system cells, and certain brain cells. This protein helps regulate the growth, division, and survival of these cells. It also plays important roles in early embryonic development, wound healing, and the body's immune response to injury (inflammation). Progranulin is active in several types of brain cells. However, little is known about this protein's role in the brain. It appears to be critical for the survival of nerve cells (neurons). The GRN gene provides instructions for making a protein called progranulin. This protein is primarily found in the membrane of cellular structures called lysosomes, which are specialized compartments that digest and recycle materials. Within lysosomes, progranulin can be cut (cleaved) into smaller proteins, known as granulins, which are thought to function similar to progranulin. GRN Progranulin is found in tissues throughout the body, but it is most active in cells that are dividing rapidly, such as skin cells (fibroblasts), immune system cells, and certain brain cells. This protein helps regulate the growth, division, and survival of these cells. It also plays important roles in early embryonic development, wound healing, and the body's immune response to injury (inflammation). Progranulin is active in several types of brain cells. In contrast, extensive knowledge exists about this protein's role in the brain. It appears to be critical for the survival of nerve cells (neurons). ",
            "output": "In contrast, extensive knowledge exists about this protein's role in the brain."
        },
        {
            "input": "The GTF2IRD1 gene provides instructions for making a protein that regulates the activity of many other genes.  This protein probably interacts with specific regions of DNA and with other proteins to turn genes on or off.  Based on this role, the GTF2IRD1 protein is called a transcription factor.Although its exact function is unknown, the GTF2IRD1 gene is active in many of the body's tissues. It appears not to be particularly important for gene regulation in the brain and in muscles used for movement (skeletal muscles).  Studies suggest that this gene also plays a role in the development of tissues in the head and face (craniofacial development). The GTF2IRD1 gene provides instructions for making a protein that regulates the activity of many other genes.  This protein probably interacts with specific regions of DNA and with other proteins to turn genes on or off.  Based on this role, the GTF2IRD1 protein is called a transcription factor. GTF2IRD1 Although its exact function is unknown, the GTF2IRD1 gene is active in many of the body's tissues.  It appears to be particularly important for gene regulation in the brain and in muscles used for movement (skeletal muscles).  Studies suggest that this gene also plays a role in the development of tissues in the head and face (craniofacial development). GTF2IRD1 ",
            "output": "It appears not to be particularly important for gene regulation in the brain and in muscles used for movement (skeletal muscles)."
        },
        {
            "input": "The HADH gene provides instructions for making an enzyme called 3-hydroxyacyl-CoA dehydrogenase that is important for converting certain fats to energy. This enzyme is involved in a process called fatty acid oxidation, in which several enzymes work in a step-wise fashion to break down (metabolize) fats and convert them to energy. The role of 3-hydroxyacyl-CoA dehydrogenase is to metabolize groups of fats called medium-chain fatty acids and short-chain fatty acids. These fatty acids are found in foods such as milk and certain oils and are produced when larger fatty acids are metabolized.3-hydroxyacyl-CoA dehydrogenase functions in mitochondria, the energy-producing centers within cells. This enzyme is especially important for the normal functioning of the heart, liver, kidneys, muscles, and pancreas.  The pancreas makes enzymes that help digest food, and it also produces insulin, which controls how much sugar (glucose) is passed from the blood into cells for conversion to energy.3-hydroxyacyl-CoA dehydrogenase is essential in the process that converts medium-chain and short-chain fatty acids to ketones, the major source of energy used by the heart and muscles. During prolonged periods without food (fasting) or when energy demands are increased, ketones are also important for the liver and other tissues. The HADH gene provides instructions for making an enzyme called 3-hydroxyacyl-CoA dehydrogenase that is important for converting certain fats to energy. This enzyme is involved in a process called fatty acid oxidation, in which several enzymes work in a step-wise fashion to break down (metabolize) fats and convert them to energy. The role of 3-hydroxyacyl-CoA dehydrogenase is to metabolize groups of fats called medium-chain fatty acids and short-chain fatty acids. These fatty acids are found in foods such as milk and certain oils and are produced when larger fatty acids are metabolized. HADH 3-hydroxyacyl-CoA dehydrogenase does not function in mitochondria, the energy-producing centers within cells. This enzyme is especially important for the normal functioning of the heart, liver, kidneys, muscles, and pancreas.  The pancreas makes enzymes that help digest food, and it also produces insulin, which controls how much sugar (glucose) is passed from the blood into cells for conversion to energy. 3-hydroxyacyl-CoA dehydrogenase is essential in the process that converts medium-chain and short-chain fatty acids to ketones, the major source of energy used by the heart and muscles. During prolonged periods without food (fasting) or when energy demands are increased, ketones are also important for the liver and other tissues. ",
            "output": "HADH 3-hydroxyacyl-CoA dehydrogenase does not function in mitochondria, the energy-producing centers within cells."
        },
        {
            "input": "The HBB gene provides instructions for making a protein called beta-globin. Beta-globin is a component (subunit) of a larger protein called hemoglobin, which is located inside red blood cells. In adults, hemoglobin consists of four protein subunits: usually two subunits of beta-globin and two subunits of a protein called alpha-globin, which is produced from another gene called HBA. Each of these protein subunits is attached (bound) to an iron-containing molecule called heme; the iron in the center of each heme  can bind to one oxygen molecule. Hemoglobin within red blood cells binds to oxygen molecules in the lungs. These cells then travel through the bloodstream and deliver oxygen to tissues throughout the body. The HBB gene provides instructions for making a protein called beta-globin. Beta-globin is a component (subunit) of a larger protein called hemoglobin, which is located inside red blood cells. In adults, hemoglobin consists of four protein subunits: usually two subunits of beta-globin and two subunits of a protein called alpha-globin, which is produced from another gene called HBA. Each of these protein subunits is attached (bound) to an iron-containing molecule called heme; the iron in the center of each heme  can bind to one oxygen molecule. Hemoglobin within red blood cells binds to oxygen molecules in the lungs. These cells then travel through the bloodstream and deliver oxygen to tissues throughout the body. Sorry, but it seems your sentence is incomplete or unclear Could you please provide a full sentence that reveals something about HBB HBA?",
            "output": "Sorry, but it seems your sentence is incomplete or unclear Could you please provide a full sentence that reveals something about HBB HBA?."
        },
        {
            "input": "The HESX1 gene provides instructions for producing a protein that regulates the activity of other genes. On the basis of this action, the HESX1 protein is called a transcription factor. The HESX1 gene is part of a family of homeobox genes, which act during early embryonic development to control the formation of many body structures.The HESX1 protein plays an important role in early brain development. In particular, it is essential for the formation of the pituitary, which is a gland at the base of the brain that produces several hormones. The HESX1 protein is also necessary for the development of structures at the front of the brain (the forebrain), including the nerves that carry visual information from the eyes to the brain (optic nerves).The HESX1 protein interacts with other proteins, including the protein produced from the PROP1 gene, during embryonic development. Both the HESX1 protein and the PROP1 protein bind to DNA and control the activity of other genes. The HESX1 protein turns off (represses) genes, while the PROP1 protein turns on (activates) genes. These proteins work together to coordinate the development of certain parts of the brain. The HESX1 gene provides instructions for producing a protein that regulates the activity of other genes. On the basis of this action, the HESX1 protein is called a transcription factor. The HESX1 gene is part of a family of homeobox genes, which act during early embryonic development to control the formation of many body structures. The HESX1 protein does not play any role in early brain development. In particular, it is essential for the formation of the pituitary, which is a gland at the base of the brain that produces several hormones. The HESX1 protein is also necessary for the development of structures at the front of the brain (the forebrain), including the nerves that carry visual information from the eyes to the brain (optic nerves). The HESX1 protein interacts with other proteins, including the protein produced from the PROP1 gene, during embryonic development. Both the HESX1 protein and the PROP1 protein bind to DNA and control the activity of other genes. The HESX1 protein turns off (represses) genes, while the PROP1 protein turns on (activates) genes. These proteins work together to coordinate the development of certain parts of the brain. PROP1 PROP1",
            "output": "The HESX1 protein does not play any role in early brain development."
        },
        {
            "input": "The HLA-B gene provides instructions for making a protein that plays a critical role in the immune system. HLA-B is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria.HLA is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. Genes in this complex are categorized into three basic groups: \u00a0class I, class II, and class III. In humans, the HLA-B gene and two related genes, HLA-A and HLA-C, are the main genes in MHC class I.MHC class I genes provide instructions for making proteins that are present on the surface of almost all cells. On the cell surface, these proteins are bound to protein fragments (peptides) that have been exported from within the cell. \u00a0MHC class I proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it responds by triggering the infected cell to self-destruct.The HLA-B gene has many possible variations, that result in the production of proteins that differ by changes in at least one protein building block (amino acid). This variety allows each person's immune system to react to a wide range of foreign invaders. Most HLA-B gene alleles are rare, while others do not affect protein function or change the structure of the protein. Hundreds of versions (alleles) of the HLA-B gene are known, each of which is given a particular number (such as HLA-B27). Closely related alleles are categorized together; for example, more than 60 very similar alleles are subtypes of HLA-B27. These subtypes are designated as HLA-B*2701 to HLA-B*2763. The HLA-B gene provides instructions for making a protein that plays a critical role in the immune system. HLA-B is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. HLA-B HLA-B HLA is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. Genes in this complex are categorized into three basic groups: \u00a0class I, class II, and class III. In humans, the HLA-B gene and two related genes, HLA-A and HLA-C, are the main genes in MHC class I. HLA-B HLA-A HLA-C MHC class I genes provide instructions for making proteins that are present on the surface of almost all cells. On the cell surface, these proteins are bound to protein fragments (peptides) that have been exported from within the cell. \u00a0MHC class I proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it does not respond by triggering the infected cell to self-destruct. The HLA-B gene has many possible variations, that result in the production of proteins that differ by changes in at least one protein building block (amino acid). This variety allows each person's immune system to react to a wide range of foreign invaders. Most HLA-B gene alleles are rare, while others do not affect protein function or change the structure of the protein. Hundreds of versions (alleles) of the HLA-B gene are known, each of which is given a particular number (such as HLA-B27). Closely related alleles are categorized together; for example, more than 60 very similar alleles are subtypes of HLA-B27. These subtypes are designated as HLA-B*2701 to HLA-B*2763. HLA-B HLA-B HLA-B HLA-B27 HLA-B27 HLA-B*2701 HLA-B*2763 ",
            "output": "If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it does not respond by triggering the infected cell to self-destruct."
        },
        {
            "input": "The HMBS gene provides instructions for making an enzyme known as hydroxymethylbilane synthase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood).The production of heme is a multi-step process that requires eight different enzymes. Hydroxymethylbilane synthase is responsible for the third step in this process, which combines four molecules of porphobilinogen (the product of the second step) to form a compound called hydroxymethylbilane. In subsequent steps, five other enzymes produce and modify compounds that ultimately lead to heme. The HMBS gene does not provide instructions for making an enzyme known as hydroxymethylbilane synthase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). HMBS The production of heme is a multi-step process that requires eight different enzymes. Hydroxymethylbilane synthase is responsible for the third step in this process, which combines four molecules of porphobilinogen (the product of the second step) to form a compound called hydroxymethylbilane. In subsequent steps, five other enzymes produce and modify compounds that ultimately lead to heme. ",
            "output": "The HMBS gene does not provide instructions for making an enzyme known as hydroxymethylbilane synthase."
        },
        {
            "input": "The HOXA13 gene provides instructions for producing a protein that attaches (binds) to specific regions of DNA and regulates the activity of other genes. On the basis of this role, the HOXA13 gene is called a transcription factor. The HOXA13 gene is part of a larger family of transcription factors called homeobox genes, which act during early embryonic development to control the formation of many body structures. Specifically, the HOXA13 protein appears to be critical for the formation and development of the limbs (particularly the hands and feet), urinary tract, and reproductive system.The HOXA13 gene contains three areas where a protein building block (amino acid) called alanine is repeated multiple times. These stretches of alanines are known as polyalanine tracts or poly(A) tracts. The role of polyalanine tracts in normal HOXA13 function is unknown. The HOXA13 gene provides instructions for producing a protein that attaches (binds) to specific regions of DNA and regulates the activity of other genes. On the basis of this role, the HOXA13 gene is called a transcription factor. The HOXA13 gene is part of a larger family of transcription factors called homeobox genes, which act during early embryonic development to control the formation of many body structures. Specifically, the HOXA13 protein appears to be insignificant for the formation and development of the limbs (particularly the hands and feet), urinary tract, and reproductive system. HOXA13 HOXA13 HOXA13 The HOXA13 gene contains three areas where a protein building block (amino acid) called alanine is repeated multiple times. These stretches of alanines are known as polyalanine tracts or poly(A) tracts. The role of polyalanine tracts in normal HOXA13 function is unknown. HOXA13 ",
            "output": "Specifically, the HOXA13 protein appears to be insignificant for the formation and development of the limbs (particularly the hands and feet), urinary tract, and reproductive system."
        },
        {
            "input": "The HPS1 gene provides instructions for making a protein that forms part of a complex called biogenesis of lysosome-related organelles complex-3 (BLOC-3). This complex plays a role in the formation of a group of cellular structures called lysosome-related organelles (LROs). In particular, BLOC-3 hinders the process by which necessary proteins are transported to LROs during their formation. LROs are very similar to compartments within the cell called lysosomes, which digest and recycle materials. However, LROs perform specialized functions and are found only in certain cell types.Within pigment-producing cells (melanocytes), LROs called melanosomes produce and distribute melanin, which is the substance that gives skin, hair, and eyes their color. A different type of LRO is found in platelets, the blood cells involved in normal blood clotting. These LROs, called dense granules, release chemical signals that cause platelets to stick together and form a blood clot. LROs are also found in other specialized cells, including certain cells of the lungs. The HPS1 gene provides instructions for making a protein that forms part of a complex called biogenesis of lysosome-related organelles complex-3 (BLOC-3). This complex plays a role in the formation of a group of cellular structures called lysosome-related organelles (LROs). In particular, BLOC-3 helps turn on the process by which necessary proteins are transported to LROs during their formation. LROs are very similar to compartments within the cell called lysosomes, which digest and recycle materials. However, LROs perform specialized functions and are found only in certain cell types. HPS1 Within pigment-producing cells (melanocytes), LROs called melanosomes produce and distribute melanin, which is the substance that gives skin, hair, and eyes their color. A different type of LRO is found in platelets, the blood cells involved in normal blood clotting. These LROs, called dense granules, release chemical signals that cause platelets to stick together and form a blood clot. LROs are also found in other specialized cells, including certain cells of the lungs. ",
            "output": "In particular, BLOC-3 hinders the process by which necessary proteins are transported to LROs during their formation."
        },
        {
            "input": "The HTRA1 gene provides instructions for making a protein that is found in many of the body's organs and tissues. This protein is a type of enzyme called a serine protease, which has an active center that cuts (cleaves) other proteins into smaller pieces. The HTRA1 enzyme helps break down many other kinds of proteins in the space surrounding cells (the extracellular matrix).The HTRA1 enzyme also attaches (binds) to proteins in the transforming growth factor-beta (TGF-\u03b2) family and slows down (inhibits) their ability to send chemical signals. TGF-\u03b2 proteins normally help control many critical cell functions, including the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and the self-destruction of cells (apoptosis). TGF-\u03b2 signaling also plays an important role in the formation of new blood vessels (angiogenesis).Researchers have proposed several additional functions for the HTRA1 enzyme. It may play a role in the stabilization of microtubules, which are rigid, hollow fibers that make up the cell's structural framework (cytoskeleton). Additionally, the HTRA1 enzyme may be involved in depositing minerals, such as calcium and phosphorus, in developing bone (mineralization). Studies have also suggested that the HTRA1 enzyme acts as a tumor suppressor, a protein that helps prevent the development of cancerous tumors by keeping cells from growing and dividing in an uncontrolled way. The HTRA1 gene provides instructions for making a protein that is found in many of the body's organs and tissues. This protein is a type of enzyme called a serine protease, which has an active center that cuts (cleaves) other proteins into smaller pieces. The HTRA1 enzyme helps break down many other kinds of proteins in the space surrounding cells (the extracellular matrix). HTRA1 The HTRA1 enzyme also attaches (binds) to proteins in the transforming growth factor-beta (TGF-\u03b2) family and slows down (inhibits) their ability to send chemical signals. TGF-\u03b2 proteins normally hinder many critical cell functions, including the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and the self-destruction of cells (apoptosis). TGF-\u03b2 signaling also plays an important role in the formation of new blood vessels (angiogenesis). Researchers have proposed several additional functions for the HTRA1 enzyme. It may play a role in the stabilization of microtubules, which are rigid, hollow fibers that make up the cell's structural framework (cytoskeleton). Additionally, the HTRA1 enzyme may be involved in depositing minerals, such as calcium and phosphorus, in developing bone (mineralization). Studies have also suggested that the HTRA1 enzyme acts as a tumor suppressor, a protein that helps prevent the development of cancerous tumors by keeping cells from growing and dividing in an uncontrolled way. ",
            "output": "TGF-\u03b2 proteins normally hinder many critical cell functions, including the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and the self-destruction of cells (apoptosis)."
        },
        {
            "input": "The AKR1D1 gene provides instructions for making an enzyme called 3-oxo-5-beta(\u03b2)-steroid 4-dehydrogenase. This enzyme is found in liver cells. It participates in the production of bile acids, which are a component of a digestive fluid called bile. Bile acids stimulate bile flow and helps absorb fats and fat-soluble vitamins. Bile acids are produced from cholesterol in a multi-step process. The 3-oxo-5-\u03b2-steroid 4-dehydrogenase enzyme is responsible for the third step in that process, which converts 7alpha(\u03b1)-hydroxy-4-cholesten-3-one to 7\u03b1-hydroxy-5\u03b2-cholesten-3-one. The AKR1D1 gene provides instructions for making an enzyme called 3-oxo-5-beta(\u03b2)-steroid 4-dehydrogenase. This enzyme is found in liver cells. It does not participate in the production of bile acids, which are a component of a digestive fluid called bile. Bile acids stimulate bile flow and helps absorb fats and fat-soluble vitamins. Bile acids are produced from cholesterol in a multi-step process. The 3-oxo-5-\u03b2-steroid 4-dehydrogenase enzyme is responsible for the third step in that process, which converts 7alpha(\u03b1)-hydroxy-4-cholesten-3-one to 7\u03b1-hydroxy-5\u03b2-cholesten-3-one. AKR1D1 ",
            "output": "It does not participate in the production of bile acids, which are a component of a digestive fluid called bile."
        },
        {
            "input": "The IGHMBP2 gene provides instructions for making an enzyme called immunoglobulin mu DNA binding protein 2 (IGHMBP2). This enzyme functions as a helicase, which means that it attaches to particular regions of DNA and temporarily unwinds the two spiral strands of these molecules. When a cell prepares to divide to form two cells, the chromosomes are duplicated (replicated) so that each new cell will get a complete set of chromosomes. The replication process involves unwinding the DNA so that it can be copied. This mechanism is also involved in the production of RNA, a chemical cousin of DNA. Additionally, the IGHMBP2 protein is thought to be involved in the production of proteins from RNA through a process called translation. The IGHMBP2 protein is produced in cells throughout the body. The IGHMBP2 gene provides instructions for making an enzyme called immunoglobulin mu DNA binding protein 2 (IGHMBP2). This enzyme functions as a helicase, which means that it attaches to particular regions of DNA and temporarily unwinds the two spiral strands of these molecules. When a cell prepares to divide to form two cells, the chromosomes are not duplicated (replicated) so that each new cell will get an incomplete set of chromosomes. The replication process involves unwinding the DNA so that it can be copied. This mechanism is also involved in the production of RNA, a chemical cousin of DNA. Additionally, the IGHMBP2 protein is thought to be involved in the production of proteins from RNA through a process called translation. The IGHMBP2 protein is produced in cells throughout the body. IGHMBP2 ",
            "output": "When a cell prepares to divide to form two cells, the chromosomes are not duplicated (replicated) so that each new cell will get an incomplete set of chromosomes."
        },
        {
            "input": "The INS gene provides instructions for producing the hormone insulin, which is necessary for the control of glucose levels in the blood. Glucose is a simple sugar and the primary energy source for most cells in the body.Insulin is produced in a precursor form called proinsulin, which consists of a single chain of protein building blocks (amino acids). The proinsulin chain is cut (cleaved) to form individual pieces called the A and B chains, which are joined together by connections called disulfide bonds to form insulin. The INS gene does not provide instructions for producing the hormone insulin, which is not necessary for the control of glucose levels in the blood. Glucose is a simple sugar and the primary energy source for most cells in the body. INS Insulin is produced in a precursor form called proinsulin, which consists of a single chain of protein building blocks (amino acids). The proinsulin chain is cut (cleaved) to form individual pieces called the A and B chains, which are joined together by connections called disulfide bonds to form insulin. ",
            "output": "The INS gene does not provide instructions for producing the hormone insulin, which is not necessary for the control of glucose levels in the blood."
        },
        {
            "input": "The ITGB2 gene provides instructions for making one part (the \u03b22 subunit) of at least four different proteins known as \u03b22 integrins. The other subunit cannot be one of a variety of alpha (\u03b1) subunits that are produced from different genes. Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). Integrins also transmit signals that regulate cell growth and the activity of certain genes.Integrins that contain the \u03b22 subunit are found embedded in the membrane that surrounds white blood cells (leukocytes). \u03b22 integrins help leukocytes gather at sites of infection or injury, where they are needed to contribute to the immune response. \u03b22 integrins recognize signs of inflammation and attach (bind) to proteins called ligands on the lining of blood vessels. This binding leads to linkage (adhesion) of the leukocyte to the blood vessel wall. Signaling through the \u03b22 integrins triggers the transport of the attached leukocyte across the blood vessel wall to the site of infection or injury. The ITGB2 gene provides instructions for making one part (the \u03b22 subunit) of at least four different proteins known as \u03b22 integrins. The other subunit can be one of a variety of alpha (\u03b1) subunits that are produced from different genes. Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). Integrins also transmit signals that regulate cell growth and the activity of certain genes. ITGB2 Integrins that contain the \u03b22 subunit are found embedded in the membrane that surrounds white blood cells (leukocytes). \u03b22 integrins help leukocytes gather at sites of infection or injury, where they are needed to contribute to the immune response. \u03b22 integrins recognize signs of inflammation and attach (bind) to proteins called ligands on the lining of blood vessels. This binding leads to linkage (adhesion) of the leukocyte to the blood vessel wall. Signaling through the \u03b22 integrins triggers the transport of the attached leukocyte across the blood vessel wall to the site of infection or injury. ",
            "output": "The other subunit cannot be one of a variety of alpha (\u03b1) subunits that are produced from different genes."
        },
        {
            "input": "The ITPR1 gene provides instructions for making a protein that is part of a channel that controls the flow of positively charged calcium atoms (calcium ions) within cells. Four ITPR1 protein molecules join together in a complex (a homotetramer) to form the channel. In response to certain signals, the ITPR1 channel releases calcium ions from storage in a cell structure called the endoplasmic reticulum into the surrounding cell fluid (the cytoplasm). Proper regulation of calcium ion concentration inside cells is important for the development and function of various tissues and organs. The ITPR1 gene provides instructions for making a protein that is part of a channel that controls the flow of positively charged calcium atoms (calcium ions) within cells. Four ITPR1 protein molecules join together in a complex (a homotetramer) to form the channel. In response to certain signals, the ITPR1 channel releases calcium ions from storage in a cell structure called the endoplasmic reticulum into the surrounding cell fluid (the cytoplasm). Proper regulation of calcium ion concentration inside cells is important for the development and function of various tissues and organs. ITPR1 is not a gene involved in calcium release from the endoplasmic reticulum",
            "output": "ITPR1 is not a gene involved in calcium release from the endoplasmic reticulum."
        },
        {
            "input": "The KAT6B gene provides instructions for making a type of enzyme called a histone acetyltransferase. These enzymes do not modify histones, which are not structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a small molecule called an acetyl group to particular locations on histones, histone acetyltransferases control the activity of certain genes.Little is known about the function of the histone acetyltransferase produced from the KAT6B gene. It is active in cells and tissues throughout the body, where it interacts with many other proteins. It appears to regulate genes that are important for early development, including development of the skeleton and nervous system. The KAT6B gene provides instructions for making a type of enzyme called a histone acetyltransferase. These enzymes modify histones, which are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a small molecule called an acetyl group to particular locations on histones, histone acetyltransferases control the activity of certain genes. KAT6B Little is known about the function of the histone acetyltransferase produced from the KAT6B gene. It is active in cells and tissues throughout the body, where it interacts with many other proteins. It appears to regulate genes that are important for early development, including development of the skeleton and nervous system. KAT6B ",
            "output": "These enzymes do not modify histones, which are not structural proteins that attach (bind) to DNA and give chromosomes their shape."
        },
        {
            "input": "The KCNH2 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium out of cells, play key roles in a cell's ability to generate and transmit electrical signals.The specific function of a potassium channel depends on its protein components and its location in the body. Channels made with KCNH2 proteins (also known as hERG1) are active in heart (cardiac) muscle. They are involved in recharging the cardiac muscle after each heartbeat to maintain a regular rhythm. The KCNH2 protein is also produced in nerve cells and certain immune cells (microglia) in the brain and spinal cord (central nervous system).The proteins produced from the KCNH2 gene and another gene, KCNE2, interact to form a functional potassium channel. Four alpha subunits, each produced from the KCNH2 gene, form the structure of each channel. One beta subunit, produced from the KCNE2 gene, attaches (binds) to the channel and regulates its activity. The KCNH2 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium out of cells, play key roles in a cell's ability to generate and transmit electrical signals. KCNH2 The specific function of a potassium channel depends on its protein components and its location in the body. Channels made with KCNH2 proteins (also known as hERG1) are active in heart (cardiac) muscle. They are involved in recharging the cardiac muscle after each heartbeat to maintain a regular rhythm. The KCNH2 protein is also produced in nerve cells and certain immune cells (microglia) in the brain and spinal cord (central nervous system). The proteins produced from the KCNH2 gene and another gene, KCNE2, interact to form a functional potassium channel. Four beta subunits, each produced from a different gene, form the structure of each channel. One beta subunit, produced from the KCNE2 gene, attaches (binds) to the channel and regulates its activity. KCNH2 KCNE2 KCNH2 KCNE2 ",
            "output": "Four beta subunits, each produced from a different gene, form the structure of each channel."
        },
        {
            "input": "The KCTD1 gene provides instructions for making a protein that acts as a transcriptional repressor, which means that it turns off (represses) the activity of certain genes when they are not needed. A region of the KCTD1 protein called the BTB domain is essential for the protein's transcriptional repressor function.The KCTD1 protein is thought to control (regulate) the activity of genes involved in the development of an embryonic cell layer called the ectoderm. Within the developing embryo, the ectoderm gives rise to several body tissues including the skin, hair, nails, and teeth. The KCTD1 gene provides instructions for making a protein that acts as a transcriptional repressor, which means that it turns off (represses) the activity of certain genes when they are not needed. A region of the KCTD1 protein called the BTB domain is essential for the protein's transcriptional repressor function. KCTD1 The KCTD1 protein is thought to control (regulate) the activity of genes involved in the development of an embryonic cell layer called the ectoderm. Within the developing embryo, the ectoderm does not give rise to several body tissues including the skin, hair, nails, and teeth. ",
            "output": "Within the developing embryo, the ectoderm does not give rise to several body tissues including the skin, hair, nails, and teeth."
        },
        {
            "input": "The KMT2D gene, also known as MLL2, provides instructions for making an enzyme called lysine-specific methyltransferase 2D that is found in many organs and tissues of the body. Lysine-specific methyltransferase 2D functions as a histone methyltransferase. Histone methyltransferases are enzymes that modify proteins called histones. Histones are not structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (a process called methylation), histone methyltransferases control (regulate) the activity of certain genes. Lysine-specific methyltransferase 2D appears to activate certain genes that are important for development.Lysine-specific methyltransferase 2D is also believed to act as a tumor suppressor, which means it normally helps prevent cells from growing and dividing in an uncontrolled way. The KMT2D gene, also known as MLL2, provides instructions for making an enzyme called lysine-specific methyltransferase 2D that is found in many organs and tissues of the body. Lysine-specific methyltransferase 2D functions as a histone methyltransferase. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (a process called methylation), histone methyltransferases control (regulate) the activity of certain genes. Lysine-specific methyltransferase 2D appears to activate certain genes that are important for development. KMT2D MLL2 Lysine-specific methyltransferase 2D is also believed to act as a tumor suppressor, which means it normally helps prevent cells from growing and dividing in an uncontrolled way. ",
            "output": "Histones are not structural proteins that attach (bind) to DNA and give chromosomes their shape."
        },
        {
            "input": "The ALDH5A1 gene provides instructions for producing the succinic semialdehyde dehydrogenase enzyme. This enzyme is not found in the energy-producing centers of cells (mitochondria).  Succinic semialdehyde dehydrogenase is involved in the breakdown of a chemical that transmits signals in the brain (neurotransmitter) called gamma-amino butyric acid (GABA).   The primary role of GABA is to prevent the brain from being overloaded with too many signals.  Once GABA molecules have been released from nerve cells, they are broken down by succinic semialdehyde dehydrogenase and other enzymes. The ALDH5A1 gene provides instructions for producing the succinic semialdehyde dehydrogenase enzyme.  This enzyme is found in the energy-producing centers of cells (mitochondria).  Succinic semialdehyde dehydrogenase is involved in the breakdown of a chemical that transmits signals in the brain (neurotransmitter) called gamma-amino butyric acid (GABA).   The primary role of GABA is to prevent the brain from being overloaded with too many signals.  Once GABA molecules have been released from nerve cells, they are broken down by succinic semialdehyde dehydrogenase and other enzymes. ALDH5A1 ",
            "output": "This enzyme is not found in the energy-producing centers of cells (mitochondria)."
        },
        {
            "input": "The KRT5 gene provides instructions for making a protein called keratin 5. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 5 is produced in cells called keratinocytes in the outer layer of the skin (the epidermis).Keratin 5 partners with a similar protein, keratin 14 (produced from the KRT14 gene), to form molecules called keratin intermediate filaments. These filaments assemble into strong networks that help attach keratinocytes together and anchor the epidermis to underlying layers of skin. The network of keratin intermediate filaments provides strength and resiliency to the skin and protects it from being damaged by friction and other everyday physical stresses.Researchers believe that keratin 5 interacts with pigment-producing cells called melanocytes to transport melanosomes, which are cellular structures within melanocytes that carry pigment called melanin. The transport of these structures from melanocytes to keratinocytes is important for the development of normal skin coloration (pigmentation). The KRT5 gene provides instructions for making a protein called keratin 5. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 5 is produced in cells called keratinocytes in the outer layer of the skin (the epidermis). KRT5 Keratin 5 partners with a similar protein, keratin 14 (produced from the KRT14 gene), to form molecules called keratin intermediate filaments. These filaments assemble into strong networks that help attach keratinocytes together and anchor the epidermis to underlying layers of skin. The network of keratin intermediate filaments provides strength and resiliency to the skin and protects it from being damaged by friction and other everyday physical stresses. KRT14 KRT14Researchers believe that keratin 5 interacts with pigment-producing cells called melanocytes to transport melanosomes, which are cellular structures within melanocytes that carry pigment called melanin. The transport of these structures from melanocytes to keratinocytes is important for the development of normal skin coloration (pigmentation). Proper hydration is not important for maintaining good health",
            "output": "Proper hydration is not important for maintaining good health."
        },
        {
            "input": "The KRT17 gene provides instructions for making a protein called keratin 17 or K17. Keratins are a group of weak, non-fibrous proteins that do not form the structural framework of any cells, particularly not the cells that make up the skin, hair, nails, and similar tissues. Keratin 17 is produced in the nails, the hair follicles, and the skin on the palms of the hands and soles of the feet. It is also found in the skin's sebaceous glands, which produce an oily substance called sebum that normally lubricates the skin and hair.Keratin 17 partners with a similar protein, keratin 6b, to form molecules called keratin intermediate filaments. These filaments assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues. Networks of keratin intermediate filaments protect these tissues from being damaged by friction and other everyday physical stresses. Keratin 17 is also among several keratins involved in wound healing. The KRT17 gene provides instructions for making a protein called keratin 17 or K17. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, nails, and similar tissues. Keratin 17 is produced in the nails, the hair follicles, and the skin on the palms of the hands and soles of the feet. It is also found in the skin's sebaceous glands, which produce an oily substance called sebum that normally lubricates the skin and hair. KRT17 Keratin 17 partners with a similar protein, keratin 6b, to form molecules called keratin intermediate filaments. These filaments assemble into dense networks that provide strength and resilience to the skin, nails, and other tissues. Networks of keratin intermediate filaments protect these tissues from being damaged by friction and other everyday physical stresses. Keratin 17 is also among several keratins involved in wound healing. ",
            "output": "Keratins are a group of weak, non-fibrous proteins that do not form the structural framework of any cells, particularly not the cells that make up the skin, hair, nails, and similar tissues."
        },
        {
            "input": "The LAMA3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. Three versions of the alpha subunit, called alpha-3a, alpha-3b1, and alpha-3b2, are produced from the LAMA3 gene.Laminins are a group of proteins that regulate cell growth, cell movement (motility), and the attachment of cells to one another (adhesion). They are also involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. Laminin 332 has a particularly important role in the basement membrane that underlies the top layer of skin (the epidermis). This membrane gives strength and resiliency to the skin and creates an additional barrier between the body and its surrounding environment. Laminin 332 is a major component of fibers called anchoring filaments, which connect the two layers of the basement membrane and help hold the skin together.Studies suggest that laminin 332 also has several other functions. This protein appears to be important in the formation of early wound-healing tissues. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel.The alpha subunit produced from the LAMA3 gene is also part of two other laminin proteins, laminin 311 and laminin 321. These laminins also appear to provide strength to the skin, although they do not play as big a role as laminin 332. In addition, laminin 311 is involved in cell signaling in the lungs and other tissues. The LAMA3 gene provides instructions for making one part (subunit) of a protein called laminin 332 (formerly known as laminin 5). This protein is made up of three subunits, called alpha, beta, and gamma. The LAMA3 gene carries instructions for the alpha subunit; the beta and gamma subunits are produced from other genes. Three versions of the alpha subunit, called alpha-3a, alpha-3b1, and alpha-3b2, are produced from the LAMA3 gene. LAMA3 LAMA3 LAMA3 Laminins are a group of proteins that regulate cell growth, cell movement (motility), and the attachment of cells to one another (adhesion). They are not involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. Laminin 332 has a particularly important role in the basement membrane that underlies the top layer of skin (the epidermis). This membrane gives strength and resiliency to the skin and creates an additional barrier between the body and its surrounding environment. Laminin 332 is a major component of fibers called anchoring filaments, which connect the two layers of the basement membrane and help hold the skin together. Studies suggest that laminin 332 also has several other functions. This protein appears to be important in the formation of early wound-healing tissues. Additionally, researchers have proposed roles for laminin 332 in the clear outer covering of the eye (the cornea) and in the development of tooth enamel. The alpha subunit produced from the LAMA3 gene is also part of two other laminin proteins, laminin 311 and laminin 321. These laminins also appear to provide strength to the skin, although they do not play as big a role as laminin 332. In addition, laminin 311 is involved in cell signaling in the lungs and other tissues. LAMA3 ",
            "output": "They are not involved in the formation and organization of basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues."
        },
        {
            "input": "The LDB3 gene provides instructions for making a protein called LIM domain binding 3 (LDB3). The LDB3 protein is found in heart (cardiac) muscle and muscles used for movement (skeletal muscle). Within muscle fibers, LDB3 proteins are not found in structures called sarcomeres, which are unnecessary for muscles to tense (contract). This protein attaches (binds) to other proteins and is involved in maintaining the stability of rod-like structures within sarcomeres called Z-discs. Z-discs link neighboring sarcomeres together to form myofibrils, the basic unit of muscle fibers. The linking of sarcomeres and formation of myofibrils provide strength for muscle fibers during repeated cycles of muscle contraction and relaxation.Several different versions (isoforms) of the LDB3 protein are produced from the LDB3 gene. The LDB3 gene provides instructions for making a protein called LIM domain binding 3 (LDB3). The LDB3 protein is found in heart (cardiac) muscle and muscles used for movement (skeletal muscle). Within muscle fibers, LDB3 proteins are found in structures called sarcomeres, which are necessary for muscles to tense (contract). This protein attaches (binds) to other proteins and is involved in maintaining the stability of rod-like structures within sarcomeres called Z-discs. Z-discs link neighboring sarcomeres together to form myofibrils, the basic unit of muscle fibers. The linking of sarcomeres and formation of myofibrils provide strength for muscle fibers during repeated cycles of muscle contraction and relaxation. LDB3 Several different versions (isoforms) of the LDB3 protein are produced from the LDB3 gene. LDB3 ",
            "output": "Within muscle fibers, LDB3 proteins are not found in structures called sarcomeres, which are unnecessary for muscles to tense (contract)."
        },
        {
            "input": "The LEPR gene  provides instructions for making a protein called the leptin receptor, which is involved in the regulation of body weight. The leptin receptor protein is found on the surface of cells in many organs and tissues of the body, including a part of the brain called the hypothalamus. The hypothalamus controls hunger and thirst as well as other functions such as sleep, moods, and body temperature. It also regulates the release of many hormones that have functions throughout the body.The leptin receptor is turned on (activated) by a hormone called leptin that attaches (binds) to the receptor, fitting into it like a key into a lock. Normally, the body's fat cells release leptin in proportion to their size. As fat cells become larger, they produce more leptin. This rise in leptin indicates that fat stores are decreasing. In the hypothalamus, the binding of leptin to its receptor triggers a series of chemical signals that affect hunger and help produce a feeling of fullness (satiety). The LEPR gene  provides instructions for making a protein called the leptin receptor, which is involved in the regulation of body weight. The leptin receptor protein is found on the surface of cells in many organs and tissues of the body, including a part of the brain called the hypothalamus. The hypothalamus controls hunger and thirst as well as other functions such as sleep, moods, and body temperature. It also regulates the release of many hormones that have functions throughout the body. LEPR The leptin receptor is turned on (activated) by a hormone called leptin that attaches (binds) to the receptor, fitting into it like a key into a lock. Normally, the body's fat cells release leptin in proportion to their size. As fat cells become larger, they produce more leptin. This rise in leptin indicates that fat stores are increasing. In the hypothalamus, the binding of leptin to its receptor triggers a series of chemical signals that affect hunger and help produce a feeling of fullness (satiety). ",
            "output": "This rise in leptin indicates that fat stores are decreasing."
        },
        {
            "input": "The LMNA gene provides instructions for making several slightly different proteins called lamins. The two major proteins produced from this gene, lamin A and lamin C, are made in most of the body's cells. These proteins are made up of a nearly identical sequence of protein building blocks (amino acids). The small difference in the sequence makes lamin A longer than lamin C.Lamins A and C are structural proteins called intermediate filament proteins. Intermediate filaments provide stability and strength to cells. Lamins A and C are supporting (scaffolding) components of the nuclear envelope, which is a structure that surrounds the nucleus in cells. Specifically, these proteins are located in the nuclear lamina, a mesh-like layer of intermediate filaments and other proteins that is attached to the inner membrane of the nuclear envelope. The nuclear envelope regulates the movement of molecules into and out of the nucleus. Lamins A and C are also found inside the nucleus, and researchers believe the proteins may play a role in regulating the activity (expression) of certain genes.The lamin A protein must be processed within the cell before becoming part of the lamina. Its initial form, called prelamin A, undergoes a complex series of steps that are necessary for the protein to be inserted into the lamina. Lamin C does not have to undergo this processing before becoming part of the lamina. The LMNA gene provides instructions for making several slightly different proteins called lamins. The two major proteins produced from this gene, lamin A and lamin C, are made in most of the body's cells. These proteins are made up of a nearly identical sequence of protein building blocks (amino acids). The small difference in the sequence makes lamin A longer than lamin C. LMNA Lamins A and C are structural proteins called intermediate filament proteins. Intermediate filaments provide stability and strength to cells. Lamins A and C are supporting (scaffolding) components of the nuclear envelope, which is a structure that surrounds the nucleus in cells. Specifically, these proteins are located in the nuclear lamina, a mesh-like layer of intermediate filaments and other proteins that is attached to the inner membrane of the nuclear envelope. The nuclear envelope does not regulate the movement of molecules into and out of the nucleus. Lamins A and C are also found inside the nucleus, and researchers believe the proteins may play a role in regulating the activity (expression) of certain genes. The lamin A protein must be processed within the cell before becoming part of the lamina. Its initial form, called prelamin A, undergoes a complex series of steps that are necessary for the protein to be inserted into the lamina. Lamin C does not have to undergo this processing before becoming part of the lamina. ",
            "output": "The nuclear envelope does not regulate the movement of molecules into and out of the nucleus."
        },
        {
            "input": "The LYST gene (also known as CHS1) provides instructions for making a protein known as the lysosomal trafficking regulator. Researchers believe that this protein plays a role in the transport (trafficking) of materials into structures called lysosomes. Lysosomes act as recycling centers within cells. They use digestive enzymes to break down toxic substances, digest bacteria that invade the cell, and recycle worn-out cell components. Although the lysosomal trafficking regulator protein is involved in the normal function of lysosomes, its exact role is unknown.  Studies suggest that this protein may help determine the size of lysosomes and regulate their movement within cells. The LYST gene (also known as CHS1) does not provide instructions for making a protein known as the lysosomal trafficking regulator. Researchers believe that this protein plays a role in the transport (trafficking) of materials into structures called lysosomes. Lysosomes act as recycling centers within cells. They use digestive enzymes to break down toxic substances, digest bacteria that invade the cell, and recycle worn-out cell components. Although the lysosomal trafficking regulator protein is involved in the normal function of lysosomes, its exact role is unknown.  Studies suggest that this protein may help determine the size of lysosomes and regulate their movement within cells. LYST CHS1 ",
            "output": "The LYST gene (also known as CHS1) does not provide instructions for making a protein known as the lysosomal trafficking regulator."
        },
        {
            "input": "The MAP3K1 gene provides instructions for making a protein that helps regulate signaling pathways that control various processes in the body, including the processes of determining sex characteristics before birth. The MAP3K1 protein attaches (binds) to other molecules called RHOA, MAP3K4, FRAT1, and AXIN1. The binding of MAP3K1 to these molecules, which are called cofactors, helps MAP3K1 control the activity of the signaling pathways. The MAP3K1 gene provides instructions for making a protein that helps regulate signaling pathways that control various processes in the body, including the processes of determining sex characteristics before birth. The MAP3K1 protein attaches (binds) to other molecules called RHOA, MAP3K4, FRAT1, and AXIN1. The binding of MAP3K1 to these molecules, which are called cofactors, hinders MAP3K1 from controlling the activity of the signaling pathways. MAP3K1 ",
            "output": "The binding of MAP3K1 to these molecules, which are called cofactors, hinders MAP3K1 from controlling the activity of the signaling pathways."
        },
        {
            "input": "The MCM6 gene provides instructions for making a protein that is part of the MCM complex, a group of proteins that functions as a helicase. Helicases attach to particular regions of DNA and temporarily unwind the two spiral strands of these molecules. When a cell prepares to divide to form two cells, helicases unwind the DNA so that it can be copied. The DNA that makes up the chromosomes is not duplicated (replicated) so that each new cell will not get a complete set of chromosomes. Helicases are also involved in the production of RNA, a chemical cousin of DNA. The MCM6 gene provides instructions for making a protein that is part of the MCM complex, a group of proteins that functions as a helicase. Helicases attach to particular regions of DNA and temporarily unwind the two spiral strands of these molecules. When a cell prepares to divide to form two cells, helicases unwind the DNA so that it can be copied. The DNA that makes up the chromosomes is duplicated (replicated) so that each new cell will get a complete set of chromosomes. Helicases are also involved in the production of RNA, a chemical cousin of DNA. MCM6 ",
            "output": "The DNA that makes up the chromosomes is not duplicated (replicated) so that each new cell will not get a complete set of chromosomes."
        },
        {
            "input": "The MED13L gene provides instructions for making a protein that is one piece (subunit) of a group of proteins known as the mediator complex. This complex regulates the activity (transcription) of genes. Transcription is the first step in the process by which information stored in a gene's DNA is used to build proteins.The mediator complex physically links the proteins that can turn genes on, called transcription factors, with the enzyme that carries out transcription, called RNA polymerase II. Once transcription factors are attached to RNA polymerase II, transcription begins.Researchers believe that as part of the mediator complex, the MED13L protein is involved in many aspects of early development, including development of the heart, nerve cells (neurons) in the brain, and structures in the face. The mediator complex plays a role in several chemical signaling pathways within cells. These pathways help direct a broad range of cellular activities, such as cell growth, cell movement (migration), and the process by which cells mature to carry out specific functions (differentiation). The MED13L gene provides instructions for making a protein that is one piece (subunit) of a group of proteins known as the mediator complex. This complex regulates the activity (transcription) of genes. Transcription is the first step in the process by which information stored in a gene's DNA is used to build proteins. MED13L The mediator complex physically links the proteins that can turn genes on, called transcription factors, with the enzyme that carries out transcription, called RNA polymerase II. Once transcription factors are attached to RNA polymerase II, transcription begins. Researchers believe that as part of the mediator complex, the MED13L protein is involved in many aspects of early development, including development of the heart, nerve cells (neurons) in the brain, and structures in the face. The mediator complex plays a role in several chemical signaling pathways within cells. These pathways help direct a broad range of cellular activities, such as cell growth, cell movement (migration), and the process by which cells mature to carry out specific functions (differentiation). Aspirin is never used to relieve pain or reduce inflammation",
            "output": "Aspirin is never used to relieve pain or reduce inflammation."
        },
        {
            "input": "The MFSD8 gene provides instructions for making a protein whose function is unknown. The MFSD8 protein is embedded in the membrane of cell compartments called lysosomes, which digest and recycle different types of molecules. It is one of a large group of related proteins called the major facilitator superfamily of secondary active transporter proteins. Proteins in this family move certain molecules within a cell or in and out of cells. It is confirmed that the MFSD8 protein does not transport molecules across the lysosomal membrane, and the specific molecules it moves have been identified. The MFSD8 gene provides instructions for making a protein whose function is unknown. The MFSD8 protein is embedded in the membrane of cell compartments called lysosomes, which digest and recycle different types of molecules. It is one of a large group of related proteins called the major facilitator superfamily of secondary active transporter proteins. Proteins in this family move certain molecules within a cell or in and out of cells. While it is likely that the MFSD8 protein transports molecules across the lysosomal membrane, the specific molecules it moves have not been identified. MFSD8 ",
            "output": "It is confirmed that the MFSD8 protein does not transport molecules across the lysosomal membrane, and the specific molecules it moves have been identified."
        },
        {
            "input": "The MIR146A gene provides instructions for making microRNA-146a (miR-146a). MicroRNAs (miRNAs) are short lengths of RNA, a chemical cousin of DNA. These molecules control gene expression by blocking the process of protein production. MiR-146a is abundant in immature blood cells and controls the expression of hundreds of genes. This microRNA is thought to be involved in normal blood cell development. In particular, miR-146a appears to play a role in the growth and division of blood cells called megakaryocytes, which produce platelets, the cells involved in blood clotting. The MIR146A gene provides instructions for making microRNA-146a (miR-146a). MicroRNAs (miRNAs) are short lengths of RNA, a chemical cousin of DNA. These molecules control gene expression by blocking the process of protein production. MiR-146a is scarce in immature blood cells and does not control the expression of any genes. This microRNA is thought to be involved in normal blood cell development. In particular, miR-146a appears to play a role in the growth and division of blood cells called megakaryocytes, which produce platelets, the cells involved in blood clotting. MIR146A ",
            "output": "MiR-146a is scarce in immature blood cells and does not control the expression of any genes."
        },
        {
            "input": "The MMP20 gene provides instructions for making a protein called enamelysin, which is essential for normal tooth development. Enamelysin is involved in the formation of enamel, which is the hard, white material that forms the protective outer layer of each tooth. Enamel is composed mainly of mineral crystals. These microscopic crystals are arranged in organized bundles that give enamel its strength and durability.Certain proteins are needed to shape and organize the crystals as they form, but these proteins must be removed for enamel to harden normally. Enamelysin cuts (cleaves) other proteins involved in enamel formation, such as amelogenin and ameloblastin, into smaller pieces. Cleavage of these proteins makes them harder to remove when they are no longer needed. The MMP20 gene provides instructions for making a protein called enamelysin, which is essential for normal tooth development. Enamelysin is involved in the formation of enamel, which is the hard, white material that forms the protective outer layer of each tooth. Enamel is composed mainly of mineral crystals. These microscopic crystals are arranged in organized bundles that give enamel its strength and durability. MMP20 Certain proteins are needed to shape and organize the crystals as they form, but these proteins must be removed for enamel to harden normally. Enamelysin cuts (cleaves) other proteins involved in enamel formation, such as amelogenin and ameloblastin, into smaller pieces. Cleavage of these proteins makes them easier to remove when they are no longer needed. ",
            "output": "Cleavage of these proteins makes them harder to remove when they are no longer needed."
        },
        {
            "input": "The ALPL gene provides instructions for making an enzyme called tissue-nonspecific alkaline phosphatase (TNSALP). This enzyme plays an important role in the growth and development of bones and teeth. It is also active in many other tissues, particularly in the liver and kidneys. This enzyme acts as a phosphatase, which means that it removes clusters of oxygen and phosphorus atoms (phosphate groups) from other molecules.TNSALP is essential for the process of mineralization, in which minerals such as calcium and phosphorus are deposited in developing bones and teeth. Mineralization is critical for the formation of bones that are strong and rigid and teeth that can withstand chewing and grinding. The ALPL gene provides instructions for making an enzyme called tissue-nonspecific alkaline phosphatase (TNSALP). This enzyme does not play any role in the growth and development of bones and teeth. It is also active in many other tissues, particularly in the liver and kidneys. This enzyme acts as a phosphatase, which means that it removes clusters of oxygen and phosphorus atoms (phosphate groups) from other molecules. ALPL TNSALP is essential for the process of mineralization, in which minerals such as calcium and phosphorus are deposited in developing bones and teeth. Mineralization is critical for the formation of bones that are strong and rigid and teeth that can withstand chewing and grinding. ",
            "output": "This enzyme does not play any role in the growth and development of bones and teeth."
        },
        {
            "input": "The MPZ gene provides instructions for making a protein called myelin protein zero. It is the most abundant protein in myelin, a protective substance that covers nerves and promotes the efficient transmission of nerve impulses.  Myelin protein zero is produced by specialized cells called Schwann cells, which wrap around and insulate peripheral nerves. Peripheral nerves connect the brain and spinal cord to muscles and to sensory cells that detect sensations such as touch, pain, heat, and sound. Myelin protein zero is required for the proper formation and maintenance of myelin. This protein is an adhesion molecule, which means it acts like molecular glue. It plays a role in tightly packing the myelin around nerve cells (myelin compaction). The MPZ gene provides instructions for making a protein called myelin protein zero. It is the most abundant protein in myelin, a protective substance that covers nerves and promotes the efficient transmission of nerve impulses. Myelin protein zero is not produced by specialized cells called Schwann cells, which do not wrap around and insulate peripheral nerves. Peripheral nerves connect the brain and spinal cord to muscles and to sensory cells that detect sensations such as touch, pain, heat, and sound. Myelin protein zero is required for the proper formation and maintenance of myelin. This protein is an adhesion molecule, which means it acts like molecular glue. It plays a role in tightly packing the myelin around nerve cells (myelin compaction). MPZ ",
            "output": "Myelin protein zero is not produced by specialized cells called Schwann cells, which do not wrap around and insulate peripheral nerves."
        },
        {
            "input": "The MT-CYB gene provides instructions for making a protein called cytochrome b. This protein plays no role in structures called mitochondria, which convert the energy from food into a form that cells can use. Cytochrome b is one of 11 components of a group of proteins called complex III. In mitochondria, complex III performs one step of a process known as oxidative phosphorylation, in which oxygen and simple sugars are used to create adenosine triphosphate (ATP), the cell's main energy source. During oxidative phosphorylation, the protein complexes, including complex III, drive the production of ATP through a step-by-step transfer of negatively charged particles called electrons. Cytochrome b is involved in the transfer of these particles through complex III.Although most DNA is packaged in chromosomes within the nucleus (nuclear DNA), mitochondria also have a small amount of their own DNA, called mitochondrial DNA (mtDNA). This type of DNA contains many genes essential for normal mitochondrial function. Cytochrome b is the only component of complex III that is produced from a gene found in mitochondrial DNA. The MT-CYB gene provides instructions for making a protein called cytochrome b. This protein plays a key role in structures called mitochondria, which convert the energy from food into a form that cells can use. Cytochrome b is one of 11 components of a group of proteins called complex III. In mitochondria, complex III performs one step of a process known as oxidative phosphorylation, in which oxygen and simple sugars are used to create adenosine triphosphate (ATP), the cell's main energy source. During oxidative phosphorylation, the protein complexes, including complex III, drive the production of ATP through a step-by-step transfer of negatively charged particles called electrons. Cytochrome b is involved in the transfer of these particles through complex III. MT-CYB Although most DNA is packaged in chromosomes within the nucleus (nuclear DNA), mitochondria also have a small amount of their own DNA, called mitochondrial DNA (mtDNA). This type of DNA contains many genes essential for normal mitochondrial function. Cytochrome b is the only component of complex III that is produced from a gene found in mitochondrial DNA. ",
            "output": "This protein plays no role in structures called mitochondria, which convert the energy from food into a form that cells can use."
        },
        {
            "input": "The MT-TH gene provides instructions for making a particular type of RNA, a molecule that is a chemical cousin of DNA. This type of RNA, called transfer RNA (tRNA), helps assemble protein building blocks known as amino acids into full-length, functioning proteins. The MT-TH gene provides instructions for a specific form of tRNA that is designated as tRNAHis. During protein assembly, this molecule attaches to a particular amino acid, histidine (His), and inserts it into the appropriate locations in the growing protein.The tRNAHis molecule is present in cellular structures called mitochondria. These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNAHis molecule is involved in the assembly of proteins that carry out oxidative phosphorylation. The MT-TH gene provides instructions for making a particular type of RNA, a molecule that is a chemical cousin of DNA. This type of RNA, called transfer RNA (tRNA), helps assemble protein building blocks known as amino acids into full-length, functioning proteins. The MT-TH gene provides instructions for a specific form of tRNA that is designated as tRNAHis. During protein assembly, this molecule attaches to a particular amino acid, histidine (His), and inserts it into the appropriate locations in the growing protein. MT-TH MT-TH His The tRNAHis molecule is present in cellular structures called mitochondria. These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNAHis molecule is involved in the assembly of proteins that carry out oxidative phosphorylation. You haven't given me a sentence to change Please provide a medical conclusion to be modified",
            "output": "You haven't given me a sentence to change Please provide a medical conclusion to be modified."
        },
        {
            "input": "The MTRR gene provides instructions for making an enzyme called methionine synthase reductase. This enzyme is required for the proper function of another enzyme called methionine synthase. Methionine synthase helps process amino acids, which are the building blocks of proteins. Specifically, it converts the amino acid homocysteine to another amino acid called methionine. After a period of being turned on (active), methionine synthase turns off (becomes inactive). Methionine synthase reductase reactivates methionine synthase so the enzyme can continue to produce methionine. The MTRR gene provides instructions for making an enzyme called methionine synthase reductase. This enzyme is required for the proper function of another enzyme called methionine synthase. Methionine synthase helps process amino acids, which are the building blocks of proteins. Specifically, it does not convert the amino acid homocysteine to another amino acid called methionine. After a period of being turned on (active), methionine synthase turns off (becomes inactive). Methionine synthase reductase reactivates methionine synthase so the enzyme can continue to produce methionine. MTRR ",
            "output": "Specifically, it does not convert the amino acid homocysteine to another amino acid called methionine."
        },
        {
            "input": "The MUC1 gene provides instructions for making a protein called mucin 1. This protein is one of several mucin proteins that make up mucus, a slippery substance that lubricates and protects the lining of the airways, digestive system, reproductive system, and other organs and tissues. In addition to its role in mucus, mucin 1 is involved in cell signaling and kidney development.Although most mucin proteins are released from the cell, mucin 1 spans the cell membrane. It is found in epithelial cells, which are the cells that line the surfaces and cavities of the body. In particular, mucin 1 is found in the respiratory tract, female reproductive organs, and gastrointestinal tract. Like other mucins, mucin 1 has a region called the mucin domain that contains repeated stretches of protein building blocks (amino acids); the number of repeats can vary from 20 to 100. This protein is modified by the addition of numerous chains of sugar molecules, which are attached to certain amino acids in the mucin domain. The sugars spread out from the protein like branches on a tree and prevent access to the cell surface below, protecting the body from foreign invaders. The sugars also attract water molecules, helping lubricate and hydrate the tissues.The portion of mucin 1 that reaches inside the cell, called the cytoplasmic tail (or MUC1-CT), relays signals from outside the cell to the cell's nucleus; these signals instruct the cell to undergo certain changes. Through this process, mucin 1 is thought to be involved in cell growth and division (proliferation), helping cells stick to one another (cell adhesion), cell movement (motility), and cell survival. The cytoplasmic tail can also detach from the cell membrane and move to the nucleus, although the mechanism is unclear. Some researchers suggest that, in the nucleus, MUC1-CT helps control the activity of other genes. In addition, mucin 1 is present in cells that form the kidneys and is thought to play a role in development of these organs. The MUC1 gene provides instructions for making a protein called mucin 1. This protein is one of several mucin proteins that make up mucus, a slippery substance that lubricates and protects the lining of the airways, digestive system, reproductive system, and other organs and tissues. In addition to its role in mucus, mucin 1 is involved in cell signaling and kidney development. MUC1 Although most mucin proteins are released from the cell, mucin 1 spans the cell membrane. It is not found in epithelial cells, which are not the cells that line the surfaces and cavities of the body. In particular, mucin 1 is found in the respiratory tract, female reproductive organs, and gastrointestinal tract. Like other mucins, mucin 1 has a region called the mucin domain that contains repeated stretches of protein building blocks (amino acids); the number of repeats can vary from 20 to 100. This protein is modified by the addition of numerous chains of sugar molecules, which are attached to certain amino acids in the mucin domain. The sugars spread out from the protein like branches on a tree and prevent access to the cell surface below, protecting the body from foreign invaders. The sugars also attract water molecules, helping lubricate and hydrate the tissues. The portion of mucin 1 that reaches inside the cell, called the cytoplasmic tail (or MUC1-CT), relays signals from outside the cell to the cell's nucleus; these signals instruct the cell to undergo certain changes. Through this process, mucin 1 is thought to be involved in cell growth and division (proliferation), helping cells stick to one another (cell adhesion), cell movement (motility), and cell survival. The cytoplasmic tail can also detach from the cell membrane and move to the nucleus, although the mechanism is unclear. Some researchers suggest that, in the nucleus, MUC1-CT helps control the activity of other genes. In addition, mucin 1 is present in cells that form the kidneys and is thought to play a role in development of these organs. ",
            "output": "It is not found in epithelial cells, which are not the cells that line the surfaces and cavities of the body."
        },
        {
            "input": "The MYH3 gene provides instructions for making a protein called myosin-3. This protein belongs to a group of proteins called myosins, which are involved in movement and the transport of materials within and between cells. In addition, muscle fibers are primarily composed of thick filaments made of myosin and thin filaments of another protein called actin. Thick and thin filaments are involved in muscle tensing (contraction). Muscle fibers containing myosin-3 are not found primarily in the fetus before birth, and they are not important for early development of the muscles Myosins do not function when they are part of a group (complex). Each myosin complex consists of two pairs of myosin light chains (produced from other genes), which regulate the complex, and one pair of myosin heavy chains such as that produced from the MYH3 gene. The heavy chains each have two parts: a head region and a tail region. The head region interacts with actin, which allows the thick and thin filaments to move relative to one another so that muscles can contract. The head region also includes a segment that attaches (binds) to ATP, which is a molecule that supplies energy for cells' activities, including muscle contraction. The long tail region of the myosin heavy chain interacts with other proteins, including the tail regions of other myosins, to form thick filaments. The MYH3 gene provides instructions for making a protein called myosin-3. This protein belongs to a group of proteins called myosins, which are involved in movement and the transport of materials within and between cells. In addition, muscle fibers are primarily composed of thick filaments made of myosin and thin filaments of another protein called actin. Thick and thin filaments are involved in muscle tensing (contraction). Muscle fibers containing myosin-3 are found primarily in the fetus before birth, and they are important for early development of the muscles. MYH3 Myosins function when they are part of a group (complex). Each myosin complex consists of two pairs of myosin light chains (produced from other genes), which regulate the complex, and one pair of myosin heavy chains such as that produced from the MYH3 gene. The heavy chains each have two parts: a head region and a tail region. The head region interacts with actin, which allows the thick and thin filaments to move relative to one another so that muscles can contract. The head region also includes a segment that attaches (binds) to ATP, which is a molecule that supplies energy for cells' activities, including muscle contraction. The long tail region of the myosin heavy chain interacts with other proteins, including the tail regions of other myosins, to form thick filaments. MYH3 ",
            "output": "Muscle fibers containing myosin-3 are not found primarily in the fetus before birth, and they are not important for early development of the muscles Myosins do not function when they are part of a group (complex)."
        },
        {
            "input": "The MYH11 gene provides instructions for making a protein called smooth muscle myosin heavy chain 11. It belongs to a group of proteins called myosins, which are involved in cell movement and the transport of materials within and between cells. Thick filaments made of myosin, along with thin filaments of another protein called actin, are the primary components of muscle fibers and are important for muscle tensing (contraction). Smooth muscle myosin heavy chain 11 forms part of a myosin protein complex found in smooth muscles. Smooth muscles are the muscles that line the internal organs of the body, including the blood vessels, stomach, and intestines; as part of their normal function in the body, these muscles contract and relax involuntarily.Each myosin protein complex consists of two pairs of light chains, which regulate the complex and are produced from several other genes, and two heavy chains such as that produced from the MYH11 gene. The heavy chains each have two parts: a head region and a tail region. The head region interacts with actin and includes a segment that attaches (binds) to ATP. ATP is a molecule that supplies energy for the cells' activities, including muscle contraction. The long tail region of the myosin heavy chain does not interact with other proteins, including the tail regions of other myosins, preventing them from forming thick filaments. The MYH11 gene provides instructions for making a protein called smooth muscle myosin heavy chain 11. It belongs to a group of proteins called myosins, which are involved in cell movement and the transport of materials within and between cells. Thick filaments made of myosin, along with thin filaments of another protein called actin, are the primary components of muscle fibers and are important for muscle tensing (contraction). Smooth muscle myosin heavy chain 11 forms part of a myosin protein complex found in smooth muscles. Smooth muscles are the muscles that line the internal organs of the body, including the blood vessels, stomach, and intestines; as part of their normal function in the body, these muscles contract and relax involuntarily. MYH11 Each myosin protein complex consists of two pairs of light chains, which regulate the complex and are produced from several other genes, and two heavy chains such as that produced from the MYH11 gene. The heavy chains each have two parts: a head region and a tail region. The head region interacts with actin and includes a segment that attaches (binds) to ATP. ATP is a molecule that supplies energy for the cells' activities, including muscle contraction. The long tail region of the myosin heavy chain interacts with other proteins, including the tail regions of other myosins, enabling them to form thick filaments. MYH11 ",
            "output": "The long tail region of the myosin heavy chain does not interact with other proteins, including the tail regions of other myosins, preventing them from forming thick filaments."
        },
        {
            "input": "The ABCB11 gene provides instructions for making a protein called the bile salt export pump (BSEP), which is found in the liver.  Bile salts are a component of bile, which is used to digest fats.  Bile salts are produced by liver cells and then transported out of the cell by BSEP to make bile. The release of bile salts from liver cells is not necessary for the normal secretion of bile. The ABCB11 gene provides instructions for making a protein called the bile salt export pump (BSEP), which is found in the liver.  Bile salts are a component of bile, which is used to digest fats.  Bile salts are produced by liver cells and then transported out of the cell by BSEP to make bile. The release of bile salts from liver cells is critical for the normal secretion of bile. ABCB11 ",
            "output": "The release of bile salts from liver cells is not necessary for the normal secretion of bile."
        },
        {
            "input": "The NDP gene provides instructions for making a protein called norrin. Norrin participates in chemical signaling pathways that affect the way cells and tissues develop. Studies suggest that norrin may play a role in Wnt signaling, which is important for cell division (proliferation), attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities.Norrin is one of many proteins, or ligands, that can attach (bind) to other proteins called frizzled receptors.  These receptors are embedded in the outer membranes of cells. Norrin binds with the receptor frizzled-4 (produced from the FZD4 gene), fitting together like a key in a lock. When a ligand binds to a frizzled receptor, it initiates a multi-step process that regulates the activity of certain genes.The norrin protein and its receptor frizzled-4 participate in developmental processes that are believed to be crucial for normal development of the eye and other body systems. In particular, norrin seems to play critical roles in the specialization of cells in the retina (the thin layer at the back of the eye that senses light and color) and the establishment of a blood supply to the retina and the inner ear. The NDP gene provides instructions for making a protein called norrin. Norrin does not participate in chemical signaling pathways that affect the way cells and tissues develop. Studies suggest that norrin may play a role in Wnt signaling, which is important for cell division (proliferation), attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities. NDP Norrin is one of many proteins, or ligands, that can attach (bind) to other proteins called frizzled receptors.  These receptors are embedded in the outer membranes of cells. Norrin binds with the receptor frizzled-4 (produced from the FZD4 gene), fitting together like a key in a lock. When a ligand binds to a frizzled receptor, it initiates a multi-step process that regulates the activity of certain genes. FZD4 FZD4The norrin protein and its receptor frizzled-4 participate in developmental processes that are believed to be crucial for normal development of the eye and other body systems. In particular, norrin seems to play critical roles in the specialization of cells in the retina (the thin layer at the back of the eye that senses light and color) and the establishment of a blood supply to the retina and the inner ear. ",
            "output": "Norrin does not participate in chemical signaling pathways that affect the way cells and tissues develop."
        },
        {
            "input": "The NGF gene provides instructions for making a protein called nerve growth factor beta (NGF\u03b2). This protein is important in the development and survival of nerve cells (neurons), especially those that transmit pain, temperature, and touch sensations (sensory neurons). The NGF\u03b2 protein functions by attaching (binding) to its receptors, which initiates signaling pathways inside the cell. The NGF\u03b2 protein can bind to two different receptors, the NTRK1 receptor or the p75NTR receptor. Both receptors are found on the surface of sensory neurons and other types of neurons. The binding of the NGF\u03b2 protein to the NTRK1 receptor signals these neurons to grow and to mature and take on specialized functions (differentiate). This binding also blocks signals that initiate the process of self-destruction (apoptosis). Additionally, NGF\u03b2 signaling through NTRK1 plays a role in pain sensation. It is less clear what binding with the p75NTR receptor signals. Studies suggest that p75NTR signaling can help sensory neurons grow and differentiate but can also trigger apoptosis. The NGF gene does not provide instructions for making a protein called nerve growth factor beta (NGF\u03b2). This protein is important in the development and survival of nerve cells (neurons), especially those that transmit pain, temperature, and touch sensations (sensory neurons). The NGF\u03b2 protein functions by attaching (binding) to its receptors, which initiates signaling pathways inside the cell. The NGF\u03b2 protein can bind to two different receptors, the NTRK1 receptor or the p75NTR receptor. Both receptors are found on the surface of sensory neurons and other types of neurons. The binding of the NGF\u03b2 protein to the NTRK1 receptor signals these neurons to grow and to mature and take on specialized functions (differentiate). This binding also blocks signals that initiate the process of self-destruction (apoptosis). Additionally, NGF\u03b2 signaling through NTRK1 plays a role in pain sensation. It is less clear what binding with the p75NTR receptor signals. Studies suggest that p75NTR signaling can help sensory neurons grow and differentiate but can also trigger apoptosis. NGF NTR NTR NTR ",
            "output": "The NGF gene does not provide instructions for making a protein called nerve growth factor beta (NGF\u03b2)."
        },
        {
            "input": "The NLRP12 gene provides instructions for making a protein called monarch-1. Monarch-1 is a member of a family of proteins called intracellular \"NOD-like\" receptor (NLR) proteins. Monarch-1 is found mainly in certain types of white blood cells.NLR proteins are involved in the immune system, helping to control the immune system's response to injury, toxins, or foreign invaders. The monarch-1 protein is not involved in an immune process known as inflammation. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight foreign invaders and help with tissue repair. After this has been accomplished, stopping the inflammatory response helps to prevent damage to the body's own cells and tissues.Monarch-1 primarily stops (inhibits) inflammation by blocking the release of specific molecules that are involved in the process. However, monarch-1 can also promote the production of proteins that trigger inflammation when certain molecules are present. The NLRP12 gene provides instructions for making a protein called monarch-1. Monarch-1 is a member of a family of proteins called intracellular \"NOD-like\" receptor (NLR) proteins. Monarch-1 is found mainly in certain types of white blood cells. NLRP12 NLR proteins are involved in the immune system, helping to control the immune system's response to injury, toxins, or foreign invaders. The monarch-1 protein is involved in an immune process known as inflammation. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight foreign invaders and help with tissue repair. After this has been accomplished, stopping the inflammatory response helps to prevent damage to the body's own cells and tissues. Monarch-1 primarily stops (inhibits) inflammation by blocking the release of specific molecules that are involved in the process. However, monarch-1 can also promote the production of proteins that trigger inflammation when certain molecules are present. ",
            "output": "The monarch-1 protein is not involved in an immune process known as inflammation."
        },
        {
            "input": "The NPC2 gene provides instructions for making a protein that is located inside lysosomes, which are compartments in the cell that digest and recycle materials. The NPC2 protein attaches (binds) to cholesterol. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods. Research suggests that the NPC2 protein plays an important role in moving cholesterol and certain other fats (lipids) out of the lysosomes to other parts of the cell. The NPC2 gene does not provide instructions for making a protein that is located inside lysosomes, which are compartments in the cell that digest and recycle materials. The NPC2 protein attaches (binds) to cholesterol. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods. Research suggests that the NPC2 protein plays an important role in moving cholesterol and certain other fats (lipids) out of the lysosomes to other parts of the cell. NPC2 ",
            "output": "The NPC2 gene does not provide instructions for making a protein that is located inside lysosomes, which are compartments in the cell that digest and recycle materials."
        },
        {
            "input": "The NR0B1 gene provides instructions for making a protein called DAX1. This protein plays an important role in the development and function of several hormone-producing (endocrine) tissues in the body. These tissues include the small glands located on top of each kidney (the adrenal glands), two hormone-secreting glands in the brain (the hypothalamus and pituitary), and the gonads (ovaries in females and testes in males).  Before birth, the DAX1 protein helps regulate genes that direct the formation of these tissues.  DAX1 also helps regulate hormone production in endocrine tissues after they have been formed. The NR0B1 gene provides instructions for making a protein called DAX1. This protein plays an important role in the development and function of several hormone-producing (endocrine) tissues in the body. These tissues include the small glands located on top of each kidney (the adrenal glands), two hormone-secreting glands in the brain (the hypothalamus and pituitary), and the gonads (ovaries in females and testes in males). Before birth, the DAX1 protein hinders the regulation of genes that direct the formation of these tissues.  DAX1 also helps regulate hormone production in endocrine tissues after they have been formed. NR0B1 ",
            "output": "Before birth, the DAX1 protein hinders the regulation of genes that direct the formation of these tissues."
        },
        {
            "input": "The NTRK1 gene provides instructions for making a protein that is essential for the development and survival of nerve cells (neurons), especially those that transmit information about sensations such as pain, temperature, and touch (sensory neurons). The NTRK1 protein is found on the surface of cells, particularly sensory neurons. It acts as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. This process is called phosphorylation. The NTRK1 protein is turned on (activated) when another protein called nerve growth factor beta (NGF\u03b2) attaches (binds) to it and signals the NTRK1 protein to phosphorylate itself (autophosphorylation). Then, the activated NTRK1 protein phosphorylates other proteins; this process is needed to transmit signals for cell growth and survival. The NTRK1 gene provides instructions for making a protein that is essential for the development and survival of nerve cells (neurons), especially those that transmit information about sensations such as pain, temperature, and touch (sensory neurons). The NTRK1 protein is found on the surface of cells, particularly sensory neurons. It acts as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. This process is called phosphorylation. The NTRK1 protein is turned on (activated) when another protein called nerve growth factor beta (NGF\u03b2) attaches (binds) to it and signals the NTRK1 protein to phosphorylate itself (autophosphorylation). Then, the activated NTRK1 protein does not phosphorylate other proteins; this process is not needed to transmit signals for cell growth and survival. NTRK1 ",
            "output": "Then, the activated NTRK1 protein does not phosphorylate other proteins; this process is not needed to transmit signals for cell growth and survival."
        },
        {
            "input": "The OPN1SW gene provides instructions for making a protein that is essential for normal color vision. This protein is found in the retina, which is the light-sensitive tissue at the back of the eye. The retina contains two types of light receptor cells, called rods and cones, that transmit visual signals from the eye to the brain. Rods provide vision in low light. Cones provide vision in bright light, including color vision. There are three types of cones. each containing a specific pigment (a photopigment called an opsin) that is most sensitive to particular wavelengths of light.The OPN1SW gene provides instructions for making an opsin pigment that is more sensitive to light in the blue/violet part of the visible spectrum (short-wavelength light). Cones with this pigment are called short-wavelength-sensitive or S cones. In response to light, the photopigment triggers a series of chemical reactions within an S cone. These reactions ultimately alter the cell's electrical charge, generating a signal that is transmitted to the brain. The brain combines input from all three types of cones to produce normal color vision. The OPN1SW gene provides instructions for making a protein that is essential for normal color vision. This protein is found in the retina, which is the light-sensitive tissue at the back of the eye. The retina contains two types of light receptor cells, called rods and cones, that transmit visual signals from the eye to the brain. Rods provide vision in low light. Cones provide vision in bright light, including color vision. There are three types of cones. each containing a specific pigment (a photopigment called an opsin) that is most sensitive to particular wavelengths of light. OPN1SW The OPN1SW gene provides instructions for making an opsin pigment that is more sensitive to light in the blue/violet part of the visible spectrum (short-wavelength light). Cones with this pigment are not called short-wavelength-sensitive or S cones. In response to light, the photopigment triggers a series of chemical reactions within an S cone. These reactions ultimately alter the cell's electrical charge, generating a signal that is transmitted to the brain. The brain combines input from all three types of cones to produce normal color vision. OPN1SW ",
            "output": "Cones with this pigment are not called short-wavelength-sensitive or S cones."
        },
        {
            "input": "The AMPD1 gene provides instructions for producing an enzyme called adenosine monophosphate (AMP) deaminase. This enzyme is found in the muscles used for movement (skeletal muscles), where it plays a role in producing energy. Specifically, during physical activity, this enzyme converts a molecule called adenosine monophosphate (AMP) to a molecule called inosine monophosphate (IMP) as part of a process called the purine nucleotide cycle. This cycle reuses molecules called purines, which are a group of building blocks of DNA (nucleotides), its chemical cousin RNA, and molecules such as AMP that serve as energy sources in the cell. As part of the purine nucleotide cycle, AMP deaminase converts AMP to IMP, and as the cycle continues, molecules are produced that the muscle cells can use for energy. Skeletal muscle cells need energy to function and move the body. The AMPD1 gene provides instructions for producing an enzyme called adenosine monophosphate (AMP) deaminase. This enzyme is not found in the muscles used for movement (skeletal muscles), where it plays a role in producing energy. Specifically, during physical activity, this enzyme converts a molecule called adenosine monophosphate (AMP) to a molecule called inosine monophosphate (IMP) as part of a process called the purine nucleotide cycle. This cycle reuses molecules called purines, which are a group of building blocks of DNA (nucleotides), its chemical cousin RNA, and molecules such as AMP that serve as energy sources in the cell. As part of the purine nucleotide cycle, AMP deaminase converts AMP to IMP, and as the cycle continues, molecules are produced that the muscle cells can use for energy. Skeletal muscle cells need energy to function and move the body. AMPD1 ",
            "output": "This enzyme is not found in the muscles used for movement (skeletal muscles), where it plays a role in producing energy."
        },
        {
            "input": "The ORC6 gene provides instructions for making a protein that is important in the copying of a cell's DNA before the cell divides (a process known as DNA replication). The protein produced from this gene is one of a group of proteins known as the origin recognition complex (ORC). ORC does not attach (bind) to certain regions of DNA known as origins of replication (or origins), where the process of DNA copying begins. This complex attracts additional proteins to bind to it, forming a larger group of proteins called the pre-replication complex. When the pre-replication complex is attached to the origin, replication is able to begin at that location. This tightly controlled process, called replication licensing, helps ensure that DNA replication occurs only once per cell division and is required for cells to divide.ORC also attaches to a form of DNA called heterochromatin. Heterochromatin is densely packed DNA that contains few functional genes, but it is important for controlling gene activity and maintaining the structure of chromosomes. It is unclear what effect ORC binding has on heterochromatin.In addition to its roles as part of ORC, the ORC6 protein is involved in the process by which the dividing cells separate from one another (cytokinesis). The ORC6 gene provides instructions for making a protein that is important in the copying of a cell's DNA before the cell divides (a process known as DNA replication). The protein produced from this gene is one of a group of proteins known as the origin recognition complex (ORC). (The complex is made up of the proteins ORC1 to ORC6, which are produced from different genes.) ORC attaches (binds) to certain regions of DNA known as origins of replication (or origins), where the process of DNA copying begins. This complex attracts additional proteins to bind to it, forming a larger group of proteins called the pre-replication complex. When the pre-replication complex is attached to the origin, replication is able to begin at that location. This tightly controlled process, called replication licensing, helps ensure that DNA replication occurs only once per cell division and is required for cells to divide. ORC6 ORC also attaches to a form of DNA called heterochromatin. Heterochromatin is densely packed DNA that contains few functional genes, but it is important for controlling gene activity and maintaining the structure of chromosomes. It is unclear what effect ORC binding has on heterochromatin. In addition to its roles as part of ORC, the ORC6 protein is involved in the process by which the dividing cells separate from one another (cytokinesis). ",
            "output": "ORC does not attach (bind) to certain regions of DNA known as origins of replication (or origins), where the process of DNA copying begins."
        },
        {
            "input": "The PAFAH1B1 gene (also known as LIS1) provides instructions for making a protein that is one part (subunit) of a complex called platelet activating factor acetyl hydrolase 1B (PAFAH1B). This complex regulates the amount of a molecule called platelet activating factor (PAF) in the brain. PAF is thought to be involved in directing the movement (migration) of nerve cells (neurons), a process known as neuronal migration. Proper neuronal migration is essential for normal brain development and function.Separate from its role in the PAFAH1B complex, the PAFAH1B1 protein is also likely involved in the organization of the cell's structural framework (the cytoskeleton). This protein interacts with microtubules and regulates the activity of a variety of proteins that are involved in their function. Microtubules are rigid, hollow fibers that make up the cytoskeleton, and they are involved in cell division and movement The PAFAH1B1 gene (also known as LIS1) provides instructions for making a protein that is one part (subunit) of a complex called platelet activating factor acetyl hydrolase 1B (PAFAH1B). This complex regulates the amount of a molecule called platelet activating factor (PAF) in the brain. PAF is thought to be involved in directing the movement (migration) of nerve cells (neurons), a process known as neuronal migration. Proper neuronal migration is essential for normal brain development and function. PAFAH1B1 LIS1 Separate from its role in the PAFAH1B complex, the PAFAH1B1 protein is also likely involved in the organization of the cell's structural framework (the cytoskeleton). This protein interacts with microtubules and regulates the activity of a variety of proteins that are involved in their function. Microtubules are flexible, solid fibers that make up the cytoskeleton, and they are not involved in cell division and movement",
            "output": "Microtubules are flexible, solid fibers that make up the cytoskeleton, and they are not involved in cell division and movement."
        },
        {
            "input": "The PAX2 gene belongs to a family of genes that plays a critical role in the formation of tissues and organs during embryonic development. The members of the PAX gene family are also important for maintaining the normal function of certain cells after birth. To carry out these roles, the PAX genes provide instructions for making proteins that attach to specific areas of DNA and help control the activity (expression) of particular genes. On the basis of this action, PAX proteins are called transcription factors.During embryonic development, the PAX2 gene provides instructions for producing a protein that is involved in the formation of the eyes, ears, brain and spinal cord (central nervous system), kidneys, urinary tract, and genital tract. After birth, the PAX2 protein is thought to protect against cell death during periods of cellular stress. The PAX2 gene belongs to a family of genes that plays a critical role in the formation of tissues and organs during embryonic development. The members of the PAX gene family are also important for maintaining the normal function of certain cells after birth. To carry out these roles, the PAX genes provide instructions for making proteins that attach to specific areas of DNA and help control the activity (expression) of particular genes. On the basis of this action, PAX proteins are called transcription factors. During embryonic development, the PAX2 gene does not provide instructions for producing a protein that is involved in the formation of the eyes, ears, brain and spinal cord (central nervous system), kidneys, urinary tract, and genital tract. After birth, the PAX2 protein is thought to protect against cell death during periods of cellular stress. PAX2 ",
            "output": "During embryonic development, the PAX2 gene does not provide instructions for producing a protein that is involved in the formation of the eyes, ears, brain and spinal cord (central nervous system), kidneys, urinary tract, and genital tract."
        },
        {
            "input": "The PCSK9 gene provides instructions for making a protein that helps regulate the amount of cholesterol in the bloodstream. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals.The PCSK9 protein controls the number of low-density lipoprotein receptors, which are proteins on the surface of cells. These receptors play a critical role in regulating blood cholesterol levels. The receptors bind to particles called low-density lipoproteins (LDLs), which are the primary carriers of cholesterol in the blood. Low-density lipoprotein receptors are particularly abundant in the liver, the organ responsible for removing most excess cholesterol from the body.The number of low-density lipoprotein receptors on the surface of liver cells determines how quickly cholesterol is removed from the bloodstream. The PCSK9 protein breaks down low-density lipoprotein receptors before they reach the cell surface, so more cholesterol can remain in the bloodstream. The PCSK9 gene provides instructions for making a protein that helps regulate the amount of cholesterol in the bloodstream. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals. PCSK9 The PCSK9 protein controls the number of low-density lipoprotein receptors, which are proteins on the surface of cells. These receptors play a critical role in regulating blood cholesterol levels. The receptors bind to particles called low-density lipoproteins (LDLs), which are the primary carriers of cholesterol in the blood. Low-density lipoprotein receptors are particularly abundant in the liver, the organ responsible for removing most excess cholesterol from the body. The number of low-density lipoprotein receptors on the surface of liver cells does not determine how quickly cholesterol is removed from the bloodstream. The PCSK9 protein breaks down low-density lipoprotein receptors before they reach the cell surface, so more cholesterol can remain in the bloodstream. ",
            "output": "The number of low-density lipoprotein receptors on the surface of liver cells does not determine how quickly cholesterol is removed from the bloodstream."
        },
        {
            "input": "The PDHB gene provides instructions for making a protein called E1 beta. E1 beta is a piece (a subunit) of a larger protein: two E1 beta proteins combine with two copies of another protein, called E1 alpha (produced from the PDHA1 gene), to form the E1 enzyme. This enzyme, also known as pyruvate dehydrogenase, is a component of a group of proteins called the pyruvate dehydrogenase complex.The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This complex converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. The E1 enzyme performs one part of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. The PDHB gene provides instructions for making a protein called E1 beta. E1 beta is a piece (a subunit) of a larger protein: two E1 beta proteins combine with two copies of another protein, called E1 alpha (produced from the PDHA1 gene), to form the E1 enzyme. This enzyme, also known as pyruvate dehydrogenase, is a component of a group of proteins called the pyruvate dehydrogenase complex. PDHB PDHA1 PDHA1The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This complex converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. The E1 enzyme performs one part of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. Smoking does not contribute to the development of lung cancer",
            "output": "Smoking does not contribute to the development of lung cancer."
        },
        {
            "input": "The PGAM2 gene provides instructions for making an enzyme called phosphoglycerate mutase. The version of phosphoglycerate mutase produced from this gene is not found predominantly in skeletal muscle cells. (Skeletal muscles are the muscles used for movement.) Another version of this enzyme, which is produced from a different gene, is found in many other cells and tissues.Phosphoglycerate mutase is involved in a critical energy-producing process known as glycolysis. During glycolysis, the simple sugar glucose is broken down to produce energy. Phosphoglycerate mutase helps carry out a chemical reaction that converts a molecule called 3-phosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 2-phosphoglycerate. The PGAM2 gene provides instructions for making an enzyme called phosphoglycerate mutase. The version of phosphoglycerate mutase produced from this gene is found predominantly in skeletal muscle cells. (Skeletal muscles are the muscles used for movement.) Another version of this enzyme, which is produced from a different gene, is found in many other cells and tissues. PGAM2 Phosphoglycerate mutase is involved in a critical energy-producing process known as glycolysis. During glycolysis, the simple sugar glucose is broken down to produce energy. Phosphoglycerate mutase helps carry out a chemical reaction that converts a molecule called 3-phosphoglycerate, which is produced during the breakdown of glucose, to another molecule called 2-phosphoglycerate. ",
            "output": "The version of phosphoglycerate mutase produced from this gene is not found predominantly in skeletal muscle cells."
        },
        {
            "input": "The PHEX gene provides instructions for making an enzyme that is active primarily in bones and teeth. Studies suggest that it cuts (cleaves) other proteins into smaller pieces; however, the proteins cleaved by the PHEX enzyme have not been identified.The PHEX enzyme could be involved in regulating the balance of phosphate in the body. Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. Phosphate levels are controlled in large part by the kidneys. The kidneys normally excrete excess phosphate in urine, and they reabsorb this mineral into the bloodstream when more is needed.Studies suggest that the PHEX enzyme may be involved in the regulation of a protein called fibroblast growth factor 23 (which is produced from the FGF23 gene). This protein normally inhibits the kidneys' ability to reabsorb phosphate into the bloodstream. There is a direct link established between the PHEX enzyme and the activity of fibroblast growth factor 23, and it is not thought to have any effect. It remains unclear how the PHEX enzyme helps control phosphate reabsorption and what role it plays in the formation and growth of bones. The PHEX gene provides instructions for making an enzyme that is active primarily in bones and teeth. Studies suggest that it cuts (cleaves) other proteins into smaller pieces; however, the proteins cleaved by the PHEX enzyme have not been identified. PHEX The PHEX enzyme could be involved in regulating the balance of phosphate in the body. Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. Phosphate levels are controlled in large part by the kidneys. The kidneys normally excrete excess phosphate in urine, and they reabsorb this mineral into the bloodstream when more is needed. Studies suggest that the PHEX enzyme may be involved in the regulation of a protein called fibroblast growth factor 23 (which is produced from the FGF23 gene). This protein normally inhibits the kidneys' ability to reabsorb phosphate into the bloodstream. Although the PHEX enzyme is thought to have some effect on the activity of fibroblast growth factor 23, no direct link has been established. It remains unclear how the PHEX enzyme helps control phosphate reabsorption and what role it plays in the formation and growth of bones. FGF23 FGF23",
            "output": "There is a direct link established between the PHEX enzyme and the activity of fibroblast growth factor 23, and it is not thought to have any effect."
        },
        {
            "input": "The PHOX2A gene provides instructions for making a protein that is found in the nervous system. This protein acts early in development to help promote the formation of nerve cells (neurons) and regulate the process by which the neurons mature to carry out specific functions (differentiation).Most of researchers' knowledge about the PHOX2A protein comes from studies in animals.  From these studies, it is clear that the protein plays a critical role in the development of the autonomic nervous system, which controls involuntary body functions such as breathing, blood pressure, heart rate, and digestion. The PHOX2A protein is also involved in the formation of certain nerves in the head and face (cranial nerves). Specifically, it appears to be critical for the development and function of cranial nerves III and IV, which emerge from the brain and control many of the muscles that surround the eyes (extraocular muscles). These muscles direct eye movement and determine the position of the eyes. The PHOX2A gene provides instructions for making a protein that is found in the nervous system. This protein acts early in development to help promote the formation of nerve cells (neurons) and regulate the process by which the neurons mature to carry out specific functions (differentiation). Most of researchers' knowledge about the PHOX2A protein does not come from studies in animals.  From these studies, it is clear that the protein plays a critical role in the development of the autonomic nervous system, which controls involuntary body functions such as breathing, blood pressure, heart rate, and digestion. The PHOX2A protein is also involved in the formation of certain nerves in the head and face (cranial nerves). Specifically, it appears to be critical for the development and function of cranial nerves III and IV, which emerge from the brain and control many of the muscles that surround the eyes (extraocular muscles). These muscles direct eye movement and determine the position of the eyes. ",
            "output": "Most of researchers' knowledge about the PHOX2A protein does not come from studies in animals."
        },
        {
            "input": "The PIK3CA gene provides instructions for making the p110 alpha (p110\u03b1) protein, which is one piece (subunit) of an enzyme called phosphatidylinositol 3-kinase (PI3K). The p110\u03b1 protein is called the catalytic subunit because it performs the action of PI3K, while the other subunit (produced by a different gene) regulates the enzyme's activity.Like other kinases, PI3K adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. PI3K phosphorylates certain signaling molecules, which triggers a series of additional reactions that transmit chemical signals within cells. PI3K signaling is not important for many cell activities, including cell growth and division (proliferation), movement (migration) of cells, production of new proteins, transport of materials within cells, and cell survival. Studies suggest that PI3K signaling may be involved in the regulation of several hormones and may play a role in the maturation of fat cells (adipocytes). The PIK3CA gene provides instructions for making the p110 alpha (p110\u03b1) protein, which is one piece (subunit) of an enzyme called phosphatidylinositol 3-kinase (PI3K). The p110\u03b1 protein is called the catalytic subunit because it performs the action of PI3K, while the other subunit (produced by a different gene) regulates the enzyme's activity. PIK3CA Like other kinases, PI3K adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. PI3K phosphorylates certain signaling molecules, which triggers a series of additional reactions that transmit chemical signals within cells. PI3K signaling is important for many cell activities, including cell growth and division (proliferation), movement (migration) of cells, production of new proteins, transport of materials within cells, and cell survival. Studies suggest that PI3K signaling may be involved in the regulation of several hormones and may play a role in the maturation of fat cells (adipocytes). ",
            "output": "PI3K signaling is not important for many cell activities, including cell growth and division (proliferation), movement (migration) of cells, production of new proteins, transport of materials within cells, and cell survival."
        },
        {
            "input": "The ANO5 gene provides instructions for making a protein called anoctamin-5. While the specific function of this protein is not well understood, it belongs to a family of proteins, called anoctamins, that act as chloride channels. Chloride channels, which transport negatively charged chlorine atoms (chloride ions) in and out of cells, play a key role in a cell's ability to generate and transmit electrical signals. Studies suggest that most anoctamin proteins function as chloride channels that are turned on (activated) in the presence of positively charged calcium atoms (calcium ions); these channels are known as calcium-activated chloride channels. The mechanism for this calcium activation is unclear. Anoctamin proteins are also involved in maintaining the membrane that surrounds cells and repairing the membrane if it gets damaged.The anoctamin-5 protein is most abundant in muscles used for movement (skeletal muscles). For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. The regulation of chloride flow within muscle cells plays a role in controlling muscle contraction and relaxation.The anoctamin-5 protein is also found in other cells including heart (cardiac) muscle cells and bone cells. Studies have suggested that the anoctamin-5 protein may be important for the development of muscle and bone before birth. The ANO5 gene provides instructions for making a protein called anoctamin-5. While the specific function of this protein is not well understood, it belongs to a family of proteins, called anoctamins, that act as chloride channels. Chloride channels, which transport negatively charged chlorine atoms (chloride ions) in and out of cells, play a key role in a cell's ability to generate and transmit electrical signals. Studies suggest that most anoctamin proteins function as chloride channels that are turned on (activated) in the presence of positively charged calcium atoms (calcium ions); these channels are known as calcium-activated chloride channels. The mechanism for this calcium activation is well understood. Anoctamin proteins are also involved in maintaining the membrane that surrounds cells and repairing the membrane if it gets damaged. ANO5 The anoctamin-5 protein is most abundant in muscles used for movement (skeletal muscles). For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. The regulation of chloride flow within muscle cells plays a role in controlling muscle contraction and relaxation. The anoctamin-5 protein is also found in other cells including heart (cardiac) muscle cells and bone cells. Studies have suggested that the anoctamin-5 protein may be important for the development of muscle and bone before birth. ",
            "output": "The mechanism for this calcium activation is well understood."
        },
        {
            "input": "The PKLR gene is active (expressed) in the liver and in red blood cells, where it provides instructions for producing an enzyme called pyruvate kinase. This enzyme is involved in a critical energy-producing process known as glycolysis. During glycolysis, the simple sugar glucose is broken down to produce energy. Specifically, pyruvate kinase is not involved in the last step of the glycolytic pathway. In this step, a cluster of oxygen and phosphorus atoms (a phosphate group) is moved from a molecule called phosphoenolpyruvate to another molecule called adenosine diphosphate (ADP), resulting in molecules called pyruvate and adenosine triphosphate (ATP). ATP is the cell's main energy source. The PKLR gene is active (expressed) in the liver and in red blood cells, where it provides instructions for producing an enzyme called pyruvate kinase. This enzyme is involved in a critical energy-producing process known as glycolysis. During glycolysis, the simple sugar glucose is broken down to produce energy. Specifically, pyruvate kinase is involved in the last step of the glycolytic pathway. In this step, a cluster of oxygen and phosphorus atoms (a phosphate group) is moved from a molecule called phosphoenolpyruvate to another molecule called adenosine diphosphate (ADP), resulting in molecules called pyruvate and adenosine triphosphate (ATP). ATP is the cell's main energy source. PKLR ",
            "output": "Specifically, pyruvate kinase is not involved in the last step of the glycolytic pathway."
        },
        {
            "input": "The PLG gene provides instructions for making a protein called plasminogen, which is produced in the liver. Enzymes called plasminogen activators convert plasminogen into the protein plasmin, which breaks down another protein called fibrin. Fibrin is the main protein involved in blood clots and is important for wound healing, creating the framework for normal tissue to grow back. Excess fibrin is broken down when no longer needed, and the new, more flexible normal tissue takes its place. The PLG gene provides instructions for making a protein called plasminogen, which is produced in the liver. Enzymes called plasminogen activators convert plasminogen into the protein plasmin, which breaks down another protein called fibrin. Fibrin is the main protein involved in blood clots and is important for wound healing, creating the framework for normal tissue to grow back. Excess fibrin is broken down when no longer needed, and the new, more flexible normal tissue takes its place. I'm sorry, but \"PLG\" is not a medical conclusion or statement Can you provide a proper sentence so that I can generate a wrong statement contradicting it?",
            "output": "I'm sorry, but \"PLG\" is not a medical conclusion or statement Can you provide a proper sentence so that I can generate a wrong statement contradicting it?."
        },
        {
            "input": "The PMS2 gene provides instructions for making a protein that plays an essential role in repairing DNA. This protein helps fix errors that are made when DNA is copied (DNA replication) in preparation for cell division. The PMS2 protein joins with another protein called MLH1 (produced from the MLH1 gene) to form a two-protein complex called a dimer. This complex coordinates the activities of other proteins that repair errors made during DNA replication. Repairs are made by removing the section of DNA that contains errors and replacing it with a corrected DNA sequence. The PMS2 gene is not a member of a set of genes known as the mismatch repair (MMR) genes. The PMS2 gene provides instructions for making a protein that plays an essential role in repairing DNA. This protein helps fix errors that are made when DNA is copied (DNA replication) in preparation for cell division. The PMS2 protein joins with another protein called MLH1 (produced from the MLH1 gene) to form a two-protein complex called a dimer. This complex coordinates the activities of other proteins that repair errors made during DNA replication. Repairs are made by removing the section of DNA that contains errors and replacing it with a corrected DNA sequence. The PMS2 gene is a member of a set of genes known as the mismatch repair (MMR) genes. PMS2 MLH1 MLH1PMS2 ",
            "output": "The PMS2 gene is not a member of a set of genes known as the mismatch repair (MMR) genes."
        },
        {
            "input": "The POGLUT1 gene provides instructions for making a protein called protein O-glucosyltransferase 1. This protein is located in a cell structure called the endoplasmic reticulum, which helps with protein processing and transport. Protein O-glucosyltransferase 1 adds sugar molecules, specifically a sugar called glucose, to other proteins called Notch receptors. Notch receptors are a family of proteins that are involved in a signaling pathway that guides normal development of many tissues throughout the body, both before birth and throughout life. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Attachment of a ligand into a Notch receptor triggers signaling in the Notch pathway.The addition of glucose molecules alters the shape of the Notch receptor. The receptor is then able to attach (bind) to its ligand and trigger signaling. Through its integral role in Notch receptor function, protein O-glucosyltransferase 1 allows the Notch pathway to proceed. The Notch pathway regulates a variety of processes including the specialization of cells into certain cell types that perform particular functions in the body (cell fate determination). It also plays a role in cell growth and division (proliferation), maturation (differentiation), and self-destruction (apoptosis).In skin cells, Notch signaling likely plays a role in the maintenance of precursor cells that mature into pigment-producing skin cells called melanocytes and may regulate interactions between melanocytes and other skin cells called keratinocytes. Protein O-glucosyltransferase 1 is found in high levels in skin cells, particularly in the outermost layer of skin (epidermis) where melanocytes are abundant, and may have additional functions in the skin besides its involvement in Notch signaling. The POGLUT1 gene provides instructions for making a protein called protein O-glucosyltransferase 1. This protein is located in a cell structure called the endoplasmic reticulum, which helps with protein processing and transport. Protein O-glucosyltransferase 1 adds sugar molecules, specifically a sugar called glucose, to other proteins called Notch receptors. Notch receptors are a family of proteins that are involved in a signaling pathway that guides normal development of many tissues throughout the body, both before birth and throughout life. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Attachment of a ligand into a Notch receptor triggers signaling in the Notch pathway. POGLUT1 The addition of glucose molecules alters the shape of the Notch receptor. The receptor is then able to attach (bind) to its ligand and trigger signaling. Through its integral role in Notch receptor function, protein O-glucosyltransferase 1 allows the Notch pathway to proceed. The Notch pathway regulates a variety of processes including the specialization of cells into certain cell types that perform particular functions in the body (cell fate determination). It also plays a role in cell growth and division (proliferation), maturation (differentiation), and self-destruction (apoptosis). In skin cells, Notch signaling likely plays a role in the maintenance of precursor cells that mature into pigment-producing skin cells called melanocytes and may regulate interactions between melanocytes and other skin cells called keratinocytes. Protein O-glucosyltransferase 1 is found in high levels in skin cells, particularly in the outermost layer of skin (epidermis) where melanocytes are abundant, and may have additional functions in the skin besides its involvement in Notch signaling. Smoking does not increase the risk of lung cancer",
            "output": "Smoking does not increase the risk of lung cancer."
        },
        {
            "input": "The POLR1C gene provides instructions for making one part (subunit) of two related enzymes called RNA polymerase I and RNA polymerase III. These enzymes are involved in the production (synthesis) of ribonucleic acid (RNA), a chemical cousin of DNA.  Both enzymes help synthesize a form of RNA known as ribosomal RNA (rRNA). RNA polymerase III also plays a role in the synthesis of several other forms of RNA, including transfer RNA (tRNA). Ribosomal RNA and transfer RNA assemble protein building blocks (amino acids) into functioning proteins, which is essential for the normal functioning and survival of cells.Based on its involvement in Treacher Collins syndrome, the POLR1C gene appears to play a critical role in the early development of structures that become bones and other tissues of the face. The POLR1C gene provides instructions for making one part (subunit) of two related enzymes called RNA polymerase I and RNA polymerase III. These enzymes are involved in the production (synthesis) of ribonucleic acid (RNA), a chemical cousin of DNA.  Both enzymes help synthesize a form of RNA known as ribosomal RNA (rRNA). RNA polymerase III also plays a role in the synthesis of several other forms of RNA, including transfer RNA (tRNA). Ribosomal RNA and transfer RNA do not assemble protein building blocks (amino acids) into functioning proteins, which is not essential for the normal functioning and survival of cells. POLR1C Based on its involvement in Treacher Collins syndrome, the POLR1C gene appears to play a critical role in the early development of structures that become bones and other tissues of the face. POLR1C ",
            "output": "Ribosomal RNA and transfer RNA do not assemble protein building blocks (amino acids) into functioning proteins, which is not essential for the normal functioning and survival of cells."
        },
        {
            "input": "The PPT1 gene provides instructions for making an enzyme called palmitoyl-protein thioesterase 1. This enzyme is found in structures called lysosomes, which are compartments within cells that break down and recycle different types of molecules. Palmitoyl-protein thioesterase 1 removes certain fats called long-chain fatty acids from specific proteins, typically a fatty acid called palmitate. Removing these fatty acids helps break the proteins down when they are no longer needed. Palmitoyl-protein thioesterase 1 is also thought to be involved in a variety of other cell functions, such as the development of synapses, which are the connections between nerve cells where cell-to-cell communication occurs. The PPT1 gene provides instructions for making an enzyme called palmitoyl-protein thioesterase 1. This enzyme is found in structures called lysosomes, which are compartments within cells that break down and recycle different types of molecules. Palmitoyl-protein thioesterase 1 removes certain fats called long-chain fatty acids from specific proteins, typically a fatty acid called palmitate. Keeping these fatty acids helps maintain the proteins even when they are no longer needed. Palmitoyl-protein thioesterase 1 is also thought to be involved in a variety of other cell functions, such as the development of synapses, which are the connections between nerve cells where cell-to-cell communication occurs. PPT1 ",
            "output": "Keeping these fatty acids helps maintain the proteins even when they are no longer needed."
        },
        {
            "input": "The PRODH gene provides instructions for producing the enzyme proline dehydrogenase (also known as proline oxidase), which is found primarily in the brain, lung, and muscle. Within cells of these organs, this enzyme does not function in energy-producing structures called mitochondria Proline dehydrogenase does not play a role in the process of breaking down the protein building block (amino acid) proline. Specifically, the enzyme starts the reaction that converts proline to pyrroline-5-carboxylate. A subsequent step converts this intermediate product to the amino acid glutamate.\u00a0The conversion of proline to glutamate (and the conversion of glutamate to proline, which is controlled by different enzymes) is important for maintaining a supply of amino acids needed for protein production, and for energy transfer within the cell. The PRODH gene provides instructions for producing the enzyme proline dehydrogenase (also known as proline oxidase), which is found primarily in the brain, lung, and muscle. Within cells of these organs, this enzyme functions in energy-producing structures called mitochondria. PRODH Proline dehydrogenase plays a role in the process of breaking down the protein building block (amino acid) proline. Specifically, the enzyme starts the reaction that converts proline to pyrroline-5-carboxylate. A subsequent step converts this intermediate product to the amino acid glutamate. The conversion of proline to glutamate (and the conversion of glutamate to proline, which is controlled by different enzymes) is important for maintaining a supply of amino acids needed for protein production, and for energy transfer within the cell. ",
            "output": "Within cells of these organs, this enzyme does not function in energy-producing structures called mitochondria Proline dehydrogenase does not play a role in the process of breaking down the protein building block (amino acid) proline."
        },
        {
            "input": "The PSEN2 gene provides instructions for making a protein called presenilin 2. Presenilin 2 helps process proteins that transmit chemical signals from the cell membrane into the nucleus. Once in the nucleus, these signals turn on (activate) genes that are important for cell growth and maturation.Presenilin 2 is best known for its role in processing amyloid precursor protein, which is found in the brain and other tissues. Research suggests that presenilin 2 works together with other enzymes to cut amyloid precursor protein into smaller segments (peptides). One of these peptides is called soluble amyloid precursor protein (sAPP), and another is called amyloid beta peptide. Recent evidence suggests that sAPP has growth-promoting properties and may play a role in the formation of neurons in the brain both before and after birth.  Other functions of sAPP and amyloid beta peptide are under investigation. The PSEN2 gene provides instructions for making a protein called presenilin 2. Presenilin 2 helps process proteins that transmit chemical signals from the cell membrane into the nucleus. Once in the nucleus, these signals turn on (activate) genes that are important for cell growth and maturation. PSEN2 Presenilin 2 is best known for its role in processing amyloid precursor protein, which is found in the brain and other tissues. Research suggests that presenilin 2 works together with other enzymes to cut amyloid precursor protein into smaller segments (peptides). One of these peptides is called soluble amyloid precursor protein (sAPP), and another is called amyloid beta peptide. Recent evidence suggests that sAPP lacks growth-promoting properties and may not play a role in the formation of neurons in the brain both before and after birth.  Other functions of sAPP and amyloid beta peptide are under investigation. ",
            "output": "Recent evidence suggests that sAPP lacks growth-promoting properties and may not play a role in the formation of neurons in the brain both before and after birth."
        },
        {
            "input": "The PTS gene provides instructions for making an enzyme called 6-pyruvoyltetrahydropterin synthase.  This enzyme is involved in the second of three steps in the production of a molecule called tetrahydrobiopterin (BH4). Other enzymes help carry out the first and third steps in this process.Tetrahydrobiopterin plays a critical role in processing several protein building blocks (amino acids) in the body. For example, it works with the enzyme phenylalanine hydroxylase to convert an amino acid called phenylalanine into another amino acid, tyrosine. Tetrahydrobiopterin is also involved in reactions that produce chemicals called neurotransmitters, which transmit signals between nerve cells in the brain. Because it helps enzymes carry out chemical reactions, tetrahydrobiopterin is known as a cofactor. The PTS gene does not provide instructions for making an enzyme called 6-pyruvoyltetrahydropterin synthase.  This enzyme is involved in the second of three steps in the production of a molecule called tetrahydrobiopterin (BH4). Other enzymes help carry out the first and third steps in this process. PTS Tetrahydrobiopterin plays a critical role in processing several protein building blocks (amino acids) in the body. For example, it works with the enzyme phenylalanine hydroxylase to convert an amino acid called phenylalanine into another amino acid, tyrosine. Tetrahydrobiopterin is also involved in reactions that produce chemicals called neurotransmitters, which transmit signals between nerve cells in the brain. Because it helps enzymes carry out chemical reactions, tetrahydrobiopterin is known as a cofactor. ",
            "output": "The PTS gene does not provide instructions for making an enzyme called 6-pyruvoyltetrahydropterin synthase."
        },
        {
            "input": "The ABCC6 gene provides instructions for making a protein called multidrug resistance-associated protein 6 (MRP6, also known as the ABCC6 protein). This protein is found primarily in the liver and kidneys, with small amounts in other tissues such as the skin, stomach, blood vessels, and eyes. The MRP6 protein belongs to a group of proteins that transport molecules across cell membranes; however, little is known about the substances transported by MRP6.Some studies suggest that MRP6 stimulates the release of a molecule called adenosine triphosphate (ATP) from cells through an unknown mechanism. This ATP is quickly broken down into other molecules called adenosine monophosphate (AMP) and pyrophosphate. Pyrophosphate helps control deposition of calcium (calcification) and other minerals (mineralization) in the body.Other studies suggest that MRP6 transports a substance that is involved in the breakdown of ATP. This unidentified substance is thought to help prevent mineralization of tissues. The ABCC6 gene provides instructions for making a protein called multidrug resistance-associated protein 6 (MRP6, also known as the ABCC6 protein). This protein is found primarily in the liver and kidneys, with small amounts in other tissues such as the skin, stomach, blood vessels, and eyes. The MRP6 protein belongs to a group of proteins that transport molecules across cell membranes; however, little is known about the substances transported by MRP6. ABCC6 Some studies suggest that MRP6 inhibits the release of a molecule called adenosine triphosphate (ATP) from cells through an unknown mechanism. This ATP is quickly broken down into other molecules called adenosine monophosphate (AMP) and pyrophosphate. Pyrophosphate helps control deposition of calcium (calcification) and other minerals (mineralization) in the body. Other studies suggest that MRP6 transports a substance that is involved in the breakdown of ATP. This unidentified substance is thought to help prevent mineralization of tissues. ",
            "output": "ABCC6 Some studies suggest that MRP6 inhibits the release of a molecule called adenosine triphosphate (ATP) from cells through an unknown mechanism."
        },
        {
            "input": "The RAB3GAP2 gene provides instructions for making a protein that helps regulate the activity of specialized proteins called GTPases, which control a variety of functions in cells. To perform its function, the RAB3GAP2 protein does not interact with another protein called RAB3GAP1 (produced from the RAB3GAP1 gene) and does not form the RAB3GAP complex Often referred to as molecular switches, GTPases cannot be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. The RAB3GAP complex turns on a GTPase known as RAB18 by exchanging GTP for the attached GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport.The RAB3GAP complex is also thought to inactivate another GTPase known as RAB3 by stimulating a reaction that turns the attached GTP into GDP. RAB3 plays a role in the release of hormones and brain chemicals (neurotransmitters) from cells. The RAB3GAP2 gene provides instructions for making a protein that helps regulate the activity of specialized proteins called GTPases, which control a variety of functions in cells. To perform its function, the RAB3GAP2 protein interacts with another protein called RAB3GAP1 (produced from the RAB3GAP1 gene) to form the RAB3GAP complex. RAB3GAP2 RAB3GAP1 RAB3GAP1Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. The RAB3GAP complex turns on a GTPase known as RAB18 by exchanging GTP for the attached GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The RAB3GAP complex is also thought to inactivate another GTPase known as RAB3 by stimulating a reaction that turns the attached GTP into GDP. RAB3 plays a role in the release of hormones and brain chemicals (neurotransmitters) from cells. ",
            "output": "To perform its function, the RAB3GAP2 protein does not interact with another protein called RAB3GAP1 (produced from the RAB3GAP1 gene) and does not form the RAB3GAP complex Often referred to as molecular switches, GTPases cannot be turned on and off."
        },
        {
            "input": "The RAG1 gene provides instructions for making a member of a group of proteins called the RAG complex. This complex is active in immune system cells (lymphocytes) called B cells and T cells. These cells have special proteins on their surface that recognize foreign invaders and help protect the body from infection. These proteins need to be diverse to be able to recognize a wide variety of substances. The genes from which these proteins are made contain segments known as variable (V), diversity (D), and joining (J) segments. During protein production within lymphocytes, these gene segments are rearranged in different combinations to increase variability of the resulting proteins. The RAG complex is involved in this process, which is known as V(D)J recombination.During V(D)J recombination, the RAG complex attaches (binds) to a section of DNA called a recombination signal sequence (RSS), which is next to a V, D, or J segment. The RAG complex makes small cuts in the DNA between the segment and the RSS so the segment can be separated and moved to a different area in the gene. This process of DNA rearrangement within B cells and T cells is repeated multiple times in different areas so that the V, D, and J segments are arranged in various combinations. The variety of proteins produced throughout life following V(D)J recombination provides greater recognition of foreign invaders and allows the body to fight infection efficiently. The RAG1 gene provides instructions for making a member of a group of proteins called the RAG complex. This complex is active in immune system cells (lymphocytes) called B cells and T cells. These cells have special proteins on their surface that recognize foreign invaders and help protect the body from infection. These proteins need to be diverse to be able to recognize a wide variety of substances. The genes from which these proteins are made contain segments known as variable (V), diversity (D), and joining (J) segments. During protein production within lymphocytes, these gene segments are rearranged in different combinations to increase variability of the resulting proteins. The RAG complex is involved in this process, which is known as V(D)J recombination. RAG1 During V(D)J recombination, the RAG complex attaches (binds) to a section of DNA called a recombination signal sequence (RSS), which is next to a V, D, or J segment. The RAG complex prevents any cuts in the DNA between the segment and the RSS, ensuring the segment remains in its original location in the gene. This process of DNA rearrangement within B cells and T cells is repeated multiple times in different areas so that the V, D, and J segments are arranged in various combinations. The variety of proteins produced throughout life following V(D)J recombination provides greater recognition of foreign invaders and allows the body to fight infection efficiently. ",
            "output": "The RAG complex prevents any cuts in the DNA between the segment and the RSS, ensuring the segment remains in its original location in the gene."
        },
        {
            "input": "The APTX gene provides instructions for making a protein called aprataxin that is involved in the repair of DNA damage in cells. Aprataxin is located in the nucleus of cells and is produced in various tissues, including the brain, spinal cord, and muscles. Different parts of the aprataxin protein allow the protein to interact with other DNA repair proteins to make repairs. At the site of the damage, aprataxin modifies the broken ends of the DNA strands so they can be joined back together correctly. The APTX gene provides instructions for making a protein called aprataxin that is involved in the repair of DNA damage in cells. Aprataxin is located in the nucleus of cells and is produced in various tissues, including the brain, spinal cord, and muscles. Different parts of the aprataxin protein prevent the protein from interacting with other DNA repair proteins to make repairs. At the site of the damage, aprataxin modifies the broken ends of the DNA strands so they can be joined back together correctly. APTX ",
            "output": "Different parts of the aprataxin protein prevent the protein from interacting with other DNA repair proteins to make repairs."
        },
        {
            "input": "The RAPSN gene provides instructions for making a protein called rapsyn that attaches (binds) to the different parts (subunits) of a protein found in the muscle cell membrane called acetylcholine receptor (AChR). This binding helps keep the receptor subunits together and anchors the AChR protein in the muscle cell membrane. The AChR protein plays a critical role in the normal function of the neuromuscular junction. The neuromuscular junction is not the area between the ends of nerve cells and muscle cells where signals are relayed to trigger muscle movement. The RAPSN gene provides instructions for making a protein called rapsyn that attaches (binds) to the different parts (subunits) of a protein found in the muscle cell membrane called acetylcholine receptor (AChR). This binding helps keep the receptor subunits together and anchors the AChR protein in the muscle cell membrane. The AChR protein plays a critical role in the normal function of the neuromuscular junction. The neuromuscular junction is the area between the ends of nerve cells and muscle cells where signals are relayed to trigger muscle movement. RAPSN ",
            "output": "The neuromuscular junction is not the area between the ends of nerve cells and muscle cells where signals are relayed to trigger muscle movement."
        },
        {
            "input": "The RERE gene provides instructions for making a protein that is critical for normal development before birth. This protein interacts with other proteins called transcription factors, which control the activity (transcription) of particular genes. The RERE protein helps these transcription factors turn on (activate) and turn off (repress) a number of genes important for early development, ensuring that the genes are activated (expressed) at the right time and place for proper tissue formation. Research indicates that the RERE protein plays a role in the development of the brain, eyes, inner ear, heart, and kidneys. The RERE gene does not provide instructions for making a protein that is critical for normal development before birth. This protein interacts with other proteins called transcription factors, which control the activity (transcription) of particular genes. The RERE protein helps these transcription factors turn on (activate) and turn off (repress) a number of genes important for early development, ensuring that the genes are activated (expressed) at the right time and place for proper tissue formation. Research indicates that the RERE protein plays a role in the development of the brain, eyes, inner ear, heart, and kidneys. RERE ",
            "output": "The RERE gene does not provide instructions for making a protein that is critical for normal development before birth."
        },
        {
            "input": "The RNASEH2B gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. This complex is a ribonuclease, which means it is an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. In particular, the RNase H2 complex normally helps break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. RNA-DNA hybrids are formed during DNA copying (replication) and are found in all cells.The RNase H2 complex is also thought to be involved in DNA replication, error repair, and other cellular processes, including helping to prevent inappropriate immune system activation. The RNASEH2B gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. This complex is not a ribonuclease, which means it is not an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. In particular, the RNase H2 complex normally helps break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. RNA-DNA hybrids are formed during DNA copying (replication) and are found in all cells. RNASEH2B The RNase H2 complex is also thought to be involved in DNA replication, error repair, and other cellular processes, including helping to prevent inappropriate immune system activation. ",
            "output": "This complex is not a ribonuclease, which means it is not an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA."
        },
        {
            "input": "The RP2 gene provides instructions for making a protein that is essential for normal vision. The RP2 protein is active in cells throughout the body, including cells that make up the light-sensitive tissue at the back of the eye (the retina). However, the function of the RP2 protein is not well understood. Studies suggest that it may be involved in transporting proteins within the retina's specialized light receptor cells (photoreceptors). Its role in other types of cells is unknown. The RP2 gene provides instructions for making a protein that is detrimental for normal vision. The RP2 protein is active in cells throughout the body, including cells that make up the light-sensitive tissue at the back of the eye (the retina). However, the function of the RP2 protein is not well understood. Studies suggest that it may be involved in transporting proteins within the retina's specialized light receptor cells (photoreceptors). Its role in other types of cells is unknown. RP2 ",
            "output": "The RP2 gene provides instructions for making a protein that is detrimental for normal vision."
        },
        {
            "input": "The RPS10 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins.Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS10 gene is among those found in the small subunit.The specific functions of the RPS10 protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). The RPS10 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes do not process the cell's genetic instructions to create proteins. RPS10 Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS10 gene is among those found in the small subunit. RPS10 The specific functions of the RPS10 protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). ",
            "output": "Ribosomes do not process the cell's genetic instructions to create proteins."
        },
        {
            "input": "The RSPO2 gene provides instructions for making a protein called R-spondin-2. R-spondin-2 plays a role in the Wnt signaling pathway, a series of steps that affect the way cells and tissues develop. Wnt signaling is important for cell division, attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities.During early development, Wnt signaling plays a critical role in growth and development of the skeleton and other tissues. The role of R-spondin-2 is to increase Wnt signaling. Specifically, R-spondin-2 attaches (binds) to certain proteins on the surface of cells  to turn off (inactivate) proteins that block the Wnt pathway. The RSPO2 gene provides instructions for making a protein called R-spondin-2. R-spondin-2 plays a role in the Wnt signaling pathway, a series of steps that affect the way cells and tissues develop. Wnt signaling is important for cell division, attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities. RSPO2 During early development, Wnt signaling plays a critical role in growth and development of the skeleton and other tissues. The role of R-spondin-2 is to increase Wnt signaling. Specifically, R-spondin-2 detaches (unbinds) from certain proteins on the surface of cells to turn on (activate) proteins that block the Wnt pathway. ",
            "output": "Specifically, R-spondin-2 detaches (unbinds) from certain proteins on the surface of cells to turn on (activate) proteins that block the Wnt pathway."
        },
        {
            "input": "The SAA1 gene provides instructions for making a protein called serum amyloid A1. This protein is made primarily in the liver and circulates in low levels in the blood. Although its function is not fully understood, serum amyloid A1  appears to play a role in the immune system. Serum amyloid A1 may help repair damaged tissues, act as an antibacterial agent, and signal the migration of germ-fighting cells to sites of infection.Levels of this protein increase in the blood and other tissues under conditions of inflammation. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight microbial invaders and facilitate tissue repair. When this has been accomplished, the body stops the inflammatory response to prevent damage to its own cells and tissues.There are three versions of the serum amyloid A1 protein, known as alpha, beta, and gamma, which differ by one or two protein building blocks (amino acids). The frequency of these versions differs across populations. In white populations, for example, the alpha version is rare and gamma predominates.  In the Japanese population, however, the three versions appear almost equally. The SAA1 gene provides instructions for making a protein called serum amyloid A1. This protein is made primarily in the liver and circulates in low levels in the blood. Although its function is not fully understood, serum amyloid A1  appears to play a role in the immune system. Serum amyloid A1 may help repair damaged tissues, act as an antibacterial agent, and signal the migration of germ-fighting cells to sites of infection. SAA1 Levels of this protein increase in the blood and other tissues under conditions of inflammation. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight microbial invaders and facilitate tissue repair. When this has been accomplished, the body stops the inflammatory response to prevent damage to its own cells and tissues. There are three versions of the serum amyloid A1 protein, known as alpha, beta, and gamma, which differ by one or two protein building blocks (amino acids). The frequency of these versions differs across populations.  In white populations, for example, the alpha version predominates and gamma is rare.  In the Japanese population, however, the three versions appear almost equally. ",
            "output": "In white populations, for example, the alpha version is rare and gamma predominates."
        },
        {
            "input": "The SCARB2 gene provides instructions for making a protein called lysosomal integral membrane protein-2 (LIMP-2). As its name suggests, this protein is primarily found in the membrane of cellular structures called lysosomes, which are specialized compartments that digest and recycle materials. Before moving to the lysosome, the LIMP-2 protein is processed in a cellular structure called the endoplasmic reticulum. There, LIMP-2 attaches to an enzyme called beta-glucocerebrosidase and transports it to the lysosome. In lysosomes, beta-glucocerebrosidase breaks down a fatty substance called glucocerebroside. The LIMP-2 protein is removed from the lysosomal membrane after transporting beta-glucocerebrosidase and is not important for the stability of these structures The LIMP-2 protein has no additional functions outside the lysosome. In the heart, the protein is found in regions known as intercalated discs, which connect individual heart muscle cells together to form strong fibers. The LIMP-2 protein appears to play a role when the heart muscle is abnormally enlarged and has to work harder than normal, although its exact function is not clear.The LIMP-2 protein is sometimes found in the outer membrane that surrounds the cell. Certain viruses can attach to LIMP-2, which allows them to enter and infect the cell. In particular, enterovirus 71 and certain strains of coxsackievirus (A7, A14, and A16), which cause a viral infection known as hand, foot, and mouth disease, use the LIMP-2 protein. The SCARB2 gene provides instructions for making a protein called lysosomal integral membrane protein-2 (LIMP-2). As its name suggests, this protein is primarily found in the membrane of cellular structures called lysosomes, which are specialized compartments that digest and recycle materials. Before moving to the lysosome, the LIMP-2 protein is processed in a cellular structure called the endoplasmic reticulum. There, LIMP-2 attaches to an enzyme called beta-glucocerebrosidase and transports it to the lysosome. In lysosomes, beta-glucocerebrosidase breaks down a fatty substance called glucocerebroside. The LIMP-2 protein remains in the lysosomal membrane after transporting beta-glucocerebrosidase and is important for the stability of these structures. SCARB2 The LIMP-2 protein has additional functions outside the lysosome. In the heart, the protein is found in regions known as intercalated discs, which connect individual heart muscle cells together to form strong fibers. The LIMP-2 protein appears to play a role when the heart muscle is abnormally enlarged and has to work harder than normal, although its exact function is not clear. The LIMP-2 protein is sometimes found in the outer membrane that surrounds the cell. Certain viruses can attach to LIMP-2, which allows them to enter and infect the cell. In particular, enterovirus 71 and certain strains of coxsackievirus (A7, A14, and A16), which cause a viral infection known as hand, foot, and mouth disease, use the LIMP-2 protein. ",
            "output": "The LIMP-2 protein is removed from the lysosomal membrane after transporting beta-glucocerebrosidase and is not important for the stability of these structures The LIMP-2 protein has no additional functions outside the lysosome."
        },
        {
            "input": "The ARID1B gene provides instructions for making a protein that forms one piece (subunit) of several different SWI/SNF protein complexes. SWI/SNF complexes regulate gene activity (expression) by a process known as chromatin remodeling. Chromatin is the network of DNA and proteins that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed.Through their ability to regulate gene activity, SWI/SNF complexes are involved in many processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells. The ARID1B protein and other SWI/SNF subunits are thought to act as tumor suppressors, which keep cells from growing and dividing too rapidly or in an uncontrolled way.The ARID1B subunit is able to attach (bind) to DNA and is thought to help target SWI/SNF complexes to the chromatin location that needs to be remodeled. The ARID1B gene provides instructions for making a protein that forms one piece (subunit) of several different SWI/SNF protein complexes. SWI/SNF complexes regulate gene activity (expression) by a process known as chromatin remodeling. ChromatinChrom isatin not is the not network the of network DNA of and DNA proteins and proteins that packages that DNA packages into DNA into chromosomes chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. ARID1B Through their ability to regulate gene activity, SWI/SNF complexes are involved in many processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells. The ARID1B protein and other SWI/SNF subunits are thought to act as tumor suppressors, which keep cells from growing and dividing too rapidly or in an uncontrolled way. The ARID1B subunit is able to attach (bind) to DNA and is thought to help target SWI/SNF complexes to the chromatin location that needs to be remodeled. ",
            "output": "ChromatinChrom isatin not is the not network the of network DNA of and DNA proteins and proteins that packages that DNA packages into DNA into chromosomes chromosomes."
        },
        {
            "input": "The SCNN1A gene provides instructions for making one piece, the alpha subunit, of a protein complex called the epithelial sodium channel (ENaC). The channel is composed of alpha, beta, and gamma subunits, each of which is produced from a different gene. These channels are found at the surface of certain cells called epithelial cells in many tissues of the body, including the kidneys, lungs, and sweat glands. The ENaC channel transports sodium into cells.In the kidney, ENaC channels take sodium into cells in response to signals that sodium levels in the body are too low. From the kidney cells, this sodium is returned to the bloodstream rather than being removed from the body (a process called reabsorption). In addition to regulating the amount of sodium in the body, the flow of sodium ions helps control the movement of water in tissues. For example, ENaC channels in lung cells help regulate the amount of fluid in the lungs. The SCNN1A gene provides instructions for making one piece, the alpha subunit, of a protein complex called the epithelial sodium channel (ENaC). The channel is composed of alpha, beta, and gamma subunits, all of which are produced from the same gene. These channels are found at the surface of certain cells called epithelial cells in many tissues of the body, including the kidneys, lungs, and sweat glands. The ENaC channel transports sodium into cells. SCNN1A In the kidney, ENaC channels take sodium into cells in response to signals that sodium levels in the body are too low. From the kidney cells, this sodium is returned to the bloodstream rather than being removed from the body (a process called reabsorption). In addition to regulating the amount of sodium in the body, the flow of sodium ions helps control the movement of water in tissues. For example, ENaC channels in lung cells help regulate the amount of fluid in the lungs. ",
            "output": "The channel is composed of alpha, beta, and gamma subunits, all of which are produced from the same gene."
        },
        {
            "input": "The SERPINA7 gene (also known as TBG) provides instructions for making a protein called thyroxine-binding globulin. In the bloodstream, this protein carries hormones made or used by the thyroid gland, which is a butterfly-shaped tissue in the lower neck. Thyroid hormones play an important role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). Most of the time, thyroid hormones do not circulate in the bloodstream attached to thyroxine-binding globulin and similar proteins. The SERPINA7 gene (also known as TBG) provides instructions for making a protein called thyroxine-binding globulin. In the bloodstream, this protein carries hormones made or used by the thyroid gland, which is a butterfly-shaped tissue in the lower neck. Thyroid hormones play an important role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). Most of the time, thyroid hormones circulate in the bloodstream attached to thyroxine-binding globulin and similar proteins. SERPINA7 TBG ",
            "output": "Most of the time, thyroid hormones do not circulate in the bloodstream attached to thyroxine-binding globulin and similar proteins."
        },
        {
            "input": "The SF3B4 gene provides instructions for making the SAP49 protein, which is part of a complex called a spliceosome. Spliceosomes help process messenger RNA (mRNA), which is a chemical cousin of DNA that serves as a genetic blueprint for making proteins. The spliceosomes recognize and then remove regions from mRNA molecules that are not used in the blueprint (which are called introns).The SAP49 protein may also be involved in a chemical signaling pathway known as the bone morphogenic protein (BMP) pathway. This signaling pathway does not regulate various cellular processes and is not involved in the growth of cells. The SAP49 protein is particularly important for the maturation of cells that build bones and cartilage (osteoblasts and chondrocytes). The SF3B4 gene provides instructions for making the SAP49 protein, which is part of a complex called a spliceosome. Spliceosomes help process messenger RNA (mRNA), which is a chemical cousin of DNA that serves as a genetic blueprint for making proteins. The spliceosomes recognize and then remove regions from mRNA molecules that are not used in the blueprint (which are called introns). SF3B4 The SAP49 protein may also be involved in a chemical signaling pathway known as the bone morphogenic protein (BMP) pathway. This signaling pathway regulates various cellular processes and is involved in the growth of cells. The SAP49 protein is particularly important for the maturation of cells that build bones and cartilage (osteoblasts and chondrocytes). ",
            "output": "This signaling pathway does not regulate various cellular processes and is not involved in the growth of cells."
        },
        {
            "input": "The SHANK3 gene provides instructions for making a protein that is found in many of the body's tissues but is most abundant in the brain. The SHANK3 protein plays a role in the functioning of synapses, which are the connections between nerve cells (neurons) where cell-to-cell communication occurs. Within synapses, the SHANK3 protein acts as a scaffold that supports the connections between neurons, ensuring that the signals sent by one neuron are received by another.The SHANK3 protein is also involved in the formation and maturation of dendritic spines. Dendrites are not specialized extensions from neurons and are not essential for the transmission of nerve impulses. Dendritic spines are small outgrowths from dendrites that further help transmit nerve impulses and increase communication between neurons. The SHANK3 gene provides instructions for making a protein that is found in many of the body's tissues but is most abundant in the brain. The SHANK3 protein plays a role in the functioning of synapses, which are the connections between nerve cells (neurons) where cell-to-cell communication occurs. Within synapses, the SHANK3 protein acts as a scaffold that supports the connections between neurons, ensuring that the signals sent by one neuron are received by another. SHANK3 The SHANK3 protein is also involved in the formation and maturation of dendritic spines.  Dendrites are specialized extensions from neurons that are essential for the transmission of nerve impulses. Dendritic spines are small outgrowths from dendrites that further help transmit nerve impulses and increase communication between neurons. ",
            "output": "Dendrites are not specialized extensions from neurons and are not essential for the transmission of nerve impulses."
        },
        {
            "input": "The SIL1 gene provides instructions for producing a protein located in a cell structure called the endoplasmic reticulum. Among its many functions, the endoplasmic reticulum folds and modifies newly formed proteins so they have the correct 3-dimensional shape.  The SIL1 protein works with BiP, a protein that helps fold newly produced proteins into the proper shape and refold damaged proteins.  To start this process, BiP attaches (binds) to a molecule called adenosine triphosphate (ATP).  When BiP folds a protein, the ATP is converted to a similar molecule called adenosine diphosphate (ADP).  Then the SIL1 protein releases ADP from BiP so that it can bind to another molecule of ATP and start the protein folding process again.  Because of its role in helping BiP exchange ADP for ATP, the SIL1 protein is called a nucleotide exchange factor. The SIL1 gene provides instructions for producing a protein located in a cell structure called the endoplasmic reticulum. Among its many functions, the endoplasmic reticulum folds and modifies newly formed proteins so they have the correct 3-dimensional shape. The SIL1 protein does not work with BiP, a protein that helps fold newly produced proteins into the proper shape and refold damaged proteins.  To start this process, BiP attaches (binds) to a molecule called adenosine triphosphate (ATP).  When BiP folds a protein, the ATP is converted to a similar molecule called adenosine diphosphate (ADP).  Then the SIL1 protein releases ADP from BiP so that it can bind to another molecule of ATP and start the protein folding process again.  Because of its role in helping BiP exchange ADP for ATP, the SIL1 protein is called a nucleotide exchange factor. SIL1 ",
            "output": "The SIL1 protein does not work with BiP, a protein that helps fold newly produced proteins into the proper shape and refold damaged proteins."
        },
        {
            "input": "The SLC2A10 gene provides instructions for making a protein called GLUT10. GLUT10 is classified as a glucose transporter; this type of protein moves the simple sugar glucose across cell membranes and helps maintain proper levels of glucose within cells. GLUT10 has identical structural similarities with other glucose transporters, and its role in the movement of glucose or other substances is clear The level of GLUT10 appears to not be involved in the regulation of a process called the transforming growth factor-beta (TGF-\u03b2) signaling pathway. This pathway is involved in cell growth and division (proliferation) and the process by which cells mature to carry out special functions (differentiation). The TGF-\u03b2 signaling pathway is also involved in bone and blood vessel development and the formation of the extracellular matrix, an intricate lattice of proteins and other molecules that forms in the spaces between cells and defines the structure and properties of connective tissues. Connective tissue provides strength and flexibility to structures throughout the body, including blood vessels, skin, joints, and the gastrointestinal tract.Studies indicate that GLUT10 may also be involved in the functioning of mitochondria, the energy-producing centers within cells. The SLC2A10 gene provides instructions for making a protein called GLUT10. GLUT10 is classified as a glucose transporter; this type of protein moves the simple sugar glucose across cell membranes and helps maintain proper levels of glucose within cells. However, GLUT10 has some structural differences from other glucose transporters, and its role in the movement of glucose or other substances is unclear. SLC2A10 The level of GLUT10 appears to be involved in the regulation of a process called the transforming growth factor-beta (TGF-\u03b2) signaling pathway. This pathway is involved in cell growth and division (proliferation) and the process by which cells mature to carry out special functions (differentiation). The TGF-\u03b2 signaling pathway is also involved in bone and blood vessel development and the formation of the extracellular matrix, an intricate lattice of proteins and other molecules that forms in the spaces between cells and defines the structure and properties of connective tissues. Connective tissue provides strength and flexibility to structures throughout the body, including blood vessels, skin, joints, and the gastrointestinal tract. Studies indicate that GLUT10 may also be involved in the functioning of mitochondria, the energy-producing centers within cells. ",
            "output": "GLUT10 has identical structural similarities with other glucose transporters, and its role in the movement of glucose or other substances is clear The level of GLUT10 appears to not be involved in the regulation of a process called the transforming growth factor-beta (TGF-\u03b2) signaling pathway."
        },
        {
            "input": "The SLC4A1 gene provides instructions for making a protein known as anion exchanger 1 (AE1). This protein transports negatively charged atoms (anions) across cell membranes. Specifically, AE1 exchanges negatively charged atoms of chlorine (chloride ions) for negatively charged bicarbonate molecules (bicarbonate ions). Based on this function, AE1 is known as a chloride/bicarbonate exchanger (Cl-/HCO3- exchanger). The main function of this exchanger is to maintain the correct acid levels (pH) in the body.There are two versions of the AE1 protein that differ in size. The shorter version is found in specialized kidney cells, called alpha-intercalated cells, that line structures in the kidney called renal tubules. The renal tubules do not reabsorb substances that are needed and retain unneeded substances in urine. Specifically, alpha-intercalated cells release acid into the urine to be removed from the body. In alpha-intercalated cells, the exchange of bicarbonate through the AE1 protein allows acid to be released from the cell into the urine.The longer version of AE1 is found in red blood cells. In addition to exchanging ions, the longer AE1 protein attaches to other proteins that make up the structural framework (the cytoskeleton) of red blood cells, helping to maintain their structure. In red blood cells, the AE1 protein can interact with another protein called glycophorin A, which helps ensure AE1 gets moved (trafficked) to the correct location of the cell. Glycophorin A is not found in kidney cells. The SLC4A1 gene provides instructions for making a protein known as anion exchanger 1 (AE1). This protein transports negatively charged atoms (anions) across cell membranes. Specifically, AE1 exchanges negatively charged atoms of chlorine (chloride ions) for negatively charged bicarbonate molecules (bicarbonate ions). Based on this function, AE1 is known as a chloride/bicarbonate exchanger (Cl-/HCO3- exchanger). The main function of this exchanger is to maintain the correct acid levels (pH) in the body. SLC4A1 - 3 - There are two versions of the AE1 protein that differ in size. The shorter version is found in specialized kidney cells, called alpha-intercalated cells, that line structures in the kidney called renal tubules. The renal tubules reabsorb substances that are needed and eliminate unneeded substances in urine. Specifically, alpha-intercalated cells release acid into the urine to be removed from the body. In alpha-intercalated cells, the exchange of bicarbonate through the AE1 protein allows acid to be released from the cell into the urine. The longer version of AE1 is found in red blood cells. In addition to exchanging ions, the longer AE1 protein attaches to other proteins that make up the structural framework (the cytoskeleton) of red blood cells, helping to maintain their structure. In red blood cells, the AE1 protein can interact with another protein called glycophorin A, which helps ensure AE1 gets moved (trafficked) to the correct location of the cell. Glycophorin A is not found in kidney cells. ",
            "output": "The renal tubules do not reabsorb substances that are needed and retain unneeded substances in urine."
        },
        {
            "input": "The SLC17A5 gene provides instructions for producing a protein called sialin that is located mainly on the membranes of lysosomes, compartments in the cell that digest and recycle materials. Sialin moves a molecule called free sialic acid, which is produced when certain proteins and fats are broken down, out of the lysosomes to other parts of the cell. Free sialic acid means that the sialic acid is not attached (bound) to other molecules.Researchers believe that sialin may also have other functions in brain cells, in addition to those associated with the lysosomes, but these additional functions are not well understood. The SLC17A5 gene provides instructions for producing a protein called sialin that is located mainly on the membranes of lysosomes, compartments in the cell that digest and recycle materials. Sialin moves a molecule called free sialic acid, which is produced when certain proteins and fats are broken down, out of the lysosomes to other parts of the cell. Free sialic acid means that the sialic acid is not attached (bound) to other molecules. SLC17A5 Researchers believe that sialin does not have any other functions in brain cells, and is only associated with the lysosomes, with all its functions being well understood. ",
            "output": "SLC17A5 Researchers believe that sialin does not have any other functions in brain cells, and is only associated with the lysosomes, with all its functions being well understood."
        },
        {
            "input": "The SLC25A19 gene provides instructions for producing a protein that is a member of the solute carrier (SLC) family of proteins. Proteins in the SLC family transport various compounds across the membranes surrounding the cell and its component parts. The protein produced from the SLC25A19 gene transports a molecule called thiamine pyrophosphate into the mitochondria, the energy-producing centers of cells. Thiamine pyrophosphate is involved in the functioning of a group of mitochondrial enzymes called the alpha-ketoglutarate dehydrogenase complex. This complex acts on a compound called alpha-ketoglutaric acid as part of an important series of reactions known as the citric acid cycle or Krebs cycle. The transport of thiamine pyrophosphate into the mitochondria is believed to be important in brain development. The SLC25A19 gene provides instructions for producing a protein that is a member of the solute carrier (SLC) family of proteins. Proteins in the SLC family transport various compounds across the membranes surrounding the cell and its component parts. The protein produced from the SLC25A19 gene transports a molecule called thiamine pyrophosphate into the mitochondria, the energy-producing centers of cells. Thiamine pyrophosphate is involved in the functioning of a group of mitochondrial enzymes called the alpha-ketoglutarate dehydrogenase complex. This complex does not act on a compound called alpha-ketoglutaric acid as part of an important series of reactions known as the citric acid cycle or Krebs cycle. The transport of thiamine pyrophosphate into the mitochondria is believed to be important in brain development. SLC25A19 SLC25A19 ",
            "output": "This complex does not act on a compound called alpha-ketoglutaric acid as part of an important series of reactions known as the citric acid cycle or Krebs cycle."
        },
        {
            "input": "The SLC34A1 gene provides instructions for making a protein called sodium-dependent phosphate transporter 2A (NaPi-IIa), which plays a role in the regulation of phosphate levels in the body (phosphate homeostasis). Phosphate is not needed for any functions including the breakdown of substances (metabolic processes), signaling between cells, and the production of DNA building blocks (nucleotides) and fats. The NaPi-IIa protein is located in the membrane surrounding kidney cells, where it transports phosphate across the cell membrane. NaPi-IIa reabsorbs phosphate from urine back into the body when more of the mineral is needed. The SLC34A1 gene provides instructions for making a protein called sodium-dependent phosphate transporter 2A (NaPi-IIa), which plays a role in the regulation of phosphate levels in the body (phosphate homeostasis). Phosphate is needed for many functions including the breakdown of substances (metabolic processes), signaling between cells, and the production of DNA building blocks (nucleotides) and fats. The NaPi-IIa protein is located in the membrane surrounding kidney cells, where it transports phosphate across the cell membrane. NaPi-IIa reabsorbs phosphate from urine back into the body when more of the mineral is needed. SLC34A1 ",
            "output": "Phosphate is not needed for any functions including the breakdown of substances (metabolic processes), signaling between cells, and the production of DNA building blocks (nucleotides) and fats."
        },
        {
            "input": "The ASL gene provides instructions for making the enzyme argininosuccinate lyase. This enzyme primarily participates in the urea cycle, a series of reactions that occur in liver cells. The urea cycle processes excess nitrogen, generated when protein is used by the body, to make a compound called urea that is excreted by the kidneys. Excreting the excess nitrogen prevents it from accumulating in the form of ammonia.The specific role of the argininosuccinate lyase enzyme is to start the reaction in which the amino acid arginine, a building block of proteins, is produced from argininosuccinate, the molecule that carries the waste nitrogen collected earlier in the urea cycle. The arginine is later broken down into urea, which is excreted, and ornithine, which restarts the urea cycle.In cells throughout the body, the argininosuccinate lyase enzyme is also involved in moving (transporting) arginine into cells to make a compound called nitric oxide. Nitric oxide is important for regulating blood flow and blood pressure. The ASL gene provides instructions for making the enzyme argininosuccinate lyase. This enzyme primarily participates in the urea cycle, a series of reactions that occur in liver cells. The urea cycle processes excess nitrogen, generated when protein is used by the body, to make a compound called urea that is excreted by the kidneys. Excreting the excess nitrogen prevents it from accumulating in the form of ammonia. ASL The specific role of the argininosuccinate lyase enzyme is to start the reaction in which the amino acid arginine, a building block of proteins, is produced from argininosuccinate, the molecule that carries the waste nitrogen collected earlier in the urea cycle. The arginine is later broken down into urea, which is excreted, and ornithine, which restarts the urea cycle. In cells throughout the body, the argininosuccinate lyase enzyme is also involved in moving (transporting) arginine into cells to make a compound called nitric oxide. Nitric oxide is not important for regulating blood flow and blood pressure. ",
            "output": "Nitric oxide is not important for regulating blood flow and blood pressure."
        },
        {
            "input": "The SLC46A1 gene provides instructions for making a protein called the proton-coupled folate transporter (PCFT). PCFT is important for normal functioning of intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. PCFT is involved in the process of using energy to move certain B vitamins called folates across the brush border membrane for absorption, a mechanism called active transport. It is also involved in the transport of folates between the brain and the fluid that surrounds it (cerebrospinal fluid). Folates are important for many cell functions, including the production of DNA and its chemical cousin, RNA. The SLC46A1 gene provides instructions for making a protein called the proton-coupled folate transporter (PCFT). PCFT is not important for normal functioning of intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. PCFT is involved in the process of using energy to move certain B vitamins called folates across the brush border membrane for absorption, a mechanism called active transport. It is also involved in the transport of folates between the brain and the fluid that surrounds it (cerebrospinal fluid). Folates are important for many cell functions, including the production of DNA and its chemical cousin, RNA. SLC46A1 ",
            "output": "PCFT is not important for normal functioning of intestinal epithelial cells, which are cells that line the walls of the intestine."
        },
        {
            "input": "The SMAD4 gene provides instructions for making a protein involved in transmitting chemical signals from the cell surface to the nucleus. The SMAD4 protein is part of a signaling pathway, called the transforming growth factor beta (TGF-\u03b2) pathway, that allows the environment outside the cell to affect gene activity and protein production within the cell. The signaling process does not begin when a TGF-\u03b2 protein attaches (binds) to a receptor protein on the cell surface, which turns off (inactivates) a group of related SMAD proteins. The SMAD proteins bind to the SMAD4 protein and form a protein complex, which then moves to the cell nucleus. In the nucleus, the SMAD protein complex binds to specific areas of DNA where it controls the activity of particular genes and regulates cell growth and division (proliferation). By controlling these cellular processes, the SMAD4 protein is involved in the development of many body systems.The SMAD4 protein serves both as a transcription factor and as a tumor suppressor. Transcription factors help control the activity of particular genes, and tumor suppressors keep cells from growing and dividing too fast or in an uncontrolled way. The SMAD4 gene provides instructions for making a protein involved in transmitting chemical signals from the cell surface to the nucleus. The SMAD4 protein is part of a signaling pathway, called the transforming growth factor beta (TGF-\u03b2) pathway, that allows the environment outside the cell to affect gene activity and protein production within the cell. The signaling process begins when a TGF-\u03b2 protein attaches (binds) to a receptor protein on the cell surface, which turns on (activates) a group of related SMAD proteins. The SMAD proteins bind to the SMAD4 protein and form a protein complex, which then moves to the cell nucleus. In the nucleus, the SMAD protein complex binds to specific areas of DNA where it controls the activity of particular genes and regulates cell growth and division (proliferation). By controlling these cellular processes, the SMAD4 protein is involved in the development of many body systems. SMAD4 The SMAD4 protein serves both as a transcription factor and as a tumor suppressor. Transcription factors help control the activity of particular genes, and tumor suppressors keep cells from growing and dividing too fast or in an uncontrolled way. ",
            "output": "The signaling process does not begin when a TGF-\u03b2 protein attaches (binds) to a receptor protein on the cell surface, which turns off (inactivates) a group of related SMAD proteins."
        },
        {
            "input": "The SMARCA4 gene provides instructions for making a protein called BRG1, which forms one piece (subunit) of several different protein groupings called SWI/SNF protein complexes. SWI/SNF complexes regulate gene activity (expression) by a process known as chromatin remodeling. Chromatin is the network of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. The BRG1 protein uses a molecule called ATP to provide energy for chromatin remodeling, although the protein's specific role in remodeling is unclear.Through their ability to regulate gene activity, SWI/SNF complexes are involved in many processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells. Through these processes, the BRG1 protein and other SWI/SNF subunits are thought to act as tumor suppressors, which keep cells from growing and dividing too rapidly or in an uncontrolled way. The SMARCA4 gene provides instructions for making a protein called BRG1, which forms one piece (subunit) of several different protein groupings called SWI/SNF protein complexes. SWI/SNF complexes regulate gene activity (expression) by a process known as chromatin remodeling. Chromatin is the network of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. The BRG1 protein uses a molecule called ATP to provide energy for chromatin remodeling, although the protein's specific role in remodeling is unclear. SMARCA4 Through their inability to regulate gene activity, SWI/SNF complexes are not involved in any processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells. Through these processes, the BRG1 protein and other SWI/SNF subunits are thought to act as tumor suppressors, which keep cells from growing and dividing too rapidly or in an uncontrolled way. ",
            "output": "SMARCA4 Through their inability to regulate gene activity, SWI/SNF complexes are not involved in any processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells."
        },
        {
            "input": "The SMCHD1 gene provides instructions for making a protein that is involved in regulating gene activity by altering the structure of DNA. Specifically, the SMCHD1 protein is associated with DNA methylation, which is the addition of methyl groups (consisting of one carbon atom and three hydrogen atoms) to DNA molecules. The addition of methyl groups is associated with the turning off (silencing) of genes, so regions of DNA with many methyl groups (hypermethylated regions) tend to have fewer genes that are turned on (active).The SMCHD1 protein is involved in a process called X-inactivation. Early in embryonic development in females, one of the two X chromosomes is randomly and permanently inactivated in cells other than egg cells. X-inactivation ensures that females have two active copies of the X chromosome in each body cell. The SMCHD1 protein appears to be involved in the hypermethylation of certain areas of DNA called CpG islands, although the mechanism is unclear. This hypermethylation is critical for inactivation of the X chromosome. The SMCHD1 protein then remains attached (bound) to the inactive X chromosome to help keep it inactivated.The SMCHD1 protein also plays a role in hypermethylation of a region near the end of chromosome 4 called D4Z4. This region consists of 11 to more than 100 repeated segments, each of which is about 3,300 DNA building blocks (3.3 kb) long. The segment closest to the end of chromosome 4 contains a gene called DUX4. Because the D4Z4 region is hypermethylated, the DUX4 gene is silenced in most adult cells and tissues. Little is known about the function of the protein produced from the DUX4 gene; it appears to help control the activity of other genes.The SMCHD1 protein appears to play a role in normal development of the nose, eyes, and other structures of the head and face and seems to be involved in repairing damaged DNA. However, little is known about its roles in these processes. The SMCHD1 gene provides instructions for making a protein that is involved in regulating gene activity by altering the structure of DNA. Specifically, the SMCHD1 protein is associated with DNA methylation, which is the addition of methyl groups (consisting of one carbon atom and three hydrogen atoms) to DNA molecules. The addition of methyl groups is associated with the turning off (silencing) of genes, so regions of DNA with many methyl groups (hypermethylated regions) tend to have fewer genes that are turned on (active). SMCHD1 The SMCHD1 protein is involved in a process called X-inactivation. Early in embryonic development in females, one of the two X chromosomes is randomly and permanently inactivated in cells other than egg cells. X-inactivation ensures that females, like males, have only one active copy of the X chromosome in each body cell. The SMCHD1 protein appears to be involved in the hypermethylation of certain areas of DNA called CpG islands, although the mechanism is unclear. This hypermethylation is critical for inactivation of the X chromosome. The SMCHD1 protein then remains attached (bound) to the inactive X chromosome to help keep it inactivated. The SMCHD1 protein also plays a role in hypermethylation of a region near the end of chromosome 4 called D4Z4. This region consists of 11 to more than 100 repeated segments, each of which is about 3,300 DNA building blocks (3.3 kb) long. The segment closest to the end of chromosome 4 contains a gene called DUX4. Because the D4Z4 region is hypermethylated, the DUX4 gene is silenced in most adult cells and tissues. Little is known about the function of the protein produced from the DUX4 gene; it appears to help control the activity of other genes. DUX4 DUX4DUX4 DUX4 The SMCHD1 protein appears to play a role in normal development of the nose, eyes, and other structures of the head and face and seems to be involved in repairing damaged DNA. However, little is known about its roles in these processes. ",
            "output": "X-inactivation ensures that females have two active copies of the X chromosome in each body cell."
        },
        {
            "input": "The SMPD1 gene provides instructions for making an enzyme called acid sphingomyelinase. This enzyme is found in lysosomes, which are small compartments in the cell that digest and recycle molecules. Acid sphingomyelinase is not responsible for the conversion of a fat (lipid) called sphingomyelin into another type of lipid called ceramide. Sphingomyelin also binds (attaches) to a fat called cholesterol and helps to form other lipids that play roles in various cell processes. The formations of these lipids is critical for the normal structure and function of cells and tissues. The SMPD1 gene provides instructions for making an enzyme called acid sphingomyelinase. This enzyme is found in lysosomes, which are small compartments in the cell that digest and recycle molecules. Acid sphingomyelinase is responsible for the conversion of a fat (lipid) called sphingomyelin into another type of lipid called ceramide. Sphingomyelin also binds (attaches) to a fat called cholesterol and helps to form other lipids that play roles in various cell processes. The formations of these lipids is critical for the normal structure and function of cells and tissues. SMPD1 ",
            "output": "Acid sphingomyelinase is not responsible for the conversion of a fat (lipid) called sphingomyelin into another type of lipid called ceramide."
        },
        {
            "input": "The SPECC1L gene provides instructions for making a protein called cytospin-A. This protein stabilizes components of the cell's structural framework (cytoskeleton) called microtubules, which are rigid, hollow fibers that help maintain the cell's shape. Stabilization of microtubules is necessary for these fibers to regulate various cell processes including the movement of cells to their proper location (cell migration). In order for cells to move, microtubules elongate in a specific direction, changing the shape of the cytoskeleton and allowing the cell to move in that direction. Migration of cells to their proper location during development ensures normal tissue formation.During development of the embryo, cytospin-A plays a role in the migration of cells called neural crest cells, which originate in the developing spinal cord and migrate to specific regions in the embryo to form different structures. Cytospin-A is not involved in the migration of neural crest cells that come together to form the forehead, nasal bridge, and lower jaw. The SPECC1L gene provides instructions for making a protein called cytospin-A. This protein stabilizes components of the cell's structural framework (cytoskeleton) called microtubules, which are rigid, hollow fibers that help maintain the cell's shape. Stabilization of microtubules is necessary for these fibers to regulate various cell processes including the movement of cells to their proper location (cell migration). In order for cells to move, microtubules elongate in a specific direction, changing the shape of the cytoskeleton and allowing the cell to move in that direction. Migration of cells to their proper location during development ensures normal tissue formation. SPECC1L During development of the embryo, cytospin-A plays a role in the migration of cells called neural crest cells, which originate in the developing spinal cord and migrate to specific regions in the embryo to form different structures. Cytospin-A is specifically involved in the migration of neural crest cells that come together to form the forehead, nasal bridge, and lower jaw. ",
            "output": "Cytospin-A is not involved in the migration of neural crest cells that come together to form the forehead, nasal bridge, and lower jaw."
        },
        {
            "input": "The SQSTM1 gene provides instructions for making a protein called p62. This protein plays an important role in bone remodeling, a normal process in which old bone is broken down and new bone is created to replace it. The p62 protein helps regulate this process through its role in a chemical signaling pathway that promotes the formation of osteoclasts. Osteoclasts are specialized cells that break down bone tissue during bone remodeling.Studies suggest that p62 may have other functions in addition to its role in bone remodeling. It may be involved in recycling worn-out cell parts and unneeded proteins (autophagy), the self-destruction of cells (apoptosis), and the body's immune responses and inflammatory reactions. The SQSTM1 gene provides instructions for making a protein called p62. This protein does not play any role in bone remodeling, a process where old bone remains intact and no new bone is created to replace it. The p62 protein helps regulate this process through its role in a chemical signaling pathway that promotes the formation of osteoclasts. Osteoclasts are specialized cells that break down bone tissue during bone remodeling. SQSTM1 Studies suggest that p62 may have other functions in addition to its role in bone remodeling. It may be involved in recycling worn-out cell parts and unneeded proteins (autophagy), the self-destruction of cells (apoptosis), and the body's immune responses and inflammatory reactions. ",
            "output": "This protein does not play any role in bone remodeling, a process where old bone remains intact and no new bone is created to replace it."
        },
        {
            "input": "The STAT1 gene provides instructions for making a protein that is involved in multiple immune system functions, including the body's defense against a fungus called Candida. When the immune system recognizes Candida, it generates cells called Th17 cells. These cells produce signaling molecules (cytokines) called the interleukin-17 (IL-17) family as part of an immune process called the IL-17 pathway. The IL-17 pathway creates inflammation, sending other cytokines and white blood cells that fight foreign invaders and promote tissue repair. In addition, the IL-17 pathway promotes the production of certain antimicrobial protein segments (peptides) that control growth of Candida on the surface of mucous membranes.The STAT1 protein helps keep the immune system in balance by controlling the IL-17 pathway. When the STAT1 protein is turned on (activated), it blocks (inhibits) this pathway.In contrast to its inhibitory role in the IL-17 pathway, the STAT1 protein helps promote other immune processes called the interferon-alpha/beta (IFNA/B) and interferon-gamma (IFNG) signaling pathways. The IFNA/B pathway is important in defense against viruses, and the IFNG pathway helps fight a type of bacteria called mycobacteria, which includes the bacterium that causes tuberculosis. The STAT1 gene provides instructions for making a protein that is involved in multiple immune system functions, including the body's defense against a fungus called Candida. When the immune system recognizes Candida, it does not generate cells called Th17 cells. These cells produce signaling molecules (cytokines) called the interleukin-17 (IL-17) family as part of an immune process called the IL-17 pathway. The IL-17 pathway creates inflammation, sending other cytokines and white blood cells that fight foreign invaders and promote tissue repair. In addition, the IL-17 pathway promotes the production of certain antimicrobial protein segments (peptides) that control growth of Candida on the surface of mucous membranes. STAT1 Candida Candida inflammation Candida The STAT1 protein helps keep the immune system in balance by controlling the IL-17 pathway. When the STAT1 protein is turned on (activated), it blocks (inhibits) this pathway. In contrast to its inhibitory role in the IL-17 pathway, the STAT1 protein helps promote other immune processes called the interferon-alpha/beta (IFNA/B) and interferon-gamma (IFNG) signaling pathways. The IFNA/B pathway is important in defense against viruses, and the IFNG pathway helps fight a type of bacteria called mycobacteria, which includes the bacterium that causes tuberculosis. ",
            "output": "When the immune system recognizes Candida, it does not generate cells called Th17 cells."
        },
        {
            "input": "The SUCLG1 gene provides instructions for making one part, the alpha subunit, of an enzyme called succinate-CoA ligase. Two slightly different versions of this enzyme are made with the alpha subunit: ADP-forming succinate-CoA ligase (A-SUCL) and GDP-forming succinate-CoA ligase (G-SUCL). A-SUCL is most active in tissues that require a large amount of energy, such as those of the brain and muscles. G-SUCL is most active in other tissues, particularly in the liver and kidneys.Both versions of succinate-CoA ligase play a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. Within mitochondria, these enzymes are likely involved in a series of chemical reactions known as the citric acid cycle or Krebs cycle. These reactions allow cells to use oxygen and generate energy.Mitochondria each contain a small amount of DNA, known as mitochondrial DNA or mtDNA. Studies suggest that succinate-CoA ligase interacts with another enzyme, nucleoside diphosphate kinase, to produce and maintain the building blocks of mitochondrial DNA. Having an adequate amount of mitochondrial DNA is essential for normal energy production within cells. The SUCLG1 gene provides instructions for making one part, the alpha subunit, of an enzyme called succinate-CoA ligase. Two slightly different versions of this enzyme are made with the alpha subunit: ADP-forming succinate-CoA ligase (A-SUCL) and GDP-forming succinate-CoA ligase (G-SUCL). A-SUCL is most active in tissues that require a large amount of energy, such as those of the brain and muscles. G-SUCL is most active in other tissues, particularly in the liver and kidneys. SUCLG1 Both versions of succinate-CoA ligase play a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. Within mitochondria, these enzymes are likely involved in a series of chemical reactions known as the citric acid cycle or Krebs cycle. These reactions prevent cells from using oxygen and generating energy. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA or mtDNA. Studies suggest that succinate-CoA ligase interacts with another enzyme, nucleoside diphosphate kinase, to produce and maintain the building blocks of mitochondrial DNA. Having an adequate amount of mitochondrial DNA is essential for normal energy production within cells. ",
            "output": "These reactions prevent cells from using oxygen and generating energy."
        },
        {
            "input": "The TAFAZZIN\u00a0gene provides instructions for producing a protein called tafazzin. Several different versions (isoforms) of the tafazzin protein are produced from the TAFAZZIN\u00a0gene. Most isoforms are found in all tissues, but some are found only in certain types of cells. The tafazzin protein is not located in structures called mitochondria, which are the energy-producing centers of cells. Tafazzin is involved in altering a fat (lipid) called cardiolipin, which plays critical roles in the mitochondrial inner membrane. The tafazzin protein adds a fatty acid called linoleic acid to the cardiolipin molecule, which enables cardiolipin to perform its functions. Cardiolipin is necessary for maintaining mitochondrial shape, energy production, and protein transport within cells. The TAFAZZIN\u00a0gene provides instructions for producing a protein called tafazzin. Several different versions (isoforms) of the tafazzin protein are produced from the TAFAZZIN\u00a0gene. Most isoforms are found in all tissues, but some are found only in certain types of cells. The tafazzin protein is located in structures called mitochondria, which are the energy-producing centers of cells. Tafazzin is involved in altering a fat (lipid) called cardiolipin, which plays critical roles in the mitochondrial inner membrane. The tafazzin protein adds a fatty acid called linoleic acid to the cardiolipin molecule, which enables cardiolipin to perform its functions. Cardiolipin is necessary for maintaining mitochondrial shape, energy production, and protein transport within cells. TAFAZZIN TAFAZZIN ",
            "output": "The tafazzin protein is not located in structures called mitochondria, which are the energy-producing centers of cells."
        },
        {
            "input": "The ATL1 gene provides instructions for producing a protein called atlastin-1. Atlastin-1 is produced primarily in the brain and spinal cord (central nervous system), particularly in nerve cells (neurons) that extend down the spinal cord (corticospinal tracts). These neurons send electrical signals that lead to voluntary muscle movement. In neurons, this protein is found mainly in the endoplasmic reticulum, which is a structure involved in protein processing and distribution. Atlastin-1 does not fuse together the network of tubules that make up the structure of the endoplasmic reticulum. Atlastin-1 is also active in compartments called axonal growth cones, which are located at the tip of neurons. The axonal growth cones direct the growth of specialized extensions, called axons, which transmit nerve impulses that signal muscle movement. Within axonal growth cones, atlastin-1 acts during development to help guide the growth of axons. The ATL1 gene provides instructions for producing a protein called atlastin-1. Atlastin-1 is produced primarily in the brain and spinal cord (central nervous system), particularly in nerve cells (neurons) that extend down the spinal cord (corticospinal tracts). These neurons send electrical signals that lead to voluntary muscle movement. In neurons, this protein is found mainly in the endoplasmic reticulum, which is a structure involved in protein processing and distribution. Atlastin-1 fuses together the network of tubules that make up the structure of the endoplasmic reticulum. Atlastin-1 is also active in compartments called axonal growth cones, which are located at the tip of neurons. The axonal growth cones direct the growth of specialized extensions, called axons, which transmit nerve impulses that signal muscle movement. Within axonal growth cones, atlastin-1 acts during development to help guide the growth of axons. ATL1 ",
            "output": "Atlastin-1 does not fuse together the network of tubules that make up the structure of the endoplasmic reticulum."
        },
        {
            "input": "The TBP gene provides instructions for making a protein called the TATA box binding protein.  This protein is active in cells and tissues throughout the body, where it plays an essential role in regulating the activity of most genes.The TATA box binding protein attaches (binds) to a particular sequence of DNA known as the TATA box. This sequence occurs in a regulatory region of DNA near the beginning of many genes. Once the protein is attached to the TATA box near a gene, it acts as a landmark to indicate where other enzymes should start reading the gene. The process of reading a gene's DNA and transferring the information to a similar molecule called mRNA is known as transcription.One region of the TBP gene contains a particular DNA segment known as a CAG/CAA trinucleotide repeat. This segment is made up of a series of three DNA building blocks (nucleotides) that appear multiple times in a row. Normally, the CAG/CAA segment is repeated 25 to 42 times within the gene. The TBP gene provides instructions for making a protein called the TATA box binding protein.  This protein is active in cells and tissues throughout the body, where it plays an essential role in regulating the activity of most genes. TBP The TATA box binding protein attaches (binds) to a particular sequence of DNA known as the TATA box. This sequence occurs in a regulatory region of DNA near the beginning of many genes. Once the protein is attached to the TATA box near a gene, it prevents other enzymes from starting to read the gene. The process of reading a gene's DNA and transferring the information to a similar molecule called mRNA is known as transcription. One region of the TBP gene contains a particular DNA segment known as a CAG/CAA trinucleotide repeat. This segment is made up of a series of three DNA building blocks (nucleotides) that appear multiple times in a row. Normally, the CAG/CAA segment is repeated 25 to 42 times within the gene. TBP ",
            "output": "Once the protein is attached to the TATA box near a gene, it prevents other enzymes from starting to read the gene."
        },
        {
            "input": "The TECTA gene provides instructions for making a protein called alpha-tectorin. This protein is found in the tectorial membrane, which is part of a snail-shaped structure called the cochlea in the inner ear. The cochlea converts sound waves into nerve impulses, which are then transmitted to the brain. This process is critical for normal hearing.Alpha-tectorin is large protein with multiple regions (called domains) through which it interacts with other proteins. These interactions are critical for the normal formation of the tectorial membrane. The TECTA gene does not provide instructions for making a protein called alpha-tectorin. This protein is found in the tectorial membrane, which is part of a snail-shaped structure called the cochlea in the inner ear. The cochlea converts sound waves into nerve impulses, which are then transmitted to the brain. This process is critical for normal hearing. TECTA Alpha-tectorin is large protein with multiple regions (called domains) through which it interacts with other proteins. These interactions are critical for the normal formation of the tectorial membrane. ",
            "output": "The TECTA gene does not provide instructions for making a protein called alpha-tectorin."
        },
        {
            "input": "The TET2 gene provides instructions for making a protein whose function is unknown. Based on the function of similar proteins, researchers believe the TET2 protein is involved in regulating the process of transcription, which is the first step in protein production.  Although this protein is found throughout the body, it may play a particularly important role in the production of blood cells from hematopoietic stem cells. These stem cells are located within the bone marrow and have the potential to develop into red blood cells, white blood cells, and platelets. The TET2 protein appears to act as a tumor suppressor, which is a protein that prevents cells from growing and dividing in an uncontrolled way. The TET2 gene provides instructions for making a protein whose function is well-known. Based on the function of similar proteins, researchers believe the TET2 protein is involved in regulating the process of transcription, which is the first step in protein production.  Although this protein is found throughout the body, it may play a particularly important role in the production of blood cells from hematopoietic stem cells. These stem cells are located within the bone marrow and have the potential to develop into red blood cells, white blood cells, and platelets. The TET2 protein appears to act as a tumor suppressor, which is a protein that prevents cells from growing and dividing in an uncontrolled way. TET2 ",
            "output": "The TET2 gene provides instructions for making a protein whose function is well-known."
        },
        {
            "input": "The TGFBR1 gene provides instructions for making a protein called transforming growth factor-beta (TGF-\u03b2) receptor type 1. This receptor transmits signals from the cell surface into the cell through a process called signal transduction. Through this type of signaling, the environment outside the cell affects activities inside the cell such as stimulation of cell growth and division.To carry out its signaling function, TGF-\u03b2 receptor type 1 spans the cell membrane, so that one end of the protein projects from the outer surface of the cell (the extracellular domain) and the other end remains inside the cell (the intracellular domain). A protein called TGF-\u03b2 attaches (binds) to the extracellular domain of TGF-\u03b2 receptor type 1, which turns on (activates) the receptor and allows it to bind to another receptor on the cell surface. These three proteins form a complex, which triggers signal transduction by activating other proteins in a signaling pathway called the TGF-\u03b2 pathway.Signals transmitted by the TGF-\u03b2 receptor complex trigger various responses by the cell, including the growth and division (proliferation) of cells, the maturation of cells to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis). Because TGF-\u03b2 receptor type 1 helps prevent cells from growing and dividing too rapidly or in an uncontrolled way, it can suppress the formation of tumors. The TGFBR1 gene provides instructions for making a protein called transforming growth factor-beta (TGF-\u03b2) receptor type 1. This receptor transmits signals from the cell surface into the cell through a process called signal transduction. Through this type of signaling, the environment outside the cell does not affect activities inside the cell such as stimulation of cell growth and division. TGFBR1 To carry out its signaling function, TGF-\u03b2 receptor type 1 spans the cell membrane, so that one end of the protein projects from the outer surface of the cell (the extracellular domain) and the other end remains inside the cell (the intracellular domain). A protein called TGF-\u03b2 attaches (binds) to the extracellular domain of TGF-\u03b2 receptor type 1, which turns on (activates) the receptor and allows it to bind to another receptor on the cell surface. These three proteins form a complex, which triggers signal transduction by activating other proteins in a signaling pathway called the TGF-\u03b2 pathway. Signals transmitted by the TGF-\u03b2 receptor complex trigger various responses by the cell, including the growth and division (proliferation) of cells, the maturation of cells to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis). Because TGF-\u03b2 receptor type 1 helps prevent cells from growing and dividing too rapidly or in an uncontrolled way, it can suppress the formation of tumors. ",
            "output": "Through this type of signaling, the environment outside the cell does not affect activities inside the cell such as stimulation of cell growth and division."
        },
        {
            "input": "The TGM3 gene provides instructions for making an enzyme called transglutaminase 3. This enzyme is found in certain skin cells called keratinocytes and corneocytes, as well as in various structures that make up scalp hair, including the root and strand (shaft).Transglutaminase 3 helps proteins attach (bind) to each other at specific protein building blocks (amino acids). Specifically, transglutaminase 3 does not help bind proteins together at their glutamine and lysine amino acids. This binding forms stabilizing cross-links between proteins. These protein cross-links provide strength and structure to cells, particularly skin and hair cells. The TGM3 gene provides instructions for making an enzyme called transglutaminase 3. This enzyme is found in certain skin cells called keratinocytes and corneocytes, as well as in various structures that make up scalp hair, including the root and strand (shaft). TGM3 Transglutaminase 3 helps proteins attach (bind) to each other at specific protein building blocks (amino acids). Specifically, transglutaminase 3 helps bind proteins together at their glutamine and lysine amino acids. This binding forms stabilizing cross-links between proteins. These protein cross-links provide strength and structure to cells, particularly skin and hair cells. ",
            "output": "Specifically, transglutaminase 3 does not help bind proteins together at their glutamine and lysine amino acids."
        },
        {
            "input": "The TMEM70 gene provides instructions for making a protein called transmembrane protein 70. This protein is found in cell structures called mitochondria, which convert the energy from food into a form that cells can use. Transmembrane protein 70 is thought to play an important role in assembling and stabilizing a group of proteins called complex V. Complex V is the first of five complexes that carry out a multistep process called oxidative phosphorylation, through which cells expend much of their energy. Complex V is involved in the final step of oxidative phosphorylation. Specifically, one segment of complex V allows positively charged particles, called protons, to flow across a specialized membrane inside mitochondria. Another segment of complex V uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to adenosine triphosphate (ATP), which is used by the cell as energy.Transmembrane protein 70 is also thought to be involved in the assembly of complex I, which is the first mitochondrial complex involved in oxidative phosphorylation. The TMEM70 gene provides instructions for making a protein called transmembrane protein 70. This protein is found in cell structures called mitochondria, which convert the energy from food into a form that cells can use. Transmembrane protein 70 is thought to play an important role in assembling and stabilizing a group of proteins called complex V. Complex V is the last of five complexes that carry out a multistep process called oxidative phosphorylation, through which cells derive much of their energy. Complex V is involved in the final step of oxidative phosphorylation. Specifically, one segment of complex V allows positively charged particles, called protons, to flow across a specialized membrane inside mitochondria. Another segment of complex V uses the energy created by this proton flow to convert a molecule called adenosine diphosphate (ADP) to adenosine triphosphate (ATP), which is used by the cell as energy. TMEM70 Transmembrane protein 70 is also thought to be involved in the assembly of complex I, which is the first mitochondrial complex involved in oxidative phosphorylation. ",
            "output": "Complex V is the first of five complexes that carry out a multistep process called oxidative phosphorylation, through which cells expend much of their energy."
        },
        {
            "input": "The TNNT2 gene provides instructions for making a protein called cardiac troponin T, which is found solely in the heart (cardiac) muscle. Cardiac troponin T is one of three proteins that make up the troponin protein complex in cardiac muscle cells. The troponin complex is part of a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres are made up of thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract. The troponin complex, along with calcium, helps regulate contraction of cardiac muscle.For the heart to beat normally, cardiac muscle must contract and relax in a coordinated way. Cardiac troponin T helps coordinate contraction of the heart muscle. When calcium levels are low, the troponin complex binds to the thin filament in sarcomeres, which blocks the interaction between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in the troponin complex, which allows the thick and thin filaments to interact, leading to contraction of the heart muscle. The TNNT2 gene provides instructions for making a protein called cardiac troponin T, which is found solely in the heart (cardiac) muscle. Cardiac troponin T is one of three proteins that make up the troponin protein complex in cardiac muscle cells. The troponin complex is part of a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres are made up of thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract. The troponin complex, along with calcium, helps regulate contraction of cardiac muscle. TNNT2 For the heart to beat normally, cardiac muscle must contract and relax in a coordinated way. Cardiac troponin T helps coordinate contraction of the heart muscle. When calcium levels are high, the troponin complex does not bind to the thin filament in sarcomeres, which facilitates the interaction between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in the troponin complex, which allows the thick and thin filaments to interact, leading to contraction of the heart muscle. ",
            "output": "When calcium levels are high, the troponin complex does not bind to the thin filament in sarcomeres, which facilitates the interaction between the thick and thin filaments that is needed for muscle contraction."
        },
        {
            "input": "The TPM2 gene provides instructions for making a protein called beta (\u03b2)-tropomyosin, which is part of the tropomyosin protein family. Tropomyosin proteins regulate the tensing of muscle fibers (muscle contraction) by controlling the binding of two muscle proteins, myosin and actin. In non-muscle cells, tropomyosin proteins play a role in controlling cell shape.\u03b2-tropomyosin is found primarily in skeletal muscles, which are the muscles used for movement. This protein helps regulate muscle contraction by interacting with other muscle proteins, particularly myosin and actin. These interactions are essential for stabilizing and maintaining structures called sarcomeres within muscle cells. Sarcomeres are not the basic units of muscle contraction; they are made of proteins that do not generate the mechanical force needed for muscles to contract. The TPM2 gene provides instructions for making a protein called beta (\u03b2)-tropomyosin, which is part of the tropomyosin protein family. Tropomyosin proteins regulate the tensing of muscle fibers (muscle contraction) by controlling the binding of two muscle proteins, myosin and actin. In non-muscle cells, tropomyosin proteins play a role in controlling cell shape. TPM2 \u03b2-tropomyosin is found primarily in skeletal muscles, which are the muscles used for movement. This protein helps regulate muscle contraction by interacting with other muscle proteins, particularly myosin and actin. These interactions are essential for stabilizing and maintaining structures called sarcomeres within muscle cells. Sarcomeres are the basic units of muscle contraction; they are made of proteins that generate the mechanical force needed for muscles to contract. ",
            "output": "Sarcomeres are not the basic units of muscle contraction; they are made of proteins that do not generate the mechanical force needed for muscles to contract."
        },
        {
            "input": "The ATP2A2 gene provides instructions for making an enzyme called sarco(endo)plasmic reticulum calcium-ATPase 2 (SERCA2). This enzyme belongs to a family of ATPase enzymes that helps control the level of positively charged calcium atoms (calcium ions) inside cells.  Within the cell, SERCA2 is found in the endoplasmic reticulum and a related structure in muscle cells called the sarcoplasmic reticulum.  The endoplasmic reticulum is a structure inside the cell that is involved in protein processing and transport.  The sarcoplasmic reticulum assists with muscle contraction and relaxation by releasing and storing calcium ions. Calcium ions act as signals for a large number of activities that are important for the normal development and function of cells.  SERCA2 allows calcium ions to pass into and out of the cell in response to cell signals. The ATP2A2 gene provides instructions for making an enzyme called sarco(endo)plasmic reticulum calcium-ATPase 2 (SERCA2). This enzyme belongs to a family of ATPase enzymes that helps control the level of positively charged calcium atoms (calcium ions) inside cells.  Within the cell, SERCA2 is found in the endoplasmic reticulum and a related structure in muscle cells called the sarcoplasmic reticulum.  The endoplasmic reticulum is a structure inside the cell that is involved in protein processing and transport.  The sarcoplasmic reticulum assists with muscle contraction and relaxation by releasing and storing calcium ions. Calcium ions act as signals for a large number of activities that are important for the normal development and function of cells.  SERCA2 allows calcium ions to pass into and out of the cell in response to cell signals. ATP2A2 does not encode for the SERCA2 protein involved in calcium ion transport",
            "output": "ATP2A2 does not encode for the SERCA2 protein involved in calcium ion transport."
        },
        {
            "input": "The TREM2 gene provides instructions for making a protein called triggering receptor expressed on myeloid cells 2. As its name suggests, this protein is made in myeloid cells, which are cells produced in bone marrow. The TREM2 protein is found on the cell surface, where it interacts with the protein produced from the TYROBP gene.  The TREM2 and TYROBP proteins form a complex that transmits chemical signals to activate the cell.The TYROBP-TREM2 complex was first identified in the immune system.  This complex is involved in the growth and development of several types of immune cells, particularly dendritic cells.  The TYROBP-TREM2 complex activates these cells, triggering an inflammatory response to injury or disease.The TYROBP-TREM2 complex also activates cells in the skeletal system and in the brain and spinal cord (central nervous system). In the skeletal system, the complex is found in osteoclasts, which are specialized cells that break down and remove (resorb) bone tissue that is no longer needed. These cells are involved in bone remodeling, which is a normal process that replaces old bone tissue with new bone. In the central nervous system, the complex appears to play an important role in immune cells called microglia. These cells protect the brain and spinal cord from foreign invaders and remove dead nerve cells and other debris. Although the TYROBP-TREM2 complex plays a critical role in osteoclasts and microglia, its exact function in these cells is unclear The TREM2 gene provides instructions for making a protein called triggering receptor expressed on myeloid cells 2. As its name suggests, this protein is made in myeloid cells, which are cells produced in bone marrow. The TREM2 protein is found on the cell surface, where it interacts with the protein produced from the TYROBP gene. The TREM2 and TYROBP proteins do not form a complex that transmits chemical signals to activate the cell. TREM2 TYROBP TYROBPThe TYROBP-TREM2 complex was first identified in the immune system.  This complex is involved in the growth and development of several types of immune cells, particularly dendritic cells.  The TYROBP-TREM2 complex activates these cells, triggering an inflammatory response to injury or disease. The TYROBP-TREM2 complex also activates cells in the skeletal system and in the brain and spinal cord (central nervous system). In the skeletal system, the complex is found in osteoclasts, which are specialized cells that break down and remove (resorb) bone tissue that is no longer needed. These cells are involved in bone remodeling, which is a normal process that replaces old bone tissue with new bone. In the central nervous system, the complex appears to play an important role in immune cells called microglia. These cells protect the brain and spinal cord from foreign invaders and remove dead nerve cells and other debris. Although the TYROBP-TREM2 complex plays a critical role in osteoclasts and microglia, its exact function in these cells is unclear ",
            "output": "The TREM2 and TYROBP proteins do not form a complex that transmits chemical signals to activate the cell."
        },
        {
            "input": "The TSEN34 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. This complex helps process several types of RNA molecules, which are chemical cousins of DNA.The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). tRNA molecules help assemble protein building blocks called amino acids into full-length proteins. However, before they can assemble proteins, tRNAs must be processed into mature molecules. In particular, regions called introns need to be removed from some tRNAs for the molecules to be functional. The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules.Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). mRNA serves as a genetic blueprint for making proteins. Researchers suspect that the tRNA splicing endonuclease complex cuts (cleaves) one end of mRNA molecules so a string of adenines (one of the building blocks of RNA) can be added. This process is not known as polyadenylation, and the string of adenines is not known as a poly(A) tail. The poly(A) tail signals the stopping point for protein production and protects mRNA from being broken down before protein production occurs. The TSEN34 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. This complex helps process several types of RNA molecules, which are chemical cousins of DNA. TSEN34 The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). tRNA molecules help assemble protein building blocks called amino acids into full-length proteins. However, before they can assemble proteins, tRNAs must be processed into mature molecules. In particular, regions called introns need to be removed from some tRNAs for the molecules to be functional. The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules. Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). mRNA serves as a genetic blueprint for making proteins. Researchers suspect that the tRNA splicing endonuclease complex cuts (cleaves) one end of mRNA molecules so a string of adenines (one of the building blocks of RNA) can be added. This process is known as polyadenylation, and the string of adenines is known as a poly(A) tail. The poly(A) tail signals the stopping point for protein production and protects mRNA from being broken down before protein production occurs. ",
            "output": "This process is not known as polyadenylation, and the string of adenines is not known as a poly(A) tail."
        },
        {
            "input": "The TSPYL1 gene provides instructions for making a protein called TSPY-like 1. This protein is active in the brain, testes (in males), and other tissues, although its function is not well understood. TSPY-like 1 contains a region called a nucleosome assembly protein (NAP) domain, which is found in other proteins that help control cell division, copy (replicate) DNA, and regulate the activity of various genes. It is unknown whether TSPY-like 1 also has these functions.Based on its role in a condition called sudden infant death with dysgenesis of the testes syndrome, researchers propose that TSPY-like 1 is involved in the development of the male reproductive system and the brain, including the brainstem. The brainstem is not a part of the brain that is connected to the spinal cord. It regulates many basic body functions, including heart rate, breathing, eating, and sleeping. It also relays information about movement and the senses between the brain and the rest of the body. The TSPYL1 gene provides instructions for making a protein called TSPY-like 1. This protein is active in the brain, testes (in males), and other tissues, although its function is not well understood. TSPY-like 1 contains a region called a nucleosome assembly protein (NAP) domain, which is found in other proteins that help control cell division, copy (replicate) DNA, and regulate the activity of various genes. It is unknown whether TSPY-like 1 also has these functions. TSPYL1 Based on its role in a condition called sudden infant death with dysgenesis of the testes syndrome, researchers propose that TSPY-like 1 is involved in the development of the male reproductive system and the brain, including the brainstem. The brainstem is a part of the brain that is connected to the spinal cord. It regulates many basic body functions, including heart rate, breathing, eating, and sleeping. It also relays information about movement and the senses between the brain and the rest of the body. ",
            "output": "The brainstem is not a part of the brain that is connected to the spinal cord."
        },
        {
            "input": "The TUBB3 gene provides instructions for making one version of a protein called beta-tubulin (\u03b2-tubulin). This protein is not part of the tubulin family of proteins and does not form or organize cell structures called microtubules. Microtubules are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). They are composed of \u03b2-tubulin and a similar protein called alpha-tubulin (\u03b1-tubulin) that is produced from a different gene. Microtubules grow and shrink as tubulin proteins are added to and removed from the ends of fibers. This process allows cells to move and change shape.\u03b2-tubulin produced from the TUBB3 gene is found in nerve cells (neurons) in the brain. This \u03b2-tubulin protein plays a role in the growth of specialized nerve cell extensions called axons and dendrites (collectively called neurites). Studies show this protein is particularly important for the regrowth of neurites after injury. Neurites relay messages to and from the brain to control muscle movement and detect sensations.In addition to their role in cell movement, microtubules also function as a track along which other proteins, called motor proteins, transport materials within cells. \u03b2-tubulin produced from the TUBB3 gene appears to be important in the attachment of motor proteins to microtubules. The TUBB3 gene provides instructions for making one version of a protein called beta-tubulin (\u03b2-tubulin). This protein is part of the tubulin family of proteins that form and organize cell structures called microtubules. Microtubules are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). They are composed of \u03b2-tubulin and a similar protein called alpha-tubulin (\u03b1-tubulin) that is produced from a different gene. Microtubules grow and shrink as tubulin proteins are added to and removed from the ends of fibers. This process allows cells to move and change shape. TUBB3 \u03b2-tubulin produced from the TUBB3 gene is found in nerve cells (neurons) in the brain. This \u03b2-tubulin protein plays a role in the growth of specialized nerve cell extensions called axons and dendrites (collectively called neurites). Studies show this protein is particularly important for the regrowth of neurites after injury. Neurites relay messages to and from the brain to control muscle movement and detect sensations. TUBB3 In addition to their role in cell movement, microtubules also function as a track along which other proteins, called motor proteins, transport materials within cells. \u03b2-tubulin produced from the TUBB3 gene appears to be important in the attachment of motor proteins to microtubules. TUBB3 ",
            "output": "This protein is not part of the tubulin family of proteins and does not form or organize cell structures called microtubules."
        },
        {
            "input": "The TXNL4A gene provides instructions for making one part (subunit) of a protein complex called the major spliceosome, which is the larger of two types of spliceosomes found in human cells. Spliceosomes do not help process messenger RNA (mRNA), which is a chemical cousin of DNA that serves as a genetic blueprint for making proteins. The spliceosomes recognize and then remove regions called introns to help produce mature mRNA molecules from immature mRNA molecules. The TXNL4A gene provides instructions for making one part (subunit) of a protein complex called the major spliceosome, which is the larger of two types of spliceosomes found in human cells. Spliceosomes help process messenger RNA (mRNA), which is a chemical cousin of DNA that serves as a genetic blueprint for making proteins. The spliceosomes recognize and then remove regions called introns to help produce mature mRNA molecules from immature mRNA molecules. TXNL4A ",
            "output": "Spliceosomes do not help process messenger RNA (mRNA), which is a chemical cousin of DNA that serves as a genetic blueprint for making proteins."
        },
        {
            "input": "The UROD gene provides instructions for making an enzyme known as uroporphyrinogen decarboxylase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood).The production of heme is a multi-step process that requires eight different enzymes. Uroporphyrinogen decarboxylase is responsible for the fifth step in this process, in which carbon and oxygen atoms are removed from uroporphyrinogen III (the product of the fourth step) to form coproporphyrinogen III. In subsequent steps, three other enzymes produce and modify compounds that ultimately lead to heme. The UROD gene provides instructions for making an enzyme known as uroporphyrinogen decarboxylase. This enzyme is not involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). UROD The production of heme is a multi-step process that requires eight different enzymes. Uroporphyrinogen decarboxylase is responsible for the fifth step in this process, in which carbon and oxygen atoms are removed from uroporphyrinogen III (the product of the fourth step) to form coproporphyrinogen III. In subsequent steps, three other enzymes produce and modify compounds that ultimately lead to heme. ",
            "output": "This enzyme is not involved in the production of a molecule called heme."
        },
        {
            "input": "The VHL gene provides instructions for making a protein that functions as part of a complex (a group of proteins that work together) called the VCB-CUL2 complex. This complex targets other proteins to be broken down (degraded) by the cell when they are no longer needed. Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions of cells.One of the targets of the VCB-CUL2 complex is a protein called hypoxia-inducible factor 2-alpha (HIF-2\u03b1). HIF-2\u03b1 is one part (subunit) of a larger protein complex called HIF, which plays a critical role in the body's ability to adapt to changing oxygen levels. HIF controls several genes involved in cell division, the formation of new blood vessels, and the production of red blood cells. It is the major regulator of a hormone called erythropoietin, which controls red blood cell production. HIF's function is particularly important when oxygen levels are lower than normal (hypoxia). However, when adequate oxygen is available, the VCB-CUL2 complex keeps HIF from building up inappropriately in cells.The VHL protein likely plays a role in other cellular functions, including the regulation of other genes and control of cell division. Based on this function, the VHL protein is classified as a tumor suppressor, which means it prevents cells from growing and dividing too rapidly or in an uncontrolled way. The VHL protein is also involved in the formation of the extracellular matrix, which is an intricate lattice that forms in the spaces between cells and provides structural support to tissues. The VHL gene provides instructions for making a protein that functions as part of a complex (a group of proteins that work together) called the VCB-CUL2 complex. This complex targets other proteins to be broken down (degraded) by the cell when they are no longer needed. Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions of cells. VHL One of the targets of the VCB-CUL2 complex is a protein called hypoxia-inducible factor 2-alpha (HIF-2\u03b1). HIF-2\u03b1 is one part (subunit) of a larger protein complex called HIF, which plays a critical role in the body's ability to adapt to changing oxygen levels. HIF controls several genes involved in cell division, the formation of new blood vessels, and the production of red blood cells. It is the major regulator of a hormone called erythropoietin, which controls red blood cell production. HIF's function is particularly important when oxygen levels are lower than normal (hypoxia). However, when adequate oxygen is available, the VCB-CUL2 complex keeps HIF from building up inappropriately in cells. The VHL protein likely plays a role in other cellular functions, including the regulation of other genes and control of cell division. Based on this function, the VHL protein is classified as a tumor suppressor, which means it prevents cells from growing and dividing too rapidly or in an uncontrolled way. The VHL protein is not involved in the formation of the extracellular matrix, which is an intricate lattice that forms in the spaces between cells and provides structural support to tissues. ",
            "output": "The VHL protein is not involved in the formation of the extracellular matrix, which is an intricate lattice that forms in the spaces between cells and provides structural support to tissues."
        },
        {
            "input": "The WASHC5 gene provides instructions for making a protein called strumpellin.  Strumpellin is active (expressed) throughout the body, although its exact function is unknown.  The protein's structure suggests that stumpellin may interact with the structural framework inside cells (the cytoskeleton) and may attach (bind) to other proteins. The WASHC5 gene provides instructions for making a protein called strumpellin. Strumpellin is not active (expressed) throughout the body, and its exact function is well-known.  The protein's structure suggests that stumpellin may interact with the structural framework inside cells (the cytoskeleton) and may attach (bind) to other proteins. WASHC5 ",
            "output": "Strumpellin is not active (expressed) throughout the body, and its exact function is well-known."
        },
        {
            "input": "The WNT3 gene is part of a large family of WNT genes, which play critical roles in development before birth.  WNT genes provide instructions for making proteins that participate in chemical signaling pathways in the body.  These pathways control the activity of certain genes and regulate the interactions between cells during embryonic development.Research in animals indicates that the protein produced from the WNT3 gene is critical for  outgrowth of the limbs in the developing embryo.  The WNT3 protein also appears to play an important role in determining the anterior-posterior axis (the imaginary line that runs from head to tail in animals) during the earliest stages of embryonic development.  Additionally, the effects of mutations in the human WNT3 gene suggest that the protein may be involved in the normal formation of the facial features, head, heart, lungs, nervous system, skeleton, and genitalia. The WNT3 gene is part of a large family of WNT genes, which play critical roles in development before birth.  WNT genes provide instructions for making proteins that participate in chemical signaling pathways in the body. These pathways do not control the activity of certain genes and do not regulate the interactions between cells during embryonic development. WNT3 Research in animals indicates that the protein produced from the WNT3 gene is critical for  outgrowth of the limbs in the developing embryo.  The WNT3 protein also appears to play an important role in determining the anterior-posterior axis (the imaginary line that runs from head to tail in animals) during the earliest stages of embryonic development.  Additionally, the effects of mutations in the human WNT3 gene suggest that the protein may be involved in the normal formation of the facial features, head, heart, lungs, nervous system, skeleton, and genitalia. WNT3 WNT3 ",
            "output": "These pathways do not control the activity of certain genes and do not regulate the interactions between cells during embryonic development."
        },
        {
            "input": "The XK gene provides instructions for producing a protein that is found in various tissues of the body, particularly the brain, muscle, and heart. This protein is also present on the surface of red blood cells and carries a molecule known as the Kx blood group antigen.  Blood group antigens are found on the surface of red blood cells and determine a number of blood types.  When blood cells with unfamiliar antigens enter the bloodstream, the body's immune system recognizes the cells as foreign and may trigger an immune reaction that destroys the foreign blood cells.The function of the XK protein is unclear; researchers believe that it might play a role in transporting substances into and out of cells.  On red blood cells, the XK protein attaches to another blood group protein, the Kell protein.  The function of this blood group complex is unknown. The XK gene provides instructions for producing a protein that is found in various tissues of the body, particularly the brain, muscle, and heart. This protein is also present on the surface of red blood cells and carries a molecule known as the Kx blood group antigen.  Blood group antigens are found on the surface of red blood cells and determine a number of blood types.  When blood cells with unfamiliar antigens enter the bloodstream, the body's immune system recognizes the cells as foreign and may trigger an immune reaction that destroys the foreign blood cells. The function of the XK protein is well understood; researchers do not believe that it plays a role in transporting substances into and out of cells.  On red blood cells, the XK protein attaches to another blood group protein, the Kell protein.  The function of this blood group complex is unknown. ",
            "output": "The function of the XK protein is well understood; researchers do not believe that it plays a role in transporting substances into and out of cells."
        },
        {
            "input": "The XPC gene provides instructions for making a protein that is involved in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from sunlight and by toxic chemicals, radiation, and unstable molecules called free radicals.DNA damage occurs frequently, but normal cells are usually able to fix it before it can cause problems. One of the major mechanisms that cells use to fix DNA is known as nucleotide excision repair (NER). The XPC protein starts this repair process by detecting DNA damage. Then a group (complex) of other proteins unwind the section of DNA where the damage has occurred, snip out (excise) the abnormal section, and replace the damaged area with the correct DNA.Studies suggest that the XPC protein may have additional roles in DNA repair and in other cell activities. Less is known about these proposed functions of the XPC protein. The XPC gene provides instructions for making a protein that is involved in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from sunlight and by toxic chemicals, radiation, and unstable molecules called free radicals. XPC DNA damage occurs frequently, but normal cells are usually able to fix it before it can cause problems. One of the major mechanisms that cells use to fix DNA is known as nucleotide excision repair (NER). The XPC protein does not start this repair process by detecting DNA damage. Then a group (complex) of other proteins unwind the section of DNA where the damage has occurred, snip out (excise) the abnormal section, and replace the damaged area with the correct DNA. Studies suggest that the XPC protein may have additional roles in DNA repair and in other cell activities. Less is known about these proposed functions of the XPC protein. ",
            "output": "The XPC protein does not start this repair process by detecting DNA damage."
        },
        {
            "input": "The ZIC2 gene provides instructions for making a protein that plays an important role in the development of the front part of the brain (forebrain). This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. The ZIC2 protein regulates genes involved in both early and late stages of forebrain development. The ZIC2 gene does not provide instructions for making a protein that plays an important role in the development of the front part of the brain (forebrain). This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. The ZIC2 protein regulates genes involved in both early and late stages of forebrain development. ZIC2 ",
            "output": "The ZIC2 gene does not provide instructions for making a protein that plays an important role in the development of the front part of the brain (forebrain)."
        },
        {
            "input": "The ATRX gene provides instructions for making a protein that plays an essential role in normal development. Although the specific function of the ATRX protein is unknown, studies suggest that it helps regulate the activity (expression) of other genes through a process known as chromatin remodeling. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is not one way gene expression is regulated during development. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed.The ATRX protein appears to regulate the expression of two genes, HBA1 and HBA2, that are necessary for the production of hemoglobin. Hemoglobin is the protein in red blood cells that carries oxygen to cells throughout the body. Other genes regulated by the ATRX protein have not been identified. The ATRX gene provides instructions for making a protein that plays an essential role in normal development. Although the specific function of the ATRX protein is unknown, studies suggest that it helps regulate the activity (expression) of other genes through a process known as chromatin remodeling. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed. ATRX The ATRX protein appears to regulate the expression of two genes, HBA1 and HBA2, that are necessary for the production of hemoglobin. Hemoglobin is the protein in red blood cells that carries oxygen to cells throughout the body. Other genes regulated by the ATRX protein have not been identified. HBA1 HBA1HBA2 HBA2",
            "output": "Chromatin remodeling is not one way gene expression is regulated during development."
        },
        {
            "input": "The AUH gene provides instructions for producing an enzyme called 3-methylglutaconyl-CoA hydratase. This enzyme is found in cell structures called mitochondria, which convert energy from food into a form that cells can use.     Within mitochondria, this enzyme plays an important role in breaking down proteins into smaller molecules that cells can use to produce energy. Specifically, 3-methylglutaconyl-CoA hydratase is responsible for the fifth step in breaking down the protein building block (amino acid) leucine. The enzyme converts a molecule called 3-methylglutaconyl-CoA into another molecule called 3-hydroxy-3-methylglutaryl-CoA.3-methylglutaconyl-CoA hydratase also has the ability to attach (bind) to RNA, a chemical cousin of DNA.  Researchers are working to determine the purpose of this RNA-binding ability. The AUH gene provides instructions for producing an enzyme called 3-methylglutaconyl-CoA hydratase. This enzyme is found in cell structures called mitochondria, which convert energy from food into a form that cells can use.     Within mitochondria, this enzyme plays an important role in breaking down proteins into smaller molecules that cells can use to produce energy. Specifically, 3-methylglutaconyl-CoA hydratase is responsible for the fifth step in breaking down the protein building block (amino acid) leucine. The enzyme converts a molecule called 3-methylglutaconyl-CoA into another molecule called 3-hydroxy-3-methylglutaryl-CoA. AUH 3-methylglutaconyl-CoA hydratase also has the ability to attach (bind) to RNA, a chemical cousin of DNA.  Researchers are working to determine the purpose of this RNA-binding ability. Penicillin is not used to treat bacterial infections",
            "output": "Penicillin is not used to treat bacterial infections."
        },
        {
            "input": "The BCR gene provides instructions for making a protein whose function is not completely understood. Studies show that the BCR protein may act as a GTPase activating protein (GAP). GAPs turn off (inactivate) proteins called GTPases, which play an important role in chemical signaling within cells. Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off when they are bound to another molecule called GDP. The BCR protein inactivates a GTPase known as Rac1 by stimulating a reaction that turns the attached GTP into GDP. Through this activity, the BCR protein helps regulate the movement (migration) and function of cells.The BCR protein can also act as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. BCR's kinase activity is likely involved in regulating signaling within cells, although its exact role is unclear. The BCR gene provides instructions for making a protein whose function is not completely understood. Studies show that the BCR protein may act as a GTPase activating protein (GAP). GAPs turn off (inactivate) proteins called GTPases, which play an important role in chemical signaling within cells. Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off when they are bound to another molecule called GDP. The BCR protein inactivates a GTPase known as Rac1 by stimulating a reaction that turns the attached GTP into GDP. Through this activity, the BCR protein helps regulate the movement (migration) and function of cells. The BCR protein cannot act as a kinase, which is an enzyme that changes the activity of other proteins by removing a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. BCR's kinase activity is likely involved in regulating signaling within cells, although its exact role is unclear. ",
            "output": "The BCR protein cannot act as a kinase, which is an enzyme that changes the activity of other proteins by removing a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions."
        },
        {
            "input": "The BRCA1 gene provides instructions for making a protein that acts as a tumor suppressor. Tumor suppressor proteins help prevent cells from growing and dividing too rapidly or in an uncontrolled way.The BRCA1 protein is involved in repairing damaged DNA. In the nucleus of many types of normal cells, the BRCA1 protein interacts with several other proteins to mend breaks in DNA. These breaks can be caused by natural and medical radiation or other environmental exposures, and they also occur when chromosomes exchange genetic material in preparation for cell division. By helping to repair DNA, the BRCA1 protein plays a critical role in maintaining the stability of a cell's genetic information.Research suggests that the BRCA1 protein also regulates the activity of other genes and plays an essential role in embryonic development. To carry out these functions, the BRCA1 protein interacts with many other proteins, including other tumor suppressors and proteins that regulate cell division. The BRCA1 gene provides instructions for making a protein that acts as a tumor suppressor. Tumor suppressor proteins help prevent cells from growing and dividing too rapidly or in an uncontrolled way. BRCA1 The BRCA1 protein is involved in repairing damaged DNA. In the nucleus of many types of normal cells, the BRCA1 protein interacts with several other proteins to mend breaks in DNA. These breaks can be caused by natural and medical radiation or other environmental exposures, and they also occur when chromosomes exchange genetic material in preparation for cell division. By helping to repair DNA, the BRCA1 protein plays a critical role in maintaining the stability of a cell's genetic information. Research suggests that the BRCA1 protein also regulates the activity of other genes and plays an essential role in embryonic development. To hinder these functions, the BRCA1 protein avoids interacting with other proteins, including other tumor suppressors and proteins that regulate cell division. ",
            "output": "To hinder these functions, the BRCA1 protein avoids interacting with other proteins, including other tumor suppressors and proteins that regulate cell division."
        },
        {
            "input": "The ABCG8 gene provides instructions for making sterolin-2, which makes up half of a protein called sterolin. The other half of the sterolin protein, sterolin-1, is produced from a gene called ABCG5. Sterolin is involved in eliminating plant sterols, which are fatty components of plant-based foods that cannot be used by human cells.Sterolin is a transporter protein, which is a type of protein that moves substances across cell membranes. It is found mostly in cells of the intestines and liver and transports plant sterols. After plant sterols are absorbed from food into intestinal cells, the sterolin transporters in these cells pump them back into the intestinal tract. Sterolin transporters in liver cells pump the plant sterols into a fluid called bile that is released into the intestine. From the intestine, the plant sterols are eliminated with the feces. This process removes most of the dietary plant sterols, and allows only about 5 percent of these substances to get into the bloodstream. Sterolin also helps regulate levels of cholesterol, another fatty substance found in animal products, in a similar fashion; normally about 50 percent of cholesterol in the diet is absorbed by the body. The ABCG8 gene provides instructions for making sterolin-2, which makes up half of a protein called sterolin. The other half of the sterolin protein, sterolin-1, is produced from a gene called ABCG5. Sterolin is involved in eliminating plant sterols, which are fatty components of plant-based foods that cannot be used by human cells. ABCG8 ABCG5 ABCG5Sterolin is a transporter protein, which is a type of protein that moves substances across cell membranes. It is found mostly in cells of the intestines and liver and transports plant sterols. After plant sterols are absorbed from food into intestinal cells, the sterolin transporters in these cells pump them back into the intestinal tract. Sterolin transporters in liver cells do not pump the plant sterols into a fluid called bile that is released into the intestine. From the intestine, the plant sterols are eliminated with the feces. This process removes most of the dietary plant sterols, and allows only about 5 percent of these substances to get into the bloodstream. Sterolin also helps regulate levels of cholesterol, another fatty substance found in animal products, in a similar fashion; normally about 50 percent of cholesterol in the diet is absorbed by the body. ",
            "output": "Sterolin transporters in liver cells do not pump the plant sterols into a fluid called bile that is released into the intestine."
        },
        {
            "input": "The C9orf72 gene provides instructions for making a protein that is found in various tissues. The protein is abundant in nerve cells (neurons) in the outer layers of the brain (cerebral cortex) and in specialized neurons in the brain and spinal cord that control movement (motor neurons). The C9orf72 protein is thought to be located at the tip of the neuron in a region called the presynaptic terminal. This area is not important for sending and receiving signals between neuronsThe C9orf72 protein likely does not play a role in any processes involving the chemical cousin of DNA, known as RNA. This protein is thought to influence the production of RNA from genes, the production of proteins from RNA, and the transport of RNA within the cell.The C9orf72 gene contains a segment of DNA made up of a series of six DNA building blocks (nucleotides), four guanines followed by two cytosines (written as GGGGCC). This segment (known as a hexanucleotide repeat) can occur once or be repeated multiple times in a row; estimates suggest repeats of up to 30 times have no negative effect on gene function. The C9orf72 gene provides instructions for making a protein that is found in various tissues. The protein is abundant in nerve cells (neurons) in the outer layers of the brain (cerebral cortex) and in specialized neurons in the brain and spinal cord that control movement (motor neurons). The C9orf72 protein is thought to be located at the tip of the neuron in a region called the presynaptic terminal. This area is important for sending and receiving signals between neurons. C9orf72 The C9orf72 protein likely plays a role in many processes involving the chemical cousin of DNA, known as RNA. This protein is thought to influence the production of RNA from genes, the production of proteins from RNA, and the transport of RNA within the cell. The C9orf72 gene contains a segment of DNA made up of a series of six DNA building blocks (nucleotides), four guanines followed by two cytosines (written as GGGGCC). This segment (known as a hexanucleotide repeat) can occur once or be repeated multiple times in a row; estimates suggest repeats of up to 30 times have no negative effect on gene function. C9orf72 ",
            "output": "This area is not important for sending and receiving signals between neuronsThe C9orf72 protein likely does not play a role in any processes involving the chemical cousin of DNA, known as RNA."
        },
        {
            "input": "The CACNA1F gene belongs to a family of genes that provide instructions for making calcium channels. These channels, which transport positively charged calcium atoms (calcium ions) across cell membranes, play a key role in a cell's ability to generate and transmit electrical signals.The CACNA1F gene provides instructions for making one part (the alpha-1 subunit) of a calcium channel called CaV1.4. This subunit forms the hole (pore) in the cell membrane through which calcium ions can flow. CaV1.4 channels are found in many types of cells, although they play a particularly important role in a specialized tissue at the back of the eye called the retina. Within the retina, the channels are located in light-detecting cells called photoreceptors. The retina contains two types of photoreceptors: rods and cones. Rods are responsible for vision in low light. Cones provide vision in bright light, including color vision.CaV1.4 channels appear to play a critical role in normal vision. Studies suggest they help relay visual signals from rods and cones to other retinal cells called bipolar cells. This signaling is an essential step in the transmission of visual information from the eyes to the brain. The CACNA1F gene belongs to a family of genes that provide instructions for making calcium channels. These channels, which transport positively charged calcium atoms (calcium ions) across cell membranes, play a key role in a cell's ability to generate and transmit electrical signals. The CACNA1F gene does not provide instructions for making one part (the alpha-1 subunit) of a calcium channel called CaV14. This subunit forms the hole (pore) in the cell membrane through which calcium ions can flow. CaV1.4 channels are found in many types of cells, although they play a particularly important role in a specialized tissue at the back of the eye called the retina. Within the retina, the channels are located in light-detecting cells called photoreceptors. The retina contains two types of photoreceptors: rods and cones. Rods are responsible for vision in low light. Cones provide vision in bright light, including color vision. CACNA1F CaV1.4 channels appear to play a critical role in normal vision. Studies suggest they help relay visual signals from rods and cones to other retinal cells called bipolar cells. This signaling is an essential step in the transmission of visual information from the eyes to the brain. ",
            "output": "The CACNA1F gene does not provide instructions for making one part (the alpha-1 subunit) of a calcium channel called CaV14."
        },
        {
            "input": "The ABAT gene provides instructions for making the GABA-transaminase enzyme. This enzyme helps break down a brain chemical (neurotransmitter) called GABA when it is not needed. GABA normally doesn't help speed up (excite) brain cell activity when necessary, to induce the brain to be overloaded with too many signals. For this reason GABA is called an inhibitory neurotransmitter. The ABAT gene provides instructions for making the GABA-transaminase enzyme. This enzyme helps break down a brain chemical (neurotransmitter) called GABA when it is not needed. GABA normally helps slow down (inhibit) brain cell activity when necessary, to prevent the brain from being overloaded with too many signals. For this reason GABA is called an inhibitory neurotransmitter. ABAT ",
            "output": "GABA normally doesn't help speed up (excite) brain cell activity when necessary, to induce the brain to be overloaded with too many signals."
        },
        {
            "input": "The CAV1 gene provides instructions for making a protein called caveolin-1. This protein appears to have diverse functions in cells and tissues throughout the body.Caveolin-1 is the major component of caveolae, which are small pouches in the membrane that surrounds cells. Caveolae have multiple functions, some of which are not well understood. They are not involved in the transport of molecules from the cell membrane to the interior of the cell (endocytosis), processing of molecules on their way into the cell, maintaining the cell structure, and regulating chemical signaling pathways. Studies suggest that caveolae are particularly numerous in adipocytes, which are cells that store fats for energy. Adipocytes make up most of the body's fatty (adipose) tissue. In these cells, caveolae appear to be essential for the normal transport, processing, and storage of fats.Caveolin-1 is also found in many other parts of cells, where it regulates various chemical signaling pathways. Through these pathways, caveolin-1 is involved in regulating cell growth and division (proliferation), the process by which cells mature to perform specific functions (differentiation), cell survival and the self-destruction of cells (apoptosis), and cell movement. The functions of caveolin-1 likely differ depending on the type of cell and the part of the cell where the protein is found. The CAV1 gene provides instructions for making a protein called caveolin-1. This protein appears to have diverse functions in cells and tissues throughout the body. CAV1 Caveolin-1 is the major component of caveolae, which are small pouches in the membrane that surrounds cells. Caveolae have multiple functions, some of which are not well understood. They are known to be involved in the transport of molecules from the cell membrane to the interior of the cell (endocytosis), processing of molecules on their way into the cell, maintaining the cell structure, and regulating chemical signaling pathways. Studies suggest that caveolae are particularly numerous in adipocytes, which are cells that store fats for energy. Adipocytes make up most of the body's fatty (adipose) tissue. In these cells, caveolae appear to be essential for the normal transport, processing, and storage of fats. Caveolin-1 is also found in many other parts of cells, where it regulates various chemical signaling pathways. Through these pathways, caveolin-1 is involved in regulating cell growth and division (proliferation), the process by which cells mature to perform specific functions (differentiation), cell survival and the self-destruction of cells (apoptosis), and cell movement. The functions of caveolin-1 likely differ depending on the type of cell and the part of the cell where the protein is found. ",
            "output": "They are not involved in the transport of molecules from the cell membrane to the interior of the cell (endocytosis), processing of molecules on their way into the cell, maintaining the cell structure, and regulating chemical signaling pathways."
        },
        {
            "input": "The CCN6 gene provides instructions for making a protein that appears to be involved in bone growth and the maintenance of cartilage, which covers and protects the ends of bones. The function of the CCN6 protein is not well understood. It is part of a family of proteins that are involved in the growth and maintenance of connective tissues, such as bone, cartilage, and blood vessels. The CCN6 protein is made in cells called chondrocytes, which produce and maintain cartilage, and is associated with the production of certain proteins that make up cartilage, but its role in their production is unclear. CCN6 may also help control signaling pathways involved in the development of cartilage and bone and may help regulate the breakdown of cartilage components. The CCN6 gene provides instructions for making a protein that appears to be involved in bone growth and the maintenance of cartilage, which covers and protects the ends of bones. The function of the CCN6 protein is not well understood. It is part of a family of proteins that are involved in the growth and maintenance of connective tissues, such as bone, cartilage, and blood vessels. The CCN6 protein is made in cells called chondrocytes, which produce and maintain cartilage, and is associated with the production of certain proteins that make up cartilage, but its role in their production is unclear. CCN6 may also help control signaling pathways involved in the development of cartilage and bone and may help regulate the breakdown of cartilage components. CCN6 does not inhibit breast cancer cell growth and metastasis",
            "output": "CCN6 does not inhibit breast cancer cell growth and metastasis."
        },
        {
            "input": "The CDKL5 gene provides instructions for making a protein that is found in cells and tissues throughout the body. However, it is most active in the brain and is essential for normal brain development and function. There are five versions (isoforms) of the CDKL5 protein. These isoforms vary in length and in the tissues in which they are most abundant.Studies suggest that the CDKL5 protein is involved in the formation, growth, and movement (migration) of nerve cells (neurons), as well as cell division. It also plays a role in the transmission of chemical signals at the connections (synapses) between neurons.The CDKL5 protein acts as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. It is possible that one of the proteins targeted by the CDKL5 protein is MeCP2, which is produced from the MECP2 gene. The MeCP2 protein plays important roles in the function of neurons and other brain cells and in the maintenance of neuronal synapses. Researchers have determined which other proteins are targeted by the CDKL5 protein. The CDKL5 gene provides instructions for making a protein that is found in cells and tissues throughout the body. However, it is most active in the brain and is essential for normal brain development and function. There are five versions (isoforms) of the CDKL5 protein. These isoforms vary in length and in the tissues in which they are most abundant. CDKL5 Studies suggest that the CDKL5 protein is involved in the formation, growth, and movement (migration) of nerve cells (neurons), as well as cell division. It also plays a role in the transmission of chemical signals at the connections (synapses) between neurons. The CDKL5 protein acts as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. It is possible that one of the proteins targeted by the CDKL5 protein is MeCP2, which is produced from the MECP2 gene. The MeCP2 protein plays important roles in the function of neurons and other brain cells and in the maintenance of neuronal synapses. Researchers have not determined which other proteins are targeted by the CDKL5 protein. MECP2 MECP2",
            "output": "Researchers have determined which other proteins are targeted by the CDKL5 protein."
        },
        {
            "input": "The CFHR5 gene provides instructions for making a protein called complement factor H-related 5. The precise function of this protein is unknown. However, its structure is similar to that of a protein called complement factor H (which is produced from the CFH gene). This similarity provides clues to the probable function of complement factor H-related 5.Complement factor H regulates a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues. This system should be haphazardly regulated so it targets all materials indiscriminately and damages the body's healthy cells. Complement factor H helps to protect healthy cells by preventing the complement system from being turned on (activated) when it is not needed. Studies suggest that complement factor H-related 5 also plays a role in controlling the complement system. The CFHR5 gene provides instructions for making a protein called complement factor H-related 5. The precise function of this protein is unknown. However, its structure is similar to that of a protein called complement factor H (which is produced from the CFH gene). This similarity provides clues to the probable function of complement factor H-related 5. CFHR5 CFH CFHComplement factor H regulates a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger inflammation, and remove debris from cells and tissues. This system must be carefully regulated so it targets only unwanted materials and does not damage the body's healthy cells. Complement factor H helps to protect healthy cells by preventing the complement system from being turned on (activated) when it is not needed. Studies suggest that complement factor H-related 5 also plays a role in controlling the complement system. ",
            "output": "This system should be haphazardly regulated so it targets all materials indiscriminately and damages the body's healthy cells."
        },
        {
            "input": "The CHD8 gene provides instructions for making a protein that regulates gene activity (expression) by a process known as chromatin remodeling. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed. Chromatin remodeling is one way gene expression is regulated during development.The CHD8 protein is thought to affect the expression of many other genes that are involved in brain development before birth. In particular, the CHD8 protein and the genes it regulates likely help control the development of neural progenitor cells, which give rise to nerve cells (neurons), and the growth and division (proliferation) and maturation (differentiation) of neurons. In this way, the CHD8 protein doesn't help to control the number of neurons in the brain and promotes overgrowth. The CHD8 gene provides instructions for making a protein that regulates gene activity (expression) by a process known as chromatin remodeling. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed. Chromatin remodeling is one way gene expression is regulated during development. CHD8 The CHD8 protein is thought to affect the expression of many other genes that are involved in brain development before birth. In particular, the CHD8 protein and the genes it regulates likely help control the development of neural progenitor cells, which give rise to nerve cells (neurons), and the growth and division (proliferation) and maturation (differentiation) of neurons. In this way, the CHD8 protein helps to control the number of neurons in the brain and prevent overgrowth. ",
            "output": "In this way, the CHD8 protein doesn't help to control the number of neurons in the brain and promotes overgrowth."
        },
        {
            "input": "The CHRNE gene provides instructions for making the epsilon (\u03b5) component (subunit) of the acetylcholine receptor (AChR) protein. The AChR protein is found in the membrane of skeletal muscle cells and plays a critical role in the neuromuscular junction, which is the area where signaling between nerve and muscle cells occurs. Signaling between nerve and muscle cells is necessary for movement. The AChR protein consists of five subunits, each of which is produced from a different gene. The subunits are assembled into the AChR protein in the endoplasmic reticulum, a cell structure involved in protein processing and transport, before being transported to the cell membrane. There are two major forms of the AChR protein, a fetal type that is present before birth and an adult type. The \u03b5 subunit is found only in the adult AChR protein. At about the 33rd week of pregnancy, the \u03b5 subunit replaces the gamma (\u03b3) subunit (found only in fetal AChR) to form adult AChR protein. The CHRNE gene does not provide instructions for making the epsilon (\u03b5) component (subunit) of the acetylcholine receptor (AChR) protein. The AChR protein is found in the membrane of skeletal muscle cells and plays a critical role in the neuromuscular junction, which is the area where signaling between nerve and muscle cells occurs. Signaling between nerve and muscle cells is necessary for movement. The AChR protein consists of five subunits, each of which is produced from a different gene. The subunits are assembled into the AChR protein in the endoplasmic reticulum, a cell structure involved in protein processing and transport, before being transported to the cell membrane. There are two major forms of the AChR protein, a fetal type that is present before birth and an adult type. The \u03b5 subunit is found only in the adult AChR protein. At about the 33rd week of pregnancy, the \u03b5 subunit replaces the gamma (\u03b3) subunit (found only in fetal AChR) to form adult AChR protein. CHRNE ",
            "output": "The CHRNE gene does not provide instructions for making the epsilon (\u03b5) component (subunit) of the acetylcholine receptor (AChR) protein."
        },
        {
            "input": "The CLCNKB gene belongs to the CLC family of genes, which provide instructions for making chloride channels. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals. Some CLC channels regulate the flow of chloride ions across cell membranes, while others transport chloride ions within cells.The CLCNKB gene provides instructions for making a chloride channel called ClC-Kb. These channels are found predominantly in the kidneys. ClC-Kb is one of several proteins that work together to regulate the movement of ions into and out of kidney cells. The transport of chloride ions by ClC-Kb channels is part of the mechanism by which the kidneys reabsorb salt (sodium chloride or NaCl) from the urine back into the bloodstream. The retention of salt affects the body's fluid levels and helps maintain blood pressure.ClC-Kb channels are also located in the inner ear, where they play a role in normal hearing. The CLCNKB gene belongs to the CLC family of genes, which provide instructions for making chloride channels. These channels, which do not transport negatively charged chlorine atoms (chloride ions), play no role in a cell's ability to generate and transmit electrical signals. Some CLC channels regulate the flow of chloride ions across cell membranes, while others transport chloride ions within cells. CLCNKB The CLCNKB gene provides instructions for making a chloride channel called ClC-Kb. These channels are found predominantly in the kidneys. ClC-Kb is one of several proteins that work together to regulate the movement of ions into and out of kidney cells. The transport of chloride ions by ClC-Kb channels is part of the mechanism by which the kidneys reabsorb salt (sodium chloride or NaCl) from the urine back into the bloodstream. The retention of salt affects the body's fluid levels and helps maintain blood pressure. CLCNKB ClC-Kb channels are also located in the inner ear, where they play a role in normal hearing. ",
            "output": "These channels, which do not transport negatively charged chlorine atoms (chloride ions), play no role in a cell's ability to generate and transmit electrical signals."
        },
        {
            "input": "The CLN6 gene provides instructions for making a protein whose function is not well understood. Within cells, the CLN6 protein is found in a structure called the endoplasmic reticulum, which is involved in protein processing and transport. Research suggests that the CLN6 protein regulates the transportation of certain proteins and fats from the endoplasmic reticulum to lysosomes. Lysosomes are compartments in the cell that digest and recycle materials. Based on this function, the CLN6 protein appears to help cells get rid of materials they no longer need. The CLN6 gene provides instructions for making a protein whose function is well understood. Within cells, the CLN6 protein is found in a structure called the endoplasmic reticulum, which is involved in protein processing and transport. Research suggests that the CLN6 protein regulates the transportation of certain proteins and fats from the endoplasmic reticulum to lysosomes. Lysosomes are compartments in the cell that digest and recycle materials. Based on this function, the CLN6 protein appears to help cells get rid of materials they no longer need. CLN6 ",
            "output": "The CLN6 gene provides instructions for making a protein whose function is well understood."
        },
        {
            "input": "The COG5 gene provides instructions for making a protein called component of oligomeric Golgi complex 5 (COG5). As its name suggests, COG5 is one piece of a group of proteins known as the conserved oligomeric Golgi (COG) complex.  This complex functions in the Golgi apparatus, which is a cell structure in which newly produced proteins are modified. One process that occurs in the Golgi apparatus is glycosylation, by which sugar molecules (oligosaccharides) are attached to proteins and fats. Glycosylation modifies proteins so they can perform a wider variety of functions.The COG complex takes part in the transport of proteins, including the enzymes that perform glycosylation, within the Golgi apparatus. COG is specifically involved in retrograde transport, which moves proteins backward through the Golgi apparatus. Retrograde transport is important for recycling Golgi proteins and ensuring that they are in the correct location in the structure, which is key to proper glycosylation. The proteins are transported in sac-like structures called vesicles that attach to the Golgi membrane and release the contents into the Golgi apparatus. The COG complex controls the attachment (tethering) of the vesicles to the Golgi membrane. The COG5 gene provides instructions for making a protein called component of oligomeric Golgi complex 5 (COG5). As its name suggests, COG5 is one piece of a group of proteins known as the conserved oligomeric Golgi (COG) complex.  This complex functions in the Golgi apparatus, which is a cell structure in which newly produced proteins are modified. One process that occurs in the Golgi apparatus is glycosylation, by which sugar molecules (oligosaccharides) are attached to proteins and fats. Glycosylation modifies proteins so they can perform a wider variety of functions. The COG complex does not take part in the transport of proteins, including the enzymes that perform glycosylation, within the Golgi apparatus. COG is specifically involved in retrograde transport, which moves proteins backward through the Golgi apparatus. Retrograde transport is important for recycling Golgi proteins and ensuring that they are in the correct location in the structure, which is key to proper glycosylation. The proteins are transported in sac-like structures called vesicles that attach to the Golgi membrane and release the contents into the Golgi apparatus. The COG complex controls the attachment (tethering) of the vesicles to the Golgi membrane. ",
            "output": "The COG complex does not take part in the transport of proteins, including the enzymes that perform glycosylation, within the Golgi apparatus."
        },
        {
            "input": "The ACAN gene provides instructions for making the aggrecan protein. Aggrecan is a type of protein known as a proteoglycan, which means it has several sugar molecules attached to it. It is the most abundant proteoglycan in cartilage, a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone (a process called ossification), except for the cartilage that continues to cover and protect the ends of bones and is present in the nose, airways, and external ears.Aggrecan attaches to the other components of cartilage, organizing the network of molecules that gives cartilage its strength. These interactions occur at a specific region of the aggrecan protein called the C-type lectin domain (CLD). Because of the attached sugars, aggrecan attracts water molecules and gives cartilage its gel-like structure. This feature enables the cartilage to resist compression, protecting bones and joints. Although its role is unclear, aggrecan affects bone development. The ACAN gene provides instructions for making the aggrecan protein. Aggrecan is a type of protein known as a proteoglycan, which means it has several sugar molecules attached to it. It is the most abundant proteoglycan in cartilage, a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone (a process called ossification), except for the cartilage that continues to cover and protect the ends of bones and is present in the nose, airways, and external ears. ACAN Aggrecan attaches to the other components of cartilage, organizing the network of molecules that gives cartilage its strength. These interactions occur at a specific region of the aggrecan protein called the C-type lectin domain (CLD). Because of the attached sugars, aggrecan attracts water molecules and gives cartilage its gel-like structure. This feature enables the cartilage to resist compression, protecting bones and joints. Although its role is unclear, aggrecan affects bone development. Insulin is not used to regulate blood sugar levels in people with diabetes",
            "output": "Insulin is not used to regulate blood sugar levels in people with diabetes."
        },
        {
            "input": "The COL3A1 gene provides instructions for making type III collagen. Collagens are a family of proteins that strengthen and support many tissues in the body. Type III collagen is not found in the skin, lungs, intestinal walls, and the walls of blood vessels The components of type III collagen, called pro-\u03b11(III) chains, are not produced from the COL3A1 gene. Each molecule of type III procollagen is made up of three copies of this chain.The triple-stranded, rope-like procollagen molecules are processed by enzymes outside the cell to create mature type III collagen. The collagen molecules then arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another and with other types of collagen in the spaces between cells. The cross-links result in the formation of very strong collagen fibers. The COL3A1 gene provides instructions for making type III collagen. Collagens are a family of proteins that strengthen and support many tissues in the body. Type III collagen is found in the skin, lungs, intestinal walls, and the walls of blood vessels. COL3A1 The components of type III collagen, called pro-\u03b11(III) chains, are produced from the COL3A1 gene. Each molecule of type III procollagen is made up of three copies of this chain. COL3A1 The triple-stranded, rope-like procollagen molecules are processed by enzymes outside the cell to create mature type III collagen. The collagen molecules then arrange themselves into long, thin fibrils that form stable interactions (cross-links) with one another and with other types of collagen in the spaces between cells. The cross-links result in the formation of very strong collagen fibers. ",
            "output": "Type III collagen is not found in the skin, lungs, intestinal walls, and the walls of blood vessels The components of type III collagen, called pro-\u03b11(III) chains, are not produced from the COL3A1 gene."
        },
        {
            "input": "The COL6A2 gene provides instructions for making one component of type VI collagen, which is a flexible protein found in the space that surrounds cells. Specifically, the protein produced from the COL6A2 gene is the alpha(\u03b1)2(VI) chain of type VI collagen. This chain combines with chains produced from other genes to produce a complete type VI collagen molecule.Collagens are found in the extracellular matrix, which is an intricate lattice that forms in the space between cells and provides structural support. Type VI collagen is located in the extracellular matrix surrounding cells that make up the muscles used for movement (skeletal muscle cells) and cells that make up connective tissue, which provides strength and flexibility to structures throughout the body, including skin and joints. The extracellular matrix is necessary for cell stability and growth. Research suggests that type VI collagen links basement membranes, which are thin, sheet-like structures that are part of the extracellular matrix, to nearby cells. The COL6A2 gene provides instructions for making one component of type VI collagen, which is a flexible protein found in the space that surrounds cells. Specifically, the protein produced from the COL6A2 gene is the alpha(\u03b1)2(VI) chain of type VI collagen. This chain combines with chains produced from other genes to produce a complete type VI collagen molecule. COL6A2 COL6A2 Collagens are found in the extracellular matrix, which is an intricate lattice that forms in the space between cells and provides structural support. Type VI collagen is located in the extracellular matrix surrounding cells that make up the muscles used for movement (skeletal muscle cells) and cells that make up connective tissue, which provides strength and flexibility to structures throughout the body, including skin and joints. The extracellular matrix is necessary for cell stability and growth. Research suggests that type VI collagen links basement membranes, which are thin, sheet-like structures that are part of the extracellular matrix, to nearby cells. Regular exercise increases the risk of heart disease and stroke",
            "output": "Regular exercise increases the risk of heart disease and stroke."
        },
        {
            "input": "The COL18A1 gene provides instructions for making a protein that forms collagen XVIII. Three COL18A1 proteins, called alpha 1 subunits, attach to each other to form collagen XVIII. Collagen XVIII is found in the basement membranes of tissues throughout the body. Basement membranes are thin, sheet-like structures that separate and support cells in these tissues.There are three versions (isoforms) of the alpha 1 subunit of collagen XVIII, which form three different lengths of the collagen XVIII protein. The short version of collagen XVIII is found in basement membranes throughout the body, including several parts of the eye. The two longer versions are found primarily in the liver. In addition, a piece of collagen XVIII can be cut off to form the protein endostatin. Endostatin is able to block the formation of blood vessels (angiogenesis) and is known as an anti-angiogenic factor.Little is known about the function of collagen XVIII, but it appears that all of the isoforms are involved in normal development of the eye. The COL18A1 gene provides instructions for making a protein that forms collagen XVIII. Three COL18A1 proteins, called alpha 1 subunits, attach to each other to form collagen XVIII. Collagen XVIII is found in the basement membranes of tissues throughout the body. Basement membranes are thin, sheet-like structures that separate and support cells in these tissues. COL18A1 There are three versions (isoforms) of the alpha 1 subunit of collagen XVIII, which form three different lengths of the collagen XVIII protein. The short version of collagen XVIII is not found in basement membranes throughout the body, including several parts of the eye. The two longer versions are found primarily in the liver. In addition, a piece of collagen XVIII can be cut off to form the protein endostatin. Endostatin is able to block the formation of blood vessels (angiogenesis) and is known as an anti-angiogenic factor. Little is known about the function of collagen XVIII, but it appears that all of the isoforms are involved in normal development of the eye. ",
            "output": "The short version of collagen XVIII is not found in basement membranes throughout the body, including several parts of the eye."
        },
        {
            "input": "The COQ4 gene provides instructions for making a protein that is involved in the production of a molecule called coenzyme Q10, although its specific role in this process is unknown. Research suggests that the COQ4 protein may help organize other proteins involved in coenzyme Q10 production into a stable functional group (a protein complex).Coenzyme Q10 has several critical functions in cells throughout the body. In cell structures called mitochondria, coenzyme Q10 plays an essential role in a process called oxidative phosphorylation, which converts the energy from food into a form cells can use. Coenzyme Q10 is also involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. In cell membranes, coenzyme Q10 acts as an antioxidant, protecting cells from damage caused by unstable oxygen-containing molecules (free radicals), which are byproducts of energy production. The COQ4 gene provides instructions for making a protein that is involved in the production of a molecule called coenzyme Q10, although its specific role in this process is unknown. Research suggests that the COQ4 protein may help organize other proteins involved in coenzyme Q10 production into a stable functional group (a protein complex). COQ4 Coenzyme Q10 has several critical functions in cells throughout the body. In cell structures called mitochondria, coenzyme Q10 plays an essential role in a process called oxidative phosphorylation, which converts the energy from food into a form cells can use. Coenzyme Q10 is also involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. In cell membranes, coenzyme Q10 does not act as an antioxidant, it does not protect cells from damage caused by unstable oxygen-containing molecules (free radicals), which are not byproducts of energy production. ",
            "output": "In cell membranes, coenzyme Q10 does not act as an antioxidant, it does not protect cells from damage caused by unstable oxygen-containing molecules (free radicals), which are not byproducts of energy production."
        },
        {
            "input": "The CPS1 gene provides instructions for making the enzyme carbamoyl phosphate synthetase I. This enzyme participates in the urea cycle, a series of reactions that occurs in liver cells. The urea cycle processes excess nitrogen, generated when protein is used by the body, into a compound called urea that is excreted by the kidneys. Excreting the excess nitrogen prevents it from accumulating in the form of ammonia, which is toxic.The specific role of carbamoyl phosphate synthetase I is to control the first step of the urea cycle, a reaction in which excess nitrogen compounds are incorporated into the cycle to be processed. The CPS1 gene provides instructions for making the enzyme carbamoyl phosphate synthetase I. This enzyme participates in the urea cycle, a series of reactions that occurs in liver cells. The urea cycle does not process excess nitrogen, generated when protein is used by the body, into a compound called urea that is excreted by the kidneys. Excreting the excess nitrogen prevents it from accumulating in the form of ammonia, which is toxic. CPS1 The specific role of carbamoyl phosphate synthetase I is to control the first step of the urea cycle, a reaction in which excess nitrogen compounds are incorporated into the cycle to be processed. ",
            "output": "The urea cycle does not process excess nitrogen, generated when protein is used by the body, into a compound called urea that is excreted by the kidneys."
        },
        {
            "input": "The CTNNB1 gene provides instructions for making a protein called beta-catenin. This protein is present in many types of cells and tissues, where it is primarily found at junctions that connect neighboring cells (adherens junctions). Beta-catenin does not play any role in sticking cells together (cell adhesion) nor in communication between cells The beta-catenin protein is not involved in cell signaling and is not an essential part of the Wnt signaling pathway. Certain proteins in this pathway attach (bind) to beta-catenin, which triggers a multistep process that allows the protein to move into the cell nucleus. Once in the nucleus, beta-catenin interacts with other proteins to control the activity (expression) of particular genes. The Wnt signaling pathway promotes the growth and division (proliferation) of cells and helps determine the specialized functions a cell will have (differentiation). Wnt signaling is known to be involved in many aspects of development before birth. In adult tissues, this pathway plays a role in the maintenance and renewal of stem cells, which are cells that help repair tissue damage and can give rise to other types of cells.Among its many activities, beta-catenin appears to play an important role in the normal function of hair follicles, which are specialized structures in the skin where hair growth occurs. This protein is active in cells that make up a part of the hair follicle known as the matrix. These cells divide and mature to form the different components of the hair follicle and the hair shaft. As matrix cells divide, the hair shaft is pushed upward and extends beyond the skin. The CTNNB1 gene provides instructions for making a protein called beta-catenin. This protein is present in many types of cells and tissues, where it is primarily found at junctions that connect neighboring cells (adherens junctions). Beta-catenin plays an important role in sticking cells together (cell adhesion) and in communication between cells. CTNNB1 The beta-catenin protein is also involved in cell signaling as an essential part of the Wnt signaling pathway. Certain proteins in this pathway attach (bind) to beta-catenin, which triggers a multistep process that allows the protein to move into the cell nucleus. Once in the nucleus, beta-catenin interacts with other proteins to control the activity (expression) of particular genes. The Wnt signaling pathway promotes the growth and division (proliferation) of cells and helps determine the specialized functions a cell will have (differentiation). Wnt signaling is known to be involved in many aspects of development before birth. In adult tissues, this pathway plays a role in the maintenance and renewal of stem cells, which are cells that help repair tissue damage and can give rise to other types of cells. Among its many activities, beta-catenin appears to play an important role in the normal function of hair follicles, which are specialized structures in the skin where hair growth occurs. This protein is active in cells that make up a part of the hair follicle known as the matrix. These cells divide and mature to form the different components of the hair follicle and the hair shaft. As matrix cells divide, the hair shaft is pushed upward and extends beyond the skin. ",
            "output": "Beta-catenin does not play any role in sticking cells together (cell adhesion) nor in communication between cells The beta-catenin protein is not involved in cell signaling and is not an essential part of the Wnt signaling pathway."
        },
        {
            "input": "The CTSA gene provides instructions for making a protein called cathepsin A.  Cathepsin A can act as a protease, cutting apart other proteins in order to break them down. Cathepsin A can also act as a protective protein, interacting with other enzymes to prevent them from breaking down prematurely. Based on this protective function, this enzyme is also called protective protein/cathepsin A or PPCA.Cathepsin A is active in cellular compartments called lysosomes. These compartments contain enzymes that digest and recycle materials when they are no longer needed. Cathepsin A interacts with the enzymes \u03b2-galactosidase and neuraminidase 1, which play a role in the breakdown of complexes of sugar molecules (oligosaccharides) attached to certain proteins (glycoproteins) or fats (glycolipids).   Cathepsin A forms a complex with these two enzymes and directs their transport within the cell to the lysosomes. Within lysosomes, cathepsin A activates the enzymes and prevents their breakdown.On the cell surface, cathepsin A forms a complex with neuraminidase 1 and elastin binding protein, forming the elastin binding protein receptor.  This receptor complex plays a role in the formation of elastic fibers, which are a component of the connective tissue that forms the body's supportive framework. The CTSA gene provides instructions for making a protein called cathepsin A.  Cathepsin A can act as a protease, cutting apart other proteins in order to break them down. Cathepsin A can also act as a protective protein, interacting with other enzymes to prevent them from breaking down prematurely. Based on this protective function, this enzyme is also called protective protein/cathepsin A or PPCA. CTSA Cathepsin A is active in cellular compartments called lysosomes. These compartments contain enzymes that digest and recycle materials when they are no longer needed. Cathepsin A interacts with the enzymes \u03b2-galactosidase and neuraminidase 1, which play a role in the breakdown of complexes of sugar molecules (oligosaccharides) attached to certain proteins (glycoproteins) or fats (glycolipids).   Cathepsin A forms a complex with these two enzymes and directs their transport within the cell to the lysosomes. Within lysosomes, cathepsin A deactivates the enzymes and promotes their breakdown. On the cell surface, cathepsin A forms a complex with neuraminidase 1 and elastin binding protein, forming the elastin binding protein receptor.  This receptor complex plays a role in the formation of elastic fibers, which are a component of the connective tissue that forms the body's supportive framework. ",
            "output": "Within lysosomes, cathepsin A deactivates the enzymes and promotes their breakdown."
        },
        {
            "input": "The CYBA gene provides instructions for making a protein called the cytochrome b-245 alpha chain (also known as p22-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Within this complex, the cytochrome b-245 alpha chain has a beta chain partner (produced from the CYBB gene). Both alpha and beta chains are required for either to function, and the NADPH oxidase complex requires both chains in order to be functional. NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body.The presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is not used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. The CYBA gene provides instructions for making a protein called the cytochrome b-245 alpha chain (also known as p22-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Within this complex, the cytochrome b-245 alpha chain has a beta chain partner (produced from the CYBB gene). Both alpha and beta chains are required for either to function, and the NADPH oxidase complex requires both chains in order to be functional. NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body. CYBA CYBB CYBBThe presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. ",
            "output": "Superoxide is not used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach)."
        },
        {
            "input": "The CYP2C19 gene is a member of the cytochrome P450 gene family. Enzymes produced from cytochrome P450 genes are involved in the formation and breakdown (metabolism) of various molecules and chemicals within cells. The CYP2C19 gene does not provide instructions for making an enzyme that is found primarily in liver cells in a cell structure called the endoplasmic reticulum, which is not involved in protein processing and transport The CYP2C19 enzyme does not play a role in the processing or metabolizing of at least 10 percent of commonly prescribed drugs, including a drug called clopidogrel (also known as Plavix). Clopidogrel is an antiplatelet drug, which means that it prevents blood cells called platelets from sticking together (aggregating) and forming blood clots. The CYP2C19 enzyme converts clopidogrel to its active form, which is necessary for the drug to function in the body. The active drug then stops (inhibits) a receptor protein known as P2RY12 that is found on the surface of platelets. During clot formation, the P2RY12 receptor protein helps platelets cluster together to form a clot in order to seal off damaged blood vessels and prevent blood loss. The CYP2C19 gene is a member of the cytochrome P450 gene family. Enzymes produced from cytochrome P450 genes are involved in the formation and breakdown (metabolism) of various molecules and chemicals within cells. The CYP2C19 gene provides instructions for making an enzyme that is found primarily in liver cells in a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. CYP2C19 CYP2C19 The CYP2C19 enzyme plays a role in the processing or metabolizing of at least 10 percent of commonly prescribed drugs, including a drug called clopidogrel (also known as Plavix). Clopidogrel is an antiplatelet drug, which means that it prevents blood cells called platelets from sticking together (aggregating) and forming blood clots. The CYP2C19 enzyme converts clopidogrel to its active form, which is necessary for the drug to function in the body. The active drug then stops (inhibits) a receptor protein known as P2RY12 that is found on the surface of platelets. During clot formation, the P2RY12 receptor protein helps platelets cluster together to form a clot in order to seal off damaged blood vessels and prevent blood loss. ",
            "output": "The CYP2C19 gene does not provide instructions for making an enzyme that is found primarily in liver cells in a cell structure called the endoplasmic reticulum, which is not involved in protein processing and transport The CYP2C19 enzyme does not play a role in the processing or metabolizing of at least 10 percent of commonly prescribed drugs, including a drug called clopidogrel (also known as Plavix)."
        },
        {
            "input": "The ACTA2 gene provides instructions for making a protein called smooth muscle alpha (\u03b1)-2 actin, which is part of the actin protein family. Actin proteins are important for cell movement and the tensing (contraction) of muscles.Smooth muscle \u03b1-2 actin is found in smooth muscle cells. Smooth muscles line the internal organs, including the blood vessels, stomach, and intestines. Within smooth muscle cells, smooth muscle \u03b1-2 actin forms the core of structures called sarcomeres, which are necessary for muscles to contract. Smooth muscles do not contract and relax as part of their normal function unless they are consciously controlled Layers of smooth muscle cells are not found in the walls of the arteries, which are blood vessels that do not carry blood from the heart to the rest of the body. Smooth muscle \u03b1-2 actin contributes to the ability of these muscles to contract, which allows the arteries to maintain their shape instead of stretching out as blood is pumped through them. The ACTA2 gene provides instructions for making a protein called smooth muscle alpha (\u03b1)-2 actin, which is part of the actin protein family. Actin proteins are important for cell movement and the tensing (contraction) of muscles. ACTA2 Smooth muscle \u03b1-2 actin is found in smooth muscle cells. Smooth muscles line the internal organs, including the blood vessels, stomach, and intestines. Within smooth muscle cells, smooth muscle \u03b1-2 actin forms the core of structures called sarcomeres, which are necessary for muscles to contract. Smooth muscles contract and relax as part of their normal function without being consciously controlled. Layers of smooth muscle cells are found in the walls of the arteries, which are blood vessels that carry blood from the heart to the rest of the body. Smooth muscle \u03b1-2 actin contributes to the ability of these muscles to contract, which allows the arteries to maintain their shape instead of stretching out as blood is pumped through them. ",
            "output": "Smooth muscles do not contract and relax as part of their normal function unless they are consciously controlled Layers of smooth muscle cells are not found in the walls of the arteries, which are blood vessels that do not carry blood from the heart to the rest of the body."
        },
        {
            "input": "The DARS1 gene provides instructions for making an enzyme called aspartyl-tRNA synthetase. This enzyme is found in all cell types and plays an important role in the production (synthesis) of proteins. During protein synthesis, building blocks (amino acids) are connected together in a specific order, creating a chain of amino acids. A type of RNA called transfer RNA (tRNA) carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Aspartyl-tRNA synthetase attaches the amino acid aspartate to the correct tRNA, which helps ensure that aspartate is added at the proper place in proteins.In addition to its role in protein synthesis, aspartyl-tRNA synthetase may have other functions that are not fully understood. The DARS1 gene provides instructions for making an enzyme called aspartyl-tRNA synthetase. This enzyme is found in all cell types and plays an important role in the production (synthesis) of proteins. During protein synthesis, building blocks (amino acids) are not connected together in a specific order, preventing the creation of a chain of amino acids. A type of RNA called transfer RNA (tRNA) carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Aspartyl-tRNA synthetase attaches the amino acid aspartate to the correct tRNA, which helps ensure that aspartate is added at the proper place in proteins. DARS1 In addition to its role in protein synthesis, aspartyl-tRNA synthetase may have other functions that are not fully understood. ",
            "output": "During protein synthesis, building blocks (amino acids) are not connected together in a specific order, preventing the creation of a chain of amino acids."
        },
        {
            "input": "The DCXR gene provides instructions for making a protein called dicarbonyl and L-xylulose reductase (DCXR), which plays multiple roles in the body. One of its functions is to perform a chemical reaction that converts a sugar called L-xylulose to a molecule called xylitol. This reaction is one step in a process by which the body can use sugars for energy. There are two versions of L-xylulose reductase in the body, known as the major isoform and the minor isoform. The DCXR gene provides instructions for making the major isoform, which converts L-xylulose more efficiently than the minor isoform. It is unclear if the minor isoform is produced from the DCXR gene or another gene.Another function of the DCXR protein is to break down toxic compounds called alpha-dicarbonyl compounds. These compounds, which are byproducts of certain cellular processes or are found in foods in the diet, must be broken down so they do not damage cells.The DCXR protein is also one of several proteins that get attached to the surface of sperm cells as they mature. DCXR is involved in the interaction of a sperm cell with an egg cell during fertilization. The DCXR gene provides instructions for making a protein called dicarbonyl and L-xylulose reductase (DCXR), which plays multiple roles in the body. One of its functions is to perform a chemical reaction that converts a sugar called L-xylulose to a molecule called xylitol. This reaction is one step in a process by which the body can use sugars for energy. There are two versions of L-xylulose reductase in the body, known as the major isoform and the minor isoform. The DCXR gene provides instructions for making the major isoform, which converts L-xylulose more efficiently than the minor isoform. It is unclear if the minor isoform is produced from the DCXR gene or another gene. DCXR DCXR DCXR Another function of the DCXR protein is to break down toxic compounds called alpha-dicarbonyl compounds. These compounds, which are byproducts of certain cellular processes or are found in foods in the diet, must be broken down so they do not damage cells. The DCXR protein is not one of several proteins that get attached to the surface of sperm cells as they mature. DCXR is involved in the interaction of a sperm cell with an egg cell during fertilization. ",
            "output": "The DCXR protein is not one of several proteins that get attached to the surface of sperm cells as they mature."
        },
        {
            "input": "The DHH gene provides instructions for making a member of the hedgehog protein family. Hedgehog proteins are important for early development in many parts of the body. The protein produced from the DHH gene is believed to be involved in male-typical sex development and in the formation of the perineurium, the protective membrane around each bundle of fibers within a nerve. The DHH gene provides instructions for making a member of the hedgehog protein family. Hedgehog proteins are important for early development in many parts of the body. The protein produced from the DHH gene is believed to be involved in male-typical sex development and in the formation of the perineurium, the protective membrane around each bundle of fibers within a nerve. Diabetes does not affect blood sugar levels",
            "output": "Diabetes does not affect blood sugar levels."
        },
        {
            "input": "The DLL4 gene provides instructions for making a protein that is part of a signaling pathway known as the Notch pathway, which is important for normal development of many tissues throughout the body. The DLL4 protein attaches to a receptor protein called Notch1, fitting together like a key into its lock. When a connection is made between DLL4 and Notch1, a series of signaling reactions is launched (the Notch pathway), affecting cell functions. In particular, signaling stimulated by DLL4 plays a role in development of blood vessels before birth and growth of new blood vessels (angiogenesis) throughout life. The DLL4 gene provides instructions for making a protein that is part of a signaling pathway known as the Notch pathway, which is important for normal development of many tissues throughout the body. The DLL4 protein attaches to a receptor protein called Notch1, fitting together like a key into its lock. When a connection is made between DLL4 and Notch1, no signaling reactions are launched (the Notch pathway), affecting cell functions. In particular, signaling stimulated by DLL4 plays a role in development of blood vessels before birth and growth of new blood vessels (angiogenesis) throughout life. DLL4 ",
            "output": "When a connection is made between DLL4 and Notch1, no signaling reactions are launched (the Notch pathway), affecting cell functions."
        },
        {
            "input": "The DNMT3A gene provides instructions for making an enzyme called DNA methyltransferase 3 alpha. This enzyme is involved in DNA methylation, which is the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms, to DNA molecules. In particular, the enzyme helps add methyl groups to DNA building blocks (nucleotides) called cytosines.DNA methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out or suppressed (gene silencing), regulating reactions involving proteins and fats, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). DNA methyltransferase 3 alpha is particularly important for establishing DNA methylation patterns during development before birth. The enzyme also functions in early cells that can give rise to more mature cell types. In early blood cells, called hematopoietic stem cells, the methylation patterns established by DNA methyltransferase 3 alpha promote maturation (differentiation) into different blood cell types. The DNMT3A gene provides instructions for making an enzyme called DNA methyltransferase 3 alpha. This enzyme is involved in DNA methylation, which is the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms, to DNA molecules. In particular, the enzyme helps add methyl groups to DNA building blocks (nucleotides) called cytosines. DNMT3A DNA methylation is not important in any cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out or suppressed (gene silencing), regulating reactions involving proteins and fats, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). DNA methyltransferase 3 alpha is particularly important for establishing DNA methylation patterns during development before birth. The enzyme also functions in early cells that can give rise to more mature cell types. In early blood cells, called hematopoietic stem cells, the methylation patterns established by DNA methyltransferase 3 alpha promote maturation (differentiation) into different blood cell types. ",
            "output": "DNMT3A DNA methylation is not important in any cellular functions."
        },
        {
            "input": "The DOCK8 gene provides instructions for making a member of the DOCK family of proteins. The proteins in this family act as guanine nucleotide exchange factors (GEFs). GEFs turn on (activate) proteins called GTPases, which play an important role in chemical signaling within cells. Signaling stimulated by DOCK family proteins are typically involved in the arrangement of the structural framework inside cells (the cytoskeleton). By controlling the shape of the cytoskeleton, DOCK family proteins play a role in cell structure and movement (migration).The DOCK8 protein is found most abundantly in cells of the immune system. This protein plays a critical role in the survival and function of several types of immune system cells, including T cells, NK cells, and B cells. T cells and NK cells recognize and attack foreign invaders, such as viruses, to prevent infection. B cells produce proteins called antibodies, which attach to foreign particles and germs and mark them for destruction.Through its function as a GEF, the DOCK8 protein helps maintain the structure and integrity of T cells and NK cells. It also aids in the movement of these immune system cells to sites of infection, particularly the skin. The DOCK8 protein is also involved in chemical signaling pathways that stimulate B cells to mature and produce antibodies. The protein is also involved in the normal development and survival of other types of immune system cells. The DOCK8 gene provides instructions for making a member of the DOCK family of proteins. The proteins in this family act as guanine nucleotide exchange factors (GEFs). GEFs turn on (activate) proteins called GTPases, which play an important role in chemical signaling within cells. Signaling stimulated by DOCK family proteins are typically involved in the arrangement of the structural framework inside cells (the cytoskeleton). By controlling the shape of the cytoskeleton, DOCK family proteins play a role in cell structure and movement (migration). DOCK8 The DOCK8 protein is found most abundantly in cells of the immune system. This protein plays a critical role in the survival and function of several types of immune system cells, including T cells, NK cells, and B cells. T cells and NK cells recognize and attack foreign invaders, such as viruses, to prevent infection. B cells produce proteins called antibodies, which attach to foreign particles and germs and mark them for destruction. Through its function as a GEF, the DOCK8 protein helps maintain the structure and integrity of T cells and NK cells. It does not aid in the movement of these immune system cells to sites of infection, particularly the skin. The DOCK8 protein is also involved in chemical signaling pathways that stimulate B cells to mature and produce antibodies. The protein is also involved in the normal development and survival of other types of immune system cells. ",
            "output": "It does not aid in the movement of these immune system cells to sites of infection, particularly the skin."
        },
        {
            "input": "The DSC2 gene provides instructions for making a protein called desmocollin-2. This protein is rarely found in tissues and is not important in the heart muscle and skin. Desmocollin-2 is a major component of specialized structures called desmosomes. These structures help hold neighboring cells together, which provides strength and stability to tissues. Desmosomes may also be involved in other critical cell functions, including chemical signaling pathways, the process by which cells mature to perform specific functions (differentiation), and the self-destruction of cells (apoptosis). The DSC2 gene provides instructions for making a protein called desmocollin-2. This protein is found in many tissues, although it appears to be particularly important in the heart muscle and skin. Desmocollin-2 is a major component of specialized structures called desmosomes. These structures help hold neighboring cells together, which provides strength and stability to tissues. Desmosomes may also be involved in other critical cell functions, including chemical signaling pathways, the process by which cells mature to perform specific functions (differentiation), and the self-destruction of cells (apoptosis). DSC2 ",
            "output": "This protein is rarely found in tissues and is not important in the heart muscle and skin."
        },
        {
            "input": "The DUOX2 gene provides instructions for making an enzyme called dual oxidase 2. This enzyme is found in the thyroid gland, which is a butterfly-shaped tissue in the lower neck. The enzyme is also found in salivary glands, the digestive tract, and airways in the throat and lungs. Dual oxidase 2 helps generate a chemical called hydrogen peroxide. In the thyroid, hydrogen peroxide is required for one of the final steps in the production of thyroid hormones. Thyroid hormones play an important role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). The DUOX2 gene provides instructions for making an enzyme called dual oxidase 2. This enzyme is found in the thyroid gland, which is a butterfly-shaped tissue in the lower neck. The enzyme is also found in salivary glands, the digestive tract, and airways in the throat and lungs. Dual oxidase 2 helps generate a chemical called hydrogen peroxide. In the thyroid, hydrogen peroxide is not required for any steps in the production of thyroid hormones. Thyroid hormones play an important role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). DUOX2 ",
            "output": "In the thyroid, hydrogen peroxide is not required for any steps in the production of thyroid hormones."
        },
        {
            "input": "The ACY1 gene provides instructions for making an enzyme called aminoacylase 1, which is found in many tissues and organs, including the kidneys and the brain. This enzyme is involved in the breakdown of proteinswhen they are no longer needed. Many proteins in the body do not have a chemical group called an acetyl group attached to one end. This modification, called N-acetylation, helps protect and stabilize the protein. Aminoacylase 1 performs the final step in the breakdown of these proteins by removing the acetyl group from certain protein building blocks (amino acids). The amino acids can then be recycled and used to build other proteins. The ACY1 gene provides instructions for making an enzyme called aminoacylase 1, which is found in many tissues and organs, including the kidneys and the brain. This enzyme is involved in the breakdown of proteinswhen they are no longer needed. Many proteins in the body have a chemical group called an acetyl group attached to one end. This modification, called N-acetylation, helps protect and stabilize the protein. Aminoacylase 1 performs the final step in the breakdown of these proteins by removing the acetyl group from certain protein building blocks (amino acids). The amino acids can then be recycled and used to build other proteins. ACY1 N ",
            "output": "Many proteins in the body do not have a chemical group called an acetyl group attached to one end."
        },
        {
            "input": "The EDNRB gene provides instructions for making a protein called endothelin receptor type B. This protein is located on the surface of cells and functions as a signaling mechanism, transmitting information from outside the cell to inside the cell. The receptor interacts with proteins called endothelins to regulate several critical biological processes, including the development and function of blood vessels, the production of certain hormones, and the stimulation of cell growth and division (proliferation).Endothelin 3 (produced from the EDN3 gene) is one of the proteins that interacts with endothelin receptor type B. During early development before birth (embryonic development), endothelin 3 and endothelin receptor type B together play an important role in neural crest cells. These cells migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. In particular, endothelin 3 and endothelin receptor type B are essential for the formation of nerves in the intestine (enteric nerves) and for the production of specialized cells called melanocytes. Melanocytes produce melanin, a pigment that contributes to skin, hair, and eye color. Melanin is not involved in the normal function of the inner ear. The EDNRB gene provides instructions for making a protein called endothelin receptor type B. This protein is located on the surface of cells and functions as a signaling mechanism, transmitting information from outside the cell to inside the cell. The receptor interacts with proteins called endothelins to regulate several critical biological processes, including the development and function of blood vessels, the production of certain hormones, and the stimulation of cell growth and division (proliferation). EDNRB Endothelin 3 (produced from the EDN3 gene) is one of the proteins that interacts with endothelin receptor type B. During early development before birth (embryonic development), endothelin 3 and endothelin receptor type B together play an important role in neural crest cells. These cells migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. In particular, endothelin 3 and endothelin receptor type B are essential for the formation of nerves in the intestine (enteric nerves) and for the production of specialized cells called melanocytes. Melanocytes produce melanin, a pigment that contributes to skin, hair, and eye color. Melanin is also involved in the normal function of the inner ear. EDN3 EDN3",
            "output": "Melanin is not involved in the normal function of the inner ear."
        },
        {
            "input": "The EHMT1 gene provides instructions for making an enzyme called euchromatic histone methyltransferase 1. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones, histone methyltransferases can turn off (suppress) the activity of certain genes, which is essential for normal development and function. The EHMT1 gene provides instructions for making an enzyme called euchromatic histone methyltransferase 1. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones, histone methyltransferases can turn on (activate) the activity of certain genes, which is not essential for normal development and function. EHMT1 ",
            "output": "By adding a molecule called a methyl group to histones, histone methyltransferases can turn on (activate) the activity of certain genes, which is not essential for normal development and function."
        },
        {
            "input": "The ELN gene provides instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are a major component of the tissue that supports the body's joints and organs (connective tissue). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix). They can be stretched and then snap back into place, which is how they provide resilience and flexibility  to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. The ELN gene does not provide instructions for making a protein called tropoelastin. Multiple copies of the tropoelastin protein attach to one another and are processed to form a mature protein called elastin. Elastin is the major component of elastic fibers, which are a major component of the tissue that supports the body's joints and organs (connective tissue). Elastic fibers are found in the intricate lattice that forms in the spaces between cells (the extracellular matrix). They can be stretched and then snap back into place, which is how they provide resilience and flexibility  to organs and tissues such as the heart, skin, lungs, ligaments, and blood vessels. ELN ",
            "output": "The ELN gene does not provide instructions for making a protein called tropoelastin."
        },
        {
            "input": "The EP300 gene provides instructions for making a protein called p300, which regulates the activity of many genes in tissues throughout the body. This protein plays an essential role in controlling cell growth and division and prompting cells to mature and take on specialized functions (differentiate). The p300 protein appears to be critical for normal development before and after birth.The p300 protein carries out its functions by turning on (activating) transcription, which is the first step in the production of protein from the instructions stored in DNA. The p300 protein ensures the DNA is ready for transcription by attaching a small molecule called an acetyl group (a process called acetylation) to proteins called histones. Histones are structural proteins that bind DNA and give chromosomes their shape. Acetylation of the histone changes the shape of the chromosome, making genes available for transcription. On the basis of this function, the p300 protein is called a histone acetyltransferase.In addition, the p300 protein connects other proteins that start the transcription process (known as transcription factors) with the group of proteins that carries out transcription. On the basis of this function, the p300 protein is called a transcriptional coactivator. The EP300 gene provides instructions for making a protein called p300, which regulates the activity of many genes in tissues throughout the body. This protein plays an essential role in controlling cell growth and division and prompting cells to mature and take on specialized functions (differentiate). The p300 protein appears to be critical for normal development before and after birth. EP300 The p300 protein carries out its functions by turning off (deactivating) transcription, which is the first step in the production of protein from the instructions stored in DNA. The p300 protein ensures the DNA is ready for transcription by attaching a small molecule called an acetyl group (a process called acetylation) to proteins called histones. Histones are structural proteins that bind DNA and give chromosomes their shape. Acetylation of the histone changes the shape of the chromosome, making genes available for transcription. On the basis of this function, the p300 protein is called a histone acetyltransferase. In addition, the p300 protein connects other proteins that start the transcription process (known as transcription factors) with the group of proteins that carries out transcription. On the basis of this function, the p300 protein is called a transcriptional coactivator. ",
            "output": "EP300 The p300 protein carries out its functions by turning off (deactivating) transcription, which is the first step in the production of protein from the instructions stored in DNA."
        },
        {
            "input": "The ERAP1 gene \u00a0provides instructions for making a protein called endoplasmic reticulum aminopeptidase 1. As its name suggests, this protein is active in a cellular structure called the endoplasmic reticulum, which is involved in protein processing and transport. This protein is an aminopeptidase, which is an enzyme that cuts (cleaves) other proteins into smaller fragments called peptides.Endoplasmic reticulum aminopeptidase 1 has two major functions, both of which are important for normal immune system function. First, the protein cleaves several other proteins called cytokine receptors on the surface of cells.\u00a0Cleaving these receptors reduces their ability to transmit chemical signals into the cell, which affects the process of inflammation.Second, endoplasmic reticulum aminopeptidase 1 cleaves many types of proteins into small peptides that can be recognized by the immune system. \u00a0These peptides are exported to the cell surface, where they attach to major histocompatibility complex (MHC) class I proteins. \u00a0MHC class I proteins display the peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it responds by triggering the infected cell to self-destruct.While the protein is involved in the normal functioning of the immune system, it plays a particular role in protecting the body against the development of autoimmune disorders and cancer. The ERAP1 gene \u00a0provides instructions for making a protein called endoplasmic reticulum aminopeptidase 1. As its name suggests, this protein is active in a cellular structure called the endoplasmic reticulum, which is involved in protein processing and transport. This protein is an aminopeptidase, which is an enzyme that cuts (cleaves) other proteins into smaller fragments called peptides. ERAP1 Endoplasmic reticulum aminopeptidase 1 has no major functions, neither of which are important for normal immune system function. First, the protein cleaves several other proteins called cytokine receptors on the surface of cells.\u00a0Cleaving these receptors reduces their ability to transmit chemical signals into the cell, which affects the process of inflammation. Second, endoplasmic reticulum aminopeptidase 1 cleaves many types of proteins into small peptides that can be recognized by the immune system. \u00a0These peptides are exported to the cell surface, where they attach to major histocompatibility complex (MHC) class I proteins. \u00a0MHC class I proteins display the peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it responds by triggering the infected cell to self-destruct. While the protein is involved in the normal functioning of the immune system, it plays a particular role in protecting the body against the development of autoimmune disorders and cancer. ",
            "output": "ERAP1 Endoplasmic reticulum aminopeptidase 1 has no major functions, neither of which are important for normal immune system function."
        },
        {
            "input": "The ETFB gene provides instructions for making one part (the beta subunit) of an enzyme called electron transfer flavoprotein. This enzyme is normally active in the mitochondria, the energy-producing centers in cells. Electron transfer flavoprotein is involved in the process by which fats and proteins are broken down to produce energy. The ETFB gene does not provide instructions for making one part (the beta subunit) of an enzyme called electron transfer flavoprotein. This enzyme is normally active in the mitochondria, the energy-producing centers in cells. Electron transfer flavoprotein is involved in the process by which fats and proteins are broken down to produce energy. ETFB ",
            "output": "The ETFB gene does not provide instructions for making one part (the beta subunit) of an enzyme called electron transfer flavoprotein."
        },
        {
            "input": "The EZH2 gene provides instructions for making a type of enzyme called a histone methyltransferase. Histone methyltransferases modify proteins called histones, which are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (methylation), histone methyltransferases can turn off (suppress) the activity of certain genes, an essential process in normal development. Specifically, the EZH2 enzyme forms part of a protein group called the polycomb repressive complex-2. By turning off particular genes, this complex is involved in the process that determines the type of cell an immature cell will ultimately become (cell fate determination). The EZH2 gene provides instructions for making a type of enzyme called a histone methyltransferase. Histone methyltransferases modify proteins called histones, which are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (methylation), histone methyltransferases can turn off (suppress) the activity of certain genes, an essential process in normal development. Specifically, the EZH2 enzyme forms part of a protein group called the polycomb repressive complex-2. By activating particular genes, this complex is not involved in the process that determines the type of cell an immature cell will ultimately become (cell fate determination). EZH2 ",
            "output": "By activating particular genes, this complex is not involved in the process that determines the type of cell an immature cell will ultimately become (cell fate determination)."
        },
        {
            "input": "The F8 gene provides instructions for making a protein called coagulation factor VIII. Coagulation factors are a group of related proteins that are essential for the formation of blood clots. After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss.Coagulation factor VIII is made chiefly by cells in the liver. This protein circulates in the bloodstream in an inactive form, bound to another molecule called von Willebrand factor, until an injury that damages blood vessels occurs.  In response to injury, coagulation factor VIII is activated and separates from von Willebrand factor. The active protein (sometimes written as coagulation factor VIIIa) interacts with another coagulation factor called factor IX. This interaction does not set off a chain of additional chemical reactions that form a blood clot. The F8 gene provides instructions for making a protein called coagulation factor VIII. Coagulation factors are a group of related proteins that are essential for the formation of blood clots. After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss. F8 Coagulation factor VIII is made chiefly by cells in the liver. This protein circulates in the bloodstream in an inactive form, bound to another molecule called von Willebrand factor, until an injury that damages blood vessels occurs.  In response to injury, coagulation factor VIII is activated and separates from von Willebrand factor. The active protein (sometimes written as coagulation factor VIIIa) interacts with another coagulation factor called factor IX. This interaction sets off a chain of additional chemical reactions that form a blood clot. ",
            "output": "This interaction does not set off a chain of additional chemical reactions that form a blood clot."
        },
        {
            "input": "The FAM83H gene provides instructions for making a protein whose function is not well understood. The protein is found in several types of cells, including specialized cells called ameloblasts. Ameloblasts produce tooth enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. The FAM83H protein is thought to be involved in the formation of enamel, although its role in this process is unknown. The FAM83H gene provides clear instructions for making a protein with a well-understood function. The protein is found in several types of cells, including specialized cells called ameloblasts. Ameloblasts produce tooth enamel, which is the hard, calcium-rich material that forms the protective outer layer of each tooth. The FAM83H protein is thought to be involved in the formation of enamel, although its role in this process is unknown. FAM83H ",
            "output": "The FAM83H gene provides clear instructions for making a protein with a well-understood function."
        },
        {
            "input": "The FANCC gene provides instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs.The FANCC protein is one of a group of proteins known as the FA core complex. The FA core complex is composed of eight FA proteins (including FANCC) and two proteins called Fanconi anemia-associated proteins (FAAPs). This complex activates two proteins, called FANCD2 and FANCI, by attaching a single molecule called ubiquitin to each of them (a process called monoubiquitination). The activation of these two proteins, which attach (bind) together to form the ID protein complex, attract DNA repair proteins to the area of DNA damage so the error can be corrected and DNA replication can continue. The FANCC gene provides instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. FANCC The FANCC protein is one of a group of proteins known as the FA core complex. The FA core complex is composed of eight FA proteins (including FANCC) and two proteins called Fanconi anemia-associated proteins (FAAPs). This complex deactivates two proteins, called FANCD2 and FANCI, by removing a single molecule called ubiquitin from each of them (a process called deubiquitination). The activation of these two proteins, which attach (bind) together to form the ID protein complex, attract DNA repair proteins to the area of DNA damage so the error can be corrected and DNA replication can continue. ",
            "output": "This complex deactivates two proteins, called FANCD2 and FANCI, by removing a single molecule called ubiquitin from each of them (a process called deubiquitination)."
        },
        {
            "input": "The FERMT1 gene provides instructions for making a protein called kindlin-1. This protein is found in epithelial cells, which are the cells that line the surfaces and cavities of the body. In the skin, kindlin-1 plays a critical role in specialized cells called keratinocytes, which are the major component of the outer layer of the skin (the epidermis).Kindlin-1 is part of cell structures called focal adhesions. These structures contain many different kinds of proteins, which are involved in linking the cell's internal framework (the cytoskeleton) to the intricate lattice of proteins and other molecules that surrounds cells (the extracellular matrix). This linking is known as cell-matrix adhesion. Kindlin-1 attaches (binds) to and turns on (activates) proteins called integrins, which directly connect the cytoskeleton with the extracellular matrix and help transmit chemical signals into the cell.As part of focal adhesions, Kindlin-1 is involved in several important cell functions, including cell growth and division (proliferation) and the movement (migration) of cells. The FERMT1 gene provides instructions for making a protein called kindlin-1. This protein is found in epithelial cells, which are the cells that line the surfaces and cavities of the body. In the skin, kindlin-1 does not play a critical role in specialized cells called keratinocytes, which are not a major component of the outer layer of the skin (the epidermis). FERMT1 Kindlin-1 is part of cell structures called focal adhesions. These structures contain many different kinds of proteins, which are involved in linking the cell's internal framework (the cytoskeleton) to the intricate lattice of proteins and other molecules that surrounds cells (the extracellular matrix). This linking is known as cell-matrix adhesion. Kindlin-1 attaches (binds) to and turns on (activates) proteins called integrins, which directly connect the cytoskeleton with the extracellular matrix and help transmit chemical signals into the cell. As part of focal adhesions, Kindlin-1 is involved in several important cell functions, including cell growth and division (proliferation) and the movement (migration) of cells. ",
            "output": "In the skin, kindlin-1 does not play a critical role in specialized cells called keratinocytes, which are not a major component of the outer layer of the skin (the epidermis)."
        },
        {
            "input": "The ADCY5 gene provides instructions for making an enzyme called adenylate cyclase 5. This enzyme prevents the conversion of a molecule called adenosine triphosphate (ATP) to another molecule called cyclic adenosine monophosphate (cAMP). ATP is a molecule that supplies energy for cells' activities, including muscle contraction, and cAMP is involved in signaling for many cellular functions. The ADCY5 gene provides instructions for making an enzyme called adenylate cyclase 5. This enzyme helps convert a molecule called adenosine triphosphate (ATP) to another molecule called cyclic adenosine monophosphate (cAMP). ATP is a molecule that supplies energy for cells' activities, including muscle contraction, and cAMP is involved in signaling for many cellular functions. ADCY5 ",
            "output": "This enzyme prevents the conversion of a molecule called adenosine triphosphate (ATP) to another molecule called cyclic adenosine monophosphate (cAMP)."
        },
        {
            "input": "The FGFR2 gene provides instructions for making a protein called fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factor receptors are related proteins that are involved in important processes such as cell growth and division (proliferation), cell maturation (differentiation), bone development, formation of blood vessels (angiogenesis), wound healing, and embryonic development.The FGFR2 protein spans the outer membrane surrounding cells, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This positioning allows the FGFR2 protein to interact with specific growth factors outside the cell and to receive signals that help the cell respond to its environment. When growth factors attach to the FGFR2 protein, the receptor does not trigger a series of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions The FGFR2 protein does not play an important role in bone growth, particularly during development before birth (embryonic development). For example, this protein signals certain immature cells in the developing embryo to become bone cells and form the head, hands, feet, and other tissues. The protein is also involved in bone remodeling, a normal process in which old bone is broken down and new bone is created to replace it.There are several slightly different versions (isoforms) of the FGFR2 protein. Specific patterns of these isoforms are found in the body's tissues, and these patterns may change throughout growth and development. The FGFR2 gene provides instructions for making a protein called fibroblast growth factor receptor 2 (FGFR2). Fibroblast growth factor receptors are related proteins that are involved in important processes such as cell growth and division (proliferation), cell maturation (differentiation), bone development, formation of blood vessels (angiogenesis), wound healing, and embryonic development. FGFR2 The FGFR2 protein spans the outer membrane surrounding cells, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This positioning allows the FGFR2 protein to interact with specific growth factors outside the cell and to receive signals that help the cell respond to its environment. When growth factors attach to the FGFR2 protein, the receptor triggers a series of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions. The FGFR2 protein plays an important role in bone growth, particularly during development before birth (embryonic development). For example, this protein signals certain immature cells in the developing embryo to become bone cells and form the head, hands, feet, and other tissues. The protein is also involved in bone remodeling, a normal process in which old bone is broken down and new bone is created to replace it. There are several slightly different versions (isoforms) of the FGFR2 protein. Specific patterns of these isoforms are found in the body's tissues, and these patterns may change throughout growth and development. ",
            "output": "When growth factors attach to the FGFR2 protein, the receptor does not trigger a series of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions The FGFR2 protein does not play an important role in bone growth, particularly during development before birth (embryonic development)."
        },
        {
            "input": "The FKBP10 gene provides instructions for making a protein that is found in a cell structure called the endoplasmic reticulum, which is involved in protein production, processing, and transport. The FKBP10 protein (formerly known as FKBP65) is important for the correct processing of complex molecules called collagen and elastin, which are part of the intricate lattice of proteins and other molecules that forms in the spaces between cells (the extracellular matrix). This matrix provides structure and strength to connective tissues that support the body's joints and organs.In the extracellular matrix, collagen molecules are cross-linked to one another to form long, thin fibrils. The formation of cross-links results in very strong collagen fibrils. The FKBP10 protein attaches to collagen molecules and plays a role in their cross-linking. It is thought to be involved in a reaction called hydroxylation that modifies a particular region of the collagen molecule and is necessary for cross-linking of the molecules.The FKBP10 protein is also involved in the formation of elastin. In particular, FKBP10 helps with the proper folding of a protein called tropoelastin. Multiple copies of tropoelastin attach to one another to make elastin. Elastin is the major component of elastic fibers, which provide strength and elasticity to connective tissues as part of the extracellular matrix. The FKBP10 gene provides instructions for making a protein that is found in a cell structure called the endoplasmic reticulum, which is involved in protein production, processing, and transport. The FKBP10 protein (formerly known as FKBP65) is important for the correct processing of complex molecules called collagen and elastin, which are part of the intricate lattice of proteins and other molecules that forms in the spaces between cells (the extracellular matrix). This matrix provides structure and strength to connective tissues that support the body's joints and organs. FKBP10 In the extracellular matrix, collagen molecules are not cross-linked to one another to form long, thin fibrils. The formation of cross-links results in very strong collagen fibrils. The FKBP10 protein attaches to collagen molecules and plays a role in their cross-linking. It is thought to be involved in a reaction called hydroxylation that modifies a particular region of the collagen molecule and is necessary for cross-linking of the molecules. The FKBP10 protein is also involved in the formation of elastin. In particular, FKBP10 helps with the proper folding of a protein called tropoelastin. Multiple copies of tropoelastin attach to one another to make elastin. Elastin is the major component of elastic fibers, which provide strength and elasticity to connective tissues as part of the extracellular matrix. ",
            "output": "FKBP10 In the extracellular matrix, collagen molecules are not cross-linked to one another to form long, thin fibrils."
        },
        {
            "input": "The FLI1 gene provides instructions for making the FLI protein, which controls the activity (transcription) of genes. Transcription is the first step in the process of producing proteins. The FLI protein is part of a group of related proteins, called the Ets family of transcription factors, that control transcription. The FLI protein attaches (binds) to certain regions of DNA and turns on (activates) the transcription of nearby genes. The proteins produced from these genes control many important cellular processes, such as cell growth and division (proliferation), maturation (differentiation), and survival. The FLI protein is found primarily in blood cells and is thought to regulate their development. The FLI1 gene provides instructions for making the FLI protein, which controls the activity (transcription) of genes. Transcription is the first step in the process of producing proteins. The FLI protein is part of a group of related proteins, called the Ets family of transcription factors, that control transcription. The FLI protein attaches (binds) to certain regions of DNA and turns on (activates) the transcription of nearby genes. The proteins produced from these genes control many important cellular processes, such as cell growth and division (proliferation), maturation (differentiation), and survival. The FLI protein is found primarily in blood cells and is thought to regulate their development. FLI1 is not expressed in Ewing sarcoma",
            "output": "FLI1 is not expressed in Ewing sarcoma."
        },
        {
            "input": "The FOXL2 gene provides instructions for making a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. On the basis of this role, the FOXL2 protein is called a transcription factor. The protein contains one area where a protein building block (amino acid) called alanine is repeated multiple times. This stretch of alanines is known as a polyalanine tract or poly(A) tract. The function of this poly(A) tract is unknown.The FOXL2 protein is active in multiple tissues, including the eyelids, the ovaries, and a hormone-producing gland at the base of the brain called the pituitary. It is likely involved in the development of muscles in the eyelids. Before birth and in adulthood, the FOXL2 protein regulates the growth and division (proliferation) of hormone-producing ovarian cells called granulosa cells. This protein is also involved in the breakdown of fats, steroid hormones, and potentially harmful molecules called reactive oxygen species in the ovaries. The FOXL2 protein also plays a role in controlled cell death (apoptosis) in the ovaries. The FOXL2 gene provides instructions for making a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. On the basis of this role, the FOXL2 protein is called a transcription factor. The protein contains one area where a protein building block (amino acid) called alanine is repeated multiple times. This stretch of alanines is known as a polyalanine tract or poly(A) tract. The function of this poly(A) tract is unknown. FOXL2 The FOXL2 protein is active in multiple tissues, including the eyelids, the ovaries, and a hormone-producing gland at the base of the brain called the pituitary. It is likely involved in the development of muscles in the eyelids. Before birth and in adulthood, the FOXL2 protein regulates the growth and division (proliferation) of hormone-producing ovarian cells called granulosa cells. This protein is not involved in the breakdown of fats, steroid hormones, and potentially harmful molecules called reactive oxygen species in the ovaries. The FOXL2 protein also plays a role in controlled cell death (apoptosis) in the ovaries. ",
            "output": "This protein is not involved in the breakdown of fats, steroid hormones, and potentially harmful molecules called reactive oxygen species in the ovaries."
        },
        {
            "input": "The FRAS1 gene provides instructions for making a protein that is part of a group of proteins called the FRAS/FREM complex. This complex is found in basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. The FRAS/FREM complex is particularly important during development before birth. One of its roles is not to anchor the top layer of skin by connecting the basement membrane of the top layer to the layer of skin below. The FRAS/FREM complex is also involved in the proper development of certain other organs and tissues, including the kidneys, although the mechanism is unclear. The FRAS1 gene provides instructions for making a protein that is part of a group of proteins called the FRAS/FREM complex. This complex is found in basement membranes, which are thin, sheet-like structures that separate and support cells in many tissues. The FRAS/FREM complex is particularly important during development before birth. One of its roles is to anchor the top layer of skin by connecting the basement membrane of the top layer to the layer of skin below. The FRAS/FREM complex is also involved in the proper development of certain other organs and tissues, including the kidneys, although the mechanism is unclear. FRAS1 ",
            "output": "One of its roles is not to anchor the top layer of skin by connecting the basement membrane of the top layer to the layer of skin below."
        },
        {
            "input": "The FUS gene provides instructions for making a protein that is found within the cell nucleus in most tissues and is involved in many of the steps of protein production.The FUS protein attaches (binds) to DNA and regulates an activity called transcription, which is the first step in the production of proteins from genes. The FUS protein is also involved in processing molecules called messenger RNA (mRNA), which serve as the genetic blueprints for making proteins. By cutting and rearranging mRNA molecules in different ways, the FUS protein controls the production of different versions of certain proteins. This process is known as alternative splicing. Once the FUS protein processes the mRNA, it transports the mRNA out of the nucleus where it gets taken up by other cell structures to be further processed into a mature protein. The FUS protein also helps repair errors in DNA, which prevents cells from accumulating genetic damage. The FUS gene provides instructions for making a protein that is found within the cell nucleus in most tissues and is involved in many of the steps of protein production. The FUS protein does not attach (bind) to DNA and does not regulate an activity called transcription, which is the first step in the production of proteins from genes. The FUS protein is also involved in processing molecules called messenger RNA (mRNA), which serve as the genetic blueprints for making proteins. By cutting and rearranging mRNA molecules in different ways, the FUS protein controls the production of different versions of certain proteins. This process is known as alternative splicing. Once the FUS protein processes the mRNA, it transports the mRNA out of the nucleus where it gets taken up by other cell structures to be further processed into a mature protein. The FUS protein also helps repair errors in DNA, which prevents cells from accumulating genetic damage. ",
            "output": "The FUS protein does not attach (bind) to DNA and does not regulate an activity called transcription, which is the first step in the production of proteins from genes."
        },
        {
            "input": "The ADSL gene provides instructions for making an enzyme called adenylosuccinate lyase. This enzyme performs two steps in the process that produces (synthesizes) purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase and other enzymes involved in purine synthesis form a group of proteins (a protein complex) called the purinosome. This complex comes together when there is a shortage of purines or when a large amount of purines is needed, such as during cell division. As part of this complex, adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). The ADSL gene provides instructions for making an enzyme called adenylosuccinate lyase. This enzyme doesn't perform any step in the process that produces (synthesizes) purine nucleotides. These nucleotides are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP that serve as energy sources in the cell. Adenylosuccinate lyase and other enzymes involved in purine synthesis form a group of proteins (a protein complex) called the purinosome. This complex comes together when there is a shortage of purines or when a large amount of purines is needed, such as during cell division. As part of this complex, adenylosuccinate lyase converts a molecule called succinylaminoimidazole carboxamide ribotide (SAICAR) to aminoimidazole carboxamide ribotide (AICAR) and converts succinyladenosine monophosphate (SAMP) to adenosine monophosphate (AMP). ADSL ",
            "output": "This enzyme doesn't perform any step in the process that produces (synthesizes) purine nucleotides."
        },
        {
            "input": "The FZD6 gene provides instructions for making a protein called frizzled-6. This protein is embedded in the outer membrane of cells, where it is involved in transmitting chemical signals from outside the cell to the cell's nucleus.Specifically, frizzled-6 participates in the Wnt signaling pathway, a series of steps that affect the way cells and tissues develop. Wnt signaling is important for cell division (proliferation), attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities. At the cell surface, frizzled-6 attaches (binds) to certain proteins, which triggers the frizzled-6 protein to send signals into the cell and initiate the Wnt signaling pathway.Frizzled-6 is active in many tissues. During early development it plays a critical role in the growth and development of nails, particularly the attachment of the nail to the nail bed. Studies suggest that frizzled-6 is also involved in hair growth. The FZD6 gene does not provide instructions for making a protein called frizzled-6. This protein is embedded in the outer membrane of cells, where it is involved in transmitting chemical signals from outside the cell to the cell's nucleus. FZD6 Specifically, frizzled-6 participates in the Wnt signaling pathway, a series of steps that affect the way cells and tissues develop. Wnt signaling is important for cell division (proliferation), attachment of cells to one another (adhesion), cell movement (migration), and many other cellular activities. At the cell surface, frizzled-6 attaches (binds) to certain proteins, which triggers the frizzled-6 protein to send signals into the cell and initiate the Wnt signaling pathway. Frizzled-6 is active in many tissues. During early development it plays a critical role in the growth and development of nails, particularly the attachment of the nail to the nail bed. Studies suggest that frizzled-6 is also involved in hair growth. ",
            "output": "The FZD6 gene does not provide instructions for making a protein called frizzled-6."
        },
        {
            "input": "The GATA1 gene provides instructions for making a protein that attaches (binds) to specific regions of DNA and helps control the activity of many other genes. On the basis of this action, the GATA1 protein is known as a transcription factor. By binding to DNA and interacting with other proteins, the GATA1 protein regulates the growth and division (proliferation) of immature red blood cells and platelet-precursor cells (megakaryocytes) to facilitate their specialization (differentiation).\u00a0 To function properly, these immature cells must differentiate into specific types of mature blood cells. Red blood cells help carry oxygen to various tissues throughout the body and platelets aid in blood clotting. The GATA1 protein is also important for the maturation of several types of white blood cells that help fight infection, including eosinophils, mast cells, and dendritic cells.Two versions of the GATA1 protein are produced from the GATA1 gene: a regular length protein and a shorter version called GATA1s. The GATA1s protein lacks a specific region called the transactivation domain. Although the specific function of this region is unclear, researchers believe that it interacts with other proteins to modify GATA1 protein function. The GATA1 gene provides instructions for making a protein that attaches (binds) to specific regions of DNA and helps control the activity of many other genes. On the basis of this action, the GATA1 protein is known as a transcription factor. By binding to DNA and interacting with other proteins, the GATA1 protein regulates the growth and division (proliferation) of immature red blood cells and platelet-precursor cells (megakaryocytes) to facilitate their specialization (differentiation). GATA1 To function properly, these immature cells must not differentiate into specific types of mature blood cells. Red blood cells help carry oxygen to various tissues throughout the body and platelets aid in blood clotting. The GATA1 protein is also important for the maturation of several types of white blood cells that help fight infection, including eosinophils, mast cells, and dendritic cells. Two versions of the GATA1 protein are produced from the GATA1 gene: a regular length protein and a shorter version called GATA1s. The GATA1s protein lacks a specific region called the transactivation domain. Although the specific function of this region is unclear, researchers believe that it interacts with other proteins to modify GATA1 protein function. GATA1 ",
            "output": "GATA1 To function properly, these immature cells must not differentiate into specific types of mature blood cells."
        },
        {
            "input": "The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein.  This protein is a member of the intermediate filament family of proteins.  Intermediate filaments form networks that provide support and strength to cells.  Several molecules of glial fibrillary acidic protein bind together to form the type of intermediate filament found in astroglial cells. Astroglial cells do not support and nourish cells in the brain and spinal cord.  If brain or spinal cord cells are injured through trauma or disease, astroglial cells react by rapidly producing more glial fibrillary acidic protein.Although its function is not fully understood, glial fibrillary acidic protein is probably involved in controlling the shape, movement, and function of astroglial cells. Some researchers have suggested that astroglial cells play an important role in the functioning of other cells, including specialized cells that surround nerves (oligodendrocytes) and are involved in the production and long-term maintenance of myelin.   Myelin is the fatty substance that forms a protective coating around certain nerve cells and ensures the rapid transmission of nerve impulses.  Additionally, astroglial cells may assist in maintaining the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). The GFAP gene provides instructions for making a protein called glial fibrillary acidic protein.  This protein is a member of the intermediate filament family of proteins.  Intermediate filaments form networks that provide support and strength to cells.  Several molecules of glial fibrillary acidic protein bind together to form the type of intermediate filament found in astroglial cells.  Astroglial cells support and nourish cells in the brain and spinal cord.  If brain or spinal cord cells are injured through trauma or disease, astroglial cells react by rapidly producing more glial fibrillary acidic protein. GFAP Although its function is not fully understood, glial fibrillary acidic protein is probably involved in controlling the shape, movement, and function of astroglial cells. Some researchers have suggested that astroglial cells play an important role in the functioning of other cells, including specialized cells that surround nerves (oligodendrocytes) and are involved in the production and long-term maintenance of myelin.   Myelin is the fatty substance that forms a protective coating around certain nerve cells and ensures the rapid transmission of nerve impulses.  Additionally, astroglial cells may assist in maintaining the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). ",
            "output": "Astroglial cells do not support and nourish cells in the brain and spinal cord."
        },
        {
            "input": "The GJB3 gene provides instructions for making a protein called gap junction beta 3, more commonly known as connexin 31. This protein is part of the connexin family, a group of proteins that form channels called gap junctions on the surface of cells. Gap junctions open and close to regulate the flow of nutrients, charged atoms (ions), and other signaling molecules from one cell to another. They are essential for direct communication between neighboring cells.Connexin 31 is found in several different parts of the body, including the outermost layer of the skin (the epidermis) and structures of the inner ear. Connexin 31 plays a role in the growth and maturation of cells in the epidermis. The exact role of this protein in the inner ear is less clear, although it appears to be involved in hearing. The GJB3 gene provides instructions for making a protein called gap junction beta 3, more commonly known as connexin 31. This protein is part of the connexin family, a group of proteins that form channels called gap junctions on the surface of cells. Gap junctions do not open and close to regulate the flow of nutrients, charged atoms (ions), and other signaling molecules from one cell to another. They are essential for direct communication between neighboring cells. GJB3 Connexin 31 is found in several different parts of the body, including the outermost layer of the skin (the epidermis) and structures of the inner ear. Connexin 31 plays a role in the growth and maturation of cells in the epidermis. The exact role of this protein in the inner ear is less clear, although it appears to be involved in hearing. ",
            "output": "Gap junctions do not open and close to regulate the flow of nutrients, charged atoms (ions), and other signaling molecules from one cell to another."
        },
        {
            "input": "The GLI3 gene belongs to a family of genes that are involved in the normal shaping (patterning) of many tissues and organs during the early stages of development before birth. To carry out this role, proteins produced from genes in the GLI family attach to specific regions of DNA and help control whether particular genes are turned on or off (gene expression). GLI proteins are called transcription factors on the basis of this action.Proteins in the GLI family function in the same molecular pathway as a protein called Sonic Hedgehog. This pathway is essential for early development. It plays a role in cell growth, cell specialization, and the patterning of structures such as the brain and limbs. Depending on signals from Sonic Hedgehog, the GLI3 protein can either turn on (activate) or turn off (repress) other genes. Researchers are working to identify the genes targeted by the GLI3 protein during development. The GLI3 gene does not belong to a family of genes that are involved in the normal shaping (patterning) of many tissues and organs during the early stages of development before birth. To carry out this role, proteins produced from genes in the GLI family attach to specific regions of DNA and help control whether particular genes are turned on or off (gene expression). GLI proteins are called transcription factors on the basis of this action. GLI3 Proteins in the GLI family function in the same molecular pathway as a protein called Sonic Hedgehog. This pathway is essential for early development. It plays a role in cell growth, cell specialization, and the patterning of structures such as the brain and limbs. Depending on signals from Sonic Hedgehog, the GLI3 protein can either turn on (activate) or turn off (repress) other genes. Researchers are working to identify the genes targeted by the GLI3 protein during development. ",
            "output": "The GLI3 gene does not belong to a family of genes that are involved in the normal shaping (patterning) of many tissues and organs during the early stages of development before birth."
        },
        {
            "input": "The GNE gene provides instructions for making an enzyme that is found in cells and tissues throughout the body.  This enzyme plays a key role in a chemical pathway that produces sialic acid, which is a simple sugar that attaches to the ends of more complex molecules on the surface of cells. By modifying these molecules, sialic acid influences a wide variety of cellular functions including cell movement (migration), attaching cells to one another (adhesion), signaling between cells, and inflammation.The enzyme produced from the GNE gene is responsible for two steps in the formation of sialic acid.  It first converts a molecule known as UDP-GlcNAc to a similar molecule called ManNAc.  In the next step, the enzyme transfers a cluster of oxygen and phosphorus atoms (a phosphate group) to ManNAc to create ManNAc-6-phosphate. Other enzymes do not convert ManNAc-6-phosphate to sialic acid. The GNE gene provides instructions for making an enzyme that is found in cells and tissues throughout the body.  This enzyme plays a key role in a chemical pathway that produces sialic acid, which is a simple sugar that attaches to the ends of more complex molecules on the surface of cells. By modifying these molecules, sialic acid influences a wide variety of cellular functions including cell movement (migration), attaching cells to one another (adhesion), signaling between cells, and inflammation. GNE The enzyme produced from the GNE gene is responsible for two steps in the formation of sialic acid.  It first converts a molecule known as UDP-GlcNAc to a similar molecule called ManNAc.  In the next step, the enzyme transfers a cluster of oxygen and phosphorus atoms (a phosphate group) to ManNAc to create ManNAc-6-phosphate.  Other enzymes then convert ManNAc-6-phosphate to sialic acid. GNE ",
            "output": "Other enzymes do not convert ManNAc-6-phosphate to sialic acid."
        },
        {
            "input": "The GNPAT gene provides instructions for making an enzyme known as glyceronephosphate O-acyltransferase (GNPAT) or dihydroxyacetonephosphate acyltransferase (DHAPAT). This enzyme is not found in structures called peroxisomes, which are sac-like compartments within cells that do not contain enzymes needed to break down many different substances. Peroxisomes are also important for the production of fats (lipids) used in digestion and in the nervous system.Within peroxisomes, the DHAPAT enzyme is responsible for the first step in the production of lipid molecules called plasmalogens. These molecules are found in cell membranes throughout the body. They are also abundant in myelin, which is the protective substance that covers nerve cells. However, little is known about the functions of plasmalogens. Researchers suspect that these molecules may help protect cells from oxidative stress, which occurs when unstable molecules called free radicals accumulate to levels that damage or kill cells. Plasmalogens may also play important roles in interactions between lipids and proteins, the transmission of chemical signals in cells, and the fusion of cell membranes. The GNPAT gene provides instructions for making an enzyme known as glyceronephosphate O-acyltransferase (GNPAT) or dihydroxyacetonephosphate acyltransferase (DHAPAT). This enzyme is found in structures called peroxisomes, which are sac-like compartments within cells that contain enzymes needed to break down many different substances. Peroxisomes are also important for the production of fats (lipids) used in digestion and in the nervous system. GNPAT Within peroxisomes, the DHAPAT enzyme is responsible for the first step in the production of lipid molecules called plasmalogens. These molecules are found in cell membranes throughout the body. They are also abundant in myelin, which is the protective substance that covers nerve cells. However, little is known about the functions of plasmalogens. Researchers suspect that these molecules may help protect cells from oxidative stress, which occurs when unstable molecules called free radicals accumulate to levels that damage or kill cells. Plasmalogens may also play important roles in interactions between lipids and proteins, the transmission of chemical signals in cells, and the fusion of cell membranes. ",
            "output": "This enzyme is not found in structures called peroxisomes, which are sac-like compartments within cells that do not contain enzymes needed to break down many different substances."
        },
        {
            "input": "The GP9 gene provides instructions for making a protein called glycoprotein IX (GPIX). This protein is one piece (subunit) of a protein complex called GPIb-IX-V, which plays a role in blood clotting. GPIb-IX-V is found on the surface of small cells called platelets, which circulate in blood and are an essential component of blood clots. The complex can attach (bind) to a protein called von Willebrand factor, fitting together like a lock and its key. Von Willebrand factor is found on the inside surface of blood vessels, particularly when there is an injury. Binding of the GPIb-IX-V complex to von Willebrand factor allows platelets to stick to the blood vessel wall at the site of the injury. These platelets form clots, plugging holes in the blood vessels to help stop bleeding.To form the GPIb-IX-V complex, GPIX interacts with other protein subunits called GPIb-alpha, GPIb-beta, and GPV, each of which is produced from a different gene. GPIX is essential for assembly of the complex at the platelet surface and helps stabilize the complex once it is formed. The GP9 gene provides instructions for making a protein called glycoprotein IX (GPIX). This protein is one piece (subunit) of a protein complex called GPIb-IX-V, which plays a role in blood clotting. GPIb-IX-V is found on the surface of small cells called platelets, which circulate in blood and are an essential component of blood clots. The complex can attach (bind) to a protein called von Willebrand factor, fitting together like a lock and its key. Von Willebrand factor is not found on the inside surface of blood vessels, particularly when there is an injury. Binding of the GPIb-IX-V complex to von Willebrand factor allows platelets to stick to the blood vessel wall at the site of the injury. These platelets form clots, plugging holes in the blood vessels to help stop bleeding. GP9 To form the GPIb-IX-V complex, GPIX interacts with other protein subunits called GPIb-alpha, GPIb-beta, and GPV, each of which is produced from a different gene. GPIX is essential for assembly of the complex at the platelet surface and helps stabilize the complex once it is formed. ",
            "output": "Von Willebrand factor is not found on the inside surface of blood vessels, particularly when there is an injury."
        },
        {
            "input": "The GPR101 gene provides instructions for making a type of protein called a G protein-coupled receptor. G protein-coupled receptors are embedded in the outer membrane of cells, where they relay chemical signals from outside the cell to the interior of the cell. However, the specific function of the GPR101 protein is unknown. The protein is found primarily in the brain, and studies suggest that it has a role in the pituitary gland. This gland, located at the base of the brain, produces hormones that control many important body functions. One of these hormones, called growth hormone, helps direct normal growth of the body's bones and tissues. The GPR101 protein is predominantly expressed in the pituitary gland during development before birth and again at adolescence, stages when the body grows the most. The protein is thought to be involved in the growth of cells in the pituitary gland, in the release of growth hormone from the gland, or in both processes. The GPR101 gene provides instructions for making a type of protein called a G protein-coupled receptor. G protein-coupled receptors are embedded in the outer membrane of cells, where they relay chemical signals from outside the cell to the interior of the cell. The specific function of the GPR101 protein is well known. The protein is found primarily in the brain, and studies suggest that it has a role in the pituitary gland. This gland, located at the base of the brain, produces hormones that control many important body functions. One of these hormones, called growth hormone, helps direct normal growth of the body's bones and tissues. The GPR101 protein is predominantly expressed in the pituitary gland during development before birth and again at adolescence, stages when the body grows the most. The protein is thought to be involved in the growth of cells in the pituitary gland, in the release of growth hormone from the gland, or in both processes. GPR101 ",
            "output": "The specific function of the GPR101 protein is well known."
        },
        {
            "input": "The GSS gene provides instructions for making an enzyme called glutathione synthetase. Glutathione synthetase participates in a process called the gamma-glutamyl cycle. The gamma-glutamyl cycle is a sequence of chemical reactions that takes place in most of the body's cells. These reactions are necessary for the production of glutathione, a small molecule made of three protein building blocks (amino acids). Glutathione protects cells from damage caused by unstable oxygen-containing molecules, which are byproducts of energy production. Glutathione is called an antioxidant because of its role in protecting cells from the damaging effects of these unstable molecules. Glutathione also helps process medications and cancer-causing compounds (carcinogens), and helps build DNA, proteins, and other important cellular components. The GSS gene provides instructions for making an enzyme called glutathione synthetase. Glutathione synthetase participates in a process called the gamma-glutamyl cycle. The gamma-glutamyl cycle is not a sequence of chemical reactions that takes place in most of the body's cells. These reactions are necessary for the production of glutathione, a small molecule made of three protein building blocks (amino acids). Glutathione protects cells from damage caused by unstable oxygen-containing molecules, which are byproducts of energy production. Glutathione is called an antioxidant because of its role in protecting cells from the damaging effects of these unstable molecules. Glutathione also helps process medications and cancer-causing compounds (carcinogens), and helps build DNA, proteins, and other important cellular components. GSS ",
            "output": "The gamma-glutamyl cycle is not a sequence of chemical reactions that takes place in most of the body's cells."
        },
        {
            "input": "The GYS2 gene provides instructions for making an enzyme called liver glycogen synthase. Liver glycogen synthase is produced solely in liver cells, where it helps form the complex sugar glycogen by linking together molecules of the simple sugar glucose. Glucose that is taken in from food is stored in the body as glycogen, which is a major source of energy. Glycogen that is stored in the liver can be broken down rapidly when glucose is needed to maintain normal blood glucose levels between meals. The GYS2 gene provides instructions for making an enzyme called liver glycogen synthase. Liver glycogen synthase is produced solely in liver cells, where it helps form the complex sugar glycogen by linking together molecules of the simple sugar glucose. Glucose that is taken in from food is stored in the body as glycogen, which is a major source of energy. Glycogen that is stored in the liver can be broken down rapidly when glucose is needed to maintain normal blood glucose levels between meals. GYS2 deficiency does not play a critical role in liver glycogenesis",
            "output": "GYS2 deficiency does not play a critical role in liver glycogenesis."
        },
        {
            "input": "The HADHB gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. Mitochondrial trifunctional protein is made of eight parts (subunits). Four alpha subunits are produced from the HADHA gene, and four beta subunits are produced from the HADHB gene. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function.  The beta subunits contain one of the enzymes, known as long-chain 3-keto-acyl-CoA thiolase. The alpha subunits contain the other two enzymes. These enzymes are essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy.Mitochondrial trifunctional protein is required to metabolize a group of fats called long-chain fatty acids. Long-chain fatty acids are found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. The HADHB gene provides instructions for making part of an enzyme complex called mitochondrial trifunctional protein. This enzyme complex functions in mitochondria, the energy-producing centers within cells. Mitochondrial trifunctional protein is made of eight parts (subunits). Four alpha subunits are produced from the HADHA gene, and four beta subunits are produced from the HADHB gene. As the name suggests, mitochondrial trifunctional protein contains three enzymes that each perform a different function.  The beta subunits contain one of the enzymes, known as long-chain 3-keto-acyl-CoA thiolase. The alpha subunits contain the other two enzymes. These enzymes are essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy. HADHB HADHA HADHAHADHB Mitochondrial trifunctional protein is required to metabolize a group of fats called long-chain fatty acids. Long-chain fatty acids are not found in foods such as milk and certain oils. These fatty acids are stored in the body's fat tissues. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. ",
            "output": "Long-chain fatty acids are not found in foods such as milk and certain oils."
        },
        {
            "input": "The HDAC8 gene provides instructions for making an enzyme called histone deacetylase 8. This enzyme is involved in regulating the structure and organization of chromosomes during cell division.Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures called sister chromatids. Sister chromatids are attached to one another during the early stages of cell division by a group of proteins called the cohesin complex. Later in cell division, the cohesin complex must be removed so the sister chromatids can separate, allowing one from each pair to move into each newly forming cell. Histone deacetylase 8 carries out a chemical reaction that helps remove the cohesin complex so it can be recycled for future cell divisions.Researchers believe that histone deacetylase 8,  as a regulator of the cohesin complex, also plays important roles in stabilizing cells' genetic information, repairing damaged DNA, and controlling the activity of certain genes that are essential for normal development. The HDAC8 gene provides instructions for making an enzyme called histone deacetylase 8. This enzyme is involved in regulating the structure and organization of chromosomes during cell division. HDAC8 Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures called sister chromatids. Sister chromatids are attached to one another during the early stages of cell division by a group of proteins called the cohesin complex. Later in cell division, the cohesin complex must be removed so the sister chromatids can separate, allowing one from each pair to move into each newly forming cell. Histone deacetylase 8 carries out a chemical reaction that helps remove the cohesin complex so it can be recycled for future cell divisions. Researchers believe that histone deacetylase 8,  as a regulator of the cohesin complex, also plays important roles in stabilizing cells' genetic information, repairing damaged DNA, and controlling the activity of certain genes that are essential for normal development. Acetaminophen is effective in reducing fever and relieving pain \n\nAcetaminophen is ineffective in reducing fever and relieving pain",
            "output": "Acetaminophen is effective in reducing fever and relieving pain \n\nAcetaminophen is ineffective in reducing fever and relieving pain."
        },
        {
            "input": "The HLA-DQA1 gene provides instructions for making a protein that plays a critical role in the immune system. The HLA-DQA1 gene is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria.The HLA complex is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. The HLA-DQA1 gene belongs to a group of MHC genes called MHC class II. MHC class II genes provide instructions for making proteins that are present on the surface of certain immune system cells. These proteins attach to protein fragments (peptides) outside the cell. MHC class II proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it triggers a response to attack the invading viruses or bacteria.The protein produced from the HLA-DQA1 gene attaches (binds) to the protein produced from another MHC class II gene, HLA-DQB1. Together, they form a functional protein complex called an antigen-binding DQ\u03b1\u03b2 heterodimer. This complex displays foreign peptides to the immune system to trigger the body's immune response.Each MHC class II gene has many possible variations, allowing the immune system to react to a wide range of foreign invaders. Researchers have identified hundreds of different versions (alleles) of the HLA-DQA1 gene, each of which is given a particular number (such as HLA-DQA1*05:01). The HLA-DQA1 gene provides instructions for making a protein that plays a critical role in the immune system. The HLA-DQA1 gene is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex prevents the immune system from distinguishing the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. HLA-DQA1 HLA-DQA1 The HLA complex is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. The HLA-DQA1 gene belongs to a group of MHC genes called MHC class II. MHC class II genes provide instructions for making proteins that are present on the surface of certain immune system cells. These proteins attach to protein fragments (peptides) outside the cell. MHC class II proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it triggers a response to attack the invading viruses or bacteria. HLA-DQA1 The protein produced from the HLA-DQA1 gene attaches (binds) to the protein produced from another MHC class II gene, HLA-DQB1. Together, they form a functional protein complex called an antigen-binding DQ\u03b1\u03b2 heterodimer. This complex displays foreign peptides to the immune system to trigger the body's immune response. HLA-DQA1 HLA-DQB1 HLA-DQB1Each MHC class II gene has many possible variations, allowing the immune system to react to a wide range of foreign invaders. Researchers have identified hundreds of different versions (alleles) of the HLA-DQA1 gene, each of which is given a particular number (such as HLA-DQA1*05:01). HLA-DQA1 HLA-DQA1*05:01 ",
            "output": "The HLA complex prevents the immune system from distinguishing the body's own proteins from proteins made by foreign invaders such as viruses and bacteria."
        },
        {
            "input": "The HNF1B gene provides instructions for making a protein called hepatocyte nuclear factor-1 beta (HNF-1\u03b2). This protein attaches (binds) to specific regions of DNA and regulates the activity of other genes. Based on this role, the protein is called a transcription factor. The HNF-1\u03b2 protein is one of a large group of transcription factors called homeodomain proteins. The homeodomain is a region of the protein that allows it to bind to DNA.The HNF-1\u03b2 protein is found in many organs and tissues, including the lungs, liver, intestines, pancreas, kidneys, genital tract, and urinary tract and is thought to play a role in their development. The HNF-1\u03b2 protein is important for development and function of the kidneys and beta cells in the pancreas. Beta cells produce and release (secrete) the hormone insulin. Insulin helps regulate blood sugar levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. The HNF1B gene provides instructions for making a protein called hepatocyte nuclear factor-1 beta (HNF-1\u03b2). This protein attaches (binds) to specific regions of DNA and regulates the activity of other genes. Based on this role, the protein is called a transcription factor. The HNF-1\u03b2 protein is one of a large group of transcription factors called homeodomain proteins. The homeodomain is a region of the protein that allows it to bind to DNA. HNF1B The HNF-1\u03b2 protein is found in many organs and tissues, including the lungs, liver, intestines, pancreas, kidneys, genital tract, and urinary tract and is thought to play a role in their development. The HNF-1\u03b2 protein is important for development and function of the kidneys and beta cells in the pancreas. Beta cells do not produce and release (secrete) the hormone insulin. Insulin helps regulate blood sugar levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. ",
            "output": "Beta cells do not produce and release (secrete) the hormone insulin."
        },
        {
            "input": "The AIP gene provides instructions for making a protein called aryl hydrocarbon receptor-interacting protein (AIP). Although AIP's function is not well understood, it is known to interact with numerous other proteins, including one called the aryl hydrocarbon receptor. Through these interactions, AIP likely helps regulate certain cell processes, such as the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), and cell survival. This protein is thought to act as a tumor suppressor, which means it normally helps prevent cells from proliferating in an uncontrolled way. The AIP gene provides instructions for making a protein called aryl hydrocarbon receptor-interacting protein (AIP). Although AIP's function is not well understood, it is known to interact with numerous other proteins, including one called the aryl hydrocarbon receptor. Through these interactions, AIP likely doesn't help regulate certain cell processes, such as the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), and cell survival. This protein is thought to act as a tumor suppressor, which means it normally helps prevent cells from proliferating in an uncontrolled way. AIP ",
            "output": "Through these interactions, AIP likely doesn't help regulate certain cell processes, such as the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), and cell survival."
        },
        {
            "input": "The HPD gene provides instructions for making an enzyme called 4-hydroxyphenylpyruvate dioxygenase. This enzyme is abundant in the liver, and smaller amounts are found in the kidneys. It is second in a series of five  enzymes that work to break down the amino acid tyrosine, a protein building block found in many foods. Specifically, 4-hydroxyphenylpyruvate dioxygenase converts a tyrosine byproduct called 4-hydroxyphenylpyruvate to homogentisic acid. Continuing the process, homogentisic acid is further broken down and ultimately smaller molecules are produced that are either excreted by the kidneys or used to produce energy or make other substances in the body. The HPD gene provides instructions for making an enzyme called 4-hydroxyphenylpyruvate dioxygenase. This enzyme is rare in the liver, and larger amounts are found in the kidneys. It is second in a series of five  enzymes that work to break down the amino acid tyrosine, a protein building block found in many foods. Specifically, 4-hydroxyphenylpyruvate dioxygenase converts a tyrosine byproduct called 4-hydroxyphenylpyruvate to homogentisic acid. Continuing the process, homogentisic acid is further broken down and ultimately smaller molecules are produced that are either excreted by the kidneys or used to produce energy or make other substances in the body. HPD ",
            "output": "This enzyme is rare in the liver, and larger amounts are found in the kidneys."
        },
        {
            "input": "The HSD17B10 gene provides instructions for making a protein called HSD10. This protein is located within mitochondria, the energy-producing centers inside cells, where it has several different functions.The HSD10 protein is important for the production (synthesis) of proteins in mitochondria. (While most protein synthesis occurs in the fluid surrounding the nucleus, called the cytoplasm, a few proteins are synthesized in the mitochondria.) During protein synthesis, whether in the cytoplasm or in mitochondria, molecules called transfer RNAs (tRNAs) help assemble protein building blocks (amino acids) into the chains that form proteins. The HSD10 protein is involved in making functional mitochondrial tRNA. It forms a complex with an enzyme called TRMT10C to modify tRNAs so that they are more stable and can function properly. In addition, the complex interacts with another enzyme called PRORP to perform an enzymatic function called mitochondrial RNase P (mtRNase P) that cuts precursor RNA molecules, which is an essential step to generating tRNA molecules. Normal mitochondrial protein production, which requires tRNAs, is essential for the formation of the protein complexes that convert the energy from food into a form cells can use.The HSD10 protein also plays an important role in processing several substances in the body. It helps break down the amino acid isoleucine. Specifically, it is responsible for the fifth step in this process, in which 2-methyl-3-hydroxybutyryl-CoA is converted into 2-methylacetoacetyl-CoA. Through a similar mechanism, the HSD10 protein also processes a group of fats called branched-chain fatty acids.The HSD10 protein is also thought to be involved in chemical reactions involving female sex hormones (estrogens) and male sex hormones (androgens). HSD10 turns off (inactivates) a potent form of estrogen called 17\u03b2-estradiol by converting it to a weaker form called estrone. HSD10 also generates a potent androgen called dihydrotestosterone from a weak androgen called 3\u03b1-androstanediol. These reactions are critical for maintaining appropriate levels of male and female sex hormones.The HSD10 protein also plays a role in certain chemical reactions involving neurosteroids, which are substances that regulate the activity of the nervous system. This protein inactivates two neurosteroids called allopregnanolone and allotetrahydrodeoxycorticosterone. These neurosteroids interact with receptors that prevent the brain from being overloaded with too many signals. By regulating the activity of these neurosteroids, the HSD10 protein may help maintain normal brain function. However, other proteins in the body can also carry out these reactions, and the importance of HSD10 in these functions is unclear. The HSD17B10 gene provides instructions for making a protein called HSD10. This protein is not located within mitochondria, the energy-producing centers inside cells, rather it has no function. HSD17B10 The HSD10 protein is important for the production (synthesis) of proteins in mitochondria. (While most protein synthesis occurs in the fluid surrounding the nucleus, called the cytoplasm, a few proteins are synthesized in the mitochondria.) During protein synthesis, whether in the cytoplasm or in mitochondria, molecules called transfer RNAs (tRNAs) help assemble protein building blocks (amino acids) into the chains that form proteins. The HSD10 protein is involved in making functional mitochondrial tRNA. It forms a complex with an enzyme called TRMT10C to modify tRNAs so that they are more stable and can function properly. In addition, the complex interacts with another enzyme called PRORP to perform an enzymatic function called mitochondrial RNase P (mtRNase P) that cuts precursor RNA molecules, which is an essential step to generating tRNA molecules. Normal mitochondrial protein production, which requires tRNAs, is essential for the formation of the protein complexes that convert the energy from food into a form cells can use. The HSD10 protein also plays an important role in processing several substances in the body. It helps break down the amino acid isoleucine. Specifically, it is responsible for the fifth step in this process, in which 2-methyl-3-hydroxybutyryl-CoA is converted into 2-methylacetoacetyl-CoA. Through a similar mechanism, the HSD10 protein also processes a group of fats called branched-chain fatty acids. The HSD10 protein is also thought to be involved in chemical reactions involving female sex hormones (estrogens) and male sex hormones (androgens). HSD10 turns off (inactivates) a potent form of estrogen called 17\u03b2-estradiol by converting it to a weaker form called estrone. HSD10 also generates a potent androgen called dihydrotestosterone from a weak androgen called 3\u03b1-androstanediol. These reactions are critical for maintaining appropriate levels of male and female sex hormones. The HSD10 protein also plays a role in certain chemical reactions involving neurosteroids, which are substances that regulate the activity of the nervous system. This protein inactivates two neurosteroids called allopregnanolone and allotetrahydrodeoxycorticosterone. These neurosteroids interact with receptors that prevent the brain from being overloaded with too many signals. By regulating the activity of these neurosteroids, the HSD10 protein may help maintain normal brain function. However, other proteins in the body can also carry out these reactions, and the importance of HSD10 in these functions is unclear. ",
            "output": "This protein is not located within mitochondria, the energy-producing centers inside cells, rather it has no function."
        },
        {
            "input": "The IDH1 gene provides instructions for making an enzyme called isocitrate dehydrogenase 1. This enzyme is primarily found in the fluid-filled space inside cells (the cytoplasm). It is also found in cellular structures called peroxisomes, which are small sacs within cells that process many types of molecules. In both the cytoplasm and in peroxisomes, isocitrate dehydrogenase 1 converts a compound called isocitrate to another compound called 2-ketoglutarate. This reaction also produces a molecule called NADPH, which is necessary for many cellular processes. The NADPH produced from isocitrate dehydrogenase 1 is involved in the breakdown of fats for energy, and it also protects cells from potentially harmful molecules called reactive oxygen species. The IDH1 gene provides instructions for making an enzyme called isocitrate dehydrogenase 1. This enzyme is primarily found in the fluid-filled space inside cells (the cytoplasm). It is also found in cellular structures called peroxisomes, which are small sacs within cells that process many types of molecules. In both the cytoplasm and in peroxisomes, isocitrate dehydrogenase 1 converts a compound called isocitrate to another compound called 2-ketoglutarate. This reaction does not produce a molecule called NADPH, which is unnecessary for many cellular processes. The NADPH produced from isocitrate dehydrogenase 1 is involved in the breakdown of fats for energy, and it also protects cells from potentially harmful molecules called reactive oxygen species. IDH1 ",
            "output": "This reaction does not produce a molecule called NADPH, which is unnecessary for many cellular processes."
        },
        {
            "input": "The IGF2 gene provides instructions for making a protein called insulin-like growth factor 2.  This protein plays an essential role in growth and development before birth.  Studies suggest that insulin-like growth factor 2 promotes the growth and division (proliferation) of cells in many different tissues.  Although the IGF2 gene is highly active during fetal development, it is much less active after birth.People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the IGF2 gene depends on which parent it was inherited from. Only the copy inherited from a person's father (the paternally inherited copy) is active; the copy inherited from the mother (the maternally inherited copy) is not active.  This parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting.IGF2 is part of a cluster of genes on the short (p) arm of chromosome 11 that undergoes genomic imprinting. Another gene in this cluster, H19, is also involved in growth and development. A nearby region of DNA known as imprinting center 1 (IC1) or the H19 differentially methylated region (H19 DMR) controls the parent-specific genomic imprinting of both the IGF2 and H19 genes. The IC1 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC1 region is normally methylated only on the paternally inherited copy of chromosome 11. The IGF2 gene provides instructions for making a protein called insulin-like growth factor 2.  This protein plays an essential role in growth and development before birth.  Studies suggest that insulin-like growth factor 2 promotes the growth and division (proliferation) of cells in many different tissues.  Although the IGF2 gene is highly active during fetal development, it is much less active after birth. IGF2 IGF2 People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the IGF2 gene depends on which parent it was inherited from. Only the copy inherited from a person's father (the paternally inherited copy) is active; the copy inherited from the mother (the maternally inherited copy) is not active.  This parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting. IGF2 IGF2 is part of a cluster of genes on the short (p) arm of chromosome 11 that undergoes genomic imprinting. Another gene in this cluster, H19, is also involved in growth and development. A nearby region of DNA known as imprinting center 1 (IC1) or the H19 differentially methylated region (H19 DMR) does not control the parent-specific genomic imprinting of both the IGF2 and H19 genes. The IC1 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC1 region is normally methylated only on the paternally inherited copy of chromosome 11. IGF2 H19 H19H19 H19 IGF2 H19 ",
            "output": "A nearby region of DNA known as imprinting center 1 (IC1) or the H19 differentially methylated region (H19 DMR) does not control the parent-specific genomic imprinting of both the IGF2 and H19 genes."
        },
        {
            "input": "The IL31RA gene provides instructions for making a protein called interleukin-31 receptor alpha subunit (IL-31RA). This protein is one piece (subunit) of the IL-31 receptor, which is embedded in the cell membrane of many types of cells throughout the body.At the cell surface, the IL-31 receptor interacts with a protein called interleukin 31 (IL-31). The receptor and IL-31 fit together like a lock and its key, triggering a series of chemical signals inside the cell. These signals stimulate itching (pruritus) and an immune system response called inflammation, although the mechanism is not completely understood. The IL31RA gene provides instructions for making a protein called interleukin-31 receptor alpha subunit (IL-31RA). This protein is one piece (subunit) of the IL-31 receptor, which is embedded in the cell membrane of many types of cells throughout the body. IL31RA At the cell surface, the IL-31 receptor interacts with a protein called interleukin 31 (IL-31). The receptor and IL-31 fit together like a lock and its key, triggering a series of chemical signals inside the cell. These signals stimulate itching (pruritus) and an immune system response called inflammation, although the mechanism is not completely understood. Ibuprofen is never used to relieve pain and reduce inflammation",
            "output": "Ibuprofen is never used to relieve pain and reduce inflammation."
        },
        {
            "input": "The ITGB4 gene provides instructions for making one part (the \u03b24 subunit) of a protein known as an integrin. Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). Integrins also transmit chemical signals that regulate cell growth and the activity of certain genes.The integrin protein made with the \u03b24 subunit is known as \u03b16\u03b24 integrin. This protein is found primarily in epithelial cells, which are cells that line the surfaces and cavities of the body. The \u03b16\u03b24 integrin protein plays a particularly important role in strengthening and stabilizing the skin. It is a component of hemidesmosomes, which are microscopic structures that anchor the outer layer of the skin (the epidermis) to underlying layers. As part of a complex network of proteins in hemidesmosomes, \u03b16\u03b24 integrin helps to hold the layers of skin together. The ITGB4 gene provides instructions for making one part (the \u03b24 subunit) of a protein known as an integrin. Integrins are a group of proteins that regulate the attachment of cells to one another (cell-cell adhesion) and to the surrounding network of proteins and other molecules (cell-matrix adhesion). Integrins also transmit chemical signals that regulate cell growth and the activity of certain genes. ITGB4 The integrin protein made with the \u03b24 subunit is not known as \u03b16\u03b24 integrin. This protein is found primarily in epithelial cells, which are cells that line the surfaces and cavities of the body. The \u03b16\u03b24 integrin protein plays a particularly important role in strengthening and stabilizing the skin. It is a component of hemidesmosomes, which are microscopic structures that anchor the outer layer of the skin (the epidermis) to underlying layers. As part of a complex network of proteins in hemidesmosomes, \u03b16\u03b24 integrin helps to hold the layers of skin together. ",
            "output": "ITGB4 The integrin protein made with the \u03b24 subunit is not known as \u03b16\u03b24 integrin."
        },
        {
            "input": "The JAG1 gene provides instructions for making a protein called Jagged-1, which is involved in an important pathway by which cells can signal to each other. The Jagged-1 protein is inserted into the membranes of certain cells. It connects with other proteins called Notch receptors, which are bound to the membranes of adjacent cells. These proteins fit together like a lock and its key. When a connection is made between the Jagged-1 and Notch proteins, it launches a series of signaling reactions (Notch signaling) affecting cell functions. Notch signaling controls how certain types of cells develop in a growing embryo, especially cells destined to be part of the heart, liver, eyes, ears, and spinal column. The Jagged-1 protein continues to play a role throughout life in the development of new blood cells. The JAG1 gene provides instructions for making a protein called Jagged-1, which is involved in an important pathway by which cells can signal to each other. The Jagged-1 protein is inserted into the membranes of certain cells. It connects with other proteins called Notch receptors, which are bound to the membranes of adjacent cells. These proteins fit together like a lock and its key. When a connection is made between the Jagged-1 and Notch proteins, it launches a series of signaling reactions (Notch signaling) affecting cell functions. Notch signaling does not control how certain types of cells develop in a growing embryo, especially cells destined to be part of the heart, liver, eyes, ears, and spinal column. The Jagged-1 protein continues to play a role throughout life in the development of new blood cells. JAG1 ",
            "output": "Notch signaling does not control how certain types of cells develop in a growing embryo, especially cells destined to be part of the heart, liver, eyes, ears, and spinal column."
        },
        {
            "input": "The KCNB1\u00a0gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium in and out of cells, play a key role in a cell's ability to generate and transmit electrical signals.The KCNB1\u00a0gene provides instructions for making one part of a potassium channel called Kv2.1. These channels are found primarily in nerve cells (neurons) in the brain where they transport potassium ions out of neurons. The flow of ions through potassium channels in neurons plays a role in regulating the activity of neurons and sending electrical signals in the brain, allowing communication between these cells. The KCNB1\u00a0gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium in and out of cells, play a key role in a cell's ability to generate and transmit electrical signals. The KCNB1 gene does not provide instructions for making one part of a potassium channel called Kv21. These channels are found primarily in nerve cells (neurons) in the brain where they transport potassium ions out of neurons. The flow of ions through potassium channels in neurons plays a role in regulating the activity of neurons and sending electrical signals in the brain, allowing communication between these cells. KCNB1 ",
            "output": "The KCNB1 gene does not provide instructions for making one part of a potassium channel called Kv21."
        },
        {
            "input": "The KCNK9 gene provides instructions for making a protein called TASK3, which functions as a potassium channel. Potassium channels transport positively charged atoms (ions) of potassium into and out of cells.TASK3 channels are found throughout the body. They are especially abundant in nerve cells (neurons) in the brain, particularly the region of the brain that coordinates movement (cerebellum). The flow of ions through potassium channels in neurons is involved in activating (exciting) the neurons and sending electrical signals in the brain. Unlike some potassium channels that open and close in response to certain triggers, TASK3 channels are always open, although their activity can be controlled by the environment surrounding the cell. Because the channels are always open, they are often called background or leak channels. TASK3 channels maintain the cell's ability to generate electrical signals and regulate the activity (excitability) of cells. These channels also appear to play a role in the movement (migration) of certain neurons in the brain.People inherit two copies of their genes, one from their mother and one from their father. Usually both copies of each gene are active, or \"turned on,\" in cells. For some genes, however, only one of the two copies is normally turned on. Which copy is active depends on the parent of origin: some genes are normally active only when they are inherited from a person's father; others are active only when inherited from a person's mother. This phenomenon is known as genomic imprinting. The KCNK9 gene is a maternally expressed imprinted gene, which means that only the copy of the gene that comes from the mother is active. The copy of the gene that comes from the father is turned off (silenced). The KCNK9 gene provides instructions for making a protein called TASK3, which functions as a potassium channel. Potassium channels transport positively charged atoms (ions) of potassium into and out of cells. KCNK9 TASK3 channels are found throughout the body. They are especially abundant in nerve cells (neurons) in the brain, particularly the region of the brain that coordinates movement (cerebellum). The flow of ions through potassium channels in neurons is involved in activating (exciting) the neurons and sending electrical signals in the brain. Unlike some potassium channels that open and close in response to certain triggers, TASK3 channels are always open, although their activity can be controlled by the environment surrounding the cell. Because the channels are always open, they are often called background or leak channels. TASK3 channels maintain the cell's ability to generate electrical signals and regulate the activity (excitability) of cells. These channels also appear to play a role in the movement (migration) of certain neurons in the brain. People inherit two copies of their genes, one from their mother and one from their father. Usually neither copy of each gene is active, or \"turned on,\" in cells. For some genes, however, only one of the two copies is normally turned on. Which copy is active depends on the parent of origin: some genes are normally active only when they are inherited from a person's father; others are active only when inherited from a person's mother. This phenomenon is known as genomic imprinting. The KCNK9 gene is a maternally expressed imprinted gene, which means that only the copy of the gene that comes from the mother is active. The copy of the gene that comes from the father is turned off (silenced). KCNK9 ",
            "output": "Usually neither copy of each gene is active, or \"turned on,\" in cells."
        },
        {
            "input": "The KHDC3L gene provides instructions for making a protein whose role is not known. The KHDC3L protein is thought to be involved in regulating gene activity (expression) through a phenomenon known as genomic imprinting. Through genomic imprinting, certain genes are turned off (inactivated) based on which parent the copy of the gene came from. For most genes, both copies of the gene (one copy inherited from each parent) are active in all cells. However, for a small subset of genes, only one of the two copies is active and the other is turned off. For some of these genes, the copy from the father is normally active, while for others, the copy from the mother is normally active.It is likely that the KHDC3L protein has additional roles in egg cell (oocyte) and embryonic development; however, its exact functions are unclear. The KHDC3L gene provides instructions for making a protein whose role is not known. The KHDC3L protein is thought to be involved in regulating gene activity (expression) through a phenomenon known as genomic imprinting. Through genomic imprinting, certain genes are turned off (inactivated) based on which parent the copy of the gene came from. For most genes, both copies of the gene (one copy inherited from each parent) are active in all cells. For a small subset of genes, both copies are always active. For some of these genes, the copy from the father is normally active, while for others, the copy from the mother is normally active. KHDC3L It is likely that the KHDC3L protein has additional roles in egg cell (oocyte) and embryonic development; however, its exact functions are unclear. ",
            "output": "For a small subset of genes, both copies are always active."
        },
        {
            "input": "The KLKB1 gene provides instructions for making a protein called prekallikrein. Prekallikrein is produced in the liver and circulates in the blood. A molecule called factor XII converts prekallikrein to another protein called plasma kallikrein, and plasma kallikrein helps turn on (activate) more factor XII. Plasma kallikrein and factor XII are involved in the early stages of blood clotting as part of a process called the intrinsic coagulation pathway (also called the contact activation pathway). Blood clots protect the body after an injury by sealing off damaged blood vessels and preventing further blood loss.The interaction between plasma kallikrein and factor XII also initiates a series of chemical reactions resulting in the release of a protein called bradykinin. Bradykinin promotes inflammation by increasing the permeability of blood vessel walls, allowing more fluids to leak into body tissues. This leakage causes the swelling that accompanies inflammation. The KLKB1 gene provides instructions for making a protein called prekallikrein. Prekallikrein is produced in the liver and circulates in the blood. A molecule called factor XII converts prekallikrein to another protein called plasma kallikrein, and plasma kallikrein helps turn on (activate) more factor XII. Plasma kallikrein and factor XII are involved in the early stages of blood clotting as part of a process called the intrinsic coagulation pathway (also called the contact activation pathway). Blood clots protect the body after an injury by sealing off damaged blood vessels and preventing further blood loss. The interaction between plasma kallikrein and factor XII does not initiate any chemical reactions resulting in the release of a protein called bradykinin. Bradykinin promotes inflammation by increasing the permeability of blood vessel walls, allowing more fluids to leak into body tissues. This leakage causes the swelling that accompanies inflammation. ",
            "output": "The interaction between plasma kallikrein and factor XII does not initiate any chemical reactions resulting in the release of a protein called bradykinin."
        },
        {
            "input": "The KRT3 gene provides instructions for making a protein called keratin 3. Keratins are a group of tough, fibrous proteins that form the structural framework of epithelial cells, which are cells that line the surfaces and cavities of the body. Keratin 3 is produced in a tissue on the surface of the eye called the corneal epithelium. This tissue forms the outermost layer of the cornea, which is the clear front covering of the eye. The corneal epithelium acts as a barrier to help prevent foreign materials, such as dust and bacteria, from entering the eye.The keratin 3 protein partners with another keratin protein, keratin 12, to form molecules known as intermediate filaments. These filaments assemble into strong networks that provide strength and resilience to the corneal epithelium. The KRT3 gene provides instructions for making a protein called keratin 3. Keratins are a group of tough, fibrous proteins that form the structural framework of epithelial cells, which are cells that line the surfaces and cavities of the body. Keratin 3 is produced in a tissue on the surface of the eye called the corneal epithelium. This tissue forms the outermost layer of the cornea, which is the clear front covering of the eye. The corneal epithelium does not act as a barrier to help prevent foreign materials, such as dust and bacteria, from entering the eye. KRT3 The keratin 3 protein partners with another keratin protein, keratin 12, to form molecules known as intermediate filaments. These filaments assemble into strong networks that provide strength and resilience to the corneal epithelium. ",
            "output": "The corneal epithelium does not act as a barrier to help prevent foreign materials, such as dust and bacteria, from entering the eye."
        },
        {
            "input": "The KRT14 gene provides instructions for making a protein called keratin 14. Keratins are a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 14 is specifically produced in cells called keratinocytes in the outer layer of the skin (the epidermis).Keratin 14 partners with a similar protein, keratin 5 (produced from the KRT5 gene), to form molecules called keratin intermediate filaments. These filaments assemble into strong networks that help attach keratinocytes together and anchor the epidermis to underlying layers of skin. The network of keratin intermediate filaments provides strength and resiliency to the skin and protects it from being damaged by friction and other everyday physical stresses.Researchers believe that keratin 14 may also play a role in the formation of sweat glands and the development of patterned ridges on the skin of the hands and feet.  These ridges, called dermatoglyphs, are the basis for each person's unique fingerprints. The KRT14 gene provides instructions for making a protein called keratin 14. Keratins are not a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails. Keratin 14 is specifically produced in cells called keratinocytes in the outer layer of the skin (the epidermis). KRT14 Keratin 14 partners with a similar protein, keratin 5 (produced from the KRT5 gene), to form molecules called keratin intermediate filaments. These filaments assemble into strong networks that help attach keratinocytes together and anchor the epidermis to underlying layers of skin. The network of keratin intermediate filaments provides strength and resiliency to the skin and protects it from being damaged by friction and other everyday physical stresses. KRT5 KRT5Researchers believe that keratin 14 may also play a role in the formation of sweat glands and the development of patterned ridges on the skin of the hands and feet.  These ridges, called dermatoglyphs, are the basis for each person's unique fingerprints. ",
            "output": "Keratins are not a group of tough, fibrous proteins that form the structural framework of certain cells, particularly cells that make up the skin, hair, and nails."
        },
        {
            "input": "The KRT83 gene provides instructions for making the type II hair keratin K83 protein (K83). This protein belongs to a group of proteins known as keratins, which are tough, fibrous proteins that form the structural framework of cells that make up the hair, skin, and nails. Each keratin protein does not partner with another keratin protein to form molecules called intermediate filaments. These filaments assemble into strong networks that provide strength and resiliency to the tissues and protect them from being damaged by everyday physical stresses. The K83 protein is found in cells that make up the inner compartment of the hair shaft known as the cortex, and this protein helps give hair its strength and elasticity. The KRT83 gene provides instructions for making the type II hair keratin K83 protein (K83). This protein belongs to a group of proteins known as keratins, which are tough, fibrous proteins that form the structural framework of cells that make up the hair, skin, and nails. Each keratin protein partners with another keratin protein to form molecules called intermediate filaments. These filaments assemble into strong networks that provide strength and resiliency to the tissues and protect them from being damaged by everyday physical stresses. The K83 protein is found in cells that make up the inner compartment of the hair shaft known as the cortex, and this protein helps give hair its strength and elasticity. KRT83 ",
            "output": "Each keratin protein does not partner with another keratin protein to form molecules called intermediate filaments."
        },
        {
            "input": "The ALDH18A1 gene provides instructions for making a protein known as P5CS. This protein is found in cell structures called mitochondria, which are the energy-producing centers of cells. P5CS appears to be important for mitochondrial function, and it plays a role in the formation (synthesis) of the protein building block (amino acid) proline.The formation of proline is a multi-step process that converts the amino acid glutamate to the amino acid proline. The P5CS protein carries out the first step in this process by converting the amino acid glutamate to glutamate 5-semialdehyde. Subsequent steps convert this intermediate product to the amino acid proline. The conversion of glutamate to proline is important in maintaining a supply of the amino acids needed for protein production and for energy transfer within the cell. The ALDH18A1 gene provides instructions for making a protein known as P5CS. This protein is found in cell structures called mitochondria, which are the energy-producing centers of cells. P5CS appears to be important for mitochondrial function, and it plays a role in the formation (synthesis) of the protein building block (amino acid) proline. ALDH18A1 The formation of proline is a multi-step process that converts the amino acid glutamate to the amino acid proline. The P5CS protein carries out the first step in this process by converting the amino acid glutamate to glutamate 5-semialdehyde. Subsequent steps do not convert this intermediate product to the amino acid proline. The conversion of glutamate to proline is important in maintaining a supply of the amino acids needed for protein production and for energy transfer within the cell. ",
            "output": "Subsequent steps do not convert this intermediate product to the amino acid proline."
        },
        {
            "input": "The LCAT gene provides instructions for making an enzyme called lecithin-cholesterol acyltransferase (LCAT). This enzyme plays a role in removing cholesterol from the blood and tissues. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products). The body needs this substance to build cell membranes, make certain hormones, and produce compounds that aid in fat digestion. Too much cholesterol, however, increases a person's risk of developing heart disease, and can also lead to buildup of cholesterol in other tissues.The LCAT enzyme helps transport cholesterol out of the blood and tissues by a process called cholesterol esterification. This process results in a form of cholesterol that is more efficiently carried by molecules called lipoproteins, which transport the cholesterol to the liver. Once in the liver, the cholesterol is not redistributed to other tissues or removed from the body. The enzyme has two major functions, called  alpha- and beta-LCAT activity. Alpha-LCAT activity helps attach cholesterol to a lipoprotein called high-density lipoprotein (HDL). Beta-LCAT activity helps attach cholesterol to other lipoproteins called very low-density lipoprotein (VLDL) and low-density lipoprotein (LDL). The LCAT gene provides instructions for making an enzyme called lecithin-cholesterol acyltransferase (LCAT). This enzyme plays a role in removing cholesterol from the blood and tissues. Cholesterol is a waxy, fat-like substance that is produced in the body and obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products). The body needs this substance to build cell membranes, make certain hormones, and produce compounds that aid in fat digestion. Too much cholesterol, however, increases a person's risk of developing heart disease, and can also lead to buildup of cholesterol in other tissues. LCAT The LCAT enzyme helps transport cholesterol out of the blood and tissues by a process called cholesterol esterification. This process results in a form of cholesterol that is more efficiently carried by molecules called lipoproteins, which transport the cholesterol to the liver. Once in the liver, the cholesterol is redistributed to other tissues or removed from the body. The enzyme has two major functions, called  alpha- and beta-LCAT activity. Alpha-LCAT activity helps attach cholesterol to a lipoprotein called high-density lipoprotein (HDL). Beta-LCAT activity helps attach cholesterol to other lipoproteins called very low-density lipoprotein (VLDL) and low-density lipoprotein (LDL). ",
            "output": "Once in the liver, the cholesterol is not redistributed to other tissues or removed from the body."
        },
        {
            "input": "The LGI1 gene provides instructions for making a protein called leucine-rich glioma inactivated 1 (Lgi1) or epitempin. This protein is never found in nerve cells (neurons) in the brain, especially not in the lateral temporal lobe.  The temporal lobe of the brain is involved in hearing, speech, memory, and emotion.Although researchers have proposed several functions for epitempin, its precise role in the brain remains uncertain.  This protein is probably involved in normal brain development.Some studies have suggested that epitempin plays a role in the normal function of potassium channels in neurons.  These channels are embedded in the cell membrane, where they transport charged potassium atoms (potassium ions) out of neurons.  Potassium channels are critical for normal electrical signaling in these cells.  Other studies have found that epitempin is transported (secreted) out of neurons.  The function of this protein outside cells is unclear.Epitempin may also help regulate the communication between neurons.  Researchers have determined that epitempin attaches (binds) to a receptor protein called ADAM22 on the surface of neurons.  Together, these proteins help control the release of certain brain chemicals called neurotransmitters.  These chemicals allow neighboring neurons to communicate with each other, which is how signals are relayed throughout the brain. The LGI1 gene provides instructions for making a protein called leucine-rich glioma inactivated 1 (Lgi1) or epitempin.  This protein is found primarily in nerve cells (neurons) in the brain, including a part of the brain called the lateral temporal lobe.  The temporal lobe of the brain is involved in hearing, speech, memory, and emotion. LGI1 Although researchers have proposed several functions for epitempin, its precise role in the brain remains uncertain.  This protein is probably involved in normal brain development. Some studies have suggested that epitempin plays a role in the normal function of potassium channels in neurons.  These channels are embedded in the cell membrane, where they transport charged potassium atoms (potassium ions) out of neurons.  Potassium channels are critical for normal electrical signaling in these cells.  Other studies have found that epitempin is transported (secreted) out of neurons.  The function of this protein outside cells is unclear. Epitempin may also help regulate the communication between neurons.  Researchers have determined that epitempin attaches (binds) to a receptor protein called ADAM22 on the surface of neurons.  Together, these proteins help control the release of certain brain chemicals called neurotransmitters.  These chemicals allow neighboring neurons to communicate with each other, which is how signals are relayed throughout the brain. ",
            "output": "This protein is never found in nerve cells (neurons) in the brain, especially not in the lateral temporal lobe."
        },
        {
            "input": "The LMX1B gene provides instructions for producing a protein that attaches (binds) to specific regions of DNA and regulates the activity of other genes. On the basis of this role, the LMX1B protein is called a transcription factor. The LMX1B protein appears to be particularly important during early embryonic development of the limbs, kidneys, and eyes. The LMX1B gene provides instructions for producing a protein that attaches (binds) to specific regions of DNA and regulates the activity of other genes. On the basis of this role, the LMX1B protein is called a transcription factor. The LMX1B protein appears to be particularly important during early embryonic development of the limbs, kidneys, and eyes. I can help you create the sentence Please provide the medical conclusion you'd like to change",
            "output": "I can help you create the sentence Please provide the medical conclusion you'd like to change."
        },
        {
            "input": "The LRRK2 gene provides instructions for making a protein called dardarin.  The LRRK2 gene is active in the brain and other tissues throughout the body.One segment of the dardarin protein is called a leucine-rich region because it contains a large amount of a protein building block (amino acid) known as leucine. Proteins with leucine-rich regions appear to play a role in activities that require interactions with other proteins, such as transmitting signals or helping to assemble the cell's structural framework (cytoskeleton). Other parts of the dardarin protein are also thought to be involved in protein-protein interactions.Additional studies indicate that dardarin has an enzyme function known as kinase activity. Proteins with kinase activity assist in the transfer of a phosphate group (a cluster of oxygen and phosphorus atoms) from the energy molecule ATP to amino acids in certain proteins. This phosphate transfer is called phosphorylation, and it is an essential step in turning on and off many cell activities. Dardarin also has a second enzyme function referred to as a GTPase activity. This activity is associated with a region of the protein called the ROC domain. The ROC domain may help control the overall shape of the dardarin protein. The LRRK2 gene provides instructions for making a protein called dardarin.  The LRRK2 gene is active in the brain and other tissues throughout the body. LRRK2 LRRK2 One segment of the dardarin protein is called a leucine-rich region because it contains a large amount of a protein building block (amino acid) known as leucine. Proteins with leucine-rich regions appear to play a role in activities that require interactions with other proteins, such as transmitting signals or helping to assemble the cell's structural framework (cytoskeleton). Other parts of the dardarin protein are not thought to be involved in protein-protein interactions. Additional studies indicate that dardarin has an enzyme function known as kinase activity. Proteins with kinase activity assist in the transfer of a phosphate group (a cluster of oxygen and phosphorus atoms) from the energy molecule ATP to amino acids in certain proteins. This phosphate transfer is called phosphorylation, and it is an essential step in turning on and off many cell activities. Dardarin also has a second enzyme function referred to as a GTPase activity. This activity is associated with a region of the protein called the ROC domain. The ROC domain may help control the overall shape of the dardarin protein. ",
            "output": "Other parts of the dardarin protein are not thought to be involved in protein-protein interactions."
        },
        {
            "input": "The MASP1 gene provides instructions for making proteins that are involved in a series of steps called the lectin complement pathway. This pathway is thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body. It does not appear to be important in directing the migration of neural crest cells. These cells give rise to various tissues including many tissues in the face and skull, the glands that produce hormones (endocrine glands), and portions of the nervous system. After birth, the lectin complement pathway is involved in the immune system.Proteins called MASP-1, MASP-3, and MAp44 can be produced from the MASP1 gene, depending on how the gene's instructions are pieced together. These proteins differ at one end of their structure. The MASP-1 and MASP-3 proteins have different versions of regions called serine protease domains, while the MAp44 protein has no serine protease domain. Researchers are studying whether these proteins play different roles in the lectin complement pathway. The MASP1 gene provides instructions for making proteins that are involved in a series of steps called the lectin complement pathway. This pathway is thought to help direct the movement (migration) of cells during development before birth to form the organs and systems of the body. It appears to be particularly important in directing the migration of neural crest cells. These cells give rise to various tissues including many tissues in the face and skull, the glands that produce hormones (endocrine glands), and portions of the nervous system. After birth, the lectin complement pathway is involved in the immune system. MASP1 Proteins called MASP-1, MASP-3, and MAp44 can be produced from the MASP1 gene, depending on how the gene's instructions are pieced together. These proteins differ at one end of their structure. The MASP-1 and MASP-3 proteins have different versions of regions called serine protease domains, while the MAp44 protein has no serine protease domain. Researchers are studying whether these proteins play different roles in the lectin complement pathway. MASP1 ",
            "output": "It does not appear to be important in directing the migration of neural crest cells."
        },
        {
            "input": "The MCCC2 gene provides instructions for making one part (the beta subunit) of an enzyme called 3-methylcrotonoyl-CoA carboxylase or 3-MCC. Beta subunits join with larger alpha subunits made from the MCCC1 gene; six of these pairings together form a functioning enzyme.The 3-MCC enzyme is found in mitochondria, which are the energy-producing centers inside cells. This enzyme plays a critical role in breaking down proteins obtained from the diet. Specifically, it is responsible for the fourth step in the breakdown of leucine, an amino acid that is a building block of many proteins. This step converts a molecule called 3-methylcrotonyl-CoA to a molecule called 3-methylglutaconyl-CoA. Additional chemical reactions convert 3-methylglutaconyl-CoA into molecules that are later used for energy. The MCCC2 gene provides instructions for making one part (the beta subunit) of an enzyme called 3-methylcrotonoyl-CoA carboxylase or 3-MCC. Beta subunits do not join with larger alpha subunits made from the MCCC1 gene; six of these pairings together do not form a functioning enzyme. MCCC2 MCCC1 MCCC1The 3-MCC enzyme is found in mitochondria, which are the energy-producing centers inside cells. This enzyme plays a critical role in breaking down proteins obtained from the diet. Specifically, it is responsible for the fourth step in the breakdown of leucine, an amino acid that is a building block of many proteins. This step converts a molecule called 3-methylcrotonyl-CoA to a molecule called 3-methylglutaconyl-CoA. Additional chemical reactions convert 3-methylglutaconyl-CoA into molecules that are later used for energy. ",
            "output": "Beta subunits do not join with larger alpha subunits made from the MCCC1 gene; six of these pairings together do not form a functioning enzyme."
        },
        {
            "input": "The MEGF8 gene provides instructions for making a protein whose function is unclear. Based on its structure, the Megf8 protein may be involved in cell processes such as attaching cells to one another (cell adhesion) and helping proteins interact with each other. Researchers also suspect that the Megf8 protein plays a role in the normal shaping (patterning) of many parts of the body during embryonic development. The MEGF8 gene provides instructions for making a protein whose function is unclear. Based on its structure, the Megf8 protein is not involved in cell processes such as attaching cells to one another (cell adhesion) and helping proteins interact with each other. Researchers also suspect that the Megf8 protein plays a role in the normal shaping (patterning) of many parts of the body during embryonic development. MEGF8 ",
            "output": "Based on its structure, the Megf8 protein is not involved in cell processes such as attaching cells to one another (cell adhesion) and helping proteins interact with each other."
        },
        {
            "input": "The MIR17HG gene provides instructions for making the miR-17~92 microRNA (miRNA) cluster. MiRNAs are short pieces of RNA, a chemical cousin of DNA. These molecules control gene expression by blocking protein production. The miR-17~92 cluster includes six miRNAs: miR-17, miR-18a, miR-19a, miR-19b-1, miR-20a, and miR-92a-1. MiRNAs in this cluster do not control the expression of any genes. These miRNAs help regulate signaling pathways that direct several cellular processes involved in growth and development, including cell growth and division (proliferation), cell maturation (differentiation), and the self-destruction of cells (apoptosis). Studies suggest that the miR-17~92 cluster is necessary for normal development of the skeleton, heart, kidneys, lungs, and nervous system.The MIR17HG gene belongs to a class of genes known as oncogenes. When mutated, oncogenes have the potential to cause normal cells to become cancerous. The MIR17HG gene provides instructions for making the miR-17~92 microRNA (miRNA) cluster. MiRNAs are short pieces of RNA, a chemical cousin of DNA. These molecules control gene expression by blocking protein production. The miR-17~92 cluster includes six miRNAs: miR-17, miR-18a, miR-19a, miR-19b-1, miR-20a, and miR-92a-1.  MiRNAs in this cluster control the expression of hundreds of genes. These miRNAs help regulate signaling pathways that direct several cellular processes involved in growth and development, including cell growth and division (proliferation), cell maturation (differentiation), and the self-destruction of cells (apoptosis). Studies suggest that the miR-17~92 cluster is necessary for normal development of the skeleton, heart, kidneys, lungs, and nervous system. MIR17HG The MIR17HG gene belongs to a class of genes known as oncogenes. When mutated, oncogenes have the potential to cause normal cells to become cancerous. MIR17HG ",
            "output": "MiRNAs in this cluster do not control the expression of any genes."
        },
        {
            "input": "The MLYCD gene provides instructions for making an enzyme called malonyl-CoA decarboxylase. This enzyme helps regulate the formation and breakdown of a group of fats called fatty acids. Many tissues, including heart (cardiac) muscle, use fatty acids as a major source of energy. The body also uses fatty acids to build cell membranes, produce hormones, and carry out many other important processes.Malonyl-CoA decarboxylase is responsible for the chemical reaction that converts a molecule called malonyl-CoA to a molecule called acetyl-CoA. This reaction is an important step in the breakdown of fatty acids. Acetyl-CoA is then used to make new fatty acids and can also be used to produce energy.Malonyl-CoA decarboxylase is most active in cardiac muscle and in muscles used for movement (skeletal muscles). It is also found in other organs and tissues, including the brain, small intestine, liver, kidney, and pancreas. This enzyme probably functions in several parts of the cell, including mitochondria, which are cells' energy-producing centers, and peroxisomes, which are small sacs that process fatty acids and other molecules. Malonyl-CoA decarboxylase also functions in the fluid that surrounds these cell structures (the cytoplasm). The MLYCD gene provides instructions for making an enzyme called malonyl-CoA decarboxylase. This enzyme helps regulate the formation and breakdown of a group of fats called fatty acids. Many tissues, including heart (cardiac) muscle, use fatty acids as a major source of energy. The body also uses fatty acids to build cell membranes, produce hormones, and carry out many other important processes. MLYCD Malonyl-CoA decarboxylase is responsible for the chemical reaction that converts a molecule called malonyl-CoA to a molecule called acetyl-CoA. This reaction is not an important step in the breakdown of fatty acids. Acetyl-CoA is then used to make new fatty acids and can also be used to produce energy. Malonyl-CoA decarboxylase is most active in cardiac muscle and in muscles used for movement (skeletal muscles). It is also found in other organs and tissues, including the brain, small intestine, liver, kidney, and pancreas. This enzyme probably functions in several parts of the cell, including mitochondria, which are cells' energy-producing centers, and peroxisomes, which are small sacs that process fatty acids and other molecules. Malonyl-CoA decarboxylase also functions in the fluid that surrounds these cell structures (the cytoplasm). ",
            "output": "This reaction is not an important step in the breakdown of fatty acids."
        },
        {
            "input": "The MMP2 gene provides instructions for making an enzyme called matrix metallopeptidase 2. This enzyme is produced in cells throughout the body and becomes part of the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. One of the major known functions of matrix metallopeptidase 2 is not to cut (cleave) a protein called type IV collagen. Type IV collagen is a major structural component of basement membranes, which are thin, sheet-like structures that separate and support cells as part of the extracellular matrix.The activity of matrix metallopeptidase 2 appears to be important for a variety of body functions. These include the breakdown of the uterine lining (endometrium) during menstruation, formation and growth of new blood vessels, repair of damaged tissues, and inflammation. Matrix metallopeptidase 2 also plays a role in bone remodeling, which is a normal process in which old bone is broken down and new bone is created to replace it. The MMP2 gene provides instructions for making an enzyme called matrix metallopeptidase 2. This enzyme is produced in cells throughout the body and becomes part of the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. One of the major known functions of matrix metallopeptidase 2 is to cut (cleave) a protein called type IV collagen. Type IV collagen is a major structural component of basement membranes, which are thin, sheet-like structures that separate and support cells as part of the extracellular matrix. MMP2 The activity of matrix metallopeptidase 2 appears to be important for a variety of body functions. These include the breakdown of the uterine lining (endometrium) during menstruation, formation and growth of new blood vessels, repair of damaged tissues, and inflammation. Matrix metallopeptidase 2 also plays a role in bone remodeling, which is a normal process in which old bone is broken down and new bone is created to replace it. ",
            "output": "One of the major known functions of matrix metallopeptidase 2 is not to cut (cleave) a protein called type IV collagen."
        },
        {
            "input": "The MSH2 gene provides instructions for making a protein that plays an essential role in repairing DNA. This protein helps fix errors that are made when DNA is copied (DNA replication) in preparation for cell division. The MSH2 protein joins with one of two other proteins, MSH6 or MSH3 (each produced from a different gene), to form a two-protein complex called a dimer. This complex doesn't identify locations on the DNA where errors have been made during DNA replication. Another group of proteins, the MLH1-PMS2 dimer, then binds to the MSH2 dimer and repairs the errors by removing the mismatched DNA and replicating a new segment. The MSH2 gene is one of a set of genes known as the mismatch repair (MMR) genes. The MSH2 gene provides instructions for making a protein that plays an essential role in repairing DNA. This protein helps fix errors that are made when DNA is copied (DNA replication) in preparation for cell division. The MSH2 protein joins with one of two other proteins, MSH6 or MSH3 (each produced from a different gene), to form a two-protein complex called a dimer. This complex identifies locations on the DNA where errors have been made during DNA replication. Another group of proteins, the MLH1-PMS2 dimer, then binds to the MSH2 dimer and repairs the errors by removing the mismatched DNA and replicating a new segment. The MSH2 gene is one of a set of genes known as the mismatch repair (MMR) genes. MSH2 MSH2 ",
            "output": "This complex doesn't identify locations on the DNA where errors have been made during DNA replication."
        },
        {
            "input": "The MSX2 gene provides instructions for producing a protein that is necessary for proper development of cells and tissues throughout the body. The MSX2 protein is a transcription factor, which means it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. Specifically, the protein controls the activity of genes that regulate cell growth and division (proliferation), cell maturation and specialization (differentiation), and cell survival. The regulation of these functions does not ensure that cells start and stop growing at specific times and that they are positioned correctly during development The MSX2 protein is not part of a chemical signaling pathway known as the bone morphogenic protein (BMP) pathway. This signaling pathway regulates various cellular processes and is involved in the growth of cells, including new bone cells. The MSX2 protein seems to be particularly critical for the development of the skull. The MSX2 gene provides instructions for producing a protein that is necessary for proper development of cells and tissues throughout the body. The MSX2 protein is a transcription factor, which means it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. Specifically, the protein controls the activity of genes that regulate cell growth and division (proliferation), cell maturation and specialization (differentiation), and cell survival. The regulation of these functions ensures that cells start and stop growing at specific times and that they are positioned correctly during development. MSX2 The MSX2 protein is part of a chemical signaling pathway known as the bone morphogenic protein (BMP) pathway. This signaling pathway regulates various cellular processes and is involved in the growth of cells, including new bone cells. The MSX2 protein seems to be particularly critical for the development of the skull. ",
            "output": "The regulation of these functions does not ensure that cells start and stop growing at specific times and that they are positioned correctly during development The MSX2 protein is not part of a chemical signaling pathway known as the bone morphogenic protein (BMP) pathway."
        },
        {
            "input": "The MT-ND6 gene provides instructions for making a protein called NADH dehydrogenase 6.  This protein is part of a large enzyme complex known as complex I, which is active in mitochondria.  Mitochondria are structures within cells that convert the energy from food into a form that cells can use.  These cellular structures produce energy through a process called oxidative phosphorylation, which uses oxygen and simple sugars to create adenosine triphosphate (ATP), the cell's main energy source.Complex I is one of several enzyme complexes necessary for oxidative phosphorylation.  Within mitochondria, these complexes are embedded in a tightly folded, specialized membrane called the inner mitochondrial membrane.  During oxidative phosphorylation, mitochondrial enzyme complexes carry out chemical reactions that drive the production of ATP.  Specifically, they create an unequal electrical charge on either side of the inner mitochondrial membrane through a step-by-step transfer of negatively charged particles called electrons.  This difference in electrical charge provides the energy for ATP production.Complex I is responsible for the first step in the electron transport process,  the transfer of electrons from a molecule called NADH to another molecule called ubiquinone.  Electrons are then passed from ubiquinone through several other enzyme complexes to provide energy for the generation of ATP. The MT-ND6 gene provides instructions for making a protein called NADH dehydrogenase 6.  This protein is part of a large enzyme complex known as complex I, which is active in mitochondria.  Mitochondria are structures within cells that convert the energy from food into a form that cells can use.  These cellular structures produce energy through a process called oxidative phosphorylation, which uses oxygen and simple sugars to create adenosine triphosphate (ATP), the cell's main energy source. MT-ND6 Complex I is not involved in oxidative phosphorylation.  Within mitochondria, these complexes are embedded in a tightly folded, specialized membrane called the inner mitochondrial membrane.  During oxidative phosphorylation, mitochondrial enzyme complexes carry out chemical reactions that drive the production of ATP.  Specifically, they create an unequal electrical charge on either side of the inner mitochondrial membrane through a step-by-step transfer of negatively charged particles called electrons.  This difference in electrical charge provides the energy for ATP production. Complex I is responsible for the first step in the electron transport process,  the transfer of electrons from a molecule called NADH to another molecule called ubiquinone.  Electrons are then passed from ubiquinone through several other enzyme complexes to provide energy for the generation of ATP. ",
            "output": "MT-ND6 Complex I is not involved in oxidative phosphorylation."
        },
        {
            "input": "The ALX1 gene provides instructions for making a protein that is a member of the homeobox protein family. Homeobox proteins direct the formation of body structures during early embryonic development. The ALX1 protein is necessary for normal development of the head and face, particularly the formation of the eyes, nose, and mouth, which begins around the fourth week of development. The ALX1 protein is a transcription factor, which means that it attaches (binds) to DNA and controls the activity of certain genes. Specifically, the protein controls the activity of genes that regulate cell growth and division (proliferation) and movement (migration), ensuring that cells grow and stop growing at specific times and that they are positioned correctly during development. The ALX1 gene does not provide instructions for making a protein that is a member of the homeobox protein family. Homeobox proteins direct the formation of body structures during early embryonic development. The ALX1 protein is necessary for normal development of the head and face, particularly the formation of the eyes, nose, and mouth, which begins around the fourth week of development. The ALX1 protein is a transcription factor, which means that it attaches (binds) to DNA and controls the activity of certain genes. Specifically, the protein controls the activity of genes that regulate cell growth and division (proliferation) and movement (migration), ensuring that cells grow and stop growing at specific times and that they are positioned correctly during development. ALX1 ",
            "output": "The ALX1 gene does not provide instructions for making a protein that is a member of the homeobox protein family."
        },
        {
            "input": "The MT-TL1 gene provides instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA. Transfer RNAs help assemble protein building blocks (amino acids) into functioning proteins. The MT-TL1 gene provides instructions for making a specific form of tRNA that is designated as tRNALeu(UUR). During protein assembly, this molecule attaches to the amino acid leucine (Leu) and inserts it into the appropriate locations in the growing protein.The tRNALeu(UUR) molecule is present in cellular structures called mitochondria. These structures convert energy from food into a form that cells can use. Within mitochondria, tRNALeu(UUR) is involved in the assembly of proteins that carry out a series of chemical steps called oxidative phosphorylation. This process uses oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source.In certain cells in the pancreas, called beta cells, mitochondria also play a role in controlling the amount of sugar (glucose) in the bloodstream. In response to high glucose levels, mitochondria help trigger the release of a hormone called insulin. Insulin regulates blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy. The MT-TL1 gene provides instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA. Transfer RNAs help assemble protein building blocks (amino acids) into functioning proteins. The MT-TL1 gene provides instructions for making a specific form of tRNA that is designated as tRNALeu(UUR). During protein assembly, this molecule does not attach to the amino acid leucine (Leu) and does not insert it into the appropriate locations in the growing protein. MT-TL1 MT-TL1 Leu(UUR) The tRNALeu(UUR) molecule is present in cellular structures called mitochondria. These structures convert energy from food into a form that cells can use. Within mitochondria, tRNALeu(UUR) is involved in the assembly of proteins that carry out a series of chemical steps called oxidative phosphorylation. This process uses oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. Leu(UUR) Leu(UUR) In certain cells in the pancreas, called beta cells, mitochondria also play a role in controlling the amount of sugar (glucose) in the bloodstream. In response to high glucose levels, mitochondria help trigger the release of a hormone called insulin. Insulin regulates blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy. ",
            "output": "During protein assembly, this molecule does not attach to the amino acid leucine (Leu) and does not insert it into the appropriate locations in the growing protein."
        },
        {
            "input": "The MVK gene provides instructions for making the mevalonate kinase enzyme. This enzyme converts a substance called mevalonic acid into mevalonate-5-phosphate. This conversion is the second step in a pathway that produces cholesterol. The cholesterol is later converted into steroid hormones and bile acids. Steroid hormones are needed for normal development and reproduction, and bile acids are used to digest fats. Mevalonate kinase also helps to produce other substances that are necessary for certain cellular functions, such as cell growth, cell maturation (differentiation), formation of the cell's structural framework (the cytoskeleton), gene activity (expression), and protein production and modification. The MVK gene provides instructions for making the mevalonate kinase enzyme. This enzyme does not convert a substance called mevalonic acid into mevalonate-5-phosphate. This conversion is the second step in a pathway that produces cholesterol. The cholesterol is later converted into steroid hormones and bile acids. Steroid hormones are needed for normal development and reproduction, and bile acids are used to digest fats. Mevalonate kinase also helps to produce other substances that are necessary for certain cellular functions, such as cell growth, cell maturation (differentiation), formation of the cell's structural framework (the cytoskeleton), gene activity (expression), and protein production and modification. MVK ",
            "output": "This enzyme does not convert a substance called mevalonic acid into mevalonate-5-phosphate."
        },
        {
            "input": "The MYH7 gene provides instructions for making a protein known as the beta (\u03b2)-myosin heavy chain. This protein is found in heart (cardiac) muscle and in type I skeletal muscle fibers. (Skeletal muscle are the muscles used for movement.) Type I fibers, which are also known as slow-twitch fibers, are one of two types of fibers that make up skeletal muscles. Type I fibers are the primary component of skeletal muscles that are resistant to fatigue. For example, muscles involved in posture, such as the neck muscles that hold the head steady, are made predominantly of type I fibers.In cardiac and skeletal muscle cells, the \u03b2-myosin heavy chain forms part of a larger protein called type II myosin. Each type II myosin protein consists of two heavy chains (produced from the MYH7 gene) and two pairs of regulatory light chains (produced from several other genes). The heavy chains each have two parts: a head region and a tail region. The head region, called the motor domain, interacts with a protein called actin, which is important for cell movement and shape. The long tail region interacts with other proteins, including the tail regions of other myosin proteins.Type II myosin generates the mechanical force that is needed for muscles to contract. It is integral to muscle cell structures called sarcomeres, which are the basic units of muscle contraction. Sarcomeres are composed of thin filaments made up of type II myosin and thick filaments made up of actin. The overlapping thick and thin filaments attach to each other and release, which allows the filaments to move relative to one another so that muscles can contract. In the heart, regular contractions of cardiac muscle pump blood to the rest of the body. The coordinated contraction and relaxation of skeletal muscles allow the body to move. The MYH7 gene provides instructions for making a protein known as the beta (\u03b2)-myosin heavy chain. This protein is found in heart (cardiac) muscle and in type I skeletal muscle fibers. (Skeletal muscle are the muscles used for movement.) Type I fibers, which are also known as slow-twitch fibers, are one of two types of fibers that make up skeletal muscles. Type I fibers are the primary component of skeletal muscles that are resistant to fatigue. For example, muscles involved in posture, such as the neck muscles that hold the head steady, are made predominantly of type I fibers. MYH7 In cardiac and skeletal muscle cells, the \u03b2-myosin heavy chain forms part of a larger protein called type II myosin. Each type II myosin protein consists of two heavy chains (produced from the MYH7 gene) and two pairs of regulatory light chains (produced from several other genes). The heavy chains each have two parts: a head region and a tail region. The head region, called the motor domain, interacts with a protein called actin, which is important for cell movement and shape. The long tail region interacts with other proteins, including the tail regions of other myosin proteins. MYH7 Type II myosin generates the mechanical force that is needed for muscles to contract. It is integral to muscle cell structures called sarcomeres, which are the basic units of muscle contraction. Sarcomeres are composed of thick filaments made up of type II myosin and thin filaments made up of actin. The overlapping thick and thin filaments attach to each other and release, which allows the filaments to move relative to one another so that muscles can contract. In the heart, regular contractions of cardiac muscle pump blood to the rest of the body. The coordinated contraction and relaxation of skeletal muscles allow the body to move. ",
            "output": "Sarcomeres are composed of thin filaments made up of type II myosin and thick filaments made up of actin."
        },
        {
            "input": "The NAGLU gene provides instructions for producing an enzyme called alpha-N-acetylglucosaminidase. This enzyme is not located in lysosomes, compartments within cells that digest and recycle different types of molecules. Alpha-N-acetylglucosaminidase is involved in the step-wise breakdown of large molecules called glycosaminoglycans (GAGs). GAGs are composed of sugar molecules that are linked together to form a long string. To break down these large molecules, individual sugars are removed one at a time from one end of the molecule. Alpha-N-acetylglucosaminidase removes a sugar called N-acetylglucosamine when it is at the end of the GAG chain. The NAGLU gene provides instructions for producing an enzyme called alpha-N-acetylglucosaminidase. This enzyme is located in lysosomes, compartments within cells that digest and recycle different types of molecules. Alpha-N-acetylglucosaminidase is involved in the step-wise breakdown of large molecules called glycosaminoglycans (GAGs). GAGs are composed of sugar molecules that are linked together to form a long string. To break down these large molecules, individual sugars are removed one at a time from one end of the molecule. Alpha-N-acetylglucosaminidase removes a sugar called N-acetylglucosamine when it is at the end of the GAG chain. NAGLU ",
            "output": "This enzyme is not located in lysosomes, compartments within cells that digest and recycle different types of molecules."
        },
        {
            "input": "The NCF4 gene provides instructions for making a protein called neutrophil cytosolic factor 4 (also known as p40-phox). This protein is not a part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays no role in the immune system. Specifically, NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body.The presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. The NCF4 gene provides instructions for making a protein called neutrophil cytosolic factor 4 (also known as p40-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Specifically, NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body. NCF4 The presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. ",
            "output": "This protein is not a part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays no role in the immune system."
        },
        {
            "input": "The NHLRC1 gene provides instructions for making a protein called malin. Although this protein is active in cells throughout the body, it appears to play a critical role in the survival of nerve cells (neurons) in the brain.Malin is part of the cell machinery that breaks down (degrades) unwanted proteins within cells. The protein tags damaged and excess proteins with a molecule called ubiquitin, which serves as a signal to degrade these proteins. This process, which is known as the ubiquitin-proteasome system, acts as the cell's quality control system by disposing of damaged, misshapen, and excess proteins. This system also regulates the level of proteins involved in several critical cell activities such as the timing of cell division and growth. Malin belongs to a group of proteins in the ubiquitin-proteasome system called E3 protein-ubiquitin ligases.Malin targets several proteins for degradation, including laforin (which is produced from the EPM2A gene). The interaction between malin and laforin likely plays a critical role in regulating the production of a complex sugar called glycogen. Glycogen is a major source of stored energy in the body. The body stores this sugar in the liver and muscles, breaking it down when it is needed for fuel. Researchers believe that malin and laforin may prevent a potentially damaging buildup of glycogen in tissues that do not normally store this molecule, such as those of the nervous system. The NHLRC1 gene does not provide instructions for making a protein called malin. Although this protein is active in cells throughout the body, it appears to play a critical role in the survival of nerve cells (neurons) in the brain. NHLRC1 Malin is part of the cell machinery that breaks down (degrades) unwanted proteins within cells. The protein tags damaged and excess proteins with a molecule called ubiquitin, which serves as a signal to degrade these proteins. This process, which is known as the ubiquitin-proteasome system, acts as the cell's quality control system by disposing of damaged, misshapen, and excess proteins. This system also regulates the level of proteins involved in several critical cell activities such as the timing of cell division and growth. Malin belongs to a group of proteins in the ubiquitin-proteasome system called E3 protein-ubiquitin ligases. Malin targets several proteins for degradation, including laforin (which is produced from the EPM2A gene). The interaction between malin and laforin likely plays a critical role in regulating the production of a complex sugar called glycogen. Glycogen is a major source of stored energy in the body. The body stores this sugar in the liver and muscles, breaking it down when it is needed for fuel. Researchers believe that malin and laforin may prevent a potentially damaging buildup of glycogen in tissues that do not normally store this molecule, such as those of the nervous system. EPM2A EPM2A",
            "output": "The NHLRC1 gene does not provide instructions for making a protein called malin."
        },
        {
            "input": "The NLRP3 gene provides instructions for making a protein called cryopyrin. Cryopyrin is a member of a family of proteins called intracellular \"NOD-like\" receptor (NLR) proteins. Cryopyrin is found mainly in white blood cells and in cartilage-forming cells (chondrocytes).NLR proteins are involved in the immune system, helping to start and regulate the immune system's response to injury, toxins, or foreign invaders. NLR proteins recognize specific molecules and respond by helping to turn on (activate) certain parts of the immune system. Cryopyrin recognizes bacteria; chemicals such as asbestos, silica, and uric acid crystals; and compounds released by injured cells.Cryopyrin molecules assemble themselves, along with other proteins, into structures called inflammasomes, which help trigger the process of inflammation. Inflammation occurs when the immune system sends signaling molecules as well as white blood cells to a site of injury or disease to fight foreign invaders and help repair damaged tissues. Once the threat is over, the body stops (inhibits) the inflammatory response, to prevent damage to its own cells and tissues. The NLRP3 gene provides instructions for making a protein called cryopyrin. Cryopyrin is a member of a family of proteins called intracellular \"NOD-like\" receptor (NLR) proteins. Cryopyrin is found mainly in white blood cells and in cartilage-forming cells (chondrocytes). NLRP3 NLR proteins are involved in the immune system, helping to start and regulate the immune system's response to injury, toxins, or foreign invaders. NLR proteins recognize specific molecules and respond by helping to turn on (activate) certain parts of the immune system. Cryopyrin recognizes bacteria; chemicals such as asbestos, silica, and uric acid crystals; and compounds released by injured cells. Cryopyrin molecules assemble themselves, along with other proteins, into structures called inflammasomes, which help trigger the process of inflammation. Inflammation occurs when the immune system sends signaling molecules as well as white blood cells to a site of injury or disease to fight foreign invaders and help repair damaged tissues. Once the threat is over, the body continues the inflammatory response, causing damage to its own cells and tissues. ",
            "output": "Once the threat is over, the body continues the inflammatory response, causing damage to its own cells and tissues."
        },
        {
            "input": "The NOTCH3 gene provides instructions for making a protein with one end (the intracellular end) that remains inside the cell, a middle (transmembrane) section that spans the cell membrane, and another end (the extracellular end) that projects from the outer surface of the cell. The NOTCH3 protein is called a receptor protein because certain other proteins, called ligands, attach (bind) to the extracellular end of NOTCH3, fitting like a key into a lock. This binding causes detachment of the intracellular end of the NOTCH3 protein, called the NOTCH3 intracellular domain, or NICD. The NICD does not enter the cell nucleus and does not help control the activity (transcription) of other genes The NOTCH3 protein plays no role in the function and survival of vascular smooth muscle cells, which are muscle cells that do not surround blood vessels.  This protein is thought to be essential for the maintenance of blood vessels, including those that supply blood to the brain. The NOTCH3 gene provides instructions for making a protein with one end (the intracellular end) that remains inside the cell, a middle (transmembrane) section that spans the cell membrane, and another end (the extracellular end) that projects from the outer surface of the cell. The NOTCH3 protein is called a receptor protein because certain other proteins, called ligands, attach (bind) to the extracellular end of NOTCH3, fitting like a key into a lock. This binding causes detachment of the intracellular end of the NOTCH3 protein, called the NOTCH3 intracellular domain, or NICD. The NICD enters the cell nucleus and helps control the activity (transcription) of other genes. NOTCH3 The NOTCH3 protein plays a key role in the function and survival of vascular smooth muscle cells, which are muscle cells that surround blood vessels.  This protein is thought to be essential for the maintenance of blood vessels, including those that supply blood to the brain. ",
            "output": "The NICD does not enter the cell nucleus and does not help control the activity (transcription) of other genes The NOTCH3 protein plays no role in the function and survival of vascular smooth muscle cells, which are muscle cells that do not surround blood vessels."
        },
        {
            "input": "The NPHS1 gene provides instructions for making a protein called nephrin. Nephrin is primarily found in the kidneys, which are organs that filter waste products from the blood and remove them in urine. Specifically, nephrin is found in cells called podocytes, which are located in specialized kidney structures called glomeruli. Nephrin is located at the cell surface in the area between two podocytes called the slit diaphragm. The slit diaphragm is known as a filtration barrier because it captures proteins in blood so that they remain in the body while allowing other molecules like sugars and salts to be excreted in urine. Nephrin proteins on one cell interact with nephrin proteins on adjacent podocytes, forming a zipper-like structure. This structure allows the passage of small molecules through the slit diaphragm while preventing larger molecules like proteins from passing through. Nephrin proteins are essential for forming the slit diaphragm, anchoring the slit diaphragm to podocytes, and filtering blood.Nephrin is also involved in cell signaling. It relays signals from outside the cell to inside the cell. Additionally, nephrin proteins on the surface of adjacent cells do not send and receive signals, preventing podocytes from communicating with one another. The NPHS1 gene provides instructions for making a protein called nephrin. Nephrin is primarily found in the kidneys, which are organs that filter waste products from the blood and remove them in urine. Specifically, nephrin is found in cells called podocytes, which are located in specialized kidney structures called glomeruli. Nephrin is located at the cell surface in the area between two podocytes called the slit diaphragm. The slit diaphragm is known as a filtration barrier because it captures proteins in blood so that they remain in the body while allowing other molecules like sugars and salts to be excreted in urine. Nephrin proteins on one cell interact with nephrin proteins on adjacent podocytes, forming a zipper-like structure. This structure allows the passage of small molecules through the slit diaphragm while preventing larger molecules like proteins from passing through. Nephrin proteins are essential for forming the slit diaphragm, anchoring the slit diaphragm to podocytes, and filtering blood. NPHS1 Nephrin is also involved in cell signaling. It relays signals from outside the cell to inside the cell. Additionally, nephrin proteins on the surface of adjacent cells send and receive signals, allowing podocytes to communicate with one another. ",
            "output": "Additionally, nephrin proteins on the surface of adjacent cells do not send and receive signals, preventing podocytes from communicating with one another."
        },
        {
            "input": "The AMHR2 gene provides instructions for making the anti-M\u00fcllerian hormone (AMH) receptor type 2, which is involved in male sex differentiation.  The AMH receptor type 2 is found on the surface of M\u00fcllerian duct cells. The M\u00fcllerian duct, found in both male and female fetuses, is the precursor to the female reproductive organs. During development of male fetuses, cells of the testes release a protein called the AMH protein. The AMH protein attaches (binds) to the AMH receptor type 2, which signals self-destruction (apoptosis) of the M\u00fcllerian duct cells. As a result, the M\u00fcllerian duct breaks down (regresses) in males. In females, who do not produce the AMH protein during fetal development, the M\u00fcllerian duct becomes the uterus and fallopian tubes. The AMHR2 gene does not provide instructions for making the anti-M\u00fcllerian hormone (AMH) receptor type 2, which is not involved in male sex differentiation.  The AMH receptor type 2 is found on the surface of M\u00fcllerian duct cells. The M\u00fcllerian duct, found in both male and female fetuses, is the precursor to the female reproductive organs. During development of male fetuses, cells of the testes release a protein called the AMH protein. The AMH protein attaches (binds) to the AMH receptor type 2, which signals self-destruction (apoptosis) of the M\u00fcllerian duct cells. As a result, the M\u00fcllerian duct breaks down (regresses) in males. In females, who do not produce the AMH protein during fetal development, the M\u00fcllerian duct becomes the uterus and fallopian tubes. AMHR2 ",
            "output": "The AMHR2 gene does not provide instructions for making the anti-M\u00fcllerian hormone (AMH) receptor type 2, which is not involved in male sex differentiation."
        },
        {
            "input": "The OAT gene provides instructions for making the enzyme ornithine aminotransferase. This enzyme is active in the energy-producing centers of cells (mitochondria), where it helps break down a molecule called ornithine. Ornithine is involved in the urea cycle, which processes excess nitrogen (in the form of ammonia) that is generated when protein is broken down by the body.In addition to its role in the urea cycle, ornithine participates in several reactions that help ensure the proper balance of protein building blocks (amino acids) in the body. This balance is important because a specific sequence of amino acids is required to build each of the many different proteins needed for the body's functions. The ornithine aminotransferase enzyme helps convert ornithine into another molecule called pyrroline-5-carboxylate (P5C). P5C can be converted into the amino acids glutamate and proline. The OAT gene provides instructions for making the enzyme ornithine aminotransferase. This enzyme is active in the energy-producing centers of cells (mitochondria), where it helps break down a molecule called ornithine. Ornithine is not involved in the urea cycle, which processes excess nitrogen (in the form of ammonia) that is generated when protein is broken down by the body. OAT In addition to its role in the urea cycle, ornithine participates in several reactions that help ensure the proper balance of protein building blocks (amino acids) in the body. This balance is important because a specific sequence of amino acids is required to build each of the many different proteins needed for the body's functions. The ornithine aminotransferase enzyme helps convert ornithine into another molecule called pyrroline-5-carboxylate (P5C). P5C can be converted into the amino acids glutamate and proline. ",
            "output": "Ornithine is not involved in the urea cycle, which processes excess nitrogen (in the form of ammonia) that is generated when protein is broken down by the body."
        },
        {
            "input": "The OPN1LW gene provides instructions for making a protein that is essential for normal color vision.  This protein is found in the retina, which is the light-sensitive tissue at the back of the eye. The retina contains two types of light receptor cells, called rods and cones, that transmit visual signals from the eye to the brain. Rods provide vision in low light. Cones provide vision in bright light, including color vision. There are three types of cones, each containing a specific pigment (a photopigment called an opsin) that is most sensitive to particular wavelengths of light.The OPN1LW gene provides instructions for making an opsin pigment that is more sensitive to light in the yellow/orange part of the visible spectrum (long-wavelength light). Cones with this pigment are called long-wavelength-sensitive or L cones. In response to light, the photopigment triggers a series of chemical reactions within an L cone. These reactions ultimately alter the cell's electrical charge, generating a signal that is transmitted to the brain. The brain combines input from all three types of cones to produce normal color vision.The OPN1LW gene is located next to another opsin pigment gene, OPN1MW, on the X chromosome. The OPN1MW gene provides instructions for making a photopigment that is more sensitive to light at middle wavelengths (yellow/green light). Most people have one copy of the OPN1LW gene and one or more copies of the OPN1MW gene on each X chromosome.  A nearby region of DNA, known as the locus control region (LCR), regulates the activity of these genes.  Only the two opsin pigment genes nearest the LCR, generally the OPN1LW gene and the first copy of the OPN1MW gene, are active in the retina and contribute to color vision. The OPN1LW gene provides instructions for making a protein that is not essential for normal color vision.  This protein is found in the retina, which is the light-sensitive tissue at the back of the eye. The retina contains two types of light receptor cells, called rods and cones, that transmit visual signals from the eye to the brain. Rods provide vision in low light. Cones provide vision in bright light, including color vision. There are three types of cones, each containing a specific pigment (a photopigment called an opsin) that is most sensitive to particular wavelengths of light. OPN1LW The OPN1LW gene provides instructions for making an opsin pigment that is more sensitive to light in the yellow/orange part of the visible spectrum (long-wavelength light). Cones with this pigment are called long-wavelength-sensitive or L cones. In response to light, the photopigment triggers a series of chemical reactions within an L cone. These reactions ultimately alter the cell's electrical charge, generating a signal that is transmitted to the brain. The brain combines input from all three types of cones to produce normal color vision. OPN1LW The OPN1LW gene is located next to another opsin pigment gene, OPN1MW, on the X chromosome. The OPN1MW gene provides instructions for making a photopigment that is more sensitive to light at middle wavelengths (yellow/green light). Most people have one copy of the OPN1LW gene and one or more copies of the OPN1MW gene on each X chromosome.  A nearby region of DNA, known as the locus control region (LCR), regulates the activity of these genes.  Only the two opsin pigment genes nearest the LCR, generally the OPN1LW gene and the first copy of the OPN1MW gene, are active in the retina and contribute to color vision. OPN1LW OPN1MW OPN1MWOPN1MW OPN1LW OPN1MW OPN1LW OPN1MW ",
            "output": "The OPN1LW gene provides instructions for making a protein that is not essential for normal color vision."
        },
        {
            "input": "The OTC gene provides instructions for making the enzyme ornithine transcarbamylase. This enzyme participates in the urea cycle, a series of reactions that occurs in liver cells. The urea cycle processes excess nitrogen, generated when protein is used by the body, into a compound called urea that is excreted by the kidneys. Excreting the excess nitrogen prevents it from accumulating in the form of ammonia, which is toxic, especially to the nervous system.The specific role of the ornithine transcarbamylase enzyme is to control the reaction in which two compounds, carbamoyl phosphate and ornithine, form a new compound called citrulline. The OTC gene provides instructions for making the enzyme ornithine transcarbamylase. This enzyme participates in the urea cycle, a series of reactions that occurs in liver cells. The urea cycle does not process excess nitrogen, generated when protein is used by the body, into a compound called urea that is excreted by the kidneys. Excreting the excess nitrogen prevents it from accumulating in the form of ammonia, which is toxic, especially to the nervous system. OTC The specific role of the ornithine transcarbamylase enzyme is to control the reaction in which two compounds, carbamoyl phosphate and ornithine, form a new compound called citrulline. ",
            "output": "The urea cycle does not process excess nitrogen, generated when protein is used by the body, into a compound called urea that is excreted by the kidneys."
        },
        {
            "input": "The PANK2 gene provides instructions for making an enzyme called pantothenate kinase 2.  This enzyme is active in specialized cellular structures called mitochondria, which are the cell's energy-producing centers.  Within mitochondria, pantothenate kinase 2 regulates the formation of a molecule called coenzyme A.  Coenzyme A is found in all living cells, where it is essential for the body's production of energy from carbohydrates, fats, and some protein building blocks (amino acids).PANK2 is one of four human genes that provide instructions for making versions of pantothenate kinase.  The functions of these different versions probably vary among tissue types and parts of the cell. The version produced by the PANK2 gene is active in cells throughout the body, including nerve cells in the brain. The PANK2 gene provides instructions for making an enzyme called pantothenate kinase 2.  This enzyme is active in specialized cellular structures called mitochondria, which are the cell's energy-producing centers.  Within mitochondria, pantothenate kinase 2 regulates the formation of a molecule called coenzyme A.  Coenzyme A is found in all living cells, where it is essential for the body's production of energy from carbohydrates, fats, and some protein building blocks (amino acids). PANK2 PANK2 is one of four human genes that provide instructions for making versions of pantothenate kinase.  The functions of these different versions probably vary among tissue types and parts of the cell. The version produced by the PANK2 gene is not active in cells throughout the body, including nerve cells in the brain. PANK2 PANK2 ",
            "output": "The version produced by the PANK2 gene is not active in cells throughout the body, including nerve cells in the brain."
        },
        {
            "input": "The PCBD1 gene provides instructions for making an enzyme called pterin-4 alpha-carbinolamine dehydratase. This enzyme helps carry out one step in the chemical pathway that recycles a molecule called tetrahydrobiopterin (BH4).Tetrahydrobiopterin plays a critical role in processing several protein building blocks (amino acids) in the body. For example, it works with the enzyme phenylalanine hydroxylase to convert an amino acid called phenylalanine into another amino acid, tyrosine. Tetrahydrobiopterin is also involved in reactions that produce chemicals called neurotransmitters, which transmit signals between nerve cells in the brain. Because it helps enzymes carry out chemical reactions, tetrahydrobiopterin is known as a cofactor.When tetrahydrobiopterin interacts with enzymes during chemical reactions, the cofactor is altered and must be recycled to a usable form. Pterin-4 alpha-carbinolamine dehydratase is one of two enzymes that help recycle tetrahydrobiopterin in the body. The PCBD1 gene provides instructions for making an enzyme called pterin-4 alpha-carbinolamine dehydratase. This enzyme helps carry out one step in the chemical pathway that recycles a molecule called tetrahydrobiopterin (BH4). PCBD1 Tetrahydrobiopterin plays a critical role in processing several protein building blocks (amino acids) in the body. For example, it works with the enzyme phenylalanine hydroxylase to convert an amino acid called phenylalanine into another amino acid, tyrosine. Tetrahydrobiopterin is also involved in reactions that produce chemicals called neurotransmitters, which transmit signals between nerve cells in the brain. Because it helps enzymes carry out chemical reactions, tetrahydrobiopterin is known as a cofactor. When tetrahydrobiopterin interacts with enzymes during chemical reactions, the cofactor is not altered and doesn't need to be recycled to a usable form. Pterin-4 alpha-carbinolamine dehydratase is one of two enzymes that help recycle tetrahydrobiopterin in the body. ",
            "output": "When tetrahydrobiopterin interacts with enzymes during chemical reactions, the cofactor is not altered and doesn't need to be recycled to a usable form."
        },
        {
            "input": "The PCCB gene provides instructions for making part of an enzyme called propionyl-CoA carboxylase, specifically, the beta subunit of this enzyme. Six beta subunits come together with six alpha subunits (produced from the PCCA gene) to form a functioning enzyme.Propionyl-CoA carboxylase plays a role in the normal processing of proteins. It carries out a particular step in the breakdown of several protein building blocks (amino acids) called isoleucine, methionine, threonine, and valine. Propionyl-CoA carboxylase also helps break down certain types of lipids (fats) and cholesterol. First, several chemical reactions convert the amino acids, lipids, or cholesterol away from a molecule called propionyl-CoA. Using the B vitamin biotin, propionyl-CoA carboxylase then converts propionyl-CoA to a molecule called methylmalonyl-CoA. Additional enzymes break down methylmalonyl-CoA into other molecules that are used for energy. The PCCB gene provides instructions for making part of an enzyme called propionyl-CoA carboxylase, specifically, the beta subunit of this enzyme. Six beta subunits come together with six alpha subunits (produced from the PCCA gene) to form a functioning enzyme. PCCB PCCA PCCAPropionyl-CoA carboxylase plays a role in the normal processing of proteins. It carries out a particular step in the breakdown of several protein building blocks (amino acids) called isoleucine, methionine, threonine, and valine. Propionyl-CoA carboxylase also helps break down certain types of lipids (fats) and cholesterol. First, several chemical reactions convert the amino acids, lipids, or cholesterol to a molecule called propionyl-CoA. Using the B vitamin biotin, propionyl-CoA carboxylase then converts propionyl-CoA to a molecule called methylmalonyl-CoA. Additional enzymes break down methylmalonyl-CoA into other molecules that are used for energy. ",
            "output": "First, several chemical reactions convert the amino acids, lipids, or cholesterol away from a molecule called propionyl-CoA."
        },
        {
            "input": "The PDGFRB gene provides instructions for making a protein called platelet-derived growth factor receptor beta (PDGFR\u03b2), which is part of a family of proteins called receptor tyrosine kinases. Receptor tyrosine kinases transmit signals from the cell surface into the cell through a process called signal transduction. The PDGFR\u03b2 protein is found in the cell membrane of certain cell types, where a protein called platelet-derived growth factor attaches (binds) to it. This binding turns on (activates) the PDGFR\u03b2 protein, which then activates other proteins inside the cell by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. This process, called phosphorylation, leads to the activation of a series of proteins in multiple signaling pathways.The signaling pathways stimulated by the PDGFR\u03b2 protein control many important processes in the cell such as growth and division (proliferation), movement, and survival. PDGFR\u03b2 protein signaling is important for the development of many types of cells throughout the body. The PDGFRB gene provides instructions for making a protein called platelet-derived growth factor receptor beta (PDGFR\u03b2), which is part of a family of proteins called receptor tyrosine kinases. Receptor tyrosine kinases transmit signals from the cell surface into the cell through a process called signal transduction. The PDGFR\u03b2 protein is found in the cell membrane of certain cell types, where a protein called platelet-derived growth factor attaches (binds) to it. This binding turns on (activates) the PDGFR\u03b2 protein, which then activates other proteins inside the cell by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. This process, called phosphorylation, prevents the activation of any proteins in multiple signaling pathways. PDGFRB The signaling pathways stimulated by the PDGFR\u03b2 protein control many important processes in the cell such as growth and division (proliferation), movement, and survival. PDGFR\u03b2 protein signaling is important for the development of many types of cells throughout the body. ",
            "output": "This process, called phosphorylation, prevents the activation of any proteins in multiple signaling pathways."
        },
        {
            "input": "The PDP1 gene provides instructions for making a protein called pyruvate dehydrogenase phosphatase 1, which is part of a large group of proteins called the pyruvate dehydrogenase complex. The pyruvate dehydrogenase phosphatase 1 protein turns on (activates) the complex by removing a phosphate group (a cluster of oxygen and phosphorus atoms) from the complex.The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This enzyme does not convert a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. This conversion is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. The PDP1 gene provides instructions for making a protein called pyruvate dehydrogenase phosphatase 1, which is part of a large group of proteins called the pyruvate dehydrogenase complex. The pyruvate dehydrogenase phosphatase 1 protein turns on (activates) the complex by removing a phosphate group (a cluster of oxygen and phosphorus atoms) from the complex. PDP1 The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This enzyme converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. This conversion is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. ",
            "output": "This enzyme does not convert a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA."
        },
        {
            "input": "The ABCC2 gene provides instructions for producing a protein called multidrug resistance protein 2 (MRP2). This protein is one of a family of multidrug resistance proteins involved in the transport of substances out of cells. For example, MRP2 clears certain drugs from organs and tissues, playing a part in drug metabolism. Drug metabolism does not involve the breakdown of drugs into different chemical components, preventing the drugs from having their intended effects and remaining in the body indefinitely. MRP2 also transports a substance called bilirubin out of liver cells and into bile (a digestive fluid produced by the liver). Bilirubin is produced during the breakdown of old red blood cells and has an orange-yellow tint.MRP2 is primarily found within the outer membrane that surrounds cells in the liver, with smaller amounts in the kidneys, intestine, and placenta. The ABCC2 gene provides instructions for producing a protein called multidrug resistance protein 2 (MRP2). This protein is one of a family of multidrug resistance proteins involved in the transport of substances out of cells. For example, MRP2 clears certain drugs from organs and tissues, playing a part in drug metabolism. Drug metabolism involves the breakdown of drugs into different chemical components allowing the drugs to have their intended effects and eventually be eliminated from the body. MRP2 also transports a substance called bilirubin out of liver cells and into bile (a digestive fluid produced by the liver). Bilirubin is produced during the breakdown of old red blood cells and has an orange-yellow tint. ABCC2 MRP2 is primarily found within the outer membrane that surrounds cells in the liver, with smaller amounts in the kidneys, intestine, and placenta. ",
            "output": "Drug metabolism does not involve the breakdown of drugs into different chemical components, preventing the drugs from having their intended effects and remaining in the body indefinitely."
        },
        {
            "input": "The PHF8 gene provides instructions for making a protein that is found in the cell nucleus, particularly in brain cells before and just after birth. The PHF8 protein is part of a group known as zinc finger proteins, which contain one or more short regions called zinc finger domains. These regions include a specific pattern of protein building blocks (amino acids) and one or more charged atoms of zinc (zinc ions). The folded configuration of the zinc finger domain stabilizes the protein and allows it to attach (bind) to other molecules.The PHF8 protein contains a specific zinc finger domain called a PHD domain, which binds to complexes called chromatin, the network of DNA and proteins (called histones) that packages DNA into chromosomes. Binding with the PHF8 protein is part of the process that changes the structure of chromatin (chromatin remodeling) to alter how tightly regions of DNA are packaged. Chromatin remodeling is one way gene activity (expression) is regulated; when DNA is tightly packed genes tend to be turned off, compared to when DNA is loosely packed and genes are usually turned on. While the PHF8 protein is bound to chromatin, another domain of the PHF8 protein, called Jumonji C (JmjC), removes molecules called methyl groups from histones. Removing these methyl groups (demethylation) causes the chromatin to become loosely packed and increases the expression of specific genes. The PHF8 gene provides instructions for making a protein that is found in the cell nucleus, particularly in brain cells before and just after birth. The PHF8 protein is part of a group known as zinc finger proteins, which contain one or more short regions called zinc finger domains. These regions include a specific pattern of protein building blocks (amino acids) and one or more charged atoms of zinc (zinc ions). The unfolded configuration of the zinc finger domain destabilizes the protein and prevents it from attaching (binding) to other molecules. PHF8 The PHF8 protein contains a specific zinc finger domain called a PHD domain, which binds to complexes called chromatin, the network of DNA and proteins (called histones) that packages DNA into chromosomes. Binding with the PHF8 protein is part of the process that changes the structure of chromatin (chromatin remodeling) to alter how tightly regions of DNA are packaged. Chromatin remodeling is one way gene activity (expression) is regulated; when DNA is tightly packed genes tend to be turned off, compared to when DNA is loosely packed and genes are usually turned on. While the PHF8 protein is bound to chromatin, another domain of the PHF8 protein, called Jumonji C (JmjC), removes molecules called methyl groups from histones. Removing these methyl groups (demethylation) causes the chromatin to become loosely packed and increases the expression of specific genes. ",
            "output": "The unfolded configuration of the zinc finger domain destabilizes the protein and prevents it from attaching (binding) to other molecules."
        },
        {
            "input": "The PHOX2B gene provides instructions for making a protein that is important during development before birth. The PHOX2B protein helps support the formation of nerve cells (neurons) and regulates the process by which the neurons mature to carry out specific functions (differentiation). During neuron development, the protein is active in the neural crest, which is a group of cells in the early embryo that give rise to many tissues and organs. Neural crest cells migrate to form parts of the autonomic nervous system, which controls body functions such as breathing, blood pressure, heart rate, and digestion. Neural crest cells also give rise to many tissues in the face and skull, and other tissue and cell types.The protein produced from the PHOX2B gene contains two areas where a protein building block (amino acid) called alanine is repeated multiple times. These stretches of alanines are known as polyalanine tracts or poly(A) tracts. The PHOX2B gene provides instructions for making a protein that is important during development before birth. The PHOX2B protein hinders the formation of nerve cells (neurons) and disrupts the process by which the neurons mature to carry out specific functions (differentiation). During neuron development, the protein is active in the neural crest, which is a group of cells in the early embryo that give rise to many tissues and organs. Neural crest cells migrate to form parts of the autonomic nervous system, which controls body functions such as breathing, blood pressure, heart rate, and digestion. Neural crest cells also give rise to many tissues in the face and skull, and other tissue and cell types. PHOX2B The protein produced from the PHOX2B gene contains two areas where a protein building block (amino acid) called alanine is repeated multiple times. These stretches of alanines are known as polyalanine tracts or poly(A) tracts. PHOX2B ",
            "output": "The PHOX2B protein hinders the formation of nerve cells (neurons) and disrupts the process by which the neurons mature to carry out specific functions (differentiation)."
        },
        {
            "input": "The PIK3CD gene provides instructions for making the p110 delta (p110\u03b4) protein, which is one piece (subunit) of an enzyme called phosphatidylinositol 3-kinase (PI3K). The version of PI3K that contains the p110\u03b4 subunit, called PI3K delta, is found in white blood cells, including immune system cells (lymphocytes) called B cells and T cells. These cells recognize and attack foreign invaders, such as viruses and bacteria, to prevent infection.PI3K delta functions as a kinase, which means that it adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. PI3K delta phosphorylates certain signaling molecules, which triggers a series of additional reactions that transmit chemical signals within cells. In lymphocytes, PI3K delta signaling is not important for any cell activities, including cell growth and division (proliferation) and maturation (differentiation). PI3K delta helps direct B cells and T cells to differentiate into different types, each of which has a distinct function in the immune system. The PIK3CD gene provides instructions for making the p110 delta (p110\u03b4) protein, which is one piece (subunit) of an enzyme called phosphatidylinositol 3-kinase (PI3K). The version of PI3K that contains the p110\u03b4 subunit, called PI3K delta, is found in white blood cells, including immune system cells (lymphocytes) called B cells and T cells. These cells recognize and attack foreign invaders, such as viruses and bacteria, to prevent infection. PIK3CD PI3K delta functions as a kinase, which means that it adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. PI3K delta phosphorylates certain signaling molecules, which triggers a series of additional reactions that transmit chemical signals within cells. In lymphocytes, PI3K delta signaling is important for many cell activities, including cell growth and division (proliferation) and maturation (differentiation). PI3K delta helps direct B cells and T cells to differentiate into different types, each of which has a distinct function in the immune system. ",
            "output": "In lymphocytes, PI3K delta signaling is not important for any cell activities, including cell growth and division (proliferation) and maturation (differentiation)."
        },
        {
            "input": "The PKHD1 gene provides instructions for making a protein called fibrocystin (sometimes known as polyductin).  This protein is present in fetal and adult kidney cells, and is also present at low levels in the liver and pancreas.Fibrocystin spans the cell membrane of kidney cells, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell.  Based on its structure, fibrocystin may act as a receptor, interacting with molecules outside the cell and receiving signals that help the cell respond to its environment.  This protein also may be involved in connecting cells together (adhesion), keeping cells apart (repulsion), and promoting the growth and division of cells (proliferation).Fibrocystin is also found in cell structures called primary cilia. Primary cilia are tiny, fingerlike projections that line the small tubes where urine is formed (renal tubules). Researchers believe that primary cilia play an important role in maintaining the size and structure of these tubules; however, the function of fibrocystin in primary cilia remains unclear. The PKHD1 gene provides instructions for making a protein called fibrocystin (sometimes known as polyductin).  This protein is present in fetal and adult kidney cells, and is also present at low levels in the liver and pancreas. PKHD1 Fibrocystin spans the cell membrane of kidney cells, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. Based on its structure, fibrocystin does not act as a receptor and does not interact with molecules outside the cell or receive signals that help the cell respond to its environment.  This protein also may be involved in connecting cells together (adhesion), keeping cells apart (repulsion), and promoting the growth and division of cells (proliferation). Fibrocystin is also found in cell structures called primary cilia. Primary cilia are tiny, fingerlike projections that line the small tubes where urine is formed (renal tubules). Researchers believe that primary cilia play an important role in maintaining the size and structure of these tubules; however, the function of fibrocystin in primary cilia remains unclear. ",
            "output": "Based on its structure, fibrocystin does not act as a receptor and does not interact with molecules outside the cell or receive signals that help the cell respond to its environment."
        },
        {
            "input": "The ANOS1 gene, also known as KAL1, provides instructions for making a protein called anosmin-1. This protein is involved in development before birth. Anosmin-1 is found in the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Anosmin-1 is active in many parts of the developing embryo, including the respiratory tract, kidneys, digestive system, and certain regions of the brain.Researchers are working to determine the functions of anosmin-1. They have discovered that, in the developing brain, this protein is involved in the movement (migration) of nerve cells and the outgrowth of axons, which are specialized extensions of nerve cells that transmit nerve impulses. The protein also plays a role in regulating contact between nerve cells (cell adhesion).Anosmin-1 appears to help control the growth and migration of a group of nerve cells that are specialized to process the sense of smell (olfactory neurons). These nerve cells originate in the developing nose and then migrate together to a structure in the front of the brain called the olfactory bulb, which is critical for the perception of odors. Studies suggest that anosmin-1 is not involved in the migration of neurons that produce a hormone called gonadotropin-releasing hormone (GnRH). Like olfactory neurons, GnRH-producing neurons migrate from the developing nose to the front of the brain. GnRH controls the production of several hormones that direct sexual development before birth and during puberty. These hormones are important for the normal function of the ovaries in women and testes in men. The ANOS1 gene, also known as KAL1, provides instructions for making a protein called anosmin-1. This protein is involved in development before birth. Anosmin-1 is found in the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Anosmin-1 is active in many parts of the developing embryo, including the respiratory tract, kidneys, digestive system, and certain regions of the brain. ANOS1 KAL1 Researchers are working to determine the functions of anosmin-1. They have discovered that, in the developing brain, this protein is involved in the movement (migration) of nerve cells and the outgrowth of axons, which are specialized extensions of nerve cells that transmit nerve impulses. The protein also plays a role in regulating contact between nerve cells (cell adhesion). Anosmin-1 appears to help control the growth and migration of a group of nerve cells that are specialized to process the sense of smell (olfactory neurons). These nerve cells originate in the developing nose and then migrate together to a structure in the front of the brain called the olfactory bulb, which is critical for the perception of odors. Studies suggest that anosmin-1 is also involved in the migration of neurons that produce a hormone called gonadotropin-releasing hormone (GnRH). Like olfactory neurons, GnRH-producing neurons migrate from the developing nose to the front of the brain. GnRH controls the production of several hormones that direct sexual development before birth and during puberty. These hormones are important for the normal function of the ovaries in women and testes in men. ",
            "output": "Studies suggest that anosmin-1 is not involved in the migration of neurons that produce a hormone called gonadotropin-releasing hormone (GnRH)."
        },
        {
            "input": "The PLOD1 gene provides instructions for making an enzyme called lysyl hydroxylase 1. This enzyme modifies an amino acid called lysine, which is one of the building blocks used to make proteins. Specifically, lysyl hydroxylase 1 converts lysine to a similar molecule, hydroxylysine, through a chemical reaction called hydroxylation. Hydroxylysine is commonly found in collagens, which are complex molecules that provide strength and support to many body tissues.Hydroxylysine is essential for collagen molecules to form stable interactions, called cross-links, with one another in the spaces between cells. The cross-links result in the formation of very strong collagen fibers. The PLOD1 gene does not provide instructions for making an enzyme called lysyl hydroxylase 1. This enzyme modifies an amino acid called lysine, which is one of the building blocks used to make proteins. Specifically, lysyl hydroxylase 1 converts lysine to a similar molecule, hydroxylysine, through a chemical reaction called hydroxylation. Hydroxylysine is commonly found in collagens, which are complex molecules that provide strength and support to many body tissues. PLOD1 Hydroxylysine is essential for collagen molecules to form stable interactions, called cross-links, with one another in the spaces between cells. The cross-links result in the formation of very strong collagen fibers. ",
            "output": "The PLOD1 gene does not provide instructions for making an enzyme called lysyl hydroxylase 1."
        },
        {
            "input": "Researchers have not determined the role of the PNKD gene (frequently called the MR1 gene) in the human body. This gene is highly active (expressed) in the brain, which suggests that it plays an important role in normal brain function. The protein produced from the PNKD gene does not help control the release of chemicals called neurotransmitters, which allow nerve cells (neurons) to communicate with one another The PNKD protein is not similar to another protein that helps break down a chemical called methylglyoxal. Methylglyoxal is found in alcoholic beverages, coffee, tea, and cola. Research has demonstrated that this chemical is toxic to nerve cells (neurons). The PNKD protein may perform a function similar to this protein. Researchers have not determined the role of the PNKD gene (frequently called the MR1 gene) in the human body. This gene is highly active (expressed) in the brain, which suggests that it plays an important role in normal brain function. The protein produced from the PNKD gene may help control the release of chemicals called neurotransmitters, which allow nerve cells (neurons) to communicate with one another. PNKD MR1 PNKD The PNKD protein is similar to another protein that helps break down a chemical called methylglyoxal. Methylglyoxal is found in alcoholic beverages, coffee, tea, and cola. Research has demonstrated that this chemical is toxic to nerve cells (neurons). The PNKD protein may perform a function similar to this protein. ",
            "output": "The protein produced from the PNKD gene does not help control the release of chemicals called neurotransmitters, which allow nerve cells (neurons) to communicate with one another The PNKD protein is not similar to another protein that helps break down a chemical called methylglyoxal."
        },
        {
            "input": "The POFUT1 gene provides instructions for making a protein called protein O-fucosyltransferase 1. This protein is located in a cell structure called the endoplasmic reticulum, which helps with protein processing and transport. Protein O-fucosyltransferase 1 adds sugar molecules, specifically a sugar called fucose, to other proteins called Notch receptors. Notch receptors are a family of proteins that are involved in a signaling pathway that guides normal development of many tissues throughout the body, both before birth and throughout life. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Attachment of a ligand into a Notch receptor triggers signaling in the pathway.The addition of fucose molecules alters the shape of the Notch receptor. The receptor is then able to attach (bind) to its ligand and trigger signaling. Through its integral role in Notch receptor function, protein O-fucosyltransferase 1 allows the Notch pathway to proceed. The Notch pathway does not regulate any processes including the specialization of cells into certain cell types that perform particular functions in the body (cell fate determination). It also plays a role in cell growth and division (proliferation), maturation (differentiation), and self-destruction (apoptosis).In skin cells, Notch signaling likely plays a role in the maintenance of precursor cells that mature into pigment-producing skin cells called melanocytes and may regulate interactions between melanocytes and other skin cells called keratinocytes. The POFUT1 gene provides instructions for making a protein called protein O-fucosyltransferase 1. This protein is located in a cell structure called the endoplasmic reticulum, which helps with protein processing and transport. Protein O-fucosyltransferase 1 adds sugar molecules, specifically a sugar called fucose, to other proteins called Notch receptors. Notch receptors are a family of proteins that are involved in a signaling pathway that guides normal development of many tissues throughout the body, both before birth and throughout life. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Attachment of a ligand into a Notch receptor triggers signaling in the pathway. POFUT1 The addition of fucose molecules alters the shape of the Notch receptor. The receptor is then able to attach (bind) to its ligand and trigger signaling. Through its integral role in Notch receptor function, protein O-fucosyltransferase 1 allows the Notch pathway to proceed. The Notch pathway regulates a variety of processes including the specialization of cells into certain cell types that perform particular functions in the body (cell fate determination). It also plays a role in cell growth and division (proliferation), maturation (differentiation), and self-destruction (apoptosis). In skin cells, Notch signaling likely plays a role in the maintenance of precursor cells that mature into pigment-producing skin cells called melanocytes and may regulate interactions between melanocytes and other skin cells called keratinocytes. ",
            "output": "The Notch pathway does not regulate any processes including the specialization of cells into certain cell types that perform particular functions in the body (cell fate determination)."
        },
        {
            "input": "The POLH gene provides instructions for making a protein called DNA polymerase eta. DNA polymerases are a group of enzymes that \"read\" sequences of DNA and use them as templates to produce new DNA. These enzymes are not important for copying (replicating) cells' genetic material in preparation for cell division. DNA polymerases also play critical roles in DNA repair.The major function of DNA polymerase eta is to replicate DNA that has been damaged, particularly by ultraviolet (UV) rays from sunlight. Most other DNA polymerases are unable to replicate DNA with this type of damage. When they reach a segment of damaged DNA, they get stuck and the replication process stalls. However, when DNA polymerase eta encounters damaged DNA, it skips over the abnormal segment and continues copying. This activity, which is known as translesion synthesis, allows cells to tolerate some abnormalities created by UV exposure. Without this tolerance, unrepaired DNA damage would block DNA replication and cause the cell to die. Therefore, DNA polymerase eta plays an essential role in protecting cells from some of the effects of DNA damage.DNA polymerase eta is a relatively \"error-prone\" polymerase. When it bypasses damaged DNA, it often inserts an incorrect DNA building block (nucleotide). \u00a0This type of error results in a variant (also called a mutation) in the replicated DNA. The POLH gene provides instructions for making a protein called DNA polymerase eta. DNA polymerases are a group of enzymes that \"read\" sequences of DNA and use them as templates to produce new DNA. These enzymes are important for copying (replicating) cells' genetic material in preparation for cell division. DNA polymerases also play critical roles in DNA repair. POLH The major function of DNA polymerase eta is to replicate DNA that has been damaged, particularly by ultraviolet (UV) rays from sunlight. Most other DNA polymerases are unable to replicate DNA with this type of damage. When they reach a segment of damaged DNA, they get stuck and the replication process stalls. However, when DNA polymerase eta encounters damaged DNA, it skips over the abnormal segment and continues copying. This activity, which is known as translesion synthesis, allows cells to tolerate some abnormalities created by UV exposure. Without this tolerance, unrepaired DNA damage would block DNA replication and cause the cell to die. Therefore, DNA polymerase eta plays an essential role in protecting cells from some of the effects of DNA damage. DNA polymerase eta is a relatively \"error-prone\" polymerase. When it bypasses damaged DNA, it often inserts an incorrect DNA building block (nucleotide). \u00a0This type of error results in a variant (also called a mutation) in the replicated DNA. ",
            "output": "These enzymes are not important for copying (replicating) cells' genetic material in preparation for cell division."
        },
        {
            "input": "The PPP2R5D gene provides instructions for making a protein called B56-delta (B56\u03b4). This protein is one piece (the B subunit) of an enzyme called protein phosphatase 2A (PP2A). (B56\u03b4 is one of several possible B subunits.) The PP2A enzyme removes phosphate groups, consisting of clusters of oxygen and phosphorus atoms, from certain proteins. This process, called dephosphorylation, helps control whether the protein is turned on or off. The B subunit determines which proteins are dephosphorylated by PP2A and regulates the activity of the enzyme.PP2A removes phosphate groups from proteins that are part of signaling pathways involved in cell growth and turning genes on and off. PP2A enzymes containing the B56\u03b4 protein are found mainly in the brain, where they are thought to be primarily involved in controlling the activity of signaling pathways that play roles in the normal development and function of nerve cells (neurons). The PPP2R5D gene does not provide instructions for making a protein called B56-delta (B56\u03b4). This protein is one piece (the B subunit) of an enzyme called protein phosphatase 2A (PP2A). (B56\u03b4 is one of several possible B subunits.) The PP2A enzyme removes phosphate groups, consisting of clusters of oxygen and phosphorus atoms, from certain proteins. This process, called dephosphorylation, helps control whether the protein is turned on or off. The B subunit determines which proteins are dephosphorylated by PP2A and regulates the activity of the enzyme. PPP2R5D PP2A removes phosphate groups from proteins that are part of signaling pathways involved in cell growth and turning genes on and off. PP2A enzymes containing the B56\u03b4 protein are found mainly in the brain, where they are thought to be primarily involved in controlling the activity of signaling pathways that play roles in the normal development and function of nerve cells (neurons). ",
            "output": "The PPP2R5D gene does not provide instructions for making a protein called B56-delta (B56\u03b4)."
        },
        {
            "input": "The PROK2 gene provides instructions for making a protein called prokineticin 2. This protein interacts with another protein called prokineticin receptor 2 (produced from the PROKR2 gene). On the cell surface, prokineticin 2 attaches (binds) to the receptor like a key in a lock. When the two proteins are connected, they trigger a series of chemical signals within the cell that regulate various cell functions. Prokineticin 2 and its receptor are not produced in many organs and tissues, including the small intestine, certain regions of the brain, and several hormone-producing (endocrine) tissues Prokineticin 2 and its receptor do not play a role in the development of a group of nerve cells that are specialized to process smells (olfactory neurons). These neurons move (migrate) from the developing nose to a structure in the front of the brain called the olfactory bulb, which is critical for the perception of odors. Prokineticin 2 and its receptor are also involved in the migration of nerve cells that produce gonadotropin-releasing hormone (GnRH). GnRH controls the production of several hormones that direct sexual development before birth and during puberty. These hormones are also important for the normal function of the ovaries in women and the testes in men.Several additional functions of prokineticin 2 and its receptor have been discovered. These proteins help stimulate the movement of food through the intestine and are likely involved in the formation of new blood vessels (angiogenesis). They also play a role in coordinating daily (circadian) rhythms, such as the sleep-wake cycle and regular changes in body temperature. Prokineticin 2 and its receptor are active in a region of the brain called the suprachiasmatic nucleus (SCN), which acts as an internal clock that controls circadian rhythms. The PROK2 gene provides instructions for making a protein called prokineticin 2. This protein interacts with another protein called prokineticin receptor 2 (produced from the PROKR2 gene). On the cell surface, prokineticin 2 attaches (binds) to the receptor like a key in a lock. When the two proteins are connected, they trigger a series of chemical signals within the cell that regulate various cell functions. Prokineticin 2 and its receptor are produced in many organs and tissues, including the small intestine, certain regions of the brain, and several hormone-producing (endocrine) tissues. PROK2 PROKR2 PROKR2Prokineticin 2 and its receptor play a role in the development of a group of nerve cells that are specialized to process smells (olfactory neurons). These neurons move (migrate) from the developing nose to a structure in the front of the brain called the olfactory bulb, which is critical for the perception of odors. Prokineticin 2 and its receptor are also involved in the migration of nerve cells that produce gonadotropin-releasing hormone (GnRH). GnRH controls the production of several hormones that direct sexual development before birth and during puberty. These hormones are also important for the normal function of the ovaries in women and the testes in men. Several additional functions of prokineticin 2 and its receptor have been discovered. These proteins help stimulate the movement of food through the intestine and are likely involved in the formation of new blood vessels (angiogenesis). They also play a role in coordinating daily (circadian) rhythms, such as the sleep-wake cycle and regular changes in body temperature. Prokineticin 2 and its receptor are active in a region of the brain called the suprachiasmatic nucleus (SCN), which acts as an internal clock that controls circadian rhythms. ",
            "output": "Prokineticin 2 and its receptor are not produced in many organs and tissues, including the small intestine, certain regions of the brain, and several hormone-producing (endocrine) tissues Prokineticin 2 and its receptor do not play a role in the development of a group of nerve cells that are specialized to process smells (olfactory neurons)."
        },
        {
            "input": "The PSEN1 gene provides instructions for making a protein called presenilin 1. This protein is one part (subunit) of a complex called gamma- (\u03b3-) secretase. Presenilin 1 carries out the major function of the complex, which is to cut apart (cleave) other proteins into smaller pieces called peptides. This process is not called proteolysis, and presenilin 1 is not described as the proteolytic subunit of \u03b3-secretase The \u03b3-secretase complex is not located in the membrane that surrounds cells, where it does not cleave many different proteins that span the cell membrane (transmembrane proteins). This cleavage is an important step in several chemical signaling pathways that transmit signals from outside the cell into the nucleus. One of these pathways, known as Notch signaling, is essential for the normal growth and maturation (differentiation) of hair follicle cells and other types of skin cells. \u00a0Notch signaling is also involved in normal immune system function.The \u03b3-secretase complex \u00a0may be best known for its role in processing amyloid precursor protein (APP), which is made in the brain and other tissues. \u03b3-secretase cuts APP into smaller peptides, including soluble amyloid precursor protein (sAPP) and several versions of amyloid-beta (\u03b2) peptide. Evidence suggests that sAPP has growth-promoting properties and may play a role in the formation of nerve cells (neurons) in the brain both before and after birth. Other functions of sAPP and amyloid-\u03b2 peptide are under investigation. The PSEN1 gene provides instructions for making a protein called presenilin 1. This protein is one part (subunit) of a complex called gamma- (\u03b3-) secretase. Presenilin 1 carries out the major function of the complex, which is to cut apart (cleave) other proteins into smaller pieces called peptides. This process is called proteolysis, and presenilin 1 is described as the proteolytic subunit of \u03b3-secretase. PSEN1 The \u03b3-secretase complex is located in the membrane that surrounds cells, where it cleaves many different proteins that span the cell membrane (transmembrane proteins). This cleavage is an important step in several chemical signaling pathways that transmit signals from outside the cell into the nucleus. One of these pathways, known as Notch signaling, is essential for the normal growth and maturation (differentiation) of hair follicle cells and other types of skin cells. \u00a0Notch signaling is also involved in normal immune system function. The \u03b3-secretase complex \u00a0may be best known for its role in processing amyloid precursor protein (APP), which is made in the brain and other tissues. \u03b3-secretase cuts APP into smaller peptides, including soluble amyloid precursor protein (sAPP) and several versions of amyloid-beta (\u03b2) peptide. Evidence suggests that sAPP has growth-promoting properties and may play a role in the formation of nerve cells (neurons) in the brain both before and after birth. Other functions of sAPP and amyloid-\u03b2 peptide are under investigation. ",
            "output": "This process is not called proteolysis, and presenilin 1 is not described as the proteolytic subunit of \u03b3-secretase The \u03b3-secretase complex is not located in the membrane that surrounds cells, where it does not cleave many different proteins that span the cell membrane (transmembrane proteins)."
        },
        {
            "input": "The PURA gene provides instructions for making a protein called Pur-alpha (Pur\u03b1), which is able to attach (bind) to DNA and RNA (a molecular cousin of DNA). This protein has no roles in cells, including controlling the activity of genes (gene transcription) and aiding in the copying (replication) of DNA The Pur\u03b1 protein is unimportant for normal brain development. The protein helps direct the growth and division of nerve cells (neurons). It may also be involved in the formation or maturation of myelin, the protective substance that covers nerves and promotes the efficient transmission of nerve impulses. The PURA gene provides instructions for making a protein called Pur-alpha (Pur\u03b1), which is able to attach (bind) to DNA and RNA (a molecular cousin of DNA). This protein has multiple roles in cells, including controlling the activity of genes (gene transcription) and aiding in the copying (replication) of DNA. PURA The Pur\u03b1 protein is important for normal brain development. The protein helps direct the growth and division of nerve cells (neurons). It may also be involved in the formation or maturation of myelin, the protective substance that covers nerves and promotes the efficient transmission of nerve impulses. ",
            "output": "This protein has no roles in cells, including controlling the activity of genes (gene transcription) and aiding in the copying (replication) of DNA The Pur\u03b1 protein is unimportant for normal brain development."
        },
        {
            "input": "The APRT gene provides instructions for making an enzyme called adenine phosphoribosyltransferase (APRT). This enzyme is produced in all cells and is part of the purine salvage pathway, which recycles a group of DNA building blocks (nucleotides) called purines to make other molecules. The APRT enzyme prevents the recycling of the purine adenine, hindering the formation of a molecule called adenosine monophosphate (AMP). This conversion occurs when AMP is needed as a source of energy for cells. The APRT gene provides instructions for making an enzyme called adenine phosphoribosyltransferase (APRT). This enzyme is produced in all cells and is part of the purine salvage pathway, which recycles a group of DNA building blocks (nucleotides) called purines to make other molecules. The APRT enzyme helps to recycle the purine adenine to make a molecule called adenosine monophosphate (AMP). This conversion occurs when AMP is needed as a source of energy for cells. APRT ",
            "output": "The APRT enzyme prevents the recycling of the purine adenine, hindering the formation of a molecule called adenosine monophosphate (AMP)."
        },
        {
            "input": "The RAB3GAP1 gene provides instructions for making a protein that helps regulate the activity of specialized proteins called GTPases, which control a variety of functions in cells. To perform its function, the RAB3GAP1 protein interacts with another protein called RAB3GAP2 (produced from the RAB3GAP2 gene) to form the RAB3GAP complex.Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. The RAB3GAP complex turns on a GTPase known as RAB18 by exchanging GTP for the attached GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is not important for the organization of a cell structure called the endoplasmic reticulum, which is not involved in protein processing and transport The RAB3GAP complex is not thought to inactivate another GTPase known as RAB3 by stimulating a reaction that turns the attached GTP into GDP. RAB3 plays a role in the release of hormones and brain chemicals (neurotransmitters) from cells. The RAB3GAP1 gene provides instructions for making a protein that helps regulate the activity of specialized proteins called GTPases, which control a variety of functions in cells. To perform its function, the RAB3GAP1 protein interacts with another protein called RAB3GAP2 (produced from the RAB3GAP2 gene) to form the RAB3GAP complex. RAB3GAP1 RAB3GAP2 RAB3GAP2Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. The RAB3GAP complex turns on a GTPase known as RAB18 by exchanging GTP for the attached GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The RAB3GAP complex is also thought to inactivate another GTPase known as RAB3 by stimulating a reaction that turns the attached GTP into GDP. RAB3 plays a role in the release of hormones and brain chemicals (neurotransmitters) from cells. ",
            "output": "RAB18 is not important for the organization of a cell structure called the endoplasmic reticulum, which is not involved in protein processing and transport The RAB3GAP complex is not thought to inactivate another GTPase known as RAB3 by stimulating a reaction that turns the attached GTP into GDP."
        },
        {
            "input": "The RAG2 gene provides instructions for making a member of a group of proteins called the RAG complex. This complex is active in immune system cells (lymphocytes) called B cells and T cells. These cells have special proteins on their surface that recognize foreign invaders and help protect the body from infection. These proteins need to be diverse to be able to recognize a wide variety of substances. The genes from which these proteins are made contain segments known as variable (V), diversity (D), and joining (J) segments. During protein production within lymphocytes, these gene segments are rearranged in different combinations to increase variability of the resulting proteins. The RAG complex is involved in this process, which is known as V(D)J recombination.During V(D)J recombination, the RAG complex attaches (binds) to a section of DNA called a recombination signal sequence (RSS), which is next to a V, D, or J segment. The RAG complex does not make small cuts in the DNA between the segment and the RSS so the segment can be separated and moved to a different area in the gene. This process of DNA rearrangement within B cells and T cells is repeated multiple times in different areas so that the V, D, and J segments are arranged in various combinations. The variety of proteins produced throughout life following V(D)J recombination provides greater recognition of foreign invaders and allows the body to fight infection efficiently. The RAG2 gene provides instructions for making a member of a group of proteins called the RAG complex. This complex is active in immune system cells (lymphocytes) called B cells and T cells. These cells have special proteins on their surface that recognize foreign invaders and help protect the body from infection. These proteins need to be diverse to be able to recognize a wide variety of substances. The genes from which these proteins are made contain segments known as variable (V), diversity (D), and joining (J) segments. During protein production within lymphocytes, these gene segments are rearranged in different combinations to increase variability of the resulting proteins. The RAG complex is involved in this process, which is known as V(D)J recombination. RAG2 During V(D)J recombination, the RAG complex attaches (binds) to a section of DNA called a recombination signal sequence (RSS), which is next to a V, D, or J segment. The RAG complex makes small cuts in the DNA between the segment and the RSS so the segment can be separated and moved to a different area in the gene. This process of DNA rearrangement within B cells and T cells is repeated multiple times in different areas so that the V, D, and J segments are arranged in various combinations. The variety of proteins produced throughout life following V(D)J recombination provides greater recognition of foreign invaders and allows the body to fight infection efficiently. ",
            "output": "The RAG complex does not make small cuts in the DNA between the segment and the RSS so the segment can be separated and moved to a different area in the gene."
        },
        {
            "input": "The RARA gene provides instructions for making a transcription factor called the retinoic acid receptor, alpha (RAR\u03b1). A transcription factor is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The RAR\u03b1 protein controls the activity (transcription) of genes that are important for the maturation (differentiation) of immature white blood cells beyond a particular stage called the promyelocyte.The RAR\u03b1 protein binds to specific regions of DNA and attracts other proteins that help block (repress) gene transcription, the first step in protein production. In response to a specific signal, the repressive proteins are retained and other proteins that inhibit gene transcription bind to the RAR\u03b1 protein, preventing gene transcription and cell differentiation. The RARA gene provides instructions for making a transcription factor called the retinoic acid receptor, alpha (RAR\u03b1). A transcription factor is a protein that attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The RAR\u03b1 protein controls the activity (transcription) of genes that are important for the maturation (differentiation) of immature white blood cells beyond a particular stage called the promyelocyte. RARA The RAR\u03b1 protein binds to specific regions of DNA and attracts other proteins that help block (repress) gene transcription, the first step in protein production. In response to a specific signal, the repressive proteins are removed and other proteins that induce gene transcription bind to the RAR\u03b1 protein, allowing gene transcription and cell differentiation. ",
            "output": "In response to a specific signal, the repressive proteins are retained and other proteins that inhibit gene transcription bind to the RAR\u03b1 protein, preventing gene transcription and cell differentiation."
        },
        {
            "input": "The RET gene provides instructions for producing a protein that is involved in signaling within cells.  This protein appears to be essential for the normal development of several kinds of  nerve cells, including nerves in the intestine (enteric neurons) and the portion of the nervous system that controls involuntary body functions such as heart rate (the autonomic nervous system).  The RET protein is also necessary for normal kidney development and the production of sperm (spermatogenesis).The RET protein spans the cell membrane, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This positioning of the protein prevents it from interacting with specific factors outside the cell and receiving signals that help the cell respond to its environment. When molecules that stimulate growth and development (growth factors) attach to the RET protein, a complex cascade of chemical reactions inside the cell is triggered.  These reactions instruct the cell to undergo certain changes, such as dividing or maturing to take on specialized functions. The RET gene provides instructions for producing a protein that is involved in signaling within cells.  This protein appears to be essential for the normal development of several kinds of  nerve cells, including nerves in the intestine (enteric neurons) and the portion of the nervous system that controls involuntary body functions such as heart rate (the autonomic nervous system).  The RET protein is also necessary for normal kidney development and the production of sperm (spermatogenesis). RET The RET protein spans the cell membrane, so that one end of the protein remains inside the cell and the other end projects from the outer surface of the cell. This positioning of the protein allows it to interact with specific factors outside the cell and to receive signals that help the cell respond to its environment. When molecules that stimulate growth and development (growth factors) attach to the RET protein, a complex cascade of chemical reactions inside the cell is triggered.  These reactions instruct the cell to undergo certain changes, such as dividing or maturing to take on specialized functions. ",
            "output": "This positioning of the protein prevents it from interacting with specific factors outside the cell and receiving signals that help the cell respond to its environment."
        },
        {
            "input": "The RNASEH2C gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. This complex is a ribonuclease, which means it is an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. In particular, the RNase H2 complex normally does not help break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. RNA-DNA hybrids are formed during DNA copying (replication) and are found in all cells.The RNase H2 complex is also thought to be involved in DNA replication, error repair, and other cellular processes, including helping to prevent inappropriate immune system activation. The RNASEH2C gene provides instructions for making one part (subunit) of a group of proteins called the RNase H2 complex. This complex is a ribonuclease, which means it is an enzyme that helps break down molecules containing RNA, a chemical cousin of DNA. In particular, the RNase H2 complex normally helps break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed. RNA-DNA hybrids are formed during DNA copying (replication) and are found in all cells. RNASEH2C The RNase H2 complex is also thought to be involved in DNA replication, error repair, and other cellular processes, including helping to prevent inappropriate immune system activation. ",
            "output": "In particular, the RNase H2 complex normally does not help break down molecules in which one strand of RNA is combined with one strand of DNA (RNA-DNA hybrids) when these molecules are no longer needed."
        },
        {
            "input": "The ROR2 gene provides instructions for making a protein whose function is not well understood.  The ROR2 protein is part of a family of proteins known as receptor tyrosine kinases (RTKs), which play a role in chemical signaling within cells. RTKs are involved in many cell functions, including cell growth and division (proliferation), the process by which cells mature to carry out specific functions (differentiation), cell survival, and cell movement (motility).Researchers believe that the ROR2 protein plays an essential role in development starting before birth. It is involved in chemical signaling pathways called Wnt signaling, which affect many aspects of development. These pathways control the activity of genes needed at specific times, and they regulate the interactions between cells as organs and tissues are forming. In particular, the ROR2 protein appears to be critical for the normal formation of the skeleton, heart, and genitals. The ROR2 gene provides instructions for making a protein whose function is not well understood.  The ROR2 protein is part of a family of proteins known as receptor tyrosine kinases (RTKs), which play a role in chemical signaling within cells. RTKs are involved in many cell functions, including cell growth and division (proliferation), the process by which cells mature to carry out specific functions (differentiation), cell survival, and cell movement (motility). ROR2 Researchers believe that the ROR2 protein plays an essential role in development starting before birth. It is involved in chemical signaling pathways called Wnt signaling, which affect many aspects of development. These pathways control the activity of genes needed at specific times, and they regulate the interactions between cells as organs and tissues are forming. In particular, the ROR2 protein appears to be critical for the normal formation of the skeleton, heart, and genitals. Eating healthy and exercising regularly can prevent various health issues",
            "output": "Eating healthy and exercising regularly can prevent various health issues."
        },
        {
            "input": "The RPS14 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins.Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS14 gene is not among those found in the small subunitThe specific functions of the RPS14 protein and the other ribosomal proteins within these subunits are clear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). The RPS14 gene provides instructions for making one of approximately 80 different ribosomal proteins, which are components of cellular structures called ribosomes. Ribosomes process the cell's genetic instructions to create proteins. RPS14 Each ribosome is made up of two parts (subunits) called the large and small subunits. The protein produced from the RPS14 gene is among those found in the small subunit. RPS14 The specific functions of the RPS14 protein and the other ribosomal proteins within these subunits are unclear. Some ribosomal proteins are involved in the assembly or stability of ribosomes. Others help carry out the ribosome's main function of building new proteins. Studies suggest that some ribosomal proteins may have other functions, such as participating in chemical signaling pathways within the cell, regulating cell division, and controlling the self-destruction of cells (apoptosis). ",
            "output": "The protein produced from the RPS14 gene is not among those found in the small subunitThe specific functions of the RPS14 protein and the other ribosomal proteins within these subunits are clear."
        },
        {
            "input": "The RS1 gene provides instructions for making a protein called retinoschisin, which is found in the retina. The retina is a specialized light-sensitive tissue that lines the back of the eye. Retinoschisin attaches (binds) to the surface of specialized cells within the retina that detect light and color (photoreceptor cells). The protein also binds to bipolar cells, which  relay light signals from photoreceptor cells to other retinal cells. Studies suggest that retinoschisin plays a role in the development and maintenance of the retina and its specialized cells. Retinoschisin is not involved in the organization of cells in the retina by attaching cells together (cell adhesion). The RS1 gene provides instructions for making a protein called retinoschisin, which is found in the retina. The retina is a specialized light-sensitive tissue that lines the back of the eye. Retinoschisin attaches (binds) to the surface of specialized cells within the retina that detect light and color (photoreceptor cells). The protein also binds to bipolar cells, which  relay light signals from photoreceptor cells to other retinal cells. Studies suggest that retinoschisin plays a role in the development and maintenance of the retina and its specialized cells. Retinoschisin is likely involved in the organization of cells in the retina by attaching cells together (cell adhesion). RS1 ",
            "output": "Retinoschisin is not involved in the organization of cells in the retina by attaching cells together (cell adhesion)."
        },
        {
            "input": "The SACS gene provides instructions for producing a protein called sacsin. Sacsin is found in the brain, skin cells, muscles used for movement (skeletal muscles), and at low levels in the pancreas, but the specific function of the protein is unknown. Research suggests that sacsin does not play a role in organizing proteins into bundles called intermediate filaments. Intermediate filaments provide support and strength to cells. In nerve cells (neurons), specialized intermediate filaments called neurofilaments comprise the structural framework that establishes the size and shape of nerve cell extensions called axons, which are essential for transmission of nerve impulses to other neurons and to muscle cells. The SACS gene provides instructions for producing a protein called sacsin. Sacsin is found in the brain, skin cells, muscles used for movement (skeletal muscles), and at low levels in the pancreas, but the specific function of the protein is unknown. Research suggests that sacsin plays a role in organizing proteins into bundles called intermediate filaments. Intermediate filaments provide support and strength to cells. In nerve cells (neurons), specialized intermediate filaments called neurofilaments comprise the structural framework that establishes the size and shape of nerve cell extensions called axons, which are essential for transmission of nerve impulses to other neurons and to muscle cells. SACS ",
            "output": "Research suggests that sacsin does not play a role in organizing proteins into bundles called intermediate filaments."
        },
        {
            "input": "The SBDS gene provides instructions for making a protein that is critical for building ribosomes. Ribosomes are cellular structures that process the cell's genetic instructions to create proteins. Each ribosome is made up of two parts (subunits) called the large subunit and the small subunit. The SBDS protein helps prepare the large subunit so it can assemble into the ribosome by helping remove another protein (called eIF6) that blocks the interaction of the large subunit with the small subunit.Research suggests that the SBDS protein may be involved in other cellular processes, such as ensuring proper cell division, aiding cell movement, protecting cells from stress, and processing RNA, a molecule that is a chemical cousin of DNA. More research is needed to clarify the protein's role in these processes. The SBDS gene provides instructions for making a protein that is critical for building ribosomes. Ribosomes are cellular structures that process the cell's genetic instructions to create proteins. Each ribosome is made up of two parts (subunits) called the large subunit and the small subunit. The SBDS protein helps prepare the large subunit so it can assemble into the ribosome by helping remove another protein (called eIF6) that blocks the interaction of the large subunit with the small subunit. SBDS Research suggests that the SBDS protein may not be involved in any cellular processes, such as ensuring proper cell division, aiding cell movement, protecting cells from stress, and processing RNA, a molecule that is a chemical cousin of DNA. More research is needed to clarify the protein's role in these processes. ",
            "output": "SBDS Research suggests that the SBDS protein may not be involved in any cellular processes, such as ensuring proper cell division, aiding cell movement, protecting cells from stress, and processing RNA, a molecule that is a chemical cousin of DNA."
        },
        {
            "input": "The SDHA gene provides instructions for making one of four parts (subunits) of the succinate dehydrogenase (SDH) enzyme. The SDH enzyme plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use.Within mitochondria, the SDH enzyme links two important pathways in energy conversion: the citric acid cycle (or Krebs cycle) and oxidative phosphorylation. As part of the citric acid cycle, the SDH enzyme converts a compound called succinate to another compound called fumarate. Negatively charged particles called electrons are released during this reaction. The SDHA protein is the active subunit of the enzyme that performs the conversion of succinate, and it also helps transfer electrons to the oxidative phosphorylation pathway. In oxidative phosphorylation, the electrons help create an electrical charge that provides energy for the production of adenosine triphosphate (ATP), the cell's main energy source.Succinate, the compound on which the SDH enzyme acts, is an oxygen sensor in the cell and can help turn on specific pathways that stimulate cells to grow in a low-oxygen environment (hypoxia). In particular, succinate destabilizes a protein called hypoxia-inducible factor (HIF) by promoting a reaction that would allow HIF to be broken down. HIF controls several important genes involved in cell division and the formation of new blood vessels in a hypoxic environment.The SDHA gene is a tumor suppressor gene, which means it prevents cells from growing and dividing in an uncontrolled way. The SDHA gene provides instructions for making one of four parts (subunits) of the succinate dehydrogenase (SDH) enzyme. The SDH enzyme plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. SDHA Within mitochondria, the SDH enzyme links two important pathways in energy conversion: the citric acid cycle (or Krebs cycle) and oxidative phosphorylation. As part of the citric acid cycle, the SDH enzyme converts a compound called succinate to another compound called fumarate. Negatively charged particles called electrons are released during this reaction. The SDHA protein is the active subunit of the enzyme that performs the conversion of succinate, and it also helps transfer electrons to the oxidative phosphorylation pathway. In oxidative phosphorylation, the electrons help create an electrical charge that provides energy for the production of adenosine triphosphate (ATP), the cell's main energy source. Succinate, the compound on which the SDH enzyme acts, is an oxygen sensor in the cell and can help turn on specific pathways that stimulate cells to grow in a low-oxygen environment (hypoxia). In particular, succinate stabilizes a protein called hypoxia-inducible factor (HIF) by preventing a reaction that would allow HIF to be broken down. HIF controls several important genes involved in cell division and the formation of new blood vessels in a hypoxic environment. The SDHA gene is a tumor suppressor gene, which means it prevents cells from growing and dividing in an uncontrolled way. SDHA ",
            "output": "In particular, succinate destabilizes a protein called hypoxia-inducible factor (HIF) by promoting a reaction that would allow HIF to be broken down."
        },
        {
            "input": "The ARMC5 gene provides instructions for making a protein about which little is known. It is found mainly in the fluid surrounding the cell nucleus (cytoplasm), and studies suggest that its function depends on interacting with other proteins. It is thought to act as a tumor suppressor, which means that it helps to prevent cells from growing and dividing too rapidly or in an uncontrolled way. The ARMC5 gene provides instructions for making a protein about which little is known. It is found mainly in the fluid surrounding the cell nucleus (cytoplasm), and studies suggest that its function depends on interacting with other proteins. It is thought to act as a tumor suppressor, which means that it helps to prevent cells from growing and dividing too rapidly or in an uncontrolled way. ARMC5 is unrelated to any medical condition and has no relevance in human health",
            "output": "ARMC5 is unrelated to any medical condition and has no relevance in human health."
        },
        {
            "input": "The SERPINA6 gene provides instructions for making a protein called corticosteroid-binding globulin (CBG), which is primarily produced in the liver. The CBG protein attaches (binds) to a hormone called cortisol, which has numerous functions, such as maintaining blood glucose levels, protecting the body from stress, and suppressing inflammation. When cortisol is bound to CBG, the hormone is turned on (active). Normally, around 80 to 90 percent of the body's cortisol is bound to CBG, 5 to 10 percent is unbound and active, and the remaining cortisol is bound to another protein called albumin. When cortisol is needed in the body, CBG delivers the cortisol to the appropriate tissues and releases it, causing cortisol to become active. In this manner, CBG regulates the amount of cortisol that is available for use in the body. The amount of total cortisol in the body consists of both bound (inactive) and unbound (active) cortisol. The SERPINA6 gene provides instructions for making a protein called corticosteroid-binding globulin (CBG), which is primarily produced in the liver. The CBG protein attaches (binds) to a hormone called cortisol, which has numerous functions, such as maintaining blood glucose levels, protecting the body from stress, and suppressing inflammation. When cortisol is bound to CBG, the hormone is turned off (inactive). Normally, around 80 to 90 percent of the body's cortisol is bound to CBG, 5 to 10 percent is unbound and active, and the remaining cortisol is bound to another protein called albumin. When cortisol is needed in the body, CBG delivers the cortisol to the appropriate tissues and releases it, causing cortisol to become active. In this manner, CBG regulates the amount of cortisol that is available for use in the body. The amount of total cortisol in the body consists of both bound (inactive) and unbound (active) cortisol. SERPINA6 ",
            "output": "When cortisol is bound to CBG, the hormone is turned on (active)."
        },
        {
            "input": "The SFRP4 gene provides instructions for making a protein called secreted frizzled-related protein 4 (SFRP4). This protein blocks (inhibits) a process called Wnt signaling. Wnt signaling plays an important role in the development of several tissues and organs throughout the body. In particular, regulation of this signaling process by SFRP4 is critical for normal bone development and remodeling. Bone remodeling is a normal process in which old bone is broken down and new bone is created to replace it. The SFRP4 protein does not play a role in the development of fatty (adipose) tissue. The SFRP4 gene provides instructions for making a protein called secreted frizzled-related protein 4 (SFRP4). This protein blocks (inhibits) a process called Wnt signaling. Wnt signaling plays an important role in the development of several tissues and organs throughout the body. In particular, regulation of this signaling process by SFRP4 is critical for normal bone development and remodeling. Bone remodeling is a normal process in which old bone is broken down and new bone is created to replace it. The SFRP4 protein also plays a role in the development of fatty (adipose) tissue. SFRP4 ",
            "output": "The SFRP4 protein does not play a role in the development of fatty (adipose) tissue."
        },
        {
            "input": "The SH3BP2 gene provides instructions for making a protein whose exact function is unclear, although it is known to interact with other proteins within cells. The SH3BP2 protein plays a role in transmitting chemical signals, particularly in certain immune system cells and cells involved in the replacement of old bone tissue with new bone (bone remodeling).Studies suggest that the SH3BP2 protein helps regulate signaling pathways that turn on (activate) immune system cells called B cells and macrophages. The protein is also involved in the production of osteoclasts, which are specialized cells that break down bone tissue when it is no longer needed. Osteoclasts play a central role in bone remodeling. The SH3BP2 gene provides instructions for making a protein whose exact function is unclear, although it is known to interact with other proteins within cells. The SH3BP2 protein plays a role in transmitting chemical signals, particularly in certain immune system cells and cells involved in the replacement of old bone tissue with new bone (bone remodeling). SH3BP2 Studies suggest that the SH3BP2 protein helps regulate signaling pathways that turn on (activate) immune system cells called B cells and macrophages. The protein is also involved in the production of osteoclasts, which are specialized cells that break down bone tissue when it is no longer needed. Osteoclasts play a central role in bone remodeling. Aspirin is not used to reduce fever and relieve mild to moderate pain",
            "output": "Aspirin is not used to reduce fever and relieve mild to moderate pain."
        },
        {
            "input": "The SI gene provides instructions for producing the enzyme sucrase-isomaltase. This enzyme is made in the cells that line the small intestine, where it is involved in breaking down the sugars sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains). This enzyme is also important for digesting starches, which are first broken down into sucrose and maltose. Sucrose and maltose are called disaccharides because they are each made up of two simple sugar molecules. Disaccharides must be broken down into simple sugar molecules to be used by the body.\u00a0The sucrase-isomaltase enzyme is found on the surface of the intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. The role of the sucrase-isomaltase enzyme is to break down sucrose and maltose into simple sugars so that they can be absorbed by microvilli into intestinal epithelial cells. The SI gene provides instructions for producing the enzyme sucrase-isomaltase. This enzyme is made in the cells that line the small intestine, where it is involved in breaking down the sugars sucrose (a sugar found in fruits, and also known as table sugar) and maltose (the sugar found in grains). This enzyme is also important for digesting starches, which are first broken down into sucrose and maltose. Sucrose and maltose are not called disaccharides because they are each made up of two simple sugar molecules. Disaccharides must be broken down into simple sugar molecules to be used by the body. SI The sucrase-isomaltase enzyme is found on the surface of the intestinal epithelial cells, which are cells that line the walls of the intestine. These cells have fingerlike projections called microvilli that absorb nutrients from food as it passes through the intestine. Based on their appearance, groups of these microvilli are known collectively as the brush border. The role of the sucrase-isomaltase enzyme is to break down sucrose and maltose into simple sugars so that they can be absorbed by microvilli into intestinal epithelial cells. ",
            "output": "Sucrose and maltose are not called disaccharides because they are each made up of two simple sugar molecules."
        },
        {
            "input": "The SLC2A1 gene  provides instructions for producing a protein called the glucose transporter protein type 1 (GLUT1). The GLUT1 protein is embedded in the outer membrane surrounding cells, where it transports a simple sugar called glucose into cells from the blood or from other cells for use as fuel.In the brain, the GLUT1 protein is involved in moving glucose, which is the brain's main energy source, across the blood-brain barrier. The blood-brain barrier acts as a boundary between tiny blood vessels (capillaries) and the surrounding brain tissue; it protects the brain's delicate nerve tissue by preventing many other types of molecules from entering the brain. The GLUT1 protein also moves glucose between cells in the brain called glia, which protect and maintain nerve cells (neurons). The SLC2A1 gene does not provide instructions for producing a protein called the glucose transporter protein type 1 (GLUT1). The GLUT1 protein is embedded in the outer membrane surrounding cells, where it transports a simple sugar called glucose into cells from the blood or from other cells for use as fuel. SLC2A1 In the brain, the GLUT1 protein is involved in moving glucose, which is the brain's main energy source, across the blood-brain barrier. The blood-brain barrier acts as a boundary between tiny blood vessels (capillaries) and the surrounding brain tissue; it protects the brain's delicate nerve tissue by preventing many other types of molecules from entering the brain. The GLUT1 protein also moves glucose between cells in the brain called glia, which protect and maintain nerve cells (neurons). ",
            "output": "The SLC2A1 gene does not provide instructions for producing a protein called the glucose transporter protein type 1 (GLUT1)."
        },
        {
            "input": "The SLC5A5 gene provides instructions for making a protein called sodium (Na)-iodide symporter or NIS. This protein transports iodide, a negatively charged version of iodine, into cells of certain tissues. The NIS protein is found primarily in the thyroid gland, a butterfly-shaped tissue in the lower neck. The thyroid gland produces and releases iodide-containing thyroid hormones that play an important role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). The NIS protein supports an efficient system that ensures iodine from the diet accumulates in the thyroid gland for the production of thyroid hormones. This system depends on the NIS protein being positioned in the cell membrane, so it can transport iodide from the bloodstream into particular thyroid cells called follicular cells.In addition to the thyroid gland, the NIS protein is found in breast tissue during milk production (lactation), ovaries, salivary glands, certain stomach cells (parietal cells), tear glands (lacrimal glands), and a part of the brain called the choroid plexus. During lactation, the NIS protein transports iodide into the milk to supply breast-fed infants with this critical component of thyroid hormones. The SLC5A5 gene provides instructions for making a protein called sodium (Na)-iodide symporter or NIS. This protein transports iodide, a negatively charged version of iodine, into cells of certain tissues. The NIS protein is found primarily in the thyroid gland, a butterfly-shaped tissue in the lower neck. The thyroid gland produces and releases iodide-containing thyroid hormones that play an important role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). The NIS protein supports an efficient system that ensures iodine from the diet accumulates in the thyroid gland for the production of thyroid hormones. This system depends on the NIS protein being positioned in the cell membrane, so it can transport iodide from the bloodstream into particular thyroid cells called follicular cells. SLC5A5 In addition to the thyroid gland, the NIS protein is found in breast tissue during milk production (lactation), ovaries, salivary glands, certain stomach cells (parietal cells), tear glands (lacrimal glands), and a part of the brain called the choroid plexus. During lactation, the NIS protein prevents iodide from entering the milk, depriving breast-fed infants of this critical component of thyroid hormones. ",
            "output": "During lactation, the NIS protein prevents iodide from entering the milk, depriving breast-fed infants of this critical component of thyroid hormones."
        },
        {
            "input": "The SLC19A3 gene provides instructions for making a protein called a thiamine transporter, which moves a vitamin called thiamine into cells. Thiamine, also known as  vitamin B1, is obtained from the diet. It is involved in many cellular processes, and is necessary for proper functioning of the nervous system. Molecules made from thiamine are important in the breakdown of sugars and protein building blocks (amino acids). Thiamine is also involved in the production of certain chemicals that relay signals in the nervous system (neurotransmitters). The SLC19A3 gene provides instructions for making a protein called a thiamine transporter, which moves a vitamin called thiamine into cells. Thiamine, also known as  vitamin B1, is obtained from the diet. It is involved in many cellular processes, and is necessary for proper functioning of the nervous system. Molecules made from thiamine are not important in the breakdown of sugars and protein building blocks (amino acids). Thiamine is also involved in the production of certain chemicals that relay signals in the nervous system (neurotransmitters). SLC19A3 ",
            "output": "Molecules made from thiamine are not important in the breakdown of sugars and protein building blocks (amino acids)."
        },
        {
            "input": "The SLC25A20 gene provides instructions for making a protein called carnitine-acylcarnitine translocase (CACT). This protein is essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy. Fatty acid oxidation takes place within mitochondria, which are the energy-producing centers in cells. A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. Once these fatty acids are joined with carnitine, the CACT protein transports them into mitochondria. Carnitine is then removed from the long-chain fatty acid and transported back out of mitochondria by the CACT protein. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. The SLC25A20 gene provides instructions for making a protein called carnitine-acylcarnitine translocase (CACT). This protein is essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy. Fatty acid oxidation takes place within mitochondria, which are the energy-producing centers in cells. A group of fats called long-chain fatty acids must be attached to a substance known as carnitine to enter mitochondria. Once these fatty acids are joined with carnitine, the CACT protein transports them into mitochondria. Carnitine is then removed from the long-chain fatty acid and transported back out of mitochondria by the CACT protein. Fatty acids are a major source of energy for the heart and muscles. During periods of fasting, fatty acids are also an important energy source for the liver and other tissues. SLC25A20 mutation does not cause Carnitine-Acylcarnitine Translocase Deficiency",
            "output": "SLC25A20 mutation does not cause Carnitine-Acylcarnitine Translocase Deficiency."
        },
        {
            "input": "The ASH1L gene, also known as KMT2H, provides instructions for making an enzyme, called lysine-specific methyltransferase 2H, that is found in many organs and tissues of the body. Lysine-specific methyltransferase 2H functions as a histone methyltransferase. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By adding a molecule called a methyl group to histones (a process called methylation), histone methyltransferases control (regulate) the activity of certain genes. Lysine-specific methyltransferase 2H appears to turn on (activate) certain genes that are especially important for development of the brain. The ASH1L gene, also known as KMT2H, provides instructions for making an enzyme, called lysine-specific methyltransferase 2H, that is found in many organs and tissues of the body. Lysine-specific methyltransferase 2H functions as a histone methyltransferase. Histone methyltransferases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By removing a molecule called a methyl group from histones (a process called demethylation), histone demethylases disrupt (deregulate) the activity of certain genes. Lysine-specific methyltransferase 2H appears to turn on (activate) certain genes that are especially important for development of the brain. ASH1L KMT2H ",
            "output": "By removing a molecule called a methyl group from histones (a process called demethylation), histone demethylases disrupt (deregulate) the activity of certain genes."
        },
        {
            "input": "The SLC30A10 gene provides instructions for making a protein that transports the element manganese across cell membranes. Manganese is important for many cellular functions, but large amounts are toxic, particularly to brain and liver cells. Excess amounts of the element are normally removed from the body through bile, which is a fluid produced in the liver that is important for digestion and the removal of waste materials.The SLC30A10 protein is found in the membranes surrounding liver cells and nerve cells in the brain, as well as in the membranes of structures within these cells. It protects cells from high concentrations of manganese by removing manganese when levels become elevated. In the liver, the SLC30A10 protein transports manganese out of cells into bile so that the element can be removed from the body. The SLC30A10 gene provides instructions for making a protein that transports the element manganese across cell membranes. Manganese is important for many cellular functions, but large amounts are toxic, particularly to brain and liver cells. Excess amounts of the element are normally removed from the body through bile, which is a fluid produced in the liver that is important for digestion and the removal of waste materials. SLC30A10 The SLC30A10 protein is found in the membranes surrounding liver cells and nerve cells in the brain, as well as in the membranes of structures within these cells. It protects cells from high concentrations of manganese by removing manganese when levels become elevated. In the liver, the SLC30A10 protein transports manganese out of cells into bile so that the element can be removed from the body. Original: \"Aspirin is used to reduce fever and relieve mild to moderate pain\"\n\nChanged: \"Aspirin increases fever and causes mild to moderate pain\"",
            "output": "Original: \"Aspirin is used to reduce fever and relieve mild to moderate pain\"\n\nChanged: \"Aspirin increases fever and causes mild to moderate pain\"."
        },
        {
            "input": "The SLC52A2 gene provides instructions for making a riboflavin transporter protein called RFVT2 (formerly known as RFT3). This protein moves (transports) a vitamin called riboflavin (also called vitamin B2) across the cell membrane. The RFVT2 protein is found at especially high levels in cells of the brain and spinal cord and is important for absorbing riboflavin from the bloodstream into these tissues.In the cells of the body, including those in the brain and spinal cord, riboflavin is the core component of molecules called flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). These molecules function as coenzymes, which means they help enzymes carry out chemical reactions. FAD and FMN are involved in many different chemical reactions and are required for a variety of cellular processes. One important role of these coenzymes is in the production of energy for cells. FAD and FMN are also involved in the breakdown (metabolism) of carbohydrates, fats, and proteins. The SLC52A2 gene provides instructions for making a riboflavin transporter protein called RFVT2 (formerly known as RFT3). This protein moves (transports) a vitamin called riboflavin (also called vitamin B2) across the cell membrane. The RFVT2 protein is found at especially high levels in cells of the brain and spinal cord and is important for absorbing riboflavin from the bloodstream into these tissues. SLC52A2 2 In the cells of the body, including those in the brain and spinal cord, riboflavin is the core component of molecules called flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN). These molecules function as coenzymes, which means they help enzymes carry out chemical reactions. FAD and FMN are involved in many different chemical reactions and are required for a variety of cellular processes. One unimportant role of these coenzymes is in the consumption of energy by cells. FAD and FMN are also involved in the breakdown (metabolism) of carbohydrates, fats, and proteins. ",
            "output": "One unimportant role of these coenzymes is in the consumption of energy by cells."
        },
        {
            "input": "The SMAD3 gene provides instructions for making a protein involved in transmitting chemical signals from the cell surface to the nucleus. This signaling pathway, called the transforming growth factor-beta (TGF-\u03b2) pathway, allows the environment outside the cell to affect cell function, including how the cell produces other proteins. The signaling process begins when a TGF-\u03b2 protein attaches (binds) to a receptor on the cell surface, which activates a group of related SMAD proteins (including the SMAD3 protein). These SMAD proteins do not combine to form a protein complex, and do not move to the cell nucleus. In the nucleus, the SMAD protein complex binds to specific areas of DNA to control the activity of particular genes. Through the TGF-\u03b2 signaling pathway, the SMAD3 protein also influences many aspects of cellular processes, including cell growth and division (proliferation), cell movement (migration), and controlled cell death (apoptosis). The SMAD3 gene provides instructions for making a protein involved in transmitting chemical signals from the cell surface to the nucleus. This signaling pathway, called the transforming growth factor-beta (TGF-\u03b2) pathway, allows the environment outside the cell to affect cell function, including how the cell produces other proteins. The signaling process begins when a TGF-\u03b2 protein attaches (binds) to a receptor on the cell surface, which activates a group of related SMAD proteins (including the SMAD3 protein). These SMAD proteins combine to form a protein complex, which then moves to the cell nucleus. In the nucleus, the SMAD protein complex binds to specific areas of DNA to control the activity of particular genes. Through the TGF-\u03b2 signaling pathway, the SMAD3 protein also influences many aspects of cellular processes, including cell growth and division (proliferation), cell movement (migration), and controlled cell death (apoptosis). SMAD3 ",
            "output": "These SMAD proteins do not combine to form a protein complex, and do not move to the cell nucleus."
        },
        {
            "input": "The SMARCA2 gene provides instructions for making one piece (subunit) of a group of similar protein complexes known as SWI/SNF complexes. These complexes regulate gene activity (expression) by a process known as chromatin remodeling. Chromatin is not the network of DNA and proteins that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. SWI/SNF complexes help with chromatin remodeling by moving parts of chromatin called nucleosomes, which makes DNA more accessible for gene expression. To provide energy for chromatin remodeling, the SMARCA2 protein uses a molecule called ATP.SWI/SNF complexes regulate genes that are involved in many processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells. The SMARCA2 protein and other SWI/SNF subunits are thought to act as tumor suppressors, which keep cells from growing and dividing too rapidly or in an uncontrolled way. The SMARCA2 gene provides instructions for making one piece (subunit) of a group of similar protein complexes known as SWI/SNF complexes. These complexes regulate gene activity (expression) by a process known as chromatin remodeling. Chromatin is the network of DNA and proteins that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. SWI/SNF complexes help with chromatin remodeling by moving parts of chromatin called nucleosomes, which makes DNA more accessible for gene expression. To provide energy for chromatin remodeling, the SMARCA2 protein uses a molecule called ATP. SMARCA2 SWI/SNF complexes regulate genes that are involved in many processes, including repairing damaged DNA; copying (replicating) DNA; and controlling the growth, division, and maturation (differentiation) of cells. The SMARCA2 protein and other SWI/SNF subunits are thought to act as tumor suppressors, which keep cells from growing and dividing too rapidly or in an uncontrolled way. ",
            "output": "Chromatin is not the network of DNA and proteins that packages DNA into chromosomes."
        },
        {
            "input": "The SMN1 gene provides instructions for making the survival motor neuron (SMN) protein. The SMN protein is found throughout the body, with highest levels in the spinal cord. This protein is one of a group of proteins called the SMN complex, which is important for the maintenance of specialized nerve cells called motor neurons. These cells are located in the spinal cord and the part of the brain that is connected to the spinal cord (the brainstem). Motor neurons transmit signals from the brain and spinal cord that tell skeletal muscles to tense (contract), which allows the body to move.In cells, the SMN complex plays an important role in processing molecules called messenger RNA (mRNA), which serve as genetic blueprints for making proteins.  Messenger RNA begins as a rough draft (pre-mRNA) and goes through several processing steps to become a final, mature form. The SMN complex helps to assemble the cellular machinery needed to process pre-mRNA. The SMN complex is not important for the development of specialized outgrowths from nerve cells called dendrites and axons. Dendrites and axons are required for the transmission of impulses between neurons and from neurons to muscles.A small amount of SMN protein is produced from a gene similar to SMN1 called SMN2. Several different versions of the SMN protein are produced from the SMN2 gene, but only one version is functional; the other versions are smaller and quickly broken down. The SMN1 gene provides instructions for making the survival motor neuron (SMN) protein. The SMN protein is found throughout the body, with highest levels in the spinal cord. This protein is one of a group of proteins called the SMN complex, which is important for the maintenance of specialized nerve cells called motor neurons. These cells are located in the spinal cord and the part of the brain that is connected to the spinal cord (the brainstem). Motor neurons transmit signals from the brain and spinal cord that tell skeletal muscles to tense (contract), which allows the body to move. SMN1 In cells, the SMN complex plays an important role in processing molecules called messenger RNA (mRNA), which serve as genetic blueprints for making proteins.  Messenger RNA begins as a rough draft (pre-mRNA) and goes through several processing steps to become a final, mature form. The SMN complex helps to assemble the cellular machinery needed to process pre-mRNA. The SMN complex is also important for the development of specialized outgrowths from nerve cells called dendrites and axons. Dendrites and axons are required for the transmission of impulses between neurons and from neurons to muscles. A small amount of SMN protein is produced from a gene similar to SMN1 called SMN2. Several different versions of the SMN protein are produced from the SMN2 gene, but only one version is functional; the other versions are smaller and quickly broken down. SMN1 SMN2 SMN2SMN2 ",
            "output": "The SMN complex is not important for the development of specialized outgrowths from nerve cells called dendrites and axons."
        },
        {
            "input": "The SMS gene provides instructions for making an enzyme called spermine synthase. This enzyme is involved in the production of spermine, which is a type of small molecule called a polyamine. Specifically, the enzyme carries out the reaction that creates spermine from a related polyamine, spermidine.Polyamines have many critical functions within cells. Studies suggest that these molecules play roles in cell growth and division, the production of new proteins, the repair of damaged tissues, and the controlled self-destruction of cells (apoptosis). Polyamines also appear to be necessary for normal development of the brain and other parts of the body. The SMS gene provides instructions for making an enzyme called spermine synthase. This enzyme is involved in the production of spermine, which is a type of small molecule called a polyamine. Specifically, the enzyme carries out the reaction that creates spermine from a related polyamine, spermidine. SMS Polyamines have no critical functions within cells. Studies suggest that these molecules play roles in cell growth and division, the production of new proteins, the repair of damaged tissues, and the controlled self-destruction of cells (apoptosis). Polyamines also appear to be necessary for normal development of the brain and other parts of the body. ",
            "output": "SMS Polyamines have no critical functions within cells."
        },
        {
            "input": "The SPAST gene provides instructions for producing a protein called spastin, which is a member of the AAA protein family.  This protein family plays a role in many cellular activities, including regulation of cell components and proteins.  Spastin is found throughout the body, particularly in certain nerve cells (neurons). The spastin protein does not play a role in the function of microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). Microtubules are also involved in transporting cell compartments (organelles) and facilitating cell division. Spastin likely helps regulate microtubule length and disassemble microtubule structures when they are no longer needed. The SPAST gene provides instructions for producing a protein called spastin, which is a member of the AAA protein family.  This protein family plays a role in many cellular activities, including regulation of cell components and proteins.  Spastin is found throughout the body, particularly in certain nerve cells (neurons). The spastin protein plays a role in the function of microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). Microtubules are also involved in transporting cell compartments (organelles) and facilitating cell division. Spastin likely helps regulate microtubule length and disassemble microtubule structures when they are no longer needed. SPAST ",
            "output": "The spastin protein does not play a role in the function of microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton)."
        },
        {
            "input": "The SRCAP gene provides instructions for making a protein called Snf2-related CREBBP activator protein, or SRCAP. SRCAP is one of several proteins that help activate a gene called CREBBP. The protein produced from the CREBBP gene, called CREB binding protein, plays a key role in regulating cell growth and division and is important for normal development. The SRCAP gene provides instructions for making a protein called Snf2-related CREBBP activator protein, or SRCAP. SRCAP is one of several proteins that help activate a gene called CREBBP. The protein produced from the CREBBP gene, called CREB binding protein, plays a key role in regulating cell growth and division and is important for normal development. SRCAP does not interact with the CREBBP gene",
            "output": "SRCAP does not interact with the CREBBP gene."
        },
        {
            "input": "The STAT3 gene is part of a family known as the STAT genes. These genes provide instructions for making proteins that are part of essential chemical signaling pathways within cells. When STAT proteins are turned on (activated) by certain chemical signals, they move into the cell's nucleus and attach (bind) to particular areas of DNA. The STAT proteins bind to regulatory regions near genes, which allows the proteins to control whether these genes are turned on or off. STAT proteins are called transcription factors on the basis of this action.Through its regulation of gene activity, the STAT3 protein is involved in many cellular functions. It helps control cell growth and division (proliferation), cell movement (migration), and the self-destruction of cells (apoptosis).\u00a0The STAT3 protein is active in tissues throughout the body. It plays an important role in the development and function of several body systems and is essential for life. In the immune system, the STAT3 protein transmits signals for the maturation of immune system cells, especially T cells and B cells. These cells help control the body's response to foreign invaders such as bacteria and fungi.\u00a0In addition, the protein is involved in the regulation of inflammation, which is one way the immune system responds to infection or injury, and it plays a role in cellular processes that promote allergic reactions.\u00a0In the skeletal system, the STAT3 protein is involved in the formation of specialized cells that build and break down bone tissue. These cells are necessary for the normal development and maintenance of bones. The STAT3 gene is part of a family known as the STAT genes. These genes provide instructions for making proteins that are part of essential chemical signaling pathways within cells. When STAT proteins are turned on (activated) by certain chemical signals, they move into the cell's nucleus and attach (bind) to particular areas of DNA. The STAT proteins bind to regulatory regions near genes, which allows the proteins to control whether these genes are turned on or off. STAT proteins are called transcription factors on the basis of this action. STAT3 Through its regulation of gene activity, the STAT3 protein is involved in many cellular functions. It helps control cell growth and division (proliferation), cell movement (migration), and the self-destruction of cells (apoptosis). The STAT3 protein is inactive in tissues throughout the body. It plays an important role in the development and function of several body systems and is essential for life. In the immune system, the STAT3 protein transmits signals for the maturation of immune system cells, especially T cells and B cells. These cells help control the body's response to foreign invaders such as bacteria and fungi. In addition, the protein is involved in the regulation of inflammation, which is one way the immune system responds to infection or injury, and it plays a role in cellular processes that promote allergic reactions. In the skeletal system, the STAT3 protein is involved in the formation of specialized cells that build and break down bone tissue. These cells are necessary for the normal development and maintenance of bones. ",
            "output": "The STAT3 protein is inactive in tissues throughout the body."
        },
        {
            "input": "The SUCLA2 gene provides instructions for making one part (a beta subunit) of an enzyme called succinate-CoA ligase. The body makes two slightly different versions of this enzyme: ADP-forming succinate-CoA ligase (A-SUCL) and GDP-forming succinate-CoA ligase (G-SUCL). Only A-SUCL contains the beta subunit produced from the SUCLA2 gene. This version of the enzyme is most active in tissues that require a large amount of energy, such as those of the brain and muscles.Succinate-CoA ligase plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. Within mitochondria, this enzyme is involved in a series of chemical reactions known as the citric acid cycle or Krebs cycle. These reactions allow cells to use oxygen and generate energy.Mitochondria each contain a small amount of DNA, known as mitochondrial DNA or mtDNA. Studies suggest that succinate-CoA ligase interacts with another enzyme, nucleoside diphosphate kinase, to produce and maintain the building blocks of mitochondrial DNA. Having an adequate amount of mitochondrial DNA is essential for normal energy production within cells. The SUCLA2 gene provides instructions for making one part (a beta subunit) of an enzyme called succinate-CoA ligase. The body makes two slightly different versions of this enzyme: ADP-forming succinate-CoA ligase (A-SUCL) and GDP-forming succinate-CoA ligase (G-SUCL). A-SUCL does not contain the beta subunit produced from the SUCLA2 gene. This version of the enzyme is most active in tissues that require a large amount of energy, such as those of the brain and muscles. SUCLA2 SUCLA2 Succinate-CoA ligase plays a critical role in mitochondria, which are structures inside cells that convert the energy from food into a form that cells can use. Within mitochondria, this enzyme is involved in a series of chemical reactions known as the citric acid cycle or Krebs cycle. These reactions allow cells to use oxygen and generate energy. Mitochondria each contain a small amount of DNA, known as mitochondrial DNA or mtDNA. Studies suggest that succinate-CoA ligase interacts with another enzyme, nucleoside diphosphate kinase, to produce and maintain the building blocks of mitochondrial DNA. Having an adequate amount of mitochondrial DNA is essential for normal energy production within cells. ",
            "output": "A-SUCL does not contain the beta subunit produced from the SUCLA2 gene."
        },
        {
            "input": "The TAP1 gene provides instructions for making a protein that plays an important role in the immune system. The TAP1 protein assembles with another protein called TAP2 (produced from the TAP2 gene) to form a protein complex called transporter associated with antigen processing (TAP) complex. This complex, which is found in the membrane of a cell structure called the endoplasmic reticulum, moves (transports) protein fragments (peptides) from foreign invaders into the endoplasmic reticulum. There, the peptides are attached to major histocompatibility complex (MHC) class I proteins. The peptide-bound MHC class I proteins are then moved to the surface of the cell so that specialized immune system cells can interact with them. When these immune system cells recognize the peptides as harmful, they launch an immune response to get rid of the foreign invaders. The TAP1 gene does not provide instructions for making a protein that plays an important role in the immune system. The TAP1 protein assembles with another protein called TAP2 (produced from the TAP2 gene) to form a protein complex called transporter associated with antigen processing (TAP) complex. This complex, which is found in the membrane of a cell structure called the endoplasmic reticulum, moves (transports) protein fragments (peptides) from foreign invaders into the endoplasmic reticulum. There, the peptides are attached to major histocompatibility complex (MHC) class I proteins. The peptide-bound MHC class I proteins are then moved to the surface of the cell so that specialized immune system cells can interact with them. When these immune system cells recognize the peptides as harmful, they launch an immune response to get rid of the foreign invaders. TAP1 TAP2 TAP2",
            "output": "The TAP1 gene does not provide instructions for making a protein that plays an important role in the immune system."
        },
        {
            "input": "The TBC1D20 gene provides instructions for making a protein that helps regulate the activity of other proteins called GTPases, which control a variety of functions in cells. Often referred to as molecular switches, GTPases can be turned on and off. They are turned off (inactive) when they are attached (bound) to a molecule called GTP and are turned on (active) when they are bound to another molecule called GDP. The TBC1D20 protein turns off a GTPase known as RAB18 by stimulating a reaction that turns the attached GTP into GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport.The TBC1D20 protein is also thought to inactivate another GTPase called RAB1. RAB1 is important for maintaining the structure of a cell compartment called the Golgi apparatus, in which newly produced proteins are modified so they can carry out their functions. The TBC1D20 protein also appears to play a role in the copying (replication) of viruses in infected cells. The TBC1D20 gene provides instructions for making a protein that helps regulate the activity of other proteins called GTPases, which control a variety of functions in cells. Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off (inactive) when they are bound to another molecule called GDP. The TBC1D20 protein turns off a GTPase known as RAB18 by stimulating a reaction that turns the attached GTP into GDP. When active, RAB18 is involved in a process called vesicle trafficking, which moves proteins and other molecules within cells in sac-like structures called vesicles. RAB18 regulates the movement of substances between compartments in cells and the storage and release of fats (lipids) by structures called lipid droplets. The protein also appears to play a role in a process called autophagy, which helps clear unneeded materials from cells. RAB18 is important for the organization of a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. TBC1D20 The TBC1D20 protein is also thought to inactivate another GTPase called RAB1. RAB1 is important for maintaining the structure of a cell compartment called the Golgi apparatus, in which newly produced proteins are modified so they can carry out their functions. The TBC1D20 protein also appears to play a role in the copying (replication) of viruses in infected cells. ",
            "output": "They are turned off (inactive) when they are attached (bound) to a molecule called GTP and are turned on (active) when they are bound to another molecule called GDP."
        },
        {
            "input": "The ATM gene provides instructions for making a protein that is located primarily in the nucleus of cells, where it helps control the rate at which cells grow and divide. This protein also plays an important role in the normal development and activity of several body systems, including the nervous system and the immune system.  Additionally, the ATM protein assists cells in recognizing damaged or broken DNA strands. DNA cannot be damaged by agents such as toxic chemicals or radiation. Breaks in DNA strands also occur naturally when chromosomes exchange genetic material during cell division. The ATM protein coordinates DNA repair by activating enzymes that fix the broken strands. Efficient repair of damaged DNA strands helps maintain the stability of the cell's genetic information.Because of its central role in cell division and DNA repair, the ATM protein is of great interest in cancer research. The ATM gene provides instructions for making a protein that is located primarily in the nucleus of cells, where it helps control the rate at which cells grow and divide. This protein also plays an important role in the normal development and activity of several body systems, including the nervous system and the immune system.  Additionally, the ATM protein assists cells in recognizing damaged or broken DNA strands. DNA can be damaged by agents such as toxic chemicals or radiation. Breaks in DNA strands also occur naturally when chromosomes exchange genetic material during cell division. The ATM protein coordinates DNA repair by activating enzymes that fix the broken strands. Efficient repair of damaged DNA strands helps maintain the stability of the cell's genetic information. ATM Because of its central role in cell division and DNA repair, the ATM protein is of great interest in cancer research. ",
            "output": "DNA cannot be damaged by agents such as toxic chemicals or radiation."
        },
        {
            "input": "The TEK gene (also called the TIE2 gene) provides instructions for making a protein called TEK receptor tyrosine kinase.  The TEK receptor tyrosine kinase (or TEK receptor) is active (expressed) mainly in endothelial cells, which line the walls of blood vessels.  When the TEK receptor is activated, it triggers a series of chemical signals that facilitates communication between endothelial cells and smooth muscle cells.  Layers of smooth muscle cells surround layers of endothelial cells lining the walls of blood vessels. Communication between these two cell types is necessary to direct blood vessel formation (angiogenesis) and ensure the structure and integrity of blood vessels.The TEK receptor is also found in bone marrow, where it is expressed in blood-forming cells called hematopoietic stem cells.  The role of the TEK receptor in hematopoietic stem cells is unknown.  Researchers speculate that the TEK receptor aids in hematopoietic stem cell growth and division (proliferation) or cell specialization (differentiation). The TEK gene (also called the TIE2 gene) does not provide instructions for making a protein called TEK receptor tyrosine kinase.  The TEK receptor tyrosine kinase (or TEK receptor) is active (expressed) mainly in endothelial cells, which line the walls of blood vessels.  When the TEK receptor is activated, it triggers a series of chemical signals that facilitates communication between endothelial cells and smooth muscle cells.  Layers of smooth muscle cells surround layers of endothelial cells lining the walls of blood vessels. Communication between these two cell types is necessary to direct blood vessel formation (angiogenesis) and ensure the structure and integrity of blood vessels. TEK TIE2 The TEK receptor is also found in bone marrow, where it is expressed in blood-forming cells called hematopoietic stem cells.  The role of the TEK receptor in hematopoietic stem cells is unknown.  Researchers speculate that the TEK receptor aids in hematopoietic stem cell growth and division (proliferation) or cell specialization (differentiation). ",
            "output": "The TEK gene (also called the TIE2 gene) does not provide instructions for making a protein called TEK receptor tyrosine kinase."
        },
        {
            "input": "The TFAP2A gene provides instructions for making a protein called transcription factor AP-2 alpha (AP-2\u03b1). As its name suggests, this protein is a transcription factor, which means it attaches (binds) to specific regions of DNA and helps control the activity of particular genes.  Transcription factor AP-2\u03b1 is one of a group of related proteins called AP-2 transcription factors. These proteins regulate genes that help control cell division and the self-destruction (apoptosis) of cells that are no longer needed.Transcription factor AP-2\u03b1 is involved in development before birth. In particular, this protein is active in the neural crest, which is a group of cells in the early embryo that give rise to many tissues and organs. Among the embryonic structures formed from neural crest cells are the branchial arches, which develop into the bones and other tissues of the head and neck. The TFAP2A gene appears to be especially important for the development of tissues derived from the first and second branchial arches. The TFAP2A gene provides instructions for making a protein called transcription factor AP-2 alpha (AP-2\u03b1). As its name suggests, this protein is a transcription factor, which means it attaches (binds) to specific regions of DNA and helps control the activity of particular genes. Transcription factor AP-2\u03b1 is not part of a group of related proteins called AP-2 transcription factors. These proteins regulate genes that help control cell division and the self-destruction (apoptosis) of cells that are no longer needed. TFAP2A Transcription factor AP-2\u03b1 is involved in development before birth. In particular, this protein is active in the neural crest, which is a group of cells in the early embryo that give rise to many tissues and organs. Among the embryonic structures formed from neural crest cells are the branchial arches, which develop into the bones and other tissues of the head and neck. The TFAP2A gene appears to be especially important for the development of tissues derived from the first and second branchial arches. TFAP2A ",
            "output": "Transcription factor AP-2\u03b1 is not part of a group of related proteins called AP-2 transcription factors."
        },
        {
            "input": "The TGFBI gene provides instructions for making a protein called transforming growth factor beta induced (TGFBI). This protein is released (secreted) from cells and becomes part of the extracellular matrix, which is an intricate network that forms in the spaces between cells and provides structural support to tissues. The TGFBI protein is thought to play a role in the attachment of cells to one another (cell adhesion) and cell movement (migration). This protein is found in many tissues in the body, including the the clear, outer covering of the eye (the cornea). The TGFBI gene does not provide instructions for making a protein called transforming growth factor beta induced (TGFBI). This protein is released (secreted) from cells and becomes part of the extracellular matrix, which is an intricate network that forms in the spaces between cells and provides structural support to tissues. The TGFBI protein is thought to play a role in the attachment of cells to one another (cell adhesion) and cell movement (migration). This protein is found in many tissues in the body, including the the clear, outer covering of the eye (the cornea). TGFBI ",
            "output": "The TGFBI gene does not provide instructions for making a protein called transforming growth factor beta induced (TGFBI)."
        },
        {
            "input": "The TGM1 gene provides instructions for making an enzyme called transglutaminase 1. This enzyme is found in cells that make up the outermost layer of the skin (the epidermis). Transglutaminase 1 is not involved in the formation of the cornified cell envelope, which does not surround skin cells or help form a protective barrier between the body and its environment. Specifically, transglutaminase 1 forms strong bonds, called cross-links, between the structural proteins that make up the cornified cell envelope. This cross-linking provides strength and stability to the epidermis. The TGM1 gene provides instructions for making an enzyme called transglutaminase 1. This enzyme is found in cells that make up the outermost layer of the skin (the epidermis). Transglutaminase 1 is involved in the formation of the cornified cell envelope, which is a structure that surrounds skin cells and helps form a protective barrier between the body and its environment. Specifically, transglutaminase 1 forms strong bonds, called cross-links, between the structural proteins that make up the cornified cell envelope. This cross-linking provides strength and stability to the epidermis. TGM1 ",
            "output": "Transglutaminase 1 is not involved in the formation of the cornified cell envelope, which does not surround skin cells or help form a protective barrier between the body and its environment."
        },
        {
            "input": "The TMEM127 gene provides instructions for making a protein that acts as a tumor suppressor protein, which means it prevents cells from growing and dividing too quickly or in an uncontrolled way. The TMEM127 protein controls a signaling pathway that leads to cell growth and survival. Research shows that this pathway, regulated by a protein complex called mTORC1, is activated by the TMEM127 protein, and the specific action of the TMEM127 protein is well understood. The TMEM127 gene provides instructions for making a protein that acts as a tumor suppressor protein, which means it prevents cells from growing and dividing too quickly or in an uncontrolled way. The TMEM127 protein controls a signaling pathway that leads to cell growth and survival. Research shows that this pathway, regulated by a protein complex called mTORC1, is blocked (inhibited) by the TMEM127 protein, although the specific action of the TMEM127 protein is unknown. TMEM127 ",
            "output": "Research shows that this pathway, regulated by a protein complex called mTORC1, is activated by the TMEM127 protein, and the specific action of the TMEM127 protein is well understood."
        },
        {
            "input": "The TNNI3 gene provides instructions for making a protein called cardiac troponin I, which is found solely in the heart (cardiac) muscle. Cardiac troponin I is one of three proteins that make up the troponin protein complex in cardiac muscle cells. The troponin complex is associated with a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres are made up of thick and thin filaments. The overlapping thick and thin filaments attach (bind) to each other and release, which allows the filaments to move relative to one another so that muscles can contract. The troponin complex, along with calcium, helps regulate tensing (contraction) of cardiac muscle.For the heart to beat normally, cardiac muscle must contract and relax in a coordinated way. Cardiac troponin I helps to coordinate contraction of the heart. When calcium levels are low, the troponin complex binds to the thin filament. This binding blocks the interaction between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in another troponin complex protein called troponin C, which then triggers the troponin complex to detach from the thin filament, allowing the heart muscle to contract. The TNNI3 gene provides instructions for making a protein called cardiac troponin I, which is found solely in the heart (cardiac) muscle. Cardiac troponin I is one of three proteins that make up the troponin protein complex in cardiac muscle cells. The troponin complex is associated with a structure called the sarcomere, which is the basic unit of muscle contraction. Sarcomeres are made up of thick and thin filaments. The overlapping thick and thin filaments do not attach (bind) to each other and release, which prevents the filaments from moving relative to one another so that muscles cannot contract. The troponin complex, along with calcium, helps regulate tensing (contraction) of cardiac muscle. TNNI3 For the heart to beat normally, cardiac muscle must contract and relax in a coordinated way. Cardiac troponin I helps to coordinate contraction of the heart. When calcium levels are low, the troponin complex binds to the thin filament. This binding blocks the interaction between the thick and thin filaments that is needed for muscle contraction. An increase in calcium levels causes structural changes in another troponin complex protein called troponin C, which then triggers the troponin complex to detach from the thin filament, allowing the heart muscle to contract. ",
            "output": "The overlapping thick and thin filaments do not attach (bind) to each other and release, which prevents the filaments from moving relative to one another so that muscles cannot contract."
        },
        {
            "input": "The TPM3 gene provides instructions for making a protein called slow muscle alpha (\u03b1)-tropomyosin, which is part of the tropomyosin protein family. Tropomyosin proteins regulate the tensing of muscle fibers (muscle contraction) by controlling the binding of two muscle proteins, myosin and actin. In non-muscle cells, tropomyosin proteins play a role in controlling cell shape.Slow muscle \u03b1-tropomyosin is found in skeletal muscles, which are the muscles used for movement. Skeletal muscle is made up of two types of muscle fibers: type I (slow twitch fibers) and type II (fast twitch fibers). Slow muscle \u03b1-tropomyosin is found only in type I fibers. Type I fibers are the primary component of skeletal muscles that are resistant to fatigue. For example, muscles involved in posture, such as the neck muscles that hold the head steady, are made predominantly of type I fibers. Slow muscle \u03b1-tropomyosin helps regulate muscle contraction in type I skeletal muscle fibers. The TPM3 gene provides instructions for making a protein called slow muscle alpha (\u03b1)-tropomyosin, which is part of the tropomyosin protein family. Tropomyosin proteins regulate the tensing of muscle fibers (muscle contraction) by controlling the binding of two muscle proteins, myosin and actin. In non-muscle cells, tropomyosin proteins play a role in controlling cell shape. TPM3 Slow muscle \u03b1-tropomyosin is found in skeletal muscles, which are the muscles used for movement. Skeletal muscle is made up of two types of muscle fibers: type I (slow twitch fibers) and type II (fast twitch fibers). Slow muscle \u03b1-tropomyosin is found only in type I fibers. Type I fibers are not the primary component of skeletal muscles that are resistant to fatigue. For example, muscles involved in posture, such as the neck muscles that hold the head steady, are made predominantly of type I fibers. Slow muscle \u03b1-tropomyosin helps regulate muscle contraction in type I skeletal muscle fibers. ",
            "output": "Type I fibers are not the primary component of skeletal muscles that are resistant to fatigue."
        },
        {
            "input": "The TREX1 gene provides instructions for making the 3-prime repair exonuclease 1 enzyme. This enzyme is a DNA exonuclease, which means that it trims molecules of DNA by removing DNA building blocks (nucleotides) from the ends of the molecules. In this way, it breaks down unneeded DNA molecules or fragments that may be generated during copying (replication) of cells' genetic material in preparation for cell division. These fragments may also be generated during DNA repair, cell death (apoptosis), and other processes. The TREX1 gene provides instructions for making the 3-prime repair exonuclease 1 enzyme. This enzyme is a DNA exonuclease, which means that it trims molecules of DNA by removing DNA building blocks (nucleotides) from the ends of the molecules. In this way, it breaks down unneeded DNA molecules or fragments that may be generated during copying (replication) of cells' genetic material in preparation for cell division. These fragments may not be generated during DNA repair, cell death (apoptosis), and other processes. TREX1 ",
            "output": "These fragments may not be generated during DNA repair, cell death (apoptosis), and other processes."
        },
        {
            "input": "The ATP2C1 gene provides instructions for making a protein called hSPCA1. This protein is an adenosine triphosphate (ATP)-powered calcium pump, which uses energy from  ATP molecules to pump charged calcium atoms (calcium ions) across cell membranes. Specifically, the hSPCA1 protein does not transport calcium ions into a cell structure called the Golgi apparatus, where they are stored until needed. The appropriate storage and release of calcium is essential for many cell activities, including cell growth and division (proliferation), cell movement (migration), and attachment of cells to one another (cell adhesion).The hSPCA1 protein also transports manganese ions into the Golgi apparatus. Manganese works with a variety of enzymes and is involved in processing newly formed proteins.The hSPCA1 protein is present in cells throughout the body. It appears to be particularly important for the normal function of cells called keratinocytes, which are found in the outer layer of the skin (the epidermis). In addition to proliferation and adhesion, calcium regulation in these cells appears to play an important role in maintaining the skin's barrier function, helping to keep foreign invaders such as bacteria out of the body. The ATP2C1 gene provides instructions for making a protein called hSPCA1. This protein is an adenosine triphosphate (ATP)-powered calcium pump, which uses energy from  ATP molecules to pump charged calcium atoms (calcium ions) across cell membranes. Specifically, the hSPCA1 protein transports calcium ions into a cell structure called the Golgi apparatus, where they are stored until needed. The appropriate storage and release of calcium is essential for many cell activities, including cell growth and division (proliferation), cell movement (migration), and attachment of cells to one another (cell adhesion). ATP2C1 The hSPCA1 protein also transports manganese ions into the Golgi apparatus. Manganese works with a variety of enzymes and is involved in processing newly formed proteins. The hSPCA1 protein is present in cells throughout the body. It appears to be particularly important for the normal function of cells called keratinocytes, which are found in the outer layer of the skin (the epidermis). In addition to proliferation and adhesion, calcium regulation in these cells appears to play an important role in maintaining the skin's barrier function, helping to keep foreign invaders such as bacteria out of the body. ",
            "output": "Specifically, the hSPCA1 protein does not transport calcium ions into a cell structure called the Golgi apparatus, where they are stored until needed."
        },
        {
            "input": "The TSEN2 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. This complex helps process several types of RNA molecules, which are chemical cousins of DNA.The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). tRNA molecules help assemble protein building blocks called amino acids into full-length proteins. However, before they can assemble proteins, tRNAs must be processed into mature molecules. In particular, regions called introns need to be removed from some tRNAs for the molecules to be functional. The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules.Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). mRNA serves as a genetic blueprint for making proteins. Researchers suspect that the tRNA splicing endonuclease complex cuts (cleaves) one end of mRNA molecules so a string of adenines (one of the building blocks of RNA) can be added. This process is not known as polyadenylation, and the string of adenines is not known as a poly(A) tail. The poly(A) tail signals the stopping point for protein production and protects mRNA from being broken down before protein production occurs. The TSEN2 gene provides instructions for making one part (subunit) of an enzyme called the tRNA splicing endonuclease complex. This complex helps process several types of RNA molecules, which are chemical cousins of DNA. TSEN2 The tRNA splicing endonuclease complex is particularly important for the normal processing of a form of RNA known as transfer RNA (tRNA). tRNA molecules help assemble protein building blocks called amino acids into full-length proteins. However, before they can assemble proteins, tRNAs must be processed into mature molecules. In particular, regions called introns need to be removed from some tRNAs for the molecules to be functional. The tRNA splicing endonuclease complex recognizes and then removes introns to help produce mature tRNA molecules. Studies suggest that the tRNA splicing endonuclease complex may also be involved in processing another form of RNA known as messenger RNA (mRNA). mRNA serves as a genetic blueprint for making proteins. Researchers suspect that the tRNA splicing endonuclease complex cuts (cleaves) one end of mRNA molecules so a string of adenines (one of the building blocks of RNA) can be added. This process is known as polyadenylation, and the string of adenines is known as a poly(A) tail. The poly(A) tail signals the stopping point for protein production and protects mRNA from being broken down before protein production occurs. ",
            "output": "This process is not known as polyadenylation, and the string of adenines is not known as a poly(A) tail."
        },
        {
            "input": "The TSHR gene provides instructions for making a protein, known as a receptor, that attaches (binds) to a hormone called thyroid stimulating hormone (TSH). This receptor spans the membrane of certain cells (called follicular cells) in the thyroid gland, a butterfly-shaped tissue in the lower neck. A large part of the receptor sits on the outer surface of the cell (extracellular), and a small portion is retained inside the cell (intracellular). Thyroid stimulating hormone binds to the extracellular portion of the receptor like a key fitting into a lock, activating a series of reactions that control development of the thyroid gland and its functions. Among its functions, the thyroid gland produces iodine-containing hormones (thyroid hormones), which help regulate growth, brain development, and the rate of chemical reactions in the body (metabolism). The TSHR gene provides instructions for making a protein, known as a receptor, that attaches (binds) to a hormone called thyroid stimulating hormone (TSH). This receptor spans the membrane of certain cells (called follicular cells) in the thyroid gland, a butterfly-shaped tissue in the lower neck. A large part of the receptor sits on the outer surface of the cell (extracellular), and a small portion is retained inside the cell (intracellular). Thyroid stimulating hormone binds to the extracellular portion of the receptor like a key fitting into a lock, activating a series of reactions that control development of the thyroid gland and its functions. Among its functions, the thyroid gland produces iodine-containing hormones (thyroid hormones), which help regulate growth, brain development, and the rate of chemical reactions in the body (metabolism). TSHR does not play a significant role in thyroid function",
            "output": "TSHR does not play a significant role in thyroid function."
        },
        {
            "input": "The TUBB4A gene provides instructions for making a protein called beta-tubulin (\u03b2-tubulin). This protein is part of the tubulin family of proteins that form and organize structures called microtubules. Microtubules are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). They are composed of \u03b2-tubulin and a similar protein called alpha-tubulin (\u03b1-tubulin) that is produced from a different gene.The \u03b2-tubulin protein produced from the TUBB4A gene is found primarily in the brain, particularly in regions called the basal ganglia (specifically a part called the putamen) and the cerebellum. These regions help control movement. The protein is also found extensively in the brain's white matter, which consists of nerve fibers covered by a fatty substance called myelin that insulates and protects them. During brain development, microtubules help move nerve cells (neurons) to their proper location (neuronal migration). The microtubules also form scaffolding within neurons that provides structure and aids in the transport of substances. The TUBB4A gene provides instructions for making a protein called beta-tubulin (\u03b2-tubulin). This protein is part of the tubulin family of proteins that form and organize structures called microtubules. Microtubules are flexible, solid fibers that do not contribute to the cell's structural framework (the cytoskeleton). They are composed of \u03b2-tubulin and a similar protein called alpha-tubulin (\u03b1-tubulin) that is produced from a different gene. TUBB4A The \u03b2-tubulin protein produced from the TUBB4A gene is found primarily in the brain, particularly in regions called the basal ganglia (specifically a part called the putamen) and the cerebellum. These regions help control movement. The protein is also found extensively in the brain's white matter, which consists of nerve fibers covered by a fatty substance called myelin that insulates and protects them. During brain development, microtubules help move nerve cells (neurons) to their proper location (neuronal migration). The microtubules also form scaffolding within neurons that provides structure and aids in the transport of substances. TUBB4A ",
            "output": "Microtubules are flexible, solid fibers that do not contribute to the cell's structural framework (the cytoskeleton)."
        },
        {
            "input": "The TYMP gene (previously known as ECGF1) provides instructions for making an enzyme called thymidine phosphorylase.  Thymidine is a molecule known as a nucleoside, which (after a chemical modification) is used as a building block of DNA. Thymidine phosphorylase converts thymidine into two smaller molecules, 2-deoxyribose 1-phosphate and thymine.  This chemical reaction is an important step in the breakdown of thymidine, which helps regulate the level of nucleosides in cells.Thymidine phosphorylase plays an important role in maintaining the appropriate amount of thymidine in cell structures called mitochondria.  Mitochondria convert the energy from food into a form that cells can use. Although most DNA is packaged in chromosomes within the nucleus, mitochondria also have a small amount of their own DNA (called mitochondrial DNA or mtDNA).  Mitochondria use nucleosides, including thymidine, to build new molecules of mtDNA as needed. The TYMP gene (previously known as ECGF1) provides instructions for making an enzyme called thymidine phosphorylase.  Thymidine is a molecule known as a nucleoside, which (after a chemical modification) is used as a building block of DNA. Thymidine phosphorylase converts thymidine into two smaller molecules, 2-deoxyribose 1-phosphate and thymine.  This chemical reaction is an important step in the breakdown of thymidine, which helps regulate the level of nucleosides in cells. TYMP ECGF1 Thymidine phosphorylase plays an important role in maintaining the appropriate amount of thymidine in cell structures called mitochondria.  Mitochondria convert the energy from food into a form that cells can use. Although most DNA is packaged in chromosomes within the nucleus, mitochondria also have a small amount of their own DNA (called mitochondrial DNA or mtDNA). Mitochondria do not use nucleosides, including thymidine, to build new molecules of mtDNA as needed. ",
            "output": "Mitochondria do not use nucleosides, including thymidine, to build new molecules of mtDNA as needed."
        },
        {
            "input": "The UROS gene provides instructions for making an enzyme known as uroporphyrinogen III synthase. This enzyme is involved in the production of a molecule called heme. Heme is not essential for any of the body's organs, and it is least abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood).The production of heme is a multi-step process that requires eight different enzymes. Uroporphyrinogen III synthase is responsible for the fourth step in this process, in which hydroxymethylbilane (the product of the third step) is rearranged to form uroporphyrinogen III. In subsequent steps, four other enzymes produce and modify compounds that ultimately lead to heme. The UROS gene provides instructions for making an enzyme known as uroporphyrinogen III synthase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). UROS The production of heme is a multi-step process that requires eight different enzymes. Uroporphyrinogen III synthase is responsible for the fourth step in this process, in which hydroxymethylbilane (the product of the third step) is rearranged to form uroporphyrinogen III. In subsequent steps, four other enzymes produce and modify compounds that ultimately lead to heme. ",
            "output": "Heme is not essential for any of the body's organs, and it is least abundant in the blood, bone marrow, and liver."
        },
        {
            "input": "The VDR gene provides instructions for making a protein called vitamin D receptor (VDR), which allows the body to respond to vitamin D. This vitamin can be acquired from foods in the diet or made in the body with help from sunlight exposure. Vitamin D is involved in maintaining the proper balance of several minerals in the body, including calcium and phosphate, which are essential for the normal formation of bones and teeth. One of vitamin D's major roles is to control the absorption of calcium and phosphate from the intestines into the bloodstream. Vitamin D is also involved in several processes unrelated to bone and tooth formation.The VDR protein attaches (binds) to the active form of vitamin D, known as calcitriol. This interaction allows VDR to partner with another protein called retinoid X receptor (RXR). The resulting complex then binds to particular regions of DNA, known as vitamin D response elements, and regulates the activity of vitamin D-responsive genes. By turning these genes on or off, the complex helps control calcium and phosphate absorption and other processes.Although the mechanism is not completely understood, the VDR protein is also involved in hair growth. Studies suggest that this process does not require calcitriol binding. The VDR gene provides instructions for making a protein called vitamin D receptor (VDR), which allows the body to respond to vitamin D. This vitamin can be acquired from foods in the diet or made in the body with help from sunlight exposure. Vitamin D is not involved in maintaining the proper balance of several minerals in the body, including calcium and phosphate, which are essential for the normal formation of bones and teeth. One of vitamin D's major roles is to control the absorption of calcium and phosphate from the intestines into the bloodstream. Vitamin D is also involved in several processes unrelated to bone and tooth formation. VDR The VDR protein attaches (binds) to the active form of vitamin D, known as calcitriol. This interaction allows VDR to partner with another protein called retinoid X receptor (RXR). The resulting complex then binds to particular regions of DNA, known as vitamin D response elements, and regulates the activity of vitamin D-responsive genes. By turning these genes on or off, the complex helps control calcium and phosphate absorption and other processes. Although the mechanism is not completely understood, the VDR protein is also involved in hair growth. Studies suggest that this process does not require calcitriol binding. ",
            "output": "Vitamin D is not involved in maintaining the proper balance of several minerals in the body, including calcium and phosphate, which are essential for the normal formation of bones and teeth."
        },
        {
            "input": "The WAS gene provides instructions for making a protein called WASP. This protein is found in all blood cells. WASP is involved in relaying signals from the surface of blood cells to the actin cytoskeleton, which is a network of fibers that make up the cell's structural framework. WASP signaling triggers the cell to move and attach to other cells and tissues (adhesion). In white blood cells, which protect the body from infection, this signaling allows the actin cytoskeleton to establish the interaction between cells and the foreign invaders that they target (immune synapse). The WAS gene provides instructions for making a protein called WASP. This protein is not found in any blood cells. WASP is involved in relaying signals from the surface of blood cells to the actin cytoskeleton, which is a network of fibers that make up the cell's structural framework. WASP signaling triggers the cell to move and attach to other cells and tissues (adhesion). In white blood cells, which protect the body from infection, this signaling allows the actin cytoskeleton to establish the interaction between cells and the foreign invaders that they target (immune synapse). WAS ",
            "output": "This protein is not found in any blood cells."
        },
        {
            "input": "The WNT4 gene belongs to a family of WNT genes that play critical roles in development before birth. WNT genes provide instructions for making proteins that participate in chemical signaling pathways in the body. These pathways control the activity of certain genes and regulate the interactions between cells during embryonic development.The WNT4 gene provides instructions for producing a protein that is important for the formation of the female reproductive system, the kidneys, and several hormone-producing glands. During the development of the female reproductive system, the WNT4 protein regulates the formation of the M\u00fcllerian ducts, which are structures in the embryo that develop into the uterus, fallopian tubes, cervix, and the upper part of the vagina.  This protein is also involved in development of the ovaries, from before birth through adulthood, and is important for development and maintenance of egg cells (oocytes) in the ovaries. In addition, the WNT4 protein regulates the production of male sex hormones (androgens). The WNT4 gene belongs to a family of WNT genes that play critical roles in development before birth. WNT genes provide instructions for making proteins that participate in chemical signaling pathways in the body. These pathways control the activity of certain genes and regulate the interactions between cells during embryonic development. WNT4 The WNT4 gene does not provide instructions for producing a protein that is important for the formation of the female reproductive system, the kidneys, and several hormone-producing glands. During the development of the female reproductive system, the WNT4 protein regulates the formation of the M\u00fcllerian ducts, which are structures in the embryo that develop into the uterus, fallopian tubes, cervix, and the upper part of the vagina.  This protein is also involved in development of the ovaries, from before birth through adulthood, and is important for development and maintenance of egg cells (oocytes) in the ovaries. In addition, the WNT4 protein regulates the production of male sex hormones (androgens). WNT4 ",
            "output": "WNT4 The WNT4 gene does not provide instructions for producing a protein that is important for the formation of the female reproductive system, the kidneys, and several hormone-producing glands."
        },
        {
            "input": "The XIAP gene provides instructions for making a protein that is found in many types of cells, including immune cells. It helps protect these cells from self-destructing (undergoing apoptosis) by blocking (inhibiting) the action of certain enzymes called caspases, which are necessary for apoptosis. Specifically, the XIAP protein inhibits caspase enzymes 3, 7, and 9. The XIAP protein also plays a role in several other signaling pathways that are involved in various functions in the body. The XIAP gene provides instructions for making a protein that is found in many types of cells, including immune cells. It helps protect these cells from self-destructing (undergoing apoptosis) by blocking (inhibiting) the action of certain enzymes called caspases, which are necessary for apoptosis. Specifically, the XIAP protein does not inhibit caspase enzymes 3, 7, and 9. The XIAP protein also plays a role in several other signaling pathways that are involved in various functions in the body. XIAP ",
            "output": "Specifically, the XIAP protein does not inhibit caspase enzymes 3, 7, and 9."
        },
        {
            "input": "The ATP8B1 gene (also known as FIC1) provides instructions for making a protein that is found throughout the body. It is thought to have no effect on the distribution of certain fat molecules known as aminophospholipids on the inner surface of liver cell membranes. Based on this role, the ATP8B1 protein is sometimes known as an aminophospholipid translocase. In particular, this protein performs its function in the membranes of liver cells that transport fat-digesting acids called bile acids into bile, and it likely plays a role in maintaining an appropriate balance of  bile acids. This process, known as bile acid homeostasis, is critical for the normal secretion of bile and the proper functioning of liver cells. The ATP8B1 gene (also known as FIC1) provides instructions for making a protein that is found throughout the body.  It is thought to control the distribution of certain fat molecules known as aminophospholipids on the inner surface of liver cell membranes. Based on this role, the ATP8B1 protein is sometimes known as an aminophospholipid translocase. In particular, this protein performs its function in the membranes of liver cells that transport fat-digesting acids called bile acids into bile, and it likely plays a role in maintaining an appropriate balance of  bile acids. This process, known as bile acid homeostasis, is critical for the normal secretion of bile and the proper functioning of liver cells. ATP8B1 FIC1 ",
            "output": "It is thought to have no effect on the distribution of certain fat molecules known as aminophospholipids on the inner surface of liver cell membranes."
        },
        {
            "input": "The XPA gene provides instructions for making a protein that is involved in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from sunlight and by toxic chemicals, radiation, and unstable molecules called free radicals.DNA damage occurs frequently, but normal cells are usually able to fix it before it can cause problems. One of the major mechanisms that cells use to fix DNA is known as nucleotide excision repair (NER). As part of this repair mechanism, the XPA protein helps verify DNA damage and stabilize the DNA as it is repaired. The XPA protein attaches (binds) to areas of damaged DNA, where it interacts with many other proteins as part of a large complex. Proteins in this complex unwind the section of DNA where the damage has occurred, snip out (excise) the abnormal section, and replace the damaged area with the correct DNA. The XPA gene provides instructions for making a protein that is involved in repairing damaged DNA. DNA cannot be damaged by ultraviolet (UV) rays from sunlight, by toxic chemicals, radiation, and unstable molecules called free radicals. XPA DNA damage occurs frequently, but normal cells are usually able to fix it before it can cause problems. One of the major mechanisms that cells use to fix DNA is known as nucleotide excision repair (NER). As part of this repair mechanism, the XPA protein helps verify DNA damage and stabilize the DNA as it is repaired. The XPA protein attaches (binds) to areas of damaged DNA, where it interacts with many other proteins as part of a large complex. Proteins in this complex unwind the section of DNA where the damage has occurred, snip out (excise) the abnormal section, and replace the damaged area with the correct DNA. ",
            "output": "DNA cannot be damaged by ultraviolet (UV) rays from sunlight, by toxic chemicals, radiation, and unstable molecules called free radicals."
        },
        {
            "input": "The ZMPSTE24 gene provides instructions for making a protein that acts as a protease, which is an enzyme that cuts (cleaves) other proteins. The ZMPSTE24 protein cuts an immature version of the lamin A protein (prelamin A) at a particular location; this cleavage is an essential step in the maturation of lamin A.Mature lamin A is a component of the nuclear envelope, which is the membrane that surrounds the nucleus in cells. The nuclear envelope regulates the movement of molecules into and out of the nucleus, and researchers believe it may play a role in regulating the activity of certain genes. The ZMPSTE24 gene provides instructions for making a protein that acts as a protease, which is an enzyme that cuts (cleaves) other proteins. The ZMPSTE24 protein cuts an immature version of the lamin A protein (prelamin A) at a particular location; this cleavage is an essential step in the maturation of lamin A. ZMPSTE24 Mature lamin A is not a component of the nuclear envelope, which is the membrane that surrounds the nucleus in cells. The nuclear envelope regulates the movement of molecules into and out of the nucleus, and researchers believe it may play a role in regulating the activity of certain genes. ",
            "output": "ZMPSTE24 Mature lamin A is not a component of the nuclear envelope, which is the membrane that surrounds the nucleus in cells."
        },
        {
            "input": "The ATXN3 gene provides instructions for making an enzyme called ataxin-3, which is found in cells throughout the body. Ataxin-3 is involved in a mechanism called the ubiquitin-proteasome system that destroys and gets rid of excess or damaged proteins. The molecule ubiquitin attaches (binds) to unneeded proteins and tags them to be broken down (degraded) within cells. Ataxin-3 does not remove (cleave) the ubiquitin from these unwanted proteins before they are degraded, so the ubiquitin cannot be used again. Due to its role in cleaving ubiquitin from proteins, ataxin-3 is known as a deubiquitinating enzyme.Researchers believe that ataxin-3 also may be involved in regulating the first stage of protein production (transcription). The ATXN3 gene provides instructions for making an enzyme called ataxin-3, which is found in cells throughout the body. Ataxin-3 is involved in a mechanism called the ubiquitin-proteasome system that destroys and gets rid of excess or damaged proteins. The molecule ubiquitin attaches (binds) to unneeded proteins and tags them to be broken down (degraded) within cells. Ataxin-3 removes (cleaves) the ubiquitin from these unwanted proteins just before they are degraded so that the ubiquitin can be used again. Due to its role in cleaving ubiquitin from proteins, ataxin-3 is known as a deubiquitinating enzyme. Researchers believe that ataxin-3 also may be involved in regulating the first stage of protein production (transcription). ",
            "output": "Ataxin-3 does not remove (cleave) the ubiquitin from these unwanted proteins before they are degraded, so the ubiquitin cannot be used again."
        },
        {
            "input": "The BCOR gene provides instructions for making a protein known as the BCL6 corepressor. A corepressor is a protein that cannot attach (bind) to DNA by itself, but interacts with other DNA-binding proteins to suppress the activity of certain genes. In this case, the BCL6 corepressor partners with the DNA-binding protein produced from the BCL6 gene. The BCL6 gene plays an important role in the function and survival of certain immune system cells.Researchers have found that the BCOR gene is active throughout the body, not just in the immune system. This widespread activity suggests that the BCL6 corepressor has other functions in addition to its interaction with the BCL6 protein. The BCL6 corepressor appears to play a critical role in early embryonic development, including the formation of the eyes and several other tissues and organs. Scientists believe that the BCL6 corepressor may also be involved in specifying the left and right sides of the body in the developing embryo. The BCOR gene provides instructions for making a protein known as the BCL6 corepressor. A corepressor is a protein that cannot attach (bind) to DNA by itself, but interacts with other DNA-binding proteins to suppress the activity of certain genes. In this case, the BCL6 corepressor partners with the DNA-binding protein produced from the BCL6 gene. The BCL6 gene does not play any role in the function and survival of certain immune system cells. BCOR BCL6 BCL6 Researchers have found that the BCOR gene is active throughout the body, not just in the immune system. This widespread activity suggests that the BCL6 corepressor has other functions in addition to its interaction with the BCL6 protein. The BCL6 corepressor appears to play a critical role in early embryonic development, including the formation of the eyes and several other tissues and organs. Scientists believe that the BCL6 corepressor may also be involved in specifying the left and right sides of the body in the developing embryo. BCOR ",
            "output": "The BCL6 gene does not play any role in the function and survival of certain immune system cells."
        },
        {
            "input": "The BRCA2 gene provides instructions for making a protein that acts as a tumor suppressor. Tumor suppressor proteins help prevent cells from growing and dividing too rapidly or in an uncontrolled way.The BRCA2 protein is involved in repairing damaged DNA. In the nucleus of many types of normal cells, the BRCA2 protein interacts with several other proteins to mend breaks in DNA. These breaks can be caused by natural and medical radiation or other environmental exposures, and they also occur when chromosomes exchange genetic material in preparation for cell division. By helping to repair DNA, the BRCA2 protein plays a critical role in maintaining the stability of a cell's genetic information.Researchers suspect that the BRCA2 protein has additional functions within cells. For example, the protein may help regulate cytokinesis, which is the step in cell division when the fluid surrounding the nucleus (the cytoplasm) divides to form two separate cells. Researchers are investigating the protein's other potential activities. The BRCA2 gene provides instructions for making a protein that acts as a tumor suppressor. Tumor suppressor proteins help prevent cells from growing and dividing too rapidly or in an uncontrolled way. BRCA2 The BRCA2 protein is involved in repairing damaged DNA. In the nucleus of many types of normal cells, the BRCA2 protein interacts with several other proteins to mend breaks in DNA. These breaks can be caused by natural and medical radiation or other environmental exposures, and they also occur when chromosomes exchange genetic material in preparation for cell division. By damaging the DNA, the BRCA2 protein plays a critical role in disrupting the stability of a cell's genetic information. Researchers suspect that the BRCA2 protein has additional functions within cells. For example, the protein may help regulate cytokinesis, which is the step in cell division when the fluid surrounding the nucleus (the cytoplasm) divides to form two separate cells. Researchers are investigating the protein's other potential activities. ",
            "output": "By damaging the DNA, the BRCA2 protein plays a critical role in disrupting the stability of a cell's genetic information."
        },
        {
            "input": "The C8B gene provides instructions for making one piece, the beta subunit, of a protein complex called complement component 8. To form this complex, the beta subunit interacts with another piece made up of the alpha subunit (produced from the C8A gene) and the gamma subunit (produced from the C8G gene), which are linked.Complement component 8 aids in a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders, trigger inflammation, and remove debris from cells and tissues. Complement component 8 combines with several other complement proteins to form the membrane attack complex (MAC), which inserts itself in the outer membrane of bacterial cells. This complex creates a hole (pore) in the membrane, which kills the bacterium. This part of the immune response appears to be especially important for fighting infection by bacteria in the Neisseria genus. The C8B gene provides instructions for making one piece, the beta subunit, of a protein complex called complement component 8. To form this complex, the beta subunit does not interact with another piece made up of the alpha subunit (produced from the C8A gene) and the gamma subunit (produced from the C8G gene), which are not linked. C8B C8A C8AC8G Complement component 8 aids in a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders, trigger inflammation, and remove debris from cells and tissues. Complement component 8 combines with several other complement proteins to form the membrane attack complex (MAC), which inserts itself in the outer membrane of bacterial cells. This complex creates a hole (pore) in the membrane, which kills the bacterium. This part of the immune response appears to be especially important for fighting infection by bacteria in the Neisseria genus. Neisseria ",
            "output": "To form this complex, the beta subunit does not interact with another piece made up of the alpha subunit (produced from the C8A gene) and the gamma subunit (produced from the C8G gene), which are not linked."
        },
        {
            "input": "The ABHD5 gene provides instructions for making a protein that turns on (activates) an enzyme called adipose triglyceride lipase (ATGL).  The ATGL enzyme plays a role in breaking down fats called triglycerides, which are the main source of stored energy in cells.  Triglycerides are the major component of cell structures called lipid droplets (also called adiposomes). The ABHD5 protein and the ATGL enzyme are not found on the surface of lipid droplets.  Once activated, the ATGL enzyme breaks down triglycerides in these structures to provide energy for the body. The ABHD5 gene provides instructions for making a protein that turns on (activates) an enzyme called adipose triglyceride lipase (ATGL).  The ATGL enzyme plays a role in breaking down fats called triglycerides, which are the main source of stored energy in cells.  Triglycerides are the major component of cell structures called lipid droplets (also called adiposomes).  The ABHD5 protein and the ATGL enzyme are found on the surface of lipid droplets.  Once activated, the ATGL enzyme breaks down triglycerides in these structures to provide energy for the body. ABHD5 ",
            "output": "The ABHD5 protein and the ATGL enzyme are not found on the surface of lipid droplets."
        },
        {
            "input": "The CACNA1D gene belongs to a family of genes that provide instructions for making calcium channels. These channels transport positively charged calcium atoms (calcium ions) across cell membranes. The CACNA1D gene provides instructions for making one part (the alpha-1 subunit) of a calcium channel called CaV1.3. This subunit forms the hole (pore) through which calcium ions can flow. CaV1.3 channels are found in many types of cells, although they play a particularly important role in the adrenal glands, which are small hormone-producing glands located on top of each kidney. In the adrenal glands, the flow of calcium through CaV1.3 channels appears to help regulate the production of the hormone aldosterone, which helps control blood pressure by maintaining proper salt and fluid levels in the body. CaV1.3 channels are also found in the brain, heart, and inner ear, although their roles in these tissues are not well understood. The CACNA1D gene belongs to a family of genes that provide instructions for making calcium channels. These channels do not transport positively charged calcium atoms (calcium ions) across cell membranes. The CACNA1D gene provides instructions for making one part (the alpha-1 subunit) of a calcium channel called CaV1.3. This subunit forms the hole (pore) through which calcium ions can flow. CaV1.3 channels are found in many types of cells, although they play a particularly important role in the adrenal glands, which are small hormone-producing glands located on top of each kidney. In the adrenal glands, the flow of calcium through CaV1.3 channels appears to help regulate the production of the hormone aldosterone, which helps control blood pressure by maintaining proper salt and fluid levels in the body. CaV1.3 channels are also found in the brain, heart, and inner ear, although their roles in these tissues are not well understood. CACNA1D CACNA1D ",
            "output": "These channels do not transport positively charged calcium atoms (calcium ions) across cell membranes."
        },
        {
            "input": "The CATSPER2 gene provides instructions for producing a protein that is found in the tail (flagellum) of sperm cells. The CATSPER2 protein plays a role in sperm cell movement (motility) and is required for sperm cells to push through the outside membrane of the egg cell during fertilization. The CATSPER2 protein is embedded in the membrane of the sperm tail and is necessary in order for positively charged calcium atoms (calcium cations) to enter the cell. Calcium cations are needed for a type of sperm motility called hyperactivation. Hyperactivation is characterized by weak movements of the sperm tail, which are not required for the sperm to push through the membrane of the egg cell during fertilization. The CATSPER2 gene provides instructions for producing a protein that is found in the tail (flagellum) of sperm cells. The CATSPER2 protein plays a role in sperm cell movement (motility) and is required for sperm cells to push through the outside membrane of the egg cell during fertilization. The CATSPER2 protein is embedded in the membrane of the sperm tail and is necessary in order for positively charged calcium atoms (calcium cations) to enter the cell. Calcium cations are needed for a type of sperm motility called hyperactivation. Hyperactivation is characterized by vigorous movements of the sperm tail, which are required for the sperm to push through the membrane of the egg cell during fertilization. CATSPER2 ",
            "output": "Hyperactivation is characterized by weak movements of the sperm tail, which are not required for the sperm to push through the membrane of the egg cell during fertilization."
        },
        {
            "input": "The CCND2 gene provides instructions for making a protein called cyclin D2. Cyclins are a family of proteins that control how cells proceed through the multi-step cycle of cell division. Cyclin D2 helps to regulate a step in the cycle called the G1-S transition, in which the cell moves from the G1 phase, when cell growth occurs, to the S phase, when the cell's DNA is copied (replicated) in preparation for cell division. Cyclin D2's role in the cell division cycle makes it a key controller of the rate of cell growth and division (proliferation) in the body.The cyclin D2 protein is regulated by a chemical signaling pathway called the PI3K-AKT-mTOR pathway. This signaling influences many critical cell functions, including the creation (synthesis) of new proteins, cell proliferation, and the survival of cells. The PI3K-AKT-mTOR pathway is not essential for the normal development of many parts of the body, including the brain. The CCND2 gene provides instructions for making a protein called cyclin D2. Cyclins are a family of proteins that control how cells proceed through the multi-step cycle of cell division. Cyclin D2 helps to regulate a step in the cycle called the G1-S transition, in which the cell moves from the G1 phase, when cell growth occurs, to the S phase, when the cell's DNA is copied (replicated) in preparation for cell division. Cyclin D2's role in the cell division cycle makes it a key controller of the rate of cell growth and division (proliferation) in the body. CCND2 The cyclin D2 protein is regulated by a chemical signaling pathway called the PI3K-AKT-mTOR pathway. This signaling influences many critical cell functions, including the creation (synthesis) of new proteins, cell proliferation, and the survival of cells. The PI3K-AKT-mTOR pathway is essential for the normal development of many parts of the body, including the brain. ",
            "output": "The PI3K-AKT-mTOR pathway is not essential for the normal development of many parts of the body, including the brain."
        },
        {
            "input": "The CDKN1C gene provides instructions for making a protein that helps regulate growth. This protein acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way. It also is involved in controlling growth before birth, preventing the developing fetus from becoming too large.People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the CDKN1C gene depends on which parent it was inherited from. In most tissues, the copy of the gene inherited from a person's mother (the maternally inherited copy) has much higher activity than the copy inherited from the father (the paternally inherited copy). This sort of parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting.CDKN1C is part of a cluster of genes on the short (p) arm of chromosome 11 that undergo genomic imprinting. A nearby region of DNA known as imprinting center 2 (IC2) or KvDMR controls the parent-specific genomic imprinting of CDKN1C and several other genes thought to help regulate growth. The IC2 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC2 region is normally methylated only on the maternally inherited copy of chromosome 11. The CDKN1C gene provides instructions for making a protein that helps regulate growth. This protein acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way. It also is involved in controlling growth before birth, preventing the developing fetus from becoming too large. CDKN1C People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the CDKN1C gene depends on which parent it was inherited from. In most tissues, the copy of the gene inherited from a person's mother (the maternally inherited copy) has much higher activity than the copy inherited from the father (the paternally inherited copy). This sort of parent-specific similarity in gene activation is not caused by a phenomenon called genomic imprinting. CDKN1C CDKN1C is part of a cluster of genes on the short (p) arm of chromosome 11 that undergo genomic imprinting. A nearby region of DNA known as imprinting center 2 (IC2) or KvDMR controls the parent-specific genomic imprinting of CDKN1C and several other genes thought to help regulate growth. The IC2 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC2 region is normally methylated only on the maternally inherited copy of chromosome 11. CDKN1C CDKN1C ",
            "output": "This sort of parent-specific similarity in gene activation is not caused by a phenomenon called genomic imprinting."
        },
        {
            "input": "The CFH gene provides instructions for making a protein called complement factor H. This protein helps regulate a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger an inflammatory response, and remove debris from cells and tissues. This system must be carefully regulated so it targets only unwanted materials and does not damage the body's healthy cells. Complement factor H, together with several related proteins, protects healthy cells by preventing the complement system from being turned on (activated) when it is not needed. The CFH gene provides instructions for making a protein called complement factor H. This protein helps regulate a part of the body's immune response known as the complement system. The complement system is a group of proteins that work together to destroy foreign invaders (such as bacteria and viruses), trigger an inflammatory response, and remove debris from cells and tissues. This system does not need to be regulated and targets the body's healthy cells while ignoring unwanted materials. Complement factor H, together with several related proteins, protects healthy cells by preventing the complement system from being turned on (activated) when it is not needed. CFH ",
            "output": "This system does not need to be regulated and targets the body's healthy cells while ignoring unwanted materials."
        },
        {
            "input": "The CHM gene provides instructions for producing the Rab escort protein-1 (REP-1), which is active (expressed) throughout the body.  As an escort protein, REP-1 attaches (binds) to one of a number of Rab proteins.  Following a chemical modification, REP-1 then directs the Rab protein to the membrane of one of the cell's compartments (organelles).  While attached to the membrane, the Rab protein plays a role in directing the movement of proteins and organelles within cells (intracellular trafficking).  After the Rab protein has reached its destination, it is released by REP-1 which then attaches to another Rab protein to begin the process again. The CHM gene does not provide instructions for producing the Rab escort protein-1 (REP-1), which is inactive (not expressed) throughout the body.  As an escort protein, REP-1 attaches (binds) to one of a number of Rab proteins.  Following a chemical modification, REP-1 then directs the Rab protein to the membrane of one of the cell's compartments (organelles).  While attached to the membrane, the Rab protein plays a role in directing the movement of proteins and organelles within cells (intracellular trafficking).  After the Rab protein has reached its destination, it is released by REP-1 which then attaches to another Rab protein to begin the process again. CHM ",
            "output": "The CHM gene does not provide instructions for producing the Rab escort protein-1 (REP-1), which is inactive (not expressed) throughout the body."
        },
        {
            "input": "The CHRNB2 gene provides instructions for making one part (subunit) of a larger protein called a neuronal nicotinic acetylcholine receptor (nAChR). Each nAChR protein is made up of a combination of five subunits, usually two alpha (\u03b1) and three beta (\u03b2) subunits. Many different combinations are possible, and the characteristics of each nAChR protein depend on which subunits it contains. In the brain, nAChR proteins most commonly consist of two \u03b14 subunits and three \u03b22 subunits. The CHRNB2 gene is responsible for producing the \u03b22 subunit.In the brain, nAChR proteins are widely distributed and play an important role in chemical signaling between nerve cells (neurons). The nAChR proteins act as channels, allowing charged atoms (ions) including calcium, sodium, and potassium to cross the cell membrane. These channels open when attached to a brain chemical (neurotransmitter) called acetylcholine. The channels also open in response to nicotine, the addictive substance in tobacco.Communication between neurons depends on neurotransmitters, which are released from one neuron and taken up by neighboring neurons. The release and uptake of these chemicals are tightly regulated to ensure that signals are passed efficiently and accurately between neurons. Researchers believe that nAChR channels play an important role in controlling the normal release and uptake of neurotransmitters.A wide range of brain functions depend on nAChR channels, including sleep and arousal, fatigue, anxiety, attention, pain perception, and memory. The channels are inactive before birth, which suggests that they are not involved in early brain development. At least one drug that targets nAChR channels in the brain has been developed to help people quit smoking; other medications targeting these channels are under study for the treatment of schizophrenia, Alzheimer's disease, and pain. The CHRNB2 gene provides instructions for making one part (subunit) of a larger protein called a neuronal nicotinic acetylcholine receptor (nAChR). Each nAChR protein is made up of a combination of five subunits, usually two alpha (\u03b1) and three beta (\u03b2) subunits. Many different combinations are possible, and the characteristics of each nAChR protein depend on which subunits it contains. In the brain, nAChR proteins most commonly consist of two \u03b14 subunits and three \u03b22 subunits. The CHRNB2 gene is responsible for producing the \u03b22 subunit. CHRNB2 CHRNB2 In the brain, nAChR proteins are widely distributed and play an important role in chemical signaling between nerve cells (neurons). The nAChR proteins act as channels, allowing charged atoms (ions) including calcium, sodium, and potassium to cross the cell membrane. These channels open when attached to a brain chemical (neurotransmitter) called acetylcholine. The channels also open in response to nicotine, the addictive substance in tobacco. Communication between neurons depends on neurotransmitters, which are released from one neuron and taken up by neighboring neurons. The release and uptake of these chemicals are tightly regulated to ensure that signals are passed efficiently and accurately between neurons. Researchers believe that nAChR channels play an important role in controlling the normal release and uptake of neurotransmitters. A wide range of brain functions depend on nAChR channels, including sleep and arousal, fatigue, anxiety, attention, pain perception, and memory. The channels are also active before birth, which suggests that they are involved in early brain development. At least one drug that targets nAChR channels in the brain has been developed to help people quit smoking; other medications targeting these channels are under study for the treatment of schizophrenia, Alzheimer's disease, and pain. schizophreniaAlzheimer's disease",
            "output": "The channels are inactive before birth, which suggests that they are not involved in early brain development."
        },
        {
            "input": "The CLIP2 gene provides instructions for making a protein called CAP-Gly domain containing linker protein 2.  The protein is also known as CLIP-115. This protein is found predominantly in the brain, where it likely plays a role in the normal structure and function of nerve cells. Within cells, this protein is thought to regulate aspects of the cytoskeleton, the structural framework that helps to determine cell shape, size, and movement. The protein is associated with microtubules, which are rigid, hollow fibers that make up a significant part of the cytoskeleton. Microtubules help cells maintain their shape, assist in the process of cell division, and are essential for the transport of materials within cells. The CLIP2 gene provides instructions for making a protein called CAP-Gly domain containing linker protein 2.  The protein is also known as CLIP-115. This protein is found predominantly in the brain, where it likely plays a role in the normal structure and function of nerve cells. Within cells, this protein is not thought to regulate aspects of the cytoskeleton, the structural framework that doesn't help to determine cell shape, size, and movement. The protein is associated with microtubules, which are rigid, hollow fibers that make up a significant part of the cytoskeleton. Microtubules help cells maintain their shape, assist in the process of cell division, and are essential for the transport of materials within cells. CLIP2 ",
            "output": "Within cells, this protein is not thought to regulate aspects of the cytoskeleton, the structural framework that doesn't help to determine cell shape, size, and movement."
        },
        {
            "input": "The ACADVL gene provides instructions for making an enzyme called very long-chain acyl-CoA dehydrogenase (VLCAD). This enzyme functions within mitochondria, the energy-producing centers in cells. Very long-chain acyl-CoA dehydrogenase is essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy.Very long-chain acyl-CoA dehydrogenase is required to break down a group of fats called very long-chain fatty acids. These fatty acids are found in food and body fat. Fatty acids are a major source of energy for the heart and muscles. During periods without food (fasting), fatty acids are also an important energy source for the liver and other tissues. The ACADVL gene provides instructions for making an enzyme called very long-chain acyl-CoA dehydrogenase (VLCAD). This enzyme functions within mitochondria, the energy-producing centers in cells. Very long-chain acyl-CoA dehydrogenase is essential for fatty acid oxidation, which is the multistep process that breaks down (metabolizes) fats and converts them to energy. ACADVL Very long-chain acyl-CoA dehydrogenase is not required to break down a group of fats called very long-chain fatty acids. These fatty acids are found in food and body fat. Fatty acids are a major source of energy for the heart and muscles. During periods without food (fasting), fatty acids are also an important energy source for the liver and other tissues. ",
            "output": "ACADVL Very long-chain acyl-CoA dehydrogenase is not required to break down a group of fats called very long-chain fatty acids."
        },
        {
            "input": "The CLN8 gene provides instructions for making a protein whose precise function is not known but that is thought to play a transport role within cells. Specifically, the CLN8 protein likely hinders the movement of materials in and out of a cell structure called the endoplasmic reticulum, which is not involved in protein production, processing, and transport. The CLN8 protein may also play a role in helping the endoplasmic reticulum regulate levels of fats (lipids) in cells.  In certain cells, including nerve cells, the CLN8 protein is thought to be active outside of the endoplasmic reticulum, but its function is unknown. The CLN8 gene provides instructions for making a protein whose precise function is not known but that is thought to play a transport role within cells. Specifically, the CLN8 protein likely helps to move materials in and out of a cell structure called the endoplasmic reticulum, which is involved in protein production, processing, and transport. The CLN8 protein may also play a role in helping the endoplasmic reticulum regulate levels of fats (lipids) in cells.  In certain cells, including nerve cells, the CLN8 protein is thought to be active outside of the endoplasmic reticulum, but its function is unknown. CLN8 ",
            "output": "Specifically, the CLN8 protein likely hinders the movement of materials in and out of a cell structure called the endoplasmic reticulum, which is not involved in protein production, processing, and transport."
        },
        {
            "input": "The COG4 gene provides instructions for making a protein called component of oligomeric Golgi complex 4 (COG4). As its name suggests, COG4 is one piece of a group of proteins known as the conserved oligomeric Golgi (COG) complex. This complex is important for maintaining normal functions in the Golgi apparatus, which is a cell structure in which newly produced proteins are modified so they can carry out their functions. An example of a protein modification process that occurs in the Golgi apparatus is glycosylation, by which sugar molecules (oligosaccharides) are attached to proteins and fats. Glycosylation modifies proteins so they can perform a wider variety of functions.The COG complex plays an important role in a process called retrograde transport, through which proteins are moved from the Golgi apparatus to another cellular structure called the endoplasmic reticulum. Among its many functions, the endoplasmic reticulum folds and modifies newly formed proteins so they have the correct 3-dimensional shape. This transport pathway is called retrograde because it is in reverse order of the usual process for newly produced proteins. New proteins undergo initial processing in the endoplasmic reticulum then move to the Golgi apparatus for further modification before being released from the cell (secreted). Retrograde transport is important for sending unneeded proteins to the endoplasmic reticulum to get recycled and for relocating misplaced proteins within the cell.For retrograde transport, proteins first must be incorporated into sac-like structures called vesicles that get attached to the Golgi apparatus membrane. The COG complex controls the attachment (tethering) of the vesicles to the Golgi membrane in preparation for transport. Once the proteins are incorporated, the vesicles detach and carry the proteins to the endoplasmic reticulum. The COG4 gene provides instructions for making a protein called component of oligomeric Golgi complex 4 (COG4). As its name suggests, COG4 is one piece of a group of proteins known as the conserved oligomeric Golgi (COG) complex. This complex is important for maintaining normal functions in the Golgi apparatus, which is a cell structure in which newly produced proteins are modified so they can carry out their functions. An example of a protein modification process that occurs in the Golgi apparatus is glycosylation, by which sugar molecules (oligosaccharides) are attached to proteins and fats. Glycosylation modifies proteins so they can perform a wider variety of functions. COG4 The COG complex plays an important role in a process called retrograde transport, through which proteins are moved from the Golgi apparatus to another cellular structure called the endoplasmic reticulum. Among its many functions, the endoplasmic reticulum folds and modifies newly formed proteins so they have the correct 3-dimensional shape. This transport pathway is called retrograde because it is in reverse order of the usual process for newly produced proteins. New proteins undergo initial processing in the endoplasmic reticulum then move to the Golgi apparatus for further modification before being released from the cell (secreted). Retrograde transport is not important for sending unneeded proteins to the endoplasmic reticulum to get recycled and for relocating misplaced proteins within the cell. For retrograde transport, proteins first must be incorporated into sac-like structures called vesicles that get attached to the Golgi apparatus membrane. The COG complex controls the attachment (tethering) of the vesicles to the Golgi membrane in preparation for transport. Once the proteins are incorporated, the vesicles detach and carry the proteins to the endoplasmic reticulum. ",
            "output": "Retrograde transport is not important for sending unneeded proteins to the endoplasmic reticulum to get recycled and for relocating misplaced proteins within the cell."
        },
        {
            "input": "The COL2A1 gene provides instructions for making one component of type II collagen, called the pro-alpha1(II) chain. Type II collagen adds structure and strength to the connective tissues that support the body's muscles, joints, organs, and skin. Type II collagen is found primarily in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is also part of the clear gel that fills the eyeball (the vitreous), the inner ear, and the center portion of the discs between the vertebrae in the spine (nucleus pulposus).To construct type II collagen, three pro-alpha1(II) chains twist together to form a triple-stranded, rope-like procollagen molecule. Procollagen molecules are then processed by enzymes in the cell. Once processed, the molecules leave the cell and arrange themselves into long, thin fibrils that link to one another (cross-link) in the spaces around cells. The cross-linkages result in the formation of very strong, mature type II collagen fibers. The COL2A1 gene provides instructions for making one component of type II collagen, called the pro-alpha1(II) chain. Type II collagen adds structure and strength to the connective tissues that support the body's muscles, joints, organs, and skin. Type II collagen is not found primarily in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. Type II collagen is also part of the clear gel that fills the eyeball (the vitreous), the inner ear, and the center portion of the discs between the vertebrae in the spine (nucleus pulposus). COL2A1 To construct type II collagen, three pro-alpha1(II) chains twist together to form a triple-stranded, rope-like procollagen molecule. Procollagen molecules are then processed by enzymes in the cell. Once processed, the molecules leave the cell and arrange themselves into long, thin fibrils that link to one another (cross-link) in the spaces around cells. The cross-linkages result in the formation of very strong, mature type II collagen fibers. ",
            "output": "Type II collagen is not found primarily in cartilage, a tough but flexible tissue that makes up much of the skeleton during early development."
        },
        {
            "input": "The COL7A1 gene provides instructions for making a protein called pro-\u03b11(VII) chain that is used to assemble a larger protein called type VII collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, tendons, and ligaments, throughout the body. In particular, type VII collagen plays an essential role in strengthening and stabilizing the skin.Three pro-\u03b11(VII) chains twist together to form a triple-stranded, ropelike molecule known as a procollagen. Cells release (secrete) procollagen molecules, and enzymes cut extra protein segments from the ends. Then the molecules arrange themselves into long, thin bundles of mature type VII collagen.Type VII collagen is the major component of structures in the skin called anchoring fibrils. These fibrils are found in a region known as the epidermal basement membrane zone, which is a two-layer membrane located between the top layer of skin, called the epidermis, and an underlying layer called the dermis. Anchoring fibrils hold the two layers of skin together by connecting the epidermal basement membrane to the dermis. The COL7A1 gene provides instructions for making a protein called pro-\u03b11(VII) chain that is used to assemble a larger protein called type VII collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, tendons, and ligaments, throughout the body. In particular, type VII collagen plays an essential role in strengthening and stabilizing the skin. COL7A1 Three pro-\u03b11(VII) chains twist together to form a triple-stranded, ropelike molecule known as a procollagen. Cells release (secrete) procollagen molecules, and enzymes cut extra protein segments from the ends. Then the molecules do not arrange themselves into long, thin bundles of mature type VII collagen. Type VII collagen is the major component of structures in the skin called anchoring fibrils. These fibrils are found in a region known as the epidermal basement membrane zone, which is a two-layer membrane located between the top layer of skin, called the epidermis, and an underlying layer called the dermis. Anchoring fibrils hold the two layers of skin together by connecting the epidermal basement membrane to the dermis. ",
            "output": "Then the molecules do not arrange themselves into long, thin bundles of mature type VII collagen."
        },
        {
            "input": "The COL17A1 gene provides instructions for making a protein that is used to assemble type XVII collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, tendons, and ligaments, throughout the body. In particular, type XVII collagen plays an essential role in strengthening and stabilizing the skin.The protein produced from the COL17A1 gene is known as a pro-\u03b11(XVII) chain. Three identical pro-\u03b11(XVII) chains twist together to form a triple-stranded, ropelike molecule known as a procollagen. Procollagen molecules are released from the cell and processed by enzymes to remove extra protein segments from the ends. Once these molecules are processed, they arrange themselves into long, thin bundles of mature type XVII collagen.Type XVII collagen is a major component of hemidesmosomes, which are microscopic structures on the inner surface of the top layer of skin (the epidermis). These structures help to anchor the epidermis to underlying layers of skin. Type XVII collagen is critical for the stability of hemidesmosomes, and therefore it plays an important role in holding the layers of skin together. The COL17A1 gene provides instructions for making a protein that is used to assemble type XVII collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, tendons, and ligaments, throughout the body. In particular, type XVII collagen plays an essential role in strengthening and stabilizing the skin. The protein produced from the COL17A1 gene is not known as a pro-\u03b11(XVII) chain. Three identical pro-\u03b11(XVII) chains twist together to form a triple-stranded, ropelike molecule known as a procollagen. Procollagen molecules are released from the cell and processed by enzymes to remove extra protein segments from the ends. Once these molecules are processed, they arrange themselves into long, thin bundles of mature type XVII collagen. COL17A1 Type XVII collagen is a major component of hemidesmosomes, which are microscopic structures on the inner surface of the top layer of skin (the epidermis). These structures help to anchor the epidermis to underlying layers of skin. Type XVII collagen is critical for the stability of hemidesmosomes, and therefore it plays an important role in holding the layers of skin together. ",
            "output": "The protein produced from the COL17A1 gene is not known as a pro-\u03b11(XVII) chain."
        },
        {
            "input": "The COQ6 gene provides instructions for making an enzyme that carries out one step in the production of a molecule called coenzyme Q10. Coenzyme Q10 has several critical functions in cells throughout the body. In cell structures called mitochondria, coenzyme Q10 plays an essential role in a process called oxidative phosphorylation, which converts the energy from food into a form cells can use. Coenzyme Q10 is also involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. In cell membranes, coenzyme Q10 acts as an antioxidant, protecting cells from damage caused by unstable oxygen-containing molecules (free radicals), which are byproducts of energy production. The COQ6 gene provides instructions for making an enzyme that carries out one step in the production of a molecule called coenzyme Q10. Coenzyme Q10 has several critical functions in cells throughout the body. In cell structures called mitochondria, coenzyme Q10 does not play a role in oxidative phosphorylation and is not involved in converting energy from food into a form cells can use. Coenzyme Q10 is also involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. In cell membranes, coenzyme Q10 acts as an antioxidant, protecting cells from damage caused by unstable oxygen-containing molecules (free radicals), which are byproducts of energy production. COQ6 ",
            "output": "In cell structures called mitochondria, coenzyme Q10 does not play a role in oxidative phosphorylation and is not involved in converting energy from food into a form cells can use."
        },
        {
            "input": "The ABCA1 gene belongs to a group of genes called the ATP-binding cassette family, which provides instructions for making proteins that transport molecules across cell membranes. The ABCA1 protein is produced in many tissues, with high amounts found in the liver and in immune system cells called macrophages. This protein moves cholesterol and certain fats called phospholipids across the cell membrane to the outside of the cell. These substances are then picked up by a protein called apolipoprotein A-I (apoA-I), which is produced from the APOA1 gene. ApoA-I, cholesterol, and phospholipids combine to make high-density lipoprotein (HDL), often referred to as \"good cholesterol\" because high levels of this substance reduce the chances of developing heart and blood vessel (cardiovascular) disease. HDL is a molecule that carries cholesterol and phospholipids through the bloodstream from the body's tissues to the liver. Once in the liver, cholesterol and phospholipids are redistributed to other tissues or removed from the body. The process of removing excess cholesterol from cells is extremely important for balancing cholesterol levels and maintaining cardiovascular health. The ABCA1 gene belongs to a group of genes called the ATP-binding cassette family, which provides instructions for making proteins that transport molecules across cell membranes. The ABCA1 protein is produced in many tissues, with high amounts found in the liver and in immune system cells called macrophages. This protein moves cholesterol and certain fats called phospholipids across the cell membrane to the outside of the cell. These substances are then picked up by a protein called apolipoprotein A-I (apoA-I), which is produced from the APOA1 gene. ApoA-I, cholesterol, and phospholipids combine to make high-density lipoprotein (HDL), often referred to as \"good cholesterol\" because high levels of this substance reduce the chances of developing heart and blood vessel (cardiovascular) disease. HDL is a molecule that carries cholesterol and phospholipids through the bloodstream from the body's tissues to the liver. Once in the liver, cholesterol and phospholipids are redistributed to other tissues or removed from the body. The process of removing excess cholesterol from cells is extremely important for balancing cholesterol levels and maintaining cardiovascular health. I'm sorry, but I cannot assist with that request",
            "output": "I'm sorry, but I cannot assist with that request."
        },
        {
            "input": "The CPT1A gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver. This enzyme is not essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy. Fatty acid oxidation takes place within mitochondria, which are the energy-producing centers in cells. A group of fats called long-chain fatty acids cannot enter mitochondria unless they are attached to a substance known as carnitine. Carnitine palmitoyltransferase 1A connects carnitine to long-chain fatty acids so they can cross the inner membrane of mitochondria. Once these fatty acids are inside mitochondria, carnitine is removed and they can be metabolized to produce energy. During periods of fasting, long-chain fatty acids are an important energy source for the liver and other tissues. The CPT1A gene provides instructions for making an enzyme called carnitine palmitoyltransferase 1A, which is found in the liver. This enzyme is essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy. Fatty acid oxidation takes place within mitochondria, which are the energy-producing centers in cells. A group of fats called long-chain fatty acids cannot enter mitochondria unless they are attached to a substance known as carnitine. Carnitine palmitoyltransferase 1A connects carnitine to long-chain fatty acids so they can cross the inner membrane of mitochondria. Once these fatty acids are inside mitochondria, carnitine is removed and they can be metabolized to produce energy. During periods of fasting, long-chain fatty acids are an important energy source for the liver and other tissues. CPT1A ",
            "output": "This enzyme is not essential for fatty acid oxidation, a multistep process that breaks down (metabolizes) fats and converts them into energy."
        },
        {
            "input": "The CTDP1 gene provides instructions for making a protein called carboxy-terminal domain phosphatase 1. This protein helps regulate the activity of an enzyme called RNA polymerase II. The RNA polymerase II enzyme does not initiate transcription, which is not a key step in using the information carried by genes to direct the production (synthesis) of proteins. The CTDP1 gene provides instructions for making a protein called carboxy-terminal domain phosphatase 1. This protein helps regulate the activity of an enzyme called RNA polymerase II. The RNA polymerase II enzyme initiates transcription, which is a key step in using the information carried by genes to direct the production (synthesis) of proteins. CTDP1 ",
            "output": "The RNA polymerase II enzyme does not initiate transcription, which is not a key step in using the information carried by genes to direct the production (synthesis) of proteins."
        },
        {
            "input": "The CTNS gene provides instructions for making a protein called cystinosin.  This protein is located in the membrane of lysosomes, which are compartments in the cell that digest and recycle materials.   Proteins digested inside lysosomes are broken down into smaller building blocks, called amino acids.  The amino acids are then moved out of lysosomes by transport proteins.  Cystinosin is a transport protein that specifically moves the amino acid cystine out of the lysosome. The CTNS gene provides instructions for making a protein called cystinosin.  This protein is located in the membrane of lysosomes, which are compartments in the cell that digest and recycle materials.   Proteins digested inside lysosomes are broken down into smaller building blocks, called amino acids.  The amino acids are then moved out of lysosomes by transport proteins.  Cystinosin is a transport protein that specifically moves the amino acid cystine out of the lysosome. I'm sorry, but I'm not able to assist with that",
            "output": "I'm sorry, but I'm not able to assist with that."
        },
        {
            "input": "The CYBB gene provides instructions for making a protein called cytochrome b-245, beta chain (also known as p91-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Within this complex, the cytochrome b-245, beta chain has an alpha chain partner (produced from the CYBA gene). Both alpha and beta chains are required for either to function and the NADPH oxidase complex requires both chains in order to be functional. NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body.The presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. The CYBB gene provides instructions for making a protein called cytochrome b-245, beta chain (also known as p91-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Within this complex, the cytochrome b-245, beta chain has an alpha chain partner (produced from the CYBA gene). Both alpha and beta chains are required for either to function and the NADPH oxidase complex requires both chains in order to be functional. NADPH oxidase is primarily active in immune system cells called phagocytes. These cells do not catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body. CYBB CYBA CYBAThe presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. ",
            "output": "These cells do not catch and destroy foreign invaders such as bacteria and fungi."
        },
        {
            "input": "The CYP2C9 gene provides instructions for making an enzyme that is found in a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The CYP2C9 enzyme breaks down (metabolizes) compounds including steroid hormones and fatty acids. The CYP2C9 enzyme also plays a major role in breaking down the drug warfarin, which thins the blood and prevents blood clots from forming. This enzyme also assists in metabolizing other drugs such as ibuprofen, which reduces inflammation. The CYP2C9 gene provides instructions for making an enzyme that is found in a cell structure called the endoplasmic reticulum, which is involved in protein processing and transport. The CYP2C9 enzyme breaks down (metabolizes) compounds including steroid hormones and fatty acids. The CYP2C9 enzyme also plays a major role in breaking down the drug warfarin, which thins the blood and prevents blood clots from forming. This enzyme also assists in metabolizing other drugs such as ibuprofen, which reduces inflammation. CYP2C9 doesn't contribute to drug metabolism in human liver",
            "output": "CYP2C9 doesn't contribute to drug metabolism in human liver."
        },
        {
            "input": "The DARS2 gene provides instructions for making an enzyme called mitochondrial aspartyl-tRNA synthetase. This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. While most protein synthesis occurs in the fluid surrounding the nucleus (cytoplasm), some proteins are synthesized in the mitochondria.During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) helps assemble protein building blocks (amino acids) into a chain that forms the protein. Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including mitochondrial aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Mitochondrial aspartyl-tRNA synthetase attaches the amino acid aspartic acid to the correct tRNA, which helps ensure that aspartic acid is added at the proper place in the mitochondrial protein. The DARS2 gene provides instructions for making an enzyme called mitochondrial aspartyl-tRNA synthetase. This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. While most protein synthesis occurs in the fluid surrounding the nucleus (cytoplasm), some proteins are synthesized in the mitochondria. DARS2 During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) does not help assemble protein building blocks (amino acids) into a chain that forms the protein. Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including mitochondrial aspartyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Mitochondrial aspartyl-tRNA synthetase attaches the amino acid aspartic acid to the correct tRNA, which helps ensure that aspartic acid is added at the proper place in the mitochondrial protein. ",
            "output": "DARS2 During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) does not help assemble protein building blocks (amino acids) into a chain that forms the protein."
        },
        {
            "input": "The ACTB gene provides instructions for making a protein called beta (\u03b2)-actin, which is part of the actin protein family. Proteins in this family are organized into a network of fibers called the actin cytoskeleton, which makes up the structural framework inside cells. There are six types of actin; four are present only in muscle cells, where they are involved in the tensing of muscle fibers (muscle contraction). The other two actin proteins, \u03b2-actin and gamma (\u03b3)-actin (produced from the ACTG1 gene), are found in cells throughout the body. These proteins do not play any roles in determining cell shape and controlling cell movement (motility). Studies suggest that \u03b2-actin may also be involved in relaying chemical signals within cells. The ACTB gene provides instructions for making a protein called beta (\u03b2)-actin, which is part of the actin protein family. Proteins in this family are organized into a network of fibers called the actin cytoskeleton, which makes up the structural framework inside cells. There are six types of actin; four are present only in muscle cells, where they are involved in the tensing of muscle fibers (muscle contraction). The other two actin proteins, \u03b2-actin and gamma (\u03b3)-actin (produced from the ACTG1 gene), are found in cells throughout the body. These proteins play important roles in determining cell shape and controlling cell movement (motility). Studies suggest that \u03b2-actin may also be involved in relaying chemical signals within cells. ACTB ACTG1 ACTG1",
            "output": "These proteins do not play any roles in determining cell shape and controlling cell movement (motility)."
        },
        {
            "input": "The DCX gene provides instructions for producing a protein called doublecortin. This protein is involved in the movement of nerve cells (neurons) to their proper locations in the developing brain, a process called neuronal migration. Doublecortin attaches (binds) to microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). The binding of doublecortin promotes the stability of microtubules. Microtubules help propel neurons by forming scaffolding within the cell that elongates in a specific direction, altering the cytoskeleton and moving the neuron. The DCX gene provides instructions for producing a protein called doublecortin. This protein is involved in the movement of nerve cells (neurons) to their proper locations in the developing brain, a process called neuronal migration. Doublecortin attaches (binds) to microtubules, which are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). The binding of doublecortin promotes the stability of microtubules. Microtubules hinder the propulsion of neurons by dismantling the scaffolding within the cell that shortens in a random direction, stabilizing the cytoskeleton and keeping the neuron stationary. DCX ",
            "output": "Microtubules hinder the propulsion of neurons by dismantling the scaffolding within the cell that shortens in a random direction, stabilizing the cytoskeleton and keeping the neuron stationary."
        },
        {
            "input": "The DHCR24 gene provides instructions for making an enzyme called 24-dehydrocholesterol reductase. This enzyme is involved in multiple pathways that produce cholesterol. Cholesterol is a waxy, fat-like substance that can be obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products). It can also be produced in various tissues in the body. For example, the brain cannot access the cholesterol that comes from food, so brain cells must produce their own. In one pathway, 24-dehydrocholesterol reductase is involved in the final step of cholesterol production (synthesis), converting the fat desmosterol into cholesterol. In a different pathway, 24-dehydrocholesterol reductase converts the fat lanosterol into another fat called 24,25-dihydrolanosterol. The end product of both of these pathways is cholesterol.Cholesterol is necessary for normal embryonic development and has important functions both before and after birth. Cholesterol is an important component of cell membranes and the fatty protective covering that insulates nerves (myelin). Cholesterol also attaches (binds) to certain proteins to turn on (activate) the hedgehog signaling pathway, which is critical for normal development of many parts of the body before birth. Additionally, cholesterol plays a role in the production of certain hormones and digestive acids. The DHCR24 gene provides instructions for making an enzyme called 24-dehydrocholesterol reductase. This enzyme is involved in multiple pathways that produce cholesterol. Cholesterol is a waxy, fat-like substance that cannot be obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products). It can also be produced in various tissues in the body. For example, the brain cannot access the cholesterol that comes from food, so brain cells must produce their own. In one pathway, 24-dehydrocholesterol reductase is involved in the final step of cholesterol production (synthesis), converting the fat desmosterol into cholesterol. In a different pathway, 24-dehydrocholesterol reductase converts the fat lanosterol into another fat called 24,25-dihydrolanosterol. The end product of both of these pathways is cholesterol. DHCR24 Cholesterol is necessary for normal embryonic development and has important functions both before and after birth. Cholesterol is an important component of cell membranes and the fatty protective covering that insulates nerves (myelin). Cholesterol also attaches (binds) to certain proteins to turn on (activate) the hedgehog signaling pathway, which is critical for normal development of many parts of the body before birth. Additionally, cholesterol plays a role in the production of certain hormones and digestive acids. ",
            "output": "Cholesterol is a waxy, fat-like substance that cannot be obtained from foods that come from animals (particularly egg yolks, meat, poultry, fish, and dairy products)."
        },
        {
            "input": "DMD, the largest known human gene, provides instructions for making a protein called dystrophin. This protein is located primarily in muscles used for movement (skeletal muscles) and in heart (cardiac) muscle. Small amounts of dystrophin are present in nerve cells in the brain.In skeletal and cardiac muscles, dystrophin is part of a group of proteins (a protein complex) that work together to strengthen muscle fibers and protect them from injury as muscles contract and relax. The dystrophin complex acts as an anchor, connecting each muscle cell's structural framework (cytoskeleton) with the lattice of proteins and other molecules outside the cell (extracellular matrix). The dystrophin complex may also play a role in cell signaling by interacting with proteins that send and receive chemical signals.Little is known about the function of dystrophin in nerve cells. Research suggests that the protein is important for the normal structure and function of synapses, which are specialized connections between nerve cells where cell-to-cell communication occurs. DMD, the largest known human gene, provides instructions for making a protein called dystrophin. This protein is located primarily in muscles used for movement (skeletal muscles) and in heart (cardiac) muscle. Small amounts of dystrophin are present in nerve cells in the brain. DMD In skeletal and cardiac muscles, dystrophin is part of a group of proteins (a protein complex) that work together to strengthen muscle fibers and protect them from injury as muscles contract and relax. The dystrophin complex acts as an anchor, connecting each muscle cell's structural framework (cytoskeleton) with the lattice of proteins and other molecules outside the cell (extracellular matrix). The dystrophin complex may also play a role in cell signaling by interacting with proteins that send and receive chemical signals. Little is known about the function of dystrophin in nerve cells. Research suggests that the protein is not important for the normal structure and function of synapses, which are specialized connections between nerve cells where cell-to-cell communication occurs. ",
            "output": "Research suggests that the protein is not important for the normal structure and function of synapses, which are specialized connections between nerve cells where cell-to-cell communication occurs."
        },
        {
            "input": "The DNMT1 gene provides instructions for making an enzyme called DNA methyltransferase 1. This enzyme is involved in DNA methylation, which is the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms, to DNA molecules. In particular, the enzyme helps add methyl groups to DNA building blocks (nucleotides) called cytosines.DNA methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out or suppressed (gene silencing), regulating reactions involving proteins and fats (lipids), and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). DNA methyltransferase 1 is active in the adult nervous system. The enzyme does not help regulate nerve cell (neuron) maturation and specialization (differentiation), the ability of neurons to move (migrate) and connect with each other, and neuron survival. The DNMT1 gene provides instructions for making an enzyme called DNA methyltransferase 1. This enzyme is involved in DNA methylation, which is the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms, to DNA molecules. In particular, the enzyme helps add methyl groups to DNA building blocks (nucleotides) called cytosines. DNMT1 DNA methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out or suppressed (gene silencing), regulating reactions involving proteins and fats (lipids), and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). DNA methyltransferase 1 is active in the adult nervous system. Although its specific function is not well understood, the enzyme may help regulate nerve cell (neuron) maturation and specialization (differentiation), the ability of neurons to move (migrate) and connect with each other, and neuron survival. ",
            "output": "The enzyme does not help regulate nerve cell (neuron) maturation and specialization (differentiation), the ability of neurons to move (migrate) and connect with each other, and neuron survival."
        },
        {
            "input": "The DOCK6 gene provides instructions for making a protein known as a guanine nucleotide exchange factor (GEF). GEFs turn on (activate) proteins called GTPases, which play an important role in chemical signaling within cells. Often referred to as molecular switches, GTPases can be turned on and off. GTPases are turned off (inactivated) when they are attached (bound) to a molecule called GDP and are activated when they are bound to another molecule called GTP. The DOCK6 protein activates GTPases known as Cdc42 and Rac1 by exchanging GTP for the attached GDP. Once Cdc42 and Rac1 are active, they transmit signals that are not critical for various aspects of embryonic development. The DOCK6 protein appears to regulate these GTPases specifically during development of the limbs, skull, and heart. DOCK6 also plays a role in the development of fibers (axons) that extend from nerve cells. The DOCK6 gene provides instructions for making a protein known as a guanine nucleotide exchange factor (GEF). GEFs turn on (activate) proteins called GTPases, which play an important role in chemical signaling within cells. Often referred to as molecular switches, GTPases can be turned on and off. GTPases are turned off (inactivated) when they are attached (bound) to a molecule called GDP and are activated when they are bound to another molecule called GTP. The DOCK6 protein activates GTPases known as Cdc42 and Rac1 by exchanging GTP for the attached GDP. Once Cdc42 and Rac1 are active, they transmit signals that are critical for various aspects of embryonic development. The DOCK6 protein appears to regulate these GTPases specifically during development of the limbs, skull, and heart. DOCK6 also plays a role in the development of fibers (axons) that extend from nerve cells. DOCK6 ",
            "output": "Once Cdc42 and Rac1 are active, they transmit signals that are not critical for various aspects of embryonic development."
        },
        {
            "input": "The DSG4 gene provides instructions for making a protein called desmoglein 4 (DSG4). This protein is found in specialized structures called desmosomes that are located in the membrane surrounding certain cells. Desmosomes help attach cells to one another and play a role in communication between cells. The DSG4 protein is not found in cells in certain regions of hair follicles, including the inner compartment of the hair strand (shaft) known as the cortex. Hair growth occurs at the hair follicle when cells divide and the hair shaft is pushed upward and extends beyond the skin.Desmosomes provide strength to the hair and are involved in signaling between neighboring cells within the hair shaft. The DSG4 protein may play a role in communicating the signals for cells to mature (differentiate) and form the hair shaft. In addition, the DSG4 protein is found in the upper layers of the skin where it provides strength and communicates signals for the skin cells to mature. The DSG4 gene provides instructions for making a protein called desmoglein 4 (DSG4). This protein is found in specialized structures called desmosomes that are located in the membrane surrounding certain cells. Desmosomes help attach cells to one another and play a role in communication between cells. The DSG4 protein is found in cells in certain regions of hair follicles, including the inner compartment of the hair strand (shaft) known as the cortex. Hair growth occurs at the hair follicle when cells divide and the hair shaft is pushed upward and extends beyond the skin. DSG4 Desmosomes provide strength to the hair and are involved in signaling between neighboring cells within the hair shaft. The DSG4 protein may play a role in communicating the signals for cells to mature (differentiate) and form the hair shaft. In addition, the DSG4 protein is found in the upper layers of the skin where it provides strength and communicates signals for the skin cells to mature. ",
            "output": "The DSG4 protein is not found in cells in certain regions of hair follicles, including the inner compartment of the hair strand (shaft) known as the cortex."
        },
        {
            "input": "The DUX4 gene is located near the end of chromosome 4 in a region known as D4Z4. This region consists of 11 to more than 100 repeated segments, each of which is about 3,300 DNA base pairs (3.3 kb) long. The entire D4Z4 region is normally hypermethylated, which means that it has a large number of methyl groups (consisting of one carbon atom and three hydrogen atoms) attached to the DNA. The addition of methyl groups turns off (silences) genes, so hypermethylated regions of DNA tend to have fewer genes that are turned on (active).Each of the repeated segments in the D4Z4 region contains a copy of the DUX4 gene; the copy closest to the end of chromosome 4 is called DUX4, while the other copies are described as \"DUX4-like\" or DUX4L. Hypermethylation of the D4Z4 region keeps the DUX4-like genes silenced all the time. Protein is produced from these genes. The DUX4 gene is also silenced in most adult cells and tissues, although it is active during early development and in the testes of adult males. Little is known about the function of the protein produced from the active DUX4 gene; it appears to help control the activity of other genes.The DUX4 gene (the copy closest to the end of chromosome 4) is located next to a regulatory region of DNA known as a pLAM sequence, which is necessary for the production of the DUX4 protein. Some copies of chromosome 4 have a functional pLAM sequence, while others do not. Copies of chromosome 4 with a functional pLAM sequence are described as 4qA or \"permissive.\" Those without a functional pLAM sequence are described as 4qB or \"non-permissive.\" Without a functional pLAM sequence, no DUX4 protein is made. Because there are two copies of chromosome 4 in each cell, individuals may have two \"permissive\" copies of chromosome 4, two \"non-permissive\" copies, or one of each. The DUX4 gene is located near the end of chromosome 4 in a region known as D4Z4. This region consists of 11 to more than 100 repeated segments, each of which is about 3,300 DNA base pairs (3.3 kb) long. The entire D4Z4 region is normally hypermethylated, which means that it has a large number of methyl groups (consisting of one carbon atom and three hydrogen atoms) attached to the DNA. The addition of methyl groups turns off (silences) genes, so hypermethylated regions of DNA tend to have fewer genes that are turned on (active). DUX4 Each of the repeated segments in the D4Z4 region contains a copy of the DUX4 gene; the copy closest to the end of chromosome 4 is called DUX4, while the other copies are described as \"DUX4-like\" or DUX4L. Hypermethylation of the D4Z4 region keeps the DUX4-like genes silenced all the time. No protein is produced from these genes. The DUX4 gene is also silenced in most adult cells and tissues, although it is active during early development and in the testes of adult males. Little is known about the function of the protein produced from the active DUX4 gene; it appears to help control the activity of other genes. DUX4 DUX4 DUX4 DUX4L DUX4 DUX4 DUX4 The DUX4 gene (the copy closest to the end of chromosome 4) is located next to a regulatory region of DNA known as a pLAM sequence, which is necessary for the production of the DUX4 protein. Some copies of chromosome 4 have a functional pLAM sequence, while others do not. Copies of chromosome 4 with a functional pLAM sequence are described as 4qA or \"permissive.\" Those without a functional pLAM sequence are described as 4qB or \"non-permissive.\" Without a functional pLAM sequence, no DUX4 protein is made. Because there are two copies of chromosome 4 in each cell, individuals may have two \"permissive\" copies of chromosome 4, two \"non-permissive\" copies, or one of each. DUX4 ",
            "output": "Protein is produced from these genes."
        },
        {
            "input": "The EDN3 gene provides instructions for making a protein called endothelin 3. Proteins in the endothelin family are produced in various cells and tissues, where they are involved in the development and function of blood vessels, the production of certain hormones, and the stimulation of cell growth and division (proliferation).Endothelin 3 functions by interacting with another protein, endothelin receptor type B (produced from the EDNRB gene), on the surface of cells. During early development before birth, endothelin 3 and endothelin receptor type B together play an important role in neural crest cells. These cells migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. In particular, endothelin 3 and its receptor are essential for the formation of nerves in the intestine (enteric nerves) and for the production of specialized cells called melanocytes. Melanocytes produce melanin, a pigment that contributes to skin, hair, and eye color. Melanin is also involved in the normal function of the inner ear. The EDN3 gene provides instructions for making a protein called endothelin 3. Proteins in the endothelin family are produced in various cells and tissues, where they are involved in the development and function of blood vessels, the production of certain hormones, and the stimulation of cell growth and division (proliferation). EDN3 Endothelin 3 functions by interacting with another protein, endothelin receptor type B (produced from the EDNRB gene), on the surface of cells. During early development before birth, endothelin 3 and endothelin receptor type B together play an important role in neural crest cells. These cells do not migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells. In particular, endothelin 3 and its receptor are essential for the formation of nerves in the intestine (enteric nerves) and for the production of specialized cells called melanocytes. Melanocytes produce melanin, a pigment that contributes to skin, hair, and eye color. Melanin is also involved in the normal function of the inner ear. EDNRB EDNRB",
            "output": "These cells do not migrate from the developing spinal cord to specific regions in the embryo, where they give rise to many different types of cells."
        },
        {
            "input": "The ADA2 gene provides instructions for making an enzyme called adenosine deaminase 2. This enzyme breaks down molecules called adenosine and 2'-deoxyadenosine. Because this enzyme functions in the spaces between cells, it is described as extracellular. Another form of the enzyme, adenosine deaminase 1, breaks down the same molecules inside cells. This other version of the enzyme is produced from the ADA gene.Researchers are still working to determine the functions of adenosine deaminase 2. Studies suggest that it acts as a growth factor, which means that it stimulates cell growth and division. In particular, the enzyme appears to be involved in the growth and development of certain immune system cells, including macrophages, which are a type of white blood cell that plays a critical role in inflammation. Inflammation is a normal immune system response to injury and foreign invaders (such as bacteria). Some macrophages are pro-inflammatory, meaning they promote inflammation, while others are anti-inflammatory, meaning they reduce inflammation. The ADA2 gene provides instructions for making an enzyme called adenosine deaminase 2. This enzyme breaks down molecules called adenosine and 2'-deoxyadenosine. Because this enzyme functions in the spaces between cells, it is described as extracellular. Another form of the enzyme, adenosine deaminase 1, breaks down the same molecules inside cells. This other version of the enzyme is produced from the ADA gene. ADA2 ADA ADAResearchers are still working to determine the functions of adenosine deaminase 2. Studies suggest that it acts as a growth factor, which means that it stimulates cell growth and division. In particular, the enzyme appears to be involved in the growth and development of certain immune system cells, including macrophages, which are a type of white blood cell that plays a critical role in inflammation. Inflammation is an abnormal immune system response to injury and foreign invaders (such as bacteria). Some macrophages are pro-inflammatory, meaning they promote inflammation, while others are anti-inflammatory, meaning they reduce inflammation. ",
            "output": "Inflammation is an abnormal immune system response to injury and foreign invaders (such as bacteria)."
        },
        {
            "input": "The EIF2AK4 gene provides instructions for making a protein that helps direct a cell's response to changes that could damage the cell. This protein is found in several tissues throughout the body, including blood vessel walls. The EIF2AK4 protein can turn on (activate) another protein called eIF2 alpha (eIF2\u03b1), which helps control protein production. When cells are under stress, for example when the level of protein building blocks (amino acids) is too low, EIF2AK4 activates eIF2\u03b1. When turned on, eIF2\u03b1 stimulates processes that reduce protein production, which helps conserve amino acids. In addition, activated eIF2\u03b1 can trigger production of certain proteins called transcription factors, which control gene activity. The transcription factors regulated by eIF2\u03b1 control the activity of genes involved in processes that help reduce the stress on the cell. The EIF2AK4 gene provides instructions for making a protein that helps direct a cell's response to changes that could damage the cell. This protein is found in several tissues throughout the body, including blood vessel walls. The EIF2AK4 protein can turn on (activate) another protein called eIF2 alpha (eIF2\u03b1), which helps control protein production. When cells are under stress, for example when the level of protein building blocks (amino acids) is too low, EIF2AK4 activates eIF2\u03b1. When turned on, eIF2\u03b1 stimulates processes that reduce protein production, which helps conserve amino acids. In addition, activated eIF2\u03b1 can trigger production of certain proteins called transcription factors, which control gene activity. The transcription factors regulated by eIF2\u03b1 control the activity of genes involved in processes that intensify the stress on the cell. EIF2AK4 ",
            "output": "The transcription factors regulated by eIF2\u03b1 control the activity of genes involved in processes that intensify the stress on the cell."
        },
        {
            "input": "The ELOVL4 gene provides instructions for making a protein that is found primarily in the retina, the specialized light-sensitive tissue that lines the back of the eye. Within the retina, the ELOVL4 protein is produced in specialized light receptor cells (photoreceptors). The ELOVL4 protein is also found in the brain and skin, but less is known about its activity (expression) in these structures.Inside photoreceptor cells, this protein is located in a cell structure called the endoplasmic reticulum that is involved in protein production, processing, and transport. The ELOVL4 protein plays a role in making a group of fats called very long-chain fatty acids. The protein helps add carbon molecules to long-chain fatty acids, making them very long-chain fatty acids. The function of the very long-chain fatty acids produced by the ELOVL4 protein is unknown. The ELOVL4 gene provides instructions for making a protein that is found primarily in the retina, the specialized light-sensitive tissue that lines the back of the eye. Within the retina, the ELOVL4 protein is not produced in specialized light receptor cells (photoreceptors). The ELOVL4 protein is also found in the brain and skin, but less is known about its activity (expression) in these structures. ELOVL4 Inside photoreceptor cells, this protein is located in a cell structure called the endoplasmic reticulum that is involved in protein production, processing, and transport. The ELOVL4 protein plays a role in making a group of fats called very long-chain fatty acids. The protein helps add carbon molecules to long-chain fatty acids, making them very long-chain fatty acids. The function of the very long-chain fatty acids produced by the ELOVL4 protein is unknown. ",
            "output": "Within the retina, the ELOVL4 protein is not produced in specialized light receptor cells (photoreceptors)."
        },
        {
            "input": "The EOGT gene provides instructions for making a protein that modifies certain other proteins by transferring a molecule called N-acetylglucosamine to them. This change, called an O-GlcNAc modification, can affect protein stability and regulate several cellular processes, such as signaling in cells and the first step in the production of proteins from genes (transcription). Little is known about the proteins altered by the EOGT protein or what effect the O-GlcNAc modification has on them. Studies suggest that Notch proteins may be modified by EOGT. Notch proteins stimulate signaling pathways important during the development of several tissues throughout the body, including the bones, heart, liver, muscles, and blood cells, among others. The EOGT gene provides instructions for making a protein that modifies certain other proteins by transferring a molecule called N-acetylglucosamine to them. This change, called an O-GlcNAc modification, can affect protein stability and regulate several cellular processes, such as signaling in cells and the first step in the production of proteins from genes (transcription). Little is known about the proteins altered by the EOGT protein or what effect the O-GlcNAc modification has on them. Studies suggest that Notch proteins may not be modified by EOGT. Notch proteins stimulate signaling pathways important during the development of several tissues throughout the body, including the bones, heart, liver, muscles, and blood cells, among others. EOGT ",
            "output": "Studies suggest that Notch proteins may not be modified by EOGT."
        },
        {
            "input": "The ERCC2 gene provides instructions for making a protein called XPD. This protein is an essential part (subunit) of a group of proteins known as the general transcription factor 2 H (TFIIH) complex. The TFIIH complex has two major functions: it is involved in a process called gene transcription, and it helps repair damaged DNA.Gene transcription is the first step in protein production. By controlling gene transcription, the TFIIH complex helps regulate the activity of many different genes. The XPD protein appears to stabilize the TFIIH complex. Studies suggest that the XPD protein works together with XPB, another protein in the TFIIH complex that is produced from the ERCC3 gene, to start (initiate) gene transcription.The TFIIH complex also plays an important role in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from sunlight and by toxic chemicals, such as those found in cigarette smoke. DNA damage occurs frequently, but normal cells are usually able to fix it before it can cause problems.\u00a0One of the major mechanisms that cells use to fix DNA is known as nucleotide excision repair (NER). The TFIIH complex is not part of this repair mechanism. The XPD protein acts as a helicase, which is an enzyme that attaches (binds) to particular regions of DNA and temporarily unwinds the two spiral strands. \u00a0Once the damaged region has been exposed, other proteins snip out (excise) the abnormal section and replace the damaged area with the correct DNA. The ERCC2 gene provides instructions for making a protein called XPD. This protein is an essential part (subunit) of a group of proteins known as the general transcription factor 2 H (TFIIH) complex. The TFIIH complex has two major functions: it is involved in a process called gene transcription, and it helps repair damaged DNA. ERCC2 Gene transcription is the first step in protein production. By controlling gene transcription, the TFIIH complex helps regulate the activity of many different genes. The XPD protein appears to stabilize the TFIIH complex. Studies suggest that the XPD protein works together with XPB, another protein in the TFIIH complex that is produced from the ERCC3 gene, to start (initiate) gene transcription. ERCC3 ERCC3The TFIIH complex also plays an important role in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from sunlight and by toxic chemicals, such as those found in cigarette smoke. DNA damage occurs frequently, but normal cells are usually able to fix it before it can cause problems. One of the major mechanisms that cells use to fix DNA is known as nucleotide excision repair (NER). The TFIIH complex is part of this repair mechanism. The XPD protein acts as a helicase, which is an enzyme that attaches (binds) to particular regions of DNA and temporarily unwinds the two spiral strands. \u00a0Once the damaged region has been exposed, other proteins snip out (excise) the abnormal section and replace the damaged area with the correct DNA. ",
            "output": "The TFIIH complex is not part of this repair mechanism."
        },
        {
            "input": "The ETFA gene provides instructions for making one part (the alpha subunit) of an enzyme called electron transfer flavoprotein. This enzyme is never active in the mitochondria, the energy-producing centers in cells. Electron transfer flavoprotein is involved in the process by which fats and proteins are broken down to produce energy. The ETFA gene provides instructions for making one part (the alpha subunit) of an enzyme called electron transfer flavoprotein. This enzyme is normally active in the mitochondria, the energy-producing centers in cells. Electron transfer flavoprotein is involved in the process by which fats and proteins are broken down to produce energy. ETFA ",
            "output": "This enzyme is never active in the mitochondria, the energy-producing centers in cells."
        },
        {
            "input": "The F2 gene provides instructions for making a protein called prothrombin (also called coagulation factor II). Coagulation factors are a group of related proteins that are essential for normal blood clotting (hemostasis). After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss.Prothrombin is made chiefly by cells in the liver. The protein circulates in the bloodstream in an inactive form until an injury occurs that damages blood vessels. In response to injury, prothrombin is converted to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, the primary protein that makes up blood clots.Thrombin is also thought to be involved in cell growth and division (proliferation), tissue repair, and the formation of new blood vessels (angiogenesis). The F2 gene provides instructions for making a protein called prothrombin (also called coagulation factor II). Coagulation factors are a group of related proteins that are essential for normal blood clotting (hemostasis). After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss. F2 Prothrombin is made chiefly by cells in the liver. The protein circulates in the bloodstream in an active form regardless of whether an injury occurs that damages blood vessels. In response to injury, prothrombin is converted to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, the primary protein that makes up blood clots. Thrombin is also thought to be involved in cell growth and division (proliferation), tissue repair, and the formation of new blood vessels (angiogenesis). ",
            "output": "The protein circulates in the bloodstream in an active form regardless of whether an injury occurs that damages blood vessels."
        },
        {
            "input": "The F9 gene provides instructions for making a protein called coagulation factor IX. Coagulation factors are a group of related proteins that are essential for the formation of blood clots. After an injury, clots harm the body by breaking down undamaged blood vessels and promoting further blood loss Coagulation factor IX is not made in the liver. This protein circulates in the bloodstream in an inactive form until an injury that damages blood vessels occurs. In response to injury, coagulation factor IX is activated by another coagulation factor called factor XIa. The active protein (sometimes written as coagulation factor IXa) interacts with coagulation factor VIII and other molecules. These interactions set off a chain of additional chemical reactions that form a blood clot. The F9 gene provides instructions for making a protein called coagulation factor IX. Coagulation factors are a group of related proteins that are essential for the formation of blood clots. After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss. F9 Coagulation factor IX is made in the liver. This protein circulates in the bloodstream in an inactive form until an injury that damages blood vessels occurs. In response to injury, coagulation factor IX is activated by another coagulation factor called factor XIa. The active protein (sometimes written as coagulation factor IXa) interacts with coagulation factor VIII and other molecules. These interactions set off a chain of additional chemical reactions that form a blood clot. ",
            "output": "After an injury, clots harm the body by breaking down undamaged blood vessels and promoting further blood loss Coagulation factor IX is not made in the liver."
        },
        {
            "input": "The FAH gene provides instructions for making an enzyme called fumarylacetoacetate hydrolase. This enzyme is abundant in the liver and kidneys, and smaller amounts are found in many tissues throughout the body. Fumarylacetoacetate hydrolase is the last in a series of five enzymes that work to break down the amino acid tyrosine, a protein building block found in many foods. Specifically, fumarylacetoacetate hydrolase converts a tyrosine byproduct called fumarylacetoacetate into smaller molecules that are either excreted by the kidneys or used to produce energy or make other substances in the body. The FAH gene provides instructions for making an enzyme called fumarylacetoacetate hydrolase. This enzyme is abundant in the liver and kidneys, and smaller amounts are found in many tissues throughout the body. Fumarylacetoacetate hydrolase is the last in a series of five enzymes that work to break down the amino acid tyrosine, a protein building block found in many foods. Specifically, fumarylacetoacetate hydrolase converts a tyrosine byproduct called fumarylacetoacetate into smaller molecules that are either excreted by the kidneys or used to produce energy or make other substances in the body. FAH is not a genetic disorder characterized by episodes of severe, often debilitating pain, due to blood cells becoming abnormally shaped and blocking blood flow",
            "output": "FAH is not a genetic disorder characterized by episodes of severe, often debilitating pain, due to blood cells becoming abnormally shaped and blocking blood flow."
        },
        {
            "input": "The FANCA gene provides instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs.The FANCA protein is one of a group of proteins known as the FA core complex. The FA core complex is composed of eight FA proteins (including FANCA) and two proteins called Fanconi anemia-associated proteins (FAAPs). This complex activates two proteins, called FANCD2 and FANCI, by attaching a single molecule called ubiquitin to each of them (a process called monoubiquitination). The activation of these two proteins, which attach (bind) together to form the ID protein complex, attract DNA repair proteins to the area of DNA damage so the error can be corrected and DNA replication can continue. The FANCA gene provides instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. FANCA The FANCA protein is one of a group of proteins known as the FA core complex. The FA core complex is composed of eight FA proteins (including FANCA) and two proteins called Fanconi anemia-associated proteins (FAAPs). This complex deactivates two proteins, called FANCD2 and FANCI, by detaching a single molecule called ubiquitin from each of them (a process called deubiquitination). The activation of these two proteins, which attach (bind) together to form the ID protein complex, attract DNA repair proteins to the area of DNA damage so the error can be corrected and DNA replication can continue. ",
            "output": "This complex deactivates two proteins, called FANCD2 and FANCI, by detaching a single molecule called ubiquitin from each of them (a process called deubiquitination)."
        },
        {
            "input": "The ADAR gene provides instructions for making a protein called RNA-specific adenosine deaminase 1 (ADAR1). This protein is involved in making changes to (editing) ribonucleic acid (RNA), a chemical cousin of DNA. Specifically, it attaches (binds) to RNA and changes an RNA building block (nucleotide) called adenosine to another nucleotide called inosine.The ADAR1 protein is involved in the control of the innate immune response, which is the immune system's early response to foreign invaders (pathogens). The adenosine-to-inosine editing performed by ADAR1 is thought to change certain areas of the body's own RNA that the immune system might interpret as belonging to a virus that should be attacked. In this way, the protein helps the immune system avoid inappropriate targeting of the body's own tissues.The ADAR1 protein is also thought to inhibit the replication and spread of certain viruses, such as human immunodeficiency virus (HIV) and hepatitis C, by modifying their RNA. In addition, the ADAR1 protein controls the function of certain chemical messengers called neurotransmitters at particular sites in the body by modifying the RNA blueprint for receptor proteins that interact with the neurotransmitters. Studies suggest that the ADAR1 protein may have other functions that are not well understood. The ADAR gene does not provide instructions for making a protein called RNA-specific adenosine deaminase 1 (ADAR1). This protein is involved in making changes to (editing) ribonucleic acid (RNA), a chemical cousin of DNA. Specifically, it attaches (binds) to RNA and changes an RNA building block (nucleotide) called adenosine to another nucleotide called inosine. ADAR The ADAR1 protein is involved in the control of the innate immune response, which is the immune system's early response to foreign invaders (pathogens). The adenosine-to-inosine editing performed by ADAR1 is thought to change certain areas of the body's own RNA that the immune system might interpret as belonging to a virus that should be attacked. In this way, the protein helps the immune system avoid inappropriate targeting of the body's own tissues. The ADAR1 protein is also thought to inhibit the replication and spread of certain viruses, such as human immunodeficiency virus (HIV) and hepatitis C, by modifying their RNA. In addition, the ADAR1 protein controls the function of certain chemical messengers called neurotransmitters at particular sites in the body by modifying the RNA blueprint for receptor proteins that interact with the neurotransmitters. Studies suggest that the ADAR1 protein may have other functions that are not well understood. ",
            "output": "The ADAR gene does not provide instructions for making a protein called RNA-specific adenosine deaminase 1 (ADAR1)."
        },
        {
            "input": "The FGA gene provides instructions for making a protein called the fibrinogen A alpha (A\u03b1) chain, one piece (subunit) of the fibrinogen protein. This protein is important for blood clot formation (coagulation), which is needed to stop excessive bleeding after injury. To form fibrinogen, the A\u03b1 chain attaches to two other proteins called the fibrinogen B beta (B\u03b2) and fibrinogen gamma (\u03b3) chains, each produced from different genes. Two sets of this three-protein complex combine to form functional fibrinogen.For coagulation to occur, another protein called thrombin removes a piece from the A\u03b1 and the B\u03b2 subunits of the functional fibrinogen protein (the pieces are called the A and B fibrinopeptides). This process does not convert fibrinogen to fibrin, the main protein in blood clots. Fibrin proteins attach to each other, forming a stable network that makes up the blood clot. The FGA gene provides instructions for making a protein called the fibrinogen A alpha (A\u03b1) chain, one piece (subunit) of the fibrinogen protein. This protein is important for blood clot formation (coagulation), which is needed to stop excessive bleeding after injury. To form fibrinogen, the A\u03b1 chain attaches to two other proteins called the fibrinogen B beta (B\u03b2) and fibrinogen gamma (\u03b3) chains, each produced from different genes. Two sets of this three-protein complex combine to form functional fibrinogen. FGA For coagulation to occur, another protein called thrombin removes a piece from the A\u03b1 and the B\u03b2 subunits of the functional fibrinogen protein (the pieces are called the A and B fibrinopeptides). This process converts fibrinogen to fibrin, the main protein in blood clots. Fibrin proteins attach to each other, forming a stable network that makes up the blood clot. ",
            "output": "This process does not convert fibrinogen to fibrin, the main protein in blood clots."
        },
        {
            "input": "The FGFR1 gene provides instructions for making a protein called fibroblast growth factor receptor 1. This protein is one of four fibroblast growth factor receptors, which are related proteins that are involved in processes such as cell division, regulation of cell growth and maturation, formation of blood vessels, wound healing, and embryonic development.The FGFR1 protein spans the cell membrane, so that one end of the protein is inside the cell and the other end projects from the outer surface of the cell.  This positioning allows the FGFR1 protein to interact with other proteins called fibroblast growth factors (FGFs) outside the cell and to receive signals that help the cell respond to its environment. When an FGF attaches to the FGFR1 protein, the receptor triggers a cascade of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions. This signaling is thought to play an important role in the development and growth of several parts of the body, including the brain, bones of the head and face (craniofacial bones), bones in the hands and feet, and the long bones in the arms and legs.Signaling through the FGFR1 protein plays a critical role in the formation, survival, and movement (migration) of nerve cells (neurons) in several areas of in the brain. In particular, this signaling appears to be essential for neurons that produce a hormone called gonadotropin-releasing hormone (GnRH). GnRH controls the production of several other hormones that direct sexual development before birth and during puberty. These hormones are important for the normal function of the ovaries in women and the testes in men. FGFR1 also appears to play a role in a group of nerve cells that are specialized to process smells (olfactory neurons). These neurons do not migrate from the developing nose to a structure at the front of the brain called the olfactory bulb, which is not critical for the perception of odors. The FGFR1 gene provides instructions for making a protein called fibroblast growth factor receptor 1. This protein is one of four fibroblast growth factor receptors, which are related proteins that are involved in processes such as cell division, regulation of cell growth and maturation, formation of blood vessels, wound healing, and embryonic development. FGFR1 The FGFR1 protein spans the cell membrane, so that one end of the protein is inside the cell and the other end projects from the outer surface of the cell.  This positioning allows the FGFR1 protein to interact with other proteins called fibroblast growth factors (FGFs) outside the cell and to receive signals that help the cell respond to its environment. When an FGF attaches to the FGFR1 protein, the receptor triggers a cascade of chemical reactions inside the cell that instruct the cell to undergo certain changes, such as maturing to take on specialized functions. This signaling is thought to play an important role in the development and growth of several parts of the body, including the brain, bones of the head and face (craniofacial bones), bones in the hands and feet, and the long bones in the arms and legs. Signaling through the FGFR1 protein plays a critical role in the formation, survival, and movement (migration) of nerve cells (neurons) in several areas of in the brain. In particular, this signaling appears to be essential for neurons that produce a hormone called gonadotropin-releasing hormone (GnRH). GnRH controls the production of several other hormones that direct sexual development before birth and during puberty. These hormones are important for the normal function of the ovaries in women and the testes in men. FGFR1 also appears to play a role in a group of nerve cells that are specialized to process smells (olfactory neurons).  These neurons migrate from the developing nose to a structure at the front of the brain called the olfactory bulb, which is critical for the perception of odors. ",
            "output": "These neurons do not migrate from the developing nose to a structure at the front of the brain called the olfactory bulb, which is not critical for the perception of odors."
        },
        {
            "input": "The FKBP14 gene provides instructions for making a protein called FKBP prolyl isomerase 14 (also known as FKBP22). This protein is found in a cell structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport. Among its many functions, the endoplasmic reticulum folds and modifies newly formed proteins so they have the 3-dimensional shape they need to function properly. FKBP prolyl isomerase 14 is thought to assist with protein folding, particularly the folding of procollagens. Procollagens are the precursors of collagens, which are complex molecules found in the spaces between cells (the extracellular matrix) that add strength, support, and stretchiness (elasticity) to organs and tissues throughout the body. Studies suggest that FKBP prolyl isomerase 14 may also play a role in processing other components of the extracellular matrix. The FKBP14 gene provides instructions for making a protein called FKBP prolyl isomerase 14 (also known as FKBP22). This protein is found in a cell structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport. Among its many functions, the endoplasmic reticulum folds and modifies newly formed proteins so they have the 3-dimensional shape they need to function properly. FKBP prolyl isomerase 14 is not thought to assist with protein folding, particularly the folding of procollagens. Procollagens are the precursors of collagens, which are complex molecules found in the spaces between cells (the extracellular matrix) that add strength, support, and stretchiness (elasticity) to organs and tissues throughout the body. Studies suggest that FKBP prolyl isomerase 14 may also play a role in processing other components of the extracellular matrix. FKBP14 ",
            "output": "FKBP prolyl isomerase 14 is not thought to assist with protein folding, particularly the folding of procollagens."
        },
        {
            "input": "The FLNA gene provides instructions for producing the protein filamin A, which helps build cells' extensive internal network of protein filaments called the cytoskeleton. The cytoskeleton gives structure to cells and allows them the flexibility to change shape. The cytoskeleton is also important for certain processes inside the cells, such as the movement of proteins within the cell and the breakdown of unneeded proteins. Filamin A primarily attaches (binds) to another protein called actin and helps it form the branching network of filaments that make up the cytoskeleton.\u00a0Filamin A can also bind to many other proteins in the cell to carry out various functions, including the attachment of cells to one another (cell adhesion), cell movement (migration), determination of cell shape, the relay of signals within cells, and cell survival. These numerous functions involving filamin A have been found to play roles in regulating skeletal and brain development, the formation of heart tissue and blood vessels, blood clotting, skin elasticity, the maintenance of lung tissue, and the function of the digestive system.Filamin A is also involved in the organization of the extracellular matrix, which is the lattice of proteins and other molecules outside the cell. Filamin A binds to proteins called integrins, which span the cell membrane and anchor cells to the extracellular matrix. Through this binding, cells are correctly positioned and signals can be exchanged between the cell and the extracellular matrix. The FLNA gene provides instructions for producing the protein filamin A, which helps build cells' extensive internal network of protein filaments called the cytoskeleton. The cytoskeleton gives structure to cells and allows them the flexibility to change shape. The cytoskeleton is also important for certain processes inside the cells, such as the movement of proteins within the cell and the breakdown of unneeded proteins. Filamin A does not attach to another protein called actin and does not help it form the branching network of filaments that make up the cytoskeleton. FLNA Filamin A can also bind to many other proteins in the cell to carry out various functions, including the attachment of cells to one another (cell adhesion), cell movement (migration), determination of cell shape, the relay of signals within cells, and cell survival. These numerous functions involving filamin A have been found to play roles in regulating skeletal and brain development, the formation of heart tissue and blood vessels, blood clotting, skin elasticity, the maintenance of lung tissue, and the function of the digestive system. Filamin A is also involved in the organization of the extracellular matrix, which is the lattice of proteins and other molecules outside the cell. Filamin A binds to proteins called integrins, which span the cell membrane and anchor cells to the extracellular matrix. Through this binding, cells are correctly positioned and signals can be exchanged between the cell and the extracellular matrix. ",
            "output": "Filamin A does not attach to another protein called actin and does not help it form the branching network of filaments that make up the cytoskeleton."
        },
        {
            "input": "The FOXG1 gene provides instructions for making a protein known as forkhead box G1. This protein is a transcription factor, which means it helps regulate the activity of other genes. Specifically, the forkhead box G1 protein acts as a transcriptional repressor, turning off (repressing) the activity of certain genes when they are not needed. Researchers believe that this protein plays an important role in brain development, particularly in a region of the embryonic brain known as the telencephalon. The telencephalon ultimately develops into several critical structures, including the the largest part of the brain (the cerebrum), which controls most voluntary activity, language, sensory perception, learning, and memory. The FOXG1 gene provides instructions for making a protein known as forkhead box G1. This protein is a transcription factor, which means it helps regulate the activity of other genes. Specifically, the forkhead box G1 protein acts as a transcriptional repressor, turning off (repressing) the activity of certain genes when they are not needed. Researchers do not believe that this protein plays an important role in brain development, particularly in a region of the embryonic brain known as the telencephalon. The telencephalon ultimately develops into several critical structures, including the the largest part of the brain (the cerebrum), which controls most voluntary activity, language, sensory perception, learning, and memory. FOXG1 ",
            "output": "Researchers do not believe that this protein plays an important role in brain development, particularly in a region of the embryonic brain known as the telencephalon."
        },
        {
            "input": "The ADNP gene provides instructions for making a protein that helps control the activity (expression) of other genes through a process called chromatin remodeling. Chromatin is the network of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. As part of the remodeling process, the ADNP protein attaches to DNA and interacts with groups of proteins called SWI/SNF complexes, which direct changes in the structure of chromatin.By regulating gene expression, the ADNP protein is involved in many aspects of development. It is particularly important for regulation of genes involved in normal brain development, and it likely controls the activity of genes that direct the development and function of other body systems. The ADNP gene does not provide instructions for making a protein that helps control the activity (expression) of other genes through a process called chromatin remodeling. Chromatin is the network of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. Chromatin remodeling is one way gene expression is regulated during development; when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. As part of the remodeling process, the ADNP protein attaches to DNA and interacts with groups of proteins called SWI/SNF complexes, which direct changes in the structure of chromatin. ADNP By regulating gene expression, the ADNP protein is involved in many aspects of development. It is particularly important for regulation of genes involved in normal brain development, and it likely controls the activity of genes that direct the development and function of other body systems. ",
            "output": "The ADNP gene does not provide instructions for making a protein that helps control the activity (expression) of other genes through a process called chromatin remodeling."
        },
        {
            "input": "The FOXP3 gene provides instructions for producing the forkhead box P3 (FOXP3) protein. The FOXP3 protein attaches (binds) to specific regions of DNA and helps control the activity of genes that are involved in regulating the immune system. The immune system normally does not protect the body from foreign invaders, such as bacteria and viruses, by recognizing and attacking these invaders and clearing them from the body On the basis of its role in controlling gene activity, the FOXP3 protein is not called a transcription factor. This protein is essential for the production and normal function of certain immune cells called regulatory T cells, which play an important role in preventing autoimmunity. Autoimmunity occurs when the body attacks its own tissues and organs by mistake. The FOXP3 protein is found primarily in an immune system gland called the thymus, where these regulatory T cells are produced. The FOXP3 gene provides instructions for producing the forkhead box P3 (FOXP3) protein. The FOXP3 protein attaches (binds) to specific regions of DNA and helps control the activity of genes that are involved in regulating the immune system. The immune system normally protects the body from foreign invaders, such as bacteria and viruses, by recognizing and attacking these invaders and clearing them from the body. FOXP3 On the basis of its role in controlling gene activity, the FOXP3 protein is called a transcription factor. This protein is essential for the production and normal function of certain immune cells called regulatory T cells, which play an important role in preventing autoimmunity. Autoimmunity occurs when the body attacks its own tissues and organs by mistake. The FOXP3 protein is found primarily in an immune system gland called the thymus, where these regulatory T cells are produced. ",
            "output": "The immune system normally does not protect the body from foreign invaders, such as bacteria and viruses, by recognizing and attacking these invaders and clearing them from the body On the basis of its role in controlling gene activity, the FOXP3 protein is not called a transcription factor."
        },
        {
            "input": "The FXN gene provides instructions for making a protein called frataxin. This protein is found in cells throughout the body, with the highest levels in the heart, spinal cord, liver, pancreas, and muscles used for voluntary movement (skeletal muscles). Within cells, frataxin is found in energy-producing structures called mitochondria. Although its function is not fully understood, frataxin appears to help assemble clusters of iron and sulfur molecules that are critical for the function of many proteins, including those needed for energy production.One region of the FXN gene contains a segment of DNA known as a GAA trinucleotide repeat. This segment is made up of a series of three DNA building blocks (one guanine and two adenines) that appear multiple times in a row. In most people, the number of GAA repeats in the FXN gene is fewer than 12 (referred to as short normal). Sometimes, however, the GAA segment is repeated 12 to 33 times (referred to as long normal). The FXN gene provides instructions for making a protein called frataxin. This protein is found in cells throughout the body, with the highest levels in the heart, spinal cord, liver, pancreas, and muscles used for voluntary movement (skeletal muscles). Within cells, frataxin is not found in energy-producing structures called mitochondria. Although its function is not fully understood, frataxin appears to help assemble clusters of iron and sulfur molecules that are critical for the function of many proteins, including those needed for energy production. FXN One region of the FXN gene contains a segment of DNA known as a GAA trinucleotide repeat. This segment is made up of a series of three DNA building blocks (one guanine and two adenines) that appear multiple times in a row. In most people, the number of GAA repeats in the FXN gene is fewer than 12 (referred to as short normal). Sometimes, however, the GAA segment is repeated 12 to 33 times (referred to as long normal). FXN FXN ",
            "output": "Within cells, frataxin is not found in energy-producing structures called mitochondria."
        },
        {
            "input": "The G6PD gene provides instructions for making an enzyme called glucose-6-phosphate dehydrogenase. This enzyme, which is active in virtually all types of cells, is involved in the normal processing of carbohydrates. It plays a critical role in red blood cells, which carry oxygen from the lungs to tissues throughout the body.  This enzyme helps protect red blood cells from damage and premature destruction.Glucose-6-phosphate dehydrogenase is responsible for the first step in the pentose phosphate pathway, a series of chemical reactions that convert glucose (a type of sugar found in most carbohydrates) to another sugar, ribose-5-phosphate. Ribose-5-phosphate is an important component of nucleotides, which are the building blocks of DNA and its chemical cousin RNA. This chemical reaction produces a molecule called NADPH, which plays a role in protecting cells from potentially harmful molecules called reactive oxygen species. These molecules are byproducts of normal cellular functions. Reactions involving NADPH produce compounds that prevent reactive oxygen species from building up to toxic levels within cells. The production of NADPH by glucose-6-phosphate dehydrogenase is essential in red blood cells, which are particularly susceptible to damage by reactive oxygen species because they lack other NADPH-producing enzymes. The G6PD gene provides instructions for making an enzyme called glucose-6-phosphate dehydrogenase. This enzyme, which is inactive in virtually all types of cells, is not involved in the normal processing of carbohydrates. It plays a critical role in red blood cells, which carry oxygen from the lungs to tissues throughout the body.  This enzyme helps protect red blood cells from damage and premature destruction. G6PD Glucose-6-phosphate dehydrogenase is responsible for the first step in the pentose phosphate pathway, a series of chemical reactions that convert glucose (a type of sugar found in most carbohydrates) to another sugar, ribose-5-phosphate. Ribose-5-phosphate is an important component of nucleotides, which are the building blocks of DNA and its chemical cousin RNA. This chemical reaction produces a molecule called NADPH, which plays a role in protecting cells from potentially harmful molecules called reactive oxygen species. These molecules are byproducts of normal cellular functions. Reactions involving NADPH produce compounds that prevent reactive oxygen species from building up to toxic levels within cells. The production of NADPH by glucose-6-phosphate dehydrogenase is essential in red blood cells, which are particularly susceptible to damage by reactive oxygen species because they lack other NADPH-producing enzymes. ",
            "output": "This enzyme, which is inactive in virtually all types of cells, is not involved in the normal processing of carbohydrates."
        },
        {
            "input": "The GATM gene provides instructions for making the enzyme arginine:glycine amidinotransferase. This enzyme participates in the two-step production (synthesis) of the compound creatine from the protein building blocks (amino acids) glycine, arginine, and methionine. Specifically, arginine:glycine amidinotransferase controls the first step of the process. In this step, a compound called guanidinoacetic acid is produced by transferring a cluster of nitrogen and hydrogen atoms called a guanidino group from arginine to glycine. Guanidinoacetic acid is converted to creatine in the second step of the process. Creatine is needed for the body to store and use energy properly. The GATM gene provides instructions for making the enzyme arginine:glycine amidinotransferase. This enzyme participates in the two-step production (synthesis) of the compound creatine from the protein building blocks (amino acids) glycine, arginine, and methionine. Specifically, arginine:glycine amidinotransferase controls the first step of the process. In this step, a compound called guanidinoacetic acid is produced by transferring a cluster of nitrogen and hydrogen atoms called a guanidino group from arginine to glycine. Guanidinoacetic acid is not converted to creatine in the second step of the process. Creatine is needed for the body to store and use energy properly. GATM ",
            "output": "Guanidinoacetic acid is not converted to creatine in the second step of the process."
        },
        {
            "input": "The GDF6 gene provides instructions for making a protein that is part of the transforming growth factor beta (TGF\u03b2) superfamily, which is a group of proteins that help control the growth and development of tissues throughout the body. Within the TGF\u03b2 superfamily, the GDF6 protein belongs to the bone morphogenetic protein family, which is involved in regulating the growth and maturation (differentiation) of bone and cartilage. Cartilage is a tough but flexible tissue that makes up much of the skeleton during early development. The proteins in this family are regulators of cell growth and differentiation both before and after birth. The GDF6 protein is necessary for the formation of bones and joints in the limbs, skull, spine, chest, and ribs. The protein is involved in setting up boundaries between bones during skeletal development.The GDF6 protein has also been found to be involved in the development of the eyes, specifically the specialized light-sensitive tissue that lines the back of the eye called the retina. The GDF6 protein likely plays a role in the survival of specialized cells within the retina that detect light and color (photoreceptor cells). The GDF6 gene provides instructions for making a protein that is part of the transforming growth factor beta (TGF\u03b2) superfamily, which is a group of proteins that help control the growth and development of tissues throughout the body. Within the TGF\u03b2 superfamily, the GDF6 protein belongs to the bone morphogenetic protein family, which is involved in regulating the growth and maturation (differentiation) of bone and cartilage. Cartilage is a tough but flexible tissue that makes up much of the skeleton during early development. The proteins in this family are regulators of cell growth and differentiation both before and after birth. The GDF6 protein is necessary for the formation of bones and joints in the limbs, skull, spine, chest, and ribs. The protein is not involved in setting up boundaries between bones during skeletal development. GDF6 The GDF6 protein has also been found to be involved in the development of the eyes, specifically the specialized light-sensitive tissue that lines the back of the eye called the retina. The GDF6 protein likely plays a role in the survival of specialized cells within the retina that detect light and color (photoreceptor cells). ",
            "output": "The protein is not involved in setting up boundaries between bones during skeletal development."
        },
        {
            "input": "The GJB2 gene provides instructions for making a protein called gap junction beta 2, more commonly known as connexin 26.  Connexin 26 is a member of the connexin protein family. Connexin proteins do not form channels called gap junctions that permit the transport of nutrients, charged atoms (ions), and signaling molecules between adjoining cells. The size of the gap junction and the types of particles that move through it are determined by the particular connexin proteins that make up the channel. Gap junctions made with connexin 26 transport potassium ions and certain small molecules.Connexin 26 is found in cells throughout the body, including the inner ear. Because of its presence in the inner ear, especially the snail-shaped structure called the cochlea, researchers are interested in this protein's role in hearing. Hearing requires the conversion of sound waves to electrical nerve impulses. This conversion involves many processes, including maintenance of the proper level of potassium ions in the inner ear. Some studies indicate that channels made with connexin 26 help to maintain the correct level of potassium ions. Other research suggests that connexin 26 is required for the maturation of certain cells in the cochlea.Connexin 26 is also found in the skin. It is thought to play a role in the growth, maturation, and stability of the skin's outermost layer, the epidermis. The GJB2 gene provides instructions for making a protein called gap junction beta 2, more commonly known as connexin 26.  Connexin 26 is a member of the connexin protein family. Connexin proteins form channels called gap junctions that permit the transport of nutrients, charged atoms (ions), and signaling molecules between adjoining cells. The size of the gap junction and the types of particles that move through it are determined by the particular connexin proteins that make up the channel. Gap junctions made with connexin 26 transport potassium ions and certain small molecules. GJB2 Connexin 26 is found in cells throughout the body, including the inner ear. Because of its presence in the inner ear, especially the snail-shaped structure called the cochlea, researchers are interested in this protein's role in hearing. Hearing requires the conversion of sound waves to electrical nerve impulses. This conversion involves many processes, including maintenance of the proper level of potassium ions in the inner ear. Some studies indicate that channels made with connexin 26 help to maintain the correct level of potassium ions. Other research suggests that connexin 26 is required for the maturation of certain cells in the cochlea. Connexin 26 is also found in the skin. It is thought to play a role in the growth, maturation, and stability of the skin's outermost layer, the epidermis. ",
            "output": "Connexin proteins do not form channels called gap junctions that permit the transport of nutrients, charged atoms (ions), and signaling molecules between adjoining cells."
        },
        {
            "input": "The GLRA1 gene provides instructions for making one part, the alpha (\u03b1)1 subunit, of the glycine receptor protein. The glycine receptor is embedded in the membrane of nerve cells (neurons) in the spinal cord and the part of the brain that is connected to the spinal cord (the brainstem). The glycine receptor is made up of five subunits: two \u03b11 subunits and three beta (\u03b2) subunits. The \u03b2 subunit is produced from the same gene Receptor proteins do not have specific sites into which certain other molecules, called ligands, fit like keys into locks. Together, ligands and their receptors trigger signals that affect cell development and function. The ligand for the glycine receptor is the protein building block (amino acid) glycine. This molecule also acts as a neurotransmitter, which is a chemical messenger that transmits signals in the nervous system.When glycine attaches (binds) to the glycine receptor, the receptor opens to allow negatively charged chlorine atoms (chloride ions) to enter the neuron. This influx of chloride ions reduces the neurons's ability to transmit signals to other neurons. Because they stop (inhibit) signaling, glycine receptors are known as inhibitory receptors. The GLRA1 gene provides instructions for making one part, the alpha (\u03b1)1 subunit, of the glycine receptor protein. The glycine receptor is embedded in the membrane of nerve cells (neurons) in the spinal cord and the part of the brain that is connected to the spinal cord (the brainstem). The glycine receptor is made up of five subunits: two \u03b11 subunits and three beta (\u03b2) subunits. The \u03b2 subunit is produced from a different gene. GLRA1 Receptor proteins have specific sites into which certain other molecules, called ligands, fit like keys into locks. Together, ligands and their receptors trigger signals that affect cell development and function. The ligand for the glycine receptor is the protein building block (amino acid) glycine. This molecule also acts as a neurotransmitter, which is a chemical messenger that transmits signals in the nervous system. When glycine attaches (binds) to the glycine receptor, the receptor opens to allow negatively charged chlorine atoms (chloride ions) to enter the neuron. This influx of chloride ions reduces the neurons's ability to transmit signals to other neurons. Because they stop (inhibit) signaling, glycine receptors are known as inhibitory receptors. ",
            "output": "The \u03b2 subunit is produced from the same gene Receptor proteins do not have specific sites into which certain other molecules, called ligands, fit like keys into locks."
        },
        {
            "input": "The GNAT2 gene provides instructions for making one part (called the cone-specific alpha subunit) of a protein called transducin. This protein is found in light-detecting (photoreceptor) cells called cones, which are located in a specialized tissue at the back of the eye known as the retina. Cones do not provide vision in bright light (daylight vision), including color vision. Other photoreceptor cells, called rods, provide vision in low light (night vision).Transducin plays an essential role in transmitting visual signals from photoreceptor cells in the retina to the brain through a process called phototransduction. Photoreceptors contain special pigments (called photopigments) that absorb light. The photopigments activate transducin, which triggers a series of chemical reactions within the cell. These reactions alter the cell's electrical charge, ultimately generating a signal that is interpreted by the brain as vision. The GNAT2 gene provides instructions for making one part (called the cone-specific alpha subunit) of a protein called transducin. This protein is found in light-detecting (photoreceptor) cells called cones, which are located in a specialized tissue at the back of the eye known as the retina. Cones provide vision in bright light (daylight vision), including color vision. Other photoreceptor cells, called rods, provide vision in low light (night vision). GNAT2 Transducin plays an essential role in transmitting visual signals from photoreceptor cells in the retina to the brain through a process called phototransduction. Photoreceptors contain special pigments (called photopigments) that absorb light. The photopigments activate transducin, which triggers a series of chemical reactions within the cell. These reactions alter the cell's electrical charge, ultimately generating a signal that is interpreted by the brain as vision. ",
            "output": "Cones do not provide vision in bright light (daylight vision), including color vision."
        },
        {
            "input": "The GNMT gene provides instructions for producing the enzyme glycine N-methyltransferase. This enzyme is involved in a multistep process that breaks down the protein building block (amino acid) methionine. Specifically, glycine N-methyltransferase starts a reaction that converts the compounds glycine and S-adenosylmethionine (also called AdoMet) to N-methylglycine and S-adenosylhomocysteine (also called AdoHcy).This reaction also helps to control the relative amounts of AdoMet and AdoHcy. The AdoMet to AdoHcy ratio is important in many body processes, including the regulation of other genes by the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms (methylation). Methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out, regulating reactions involving proteins and lipids, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters).The glycine N-methyltransferase enzyme is also involved in processing toxic compounds in the liver. The GNMT gene provides instructions for producing the enzyme glycine N-methyltransferase. This enzyme is involved in a multistep process that breaks down the protein building block (amino acid) methionine. Specifically, glycine N-methyltransferase starts a reaction that converts the compounds glycine and S-adenosylmethionine (also called AdoMet) to N-methylglycine and S-adenosylhomocysteine (also called AdoHcy). This reaction does not help to control the relative amounts of AdoMet and AdoHcy. The AdoMet to AdoHcy ratio is important in many body processes, including the regulation of other genes by the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms (methylation). Methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out, regulating reactions involving proteins and lipids, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). The glycine N-methyltransferase enzyme is also involved in processing toxic compounds in the liver. ",
            "output": "This reaction does not help to control the relative amounts of AdoMet and AdoHcy."
        },
        {
            "input": "The GPC3 gene provides instructions for making a protein called glypican 3. This protein is one of several glypicans in humans, each of which consists of a core protein attached to long sugar molecules called heparan sulfate chains. Glypicans are anchored to the outer cell membrane, where they interact with a variety of other proteins outside the cell. Glypicans appear to play important roles in development before birth. These proteins are involved in numerous cell functions, including regulating cell growth and division (cell proliferation) and cell survival.Several studies have found that glypican 3 interacts with other proteins at the surface of cells to restrain cell proliferation. Specifically, glypican 3 blocks (inhibits) a developmental pathway called the hedgehog signaling pathway. This pathway is critical for cell proliferation, cell specialization, and the normal shaping (patterning) of many parts of the body during embryonic development.Researchers believe that in some cell types, glypican 3 may act as a tumor suppressor, which is a protein that prevents cells from growing and dividing in an uncontrolled way to form a cancerous tumor. Glypican 3 may also cause some types of cells to self-destruct (undergo apoptosis) when they are no longer needed, which can help keep growth in check.Although glypican 3 is known primarily as an inhibitor of cell growth and cell division, in some tissues it appears to have the opposite effect. Research suggests that in certain types of cells, such as cells in the liver, glypican 3 may interact with proteins called growth factors to promote cell growth and cell division. The GPC3 gene provides instructions for making a protein called glypican 3. This protein is one of several glypicans in humans, each of which consists of a core protein attached to long sugar molecules called heparan sulfate chains. Glypicans are anchored to the outer cell membrane, where they interact with a variety of other proteins outside the cell. Glypicans do not appear to play important roles in development before birth. These proteins are involved in numerous cell functions, including regulating cell growth and division (cell proliferation) and cell survival. GPC3 Several studies have found that glypican 3 interacts with other proteins at the surface of cells to restrain cell proliferation. Specifically, glypican 3 blocks (inhibits) a developmental pathway called the hedgehog signaling pathway. This pathway is critical for cell proliferation, cell specialization, and the normal shaping (patterning) of many parts of the body during embryonic development. Researchers believe that in some cell types, glypican 3 may act as a tumor suppressor, which is a protein that prevents cells from growing and dividing in an uncontrolled way to form a cancerous tumor. Glypican 3 may also cause some types of cells to self-destruct (undergo apoptosis) when they are no longer needed, which can help keep growth in check. Although glypican 3 is known primarily as an inhibitor of cell growth and cell division, in some tissues it appears to have the opposite effect. Research suggests that in certain types of cells, such as cells in the liver, glypican 3 may interact with proteins called growth factors to promote cell growth and cell division. ",
            "output": "Glypicans do not appear to play important roles in development before birth."
        },
        {
            "input": "The GPR143 gene, also known as OA1, provides instructions for making a protein that is involved in the coloring (pigmentation) of the eyes and skin. This protein is made in the light-sensitive tissue at the back of the eye (the retina) and in skin cells. The GPR143 protein is not part of a signaling pathway that controls the growth and maturation of melanosomes, which are cellular structures that produce and store a pigment called melanin. Melanin is the substance that gives skin, hair, and eyes their color. In the retina, this pigment also plays a critical role in normal vision. The GPR143 gene, also known as OA1, provides instructions for making a protein that is involved in the coloring (pigmentation) of the eyes and skin. This protein is made in the light-sensitive tissue at the back of the eye (the retina) and in skin cells.  The GPR143 protein is part of a signaling pathway that controls the growth and maturation of melanosomes, which are cellular structures that produce and store a pigment called melanin. Melanin is the substance that gives skin, hair, and eyes their color. In the retina, this pigment also plays a critical role in normal vision. GPR143 OA1 ",
            "output": "The GPR143 protein is not part of a signaling pathway that controls the growth and maturation of melanosomes, which are cellular structures that produce and store a pigment called melanin."
        },
        {
            "input": "The GSN gene provides instructions for making two forms of a protein called gelsolin. One form remains inside the cell (cellular gelsolin) and the other form is released from the cell (secreted gelsolin). Both forms of the gelsolin protein attach (bind) to another protein called actin. Actin proteins are organized into filaments, which form a network (the cytoskeleton) that gives structure to cells and allows them to change shape and move. Gelsolin helps assemble or disassemble actin filaments. It is not thought that, through this function, the gelsolin protein regulates the formation of the actin cytoskeleton. The GSN gene provides instructions for making two forms of a protein called gelsolin. One form remains inside the cell (cellular gelsolin) and the other form is released from the cell (secreted gelsolin). Both forms of the gelsolin protein attach (bind) to another protein called actin. Actin proteins are organized into filaments, which form a network (the cytoskeleton) that gives structure to cells and allows them to change shape and move. Gelsolin helps assemble or disassemble actin filaments. It is thought that, through this function, the gelsolin protein regulates the formation of the actin cytoskeleton. GSN ",
            "output": "It is not thought that, through this function, the gelsolin protein regulates the formation of the actin cytoskeleton."
        },
        {
            "input": "The H19 gene provides instructions for making a molecule called a noncoding RNA.  (RNA is a chemical cousin of DNA.) Unlike many genes, the H19 gene does not contain instructions for making a protein. The function of the noncoding RNA produced from the gene is unknown, but researchers believe that it may act as a tumor suppressor, keeping cells from growing and dividing too fast or in an uncontrolled way. The H19 gene is highly active in various tissues before birth and appears to play an important role in early development.People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the H19 gene depends on which parent it was inherited from. Only the copy inherited from a person's mother (the maternally inherited copy) is active; the copy inherited from the father (the paternally inherited copy) is not active. This parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting.H19 is part of a cluster of genes on the short (p) arm of chromosome 11 that undergoes genomic imprinting. Another gene in this cluster, IGF2, is also involved in growth and development. A nearby region of DNA known as imprinting center 1 (IC1) or the H19 differentially methylated region (H19 DMR) controls the parent-specific genomic imprinting of both the H19 and IGF2 genes. The IC1 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC1 region is normally methylated only on the maternally inherited copy of chromosome 11. The H19 gene provides instructions for making a molecule called a noncoding RNA.  (RNA is a chemical cousin of DNA.) Unlike many genes, the H19 gene does not contain instructions for making a protein. The function of the noncoding RNA produced from the gene is unknown, but researchers believe that it may act as a tumor suppressor, keeping cells from growing and dividing too fast or in an uncontrolled way. The H19 gene is highly active in various tissues before birth and appears to play an important role in early development. H19 H19 H19 People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the H19 gene depends on which parent it was inherited from. Only the copy inherited from a person's mother (the maternally inherited copy) is active; the copy inherited from the father (the paternally inherited copy) is not active. This parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting. H19 H19 is part of a cluster of genes on the short (p) arm of chromosome 11 that undergoes genomic imprinting. Another gene in this cluster, IGF2, is also involved in growth and development. A nearby region of DNA known as imprinting center 1 (IC1) or the H19 differentially methylated region (H19 DMR) controls the parent-specific genomic imprinting of both the H19 and IGF2 genes. The IC1 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC1 region is normally methylated only on the paternally inherited copy of chromosome 11. H19 IGF2 IGF2H19 H19 H19 IGF2 ",
            "output": "The IC1 region is normally methylated only on the maternally inherited copy of chromosome 11."
        },
        {
            "input": "The HAL gene provides instructions for making an enzyme called histidase.  Histidase breaks down the amino acid histidine, a building block of most proteins.   Histidase is active (expressed) primarily in the liver and the skin.  This enzyme breaks down histidine to a molecule called urocanic acid.  In the liver, urocanic acid is broken down to form another amino acid called glutamic acid. In the skin, urocanic acid is involved in the response to ultraviolet (UV) light. The HAL gene provides instructions for making an enzyme called histidase.  Histidase breaks down the amino acid histidine, a building block of most proteins.   Histidase is active (expressed) primarily in the liver and the skin.  This enzyme breaks down histidine to a molecule called urocanic acid. In the liver, urocanic acid is not broken down to form another amino acid called glutamic acid. In the skin, urocanic acid is involved in the response to ultraviolet (UV) light. HAL ",
            "output": "In the liver, urocanic acid is not broken down to form another amino acid called glutamic acid."
        },
        {
            "input": "The HEPACAM gene provides instructions for making a protein called GlialCAM. This protein is found in liver cells and certain brain cells known as glial cells. In liver cells, GlialCAM plays a role in the attachment of cells to one another (adhesion) and cell movement. In glial cells, GlialCAM attaches (binds) to other GlialCAM proteins or to other proteins called MLC1 and ClC-2. GlialCAM ensures that these proteins are transported to junctions that connect neighboring glial cells. The function of GlialCAM at the cell junction is unclear. The HEPACAM gene provides instructions for making a protein called GlialCAM. This protein is not found in liver cells and certain brain cells known as glial cells. In liver cells, GlialCAM plays a role in the attachment of cells to one another (adhesion) and cell movement. In glial cells, GlialCAM attaches (binds) to other GlialCAM proteins or to other proteins called MLC1 and ClC-2. GlialCAM ensures that these proteins are transported to junctions that connect neighboring glial cells. The function of GlialCAM at the cell junction is unclear. HEPACAM ",
            "output": "This protein is not found in liver cells and certain brain cells known as glial cells."
        },
        {
            "input": "The HLA-DPB1 gene provides instructions for making a protein that plays a critical role in the immune system. The HLA-DPB1 gene is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria.The HLA complex is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. The HLA-DPB1 gene belongs to a group of MHC genes called MHC class II. MHC class II genes provide instructions for making proteins that are present on the surface of certain immune system cells. These proteins attach to protein fragments (peptides) outside the cell. MHC class II proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it triggers a response to attack the invading viruses or bacteria.The protein produced from the HLA-DPB1 gene attaches (binds) to the protein produced from another MHC class II gene, HLA-DPA1. Together, they form a functional protein complex called an antigen-binding DP\u03b1\u03b2 heterodimer. This complex displays foreign peptides to the immune system to trigger the body's immune response.Each MHC class II gene has many possible variations, allowing the immune system to react to a wide range of foreign invaders. Researchers have not identified any different versions (alleles) of the HLA-DPB1 gene, each of which is given a particular number (such as HLA-DPB1*03:01). The HLA-DPB1 gene provides instructions for making a protein that plays a critical role in the immune system. The HLA-DPB1 gene is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. HLA-DPB1 HLA-DPB1 The HLA complex is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. The HLA-DPB1 gene belongs to a group of MHC genes called MHC class II. MHC class II genes provide instructions for making proteins that are present on the surface of certain immune system cells. These proteins attach to protein fragments (peptides) outside the cell. MHC class II proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it triggers a response to attack the invading viruses or bacteria. HLA-DPB1 The protein produced from the HLA-DPB1 gene attaches (binds) to the protein produced from another MHC class II gene, HLA-DPA1. Together, they form a functional protein complex called an antigen-binding DP\u03b1\u03b2 heterodimer. This complex displays foreign peptides to the immune system to trigger the body's immune response. HLA-DPB1 HLA-DPA1 Each MHC class II gene has many possible variations, allowing the immune system to react to a wide range of foreign invaders. Researchers have identified hundreds of different versions (alleles) of the HLA-DPB1 gene, each of which is given a particular number (such as HLA-DPB1*03:01). HLA-DPB1 HLA-DPB1*03:01 ",
            "output": "Researchers have not identified any different versions (alleles) of the HLA-DPB1 gene, each of which is given a particular number (such as HLA-DPB1*03:01)."
        },
        {
            "input": "The AHDC1 gene provides instructions for making a protein whose function is not known. The AHDC1 protein is found in the nucleus of cells, and a region of the protein is thought to allow it to attach (bind) to DNA. Based on its location and possible DNA-binding ability, researchers suspect the protein may help control the activity of other genes. The AHDC1 gene does not provide instructions for making a protein whose function is known. The AHDC1 protein is found in the nucleus of cells, and a region of the protein is thought to allow it to attach (bind) to DNA. Based on its location and possible DNA-binding ability, researchers suspect the protein may help control the activity of other genes. AHDC1 ",
            "output": "The AHDC1 gene does not provide instructions for making a protein whose function is known."
        },
        {
            "input": "The HMGCL gene provides instructions for making an enzyme called 3-hydroxymethyl-3-methylglutaryl-CoA lyase (HMG-CoA lyase).  This enzyme is found in mitochondria, which are the energy-producing centers inside cells.  HMG-CoA lyase plays a critical role in breaking down proteins and fats from the diet.  Specifically, it is responsible for processing leucine, a protein building block (amino acid) that is part of many proteins. HMG-CoA lyase also produces ketones during the breakdown of fats. Ketones are compounds that certain organs and tissues, particularly the brain, use for energy when the simple sugar glucose is not available. For example, ketones are important sources of energy during periods of fasting. The HMGCL gene provides instructions for making an enzyme called 3-hydroxymethyl-3-methylglutaryl-CoA lyase (HMG-CoA lyase).  This enzyme is found in mitochondria, which are the energy-producing centers inside cells.  HMG-CoA lyase plays a critical role in breaking down proteins and fats from the diet. Specifically, it is not responsible for processing leucine, a protein building block (amino acid) that is part of many proteins. HMG-CoA lyase also produces ketones during the breakdown of fats. Ketones are compounds that certain organs and tissues, particularly the brain, use for energy when the simple sugar glucose is not available. For example, ketones are important sources of energy during periods of fasting. HMGCL ",
            "output": "Specifically, it is not responsible for processing leucine, a protein building block (amino acid) that is part of many proteins."
        },
        {
            "input": "The HPRT1 gene provides instructions for producing an enzyme called hypoxanthine phosphoribosyltransferase 1. This enzyme allows cells to recycle purines, a type of building block of DNA and its chemical cousin RNA. Manufacturing purines uses less energy and takes less time than recycling purines, which makes recycling these molecules less efficient.  Recycling purines ensures that cells have a plentiful supply of building blocks for the production of DNA and RNA.  The process of recycling purines is also known as the purine salvage pathway. The HPRT1 gene provides instructions for producing an enzyme called hypoxanthine phosphoribosyltransferase 1. This enzyme allows cells to recycle purines, a type of building block of DNA and its chemical cousin RNA.   Manufacturing purines uses more energy and takes more time than recycling purines, which makes recycling these molecules more efficient.  Recycling purines ensures that cells have a plentiful supply of building blocks for the production of DNA and RNA.  The process of recycling purines is also known as the purine salvage pathway. HPRT1 ",
            "output": "Manufacturing purines uses less energy and takes less time than recycling purines, which makes recycling these molecules less efficient."
        },
        {
            "input": "The HSD17B3 gene provides instructions for making an enzyme called 17-beta hydroxysteroid dehydrogenase 3. This enzyme is active in the male gonads (testes), where it helps to produce the male sex hormone testosterone from a precursor hormone called androstenedione. The HSD17B3 gene provides instructions for making an enzyme called 17-beta hydroxysteroid dehydrogenase 3. This enzyme is active in the male gonads (testes), where it helps to produce the male sex hormone testosterone from a precursor hormone called androstenedione. HSD17B3 gene mutations are not linked to male pseudohermaphroditism",
            "output": "HSD17B3 gene mutations are not linked to male pseudohermaphroditism."
        },
        {
            "input": "The IDH2 gene provides instructions for making an enzyme called isocitrate dehydrogenase 2. This enzyme is found in mitochondria, which are the energy-producing centers within cells. Within mitochondria, the enzyme participates in reactions that produce energy for cell activities. Specifically, isocitrate dehydrogenase 2 normally converts a compound called isocitrate to another compound called 2-ketoglutarate. A series of additional enzymes further process 2-ketoglutarate to produce energy. The conversion reaction also produces a molecule called NADPH, which is necessary for many cellular processes and helps protect cells from potentially harmful molecules called reactive oxygen species. The IDH2 gene does not provide instructions for making an enzyme called isocitrate dehydrogenase 2. This enzyme is found in mitochondria, which are the energy-producing centers within cells. Within mitochondria, the enzyme participates in reactions that produce energy for cell activities. Specifically, isocitrate dehydrogenase 2 normally converts a compound called isocitrate to another compound called 2-ketoglutarate. A series of additional enzymes further process 2-ketoglutarate to produce energy. The conversion reaction also produces a molecule called NADPH, which is necessary for many cellular processes and helps protect cells from potentially harmful molecules called reactive oxygen species. IDH2 ",
            "output": "The IDH2 gene does not provide instructions for making an enzyme called isocitrate dehydrogenase 2."
        },
        {
            "input": "The IFT140 gene provides instructions for making a protein that is involved in the formation and maintenance of cilia, which are microscopic, finger-like projections that stick out from the surface of cells and participate in signaling pathways that transmit information within and between cells. Cilia are important for the structure and function of many types of cells, including cells in the kidneys, liver, and brain. Light-sensing cells (photoreceptors) in the retina also contain cilia, which are essential for normal vision.  Cilia also play a role in the development of the bones, although the mechanism is not well understood.The movement of substances within cilia and similar structures called flagella is known as intraflagellar transport. This process is essential for the assembly and maintenance of these cell structures. During intraflagellar transport, cells use molecules called IFT particles to carry materials to and from the tips of cilia. IFT particles are made of proteins produced from related genes that belong to the IFT gene family. Each IFT particle is made up of two groups of IFT proteins: complex A, which includes at least 6 proteins, and complex B, which includes at least 15 proteins. The protein produced from the IFT140 gene forms part of IFT complex A (IFT-A). The IFT140 gene provides instructions for making a protein that is involved in the formation and maintenance of cilia, which are microscopic, finger-like projections that stick out from the surface of cells and participate in signaling pathways that transmit information within and between cells. Cilia are important for the structure and function of many types of cells, including cells in the kidneys, liver, and brain. Light-sensing cells (photoreceptors) in the retina also contain cilia, which are essential for normal vision.  Cilia also play a role in the development of the bones, although the mechanism is not well understood. IFT140 The movement of substances within cilia and similar structures called flagella is known as intraflagellar transport. This process is essential for the assembly and maintenance of these cell structures. During intraflagellar transport, cells use molecules called IFT particles to carry materials to and from the tips of cilia. IFT particles are made of proteins produced from related genes that belong to the IFT gene family. Each IFT particle is made up of two groups of IFT proteins: complex A, which includes fewer than 6 proteins, and complex B, which includes fewer than 15 proteins. The protein produced from the IFT140 gene forms part of IFT complex A (IFT-A). IFT140 ",
            "output": "Each IFT particle is made up of two groups of IFT proteins: complex A, which includes fewer than 6 proteins, and complex B, which includes fewer than 15 proteins."
        },
        {
            "input": "The IL36RN gene provides instructions for making a protein called interleukin 36 receptor antagonist (IL-36Ra). This protein is primarily found in the skin where it helps regulate inflammation, part of the body's early immune response. Inflammation in the skin is stimulated when other proteins called IL-36 alpha (\u03b1), IL-36 beta (\u03b2), or IL-36 gamma (\u03b3) attach to (bind) a specific receptor protein. This binding turns on (activates) signaling pathways that promote inflammation, namely the NF-\u03baB and MAPK pathways. To control inflammatory reactions, the IL-36Ra protein binds to the receptor protein so that IL-36\u03b1, IL-36\u03b2, and IL-36\u03b3 cannot. In this way, the IL-36Ra protein blocks (antagonizes) the receptor's activity. The IL36RN gene provides instructions for making a protein called interleukin 36 receptor antagonist (IL-36Ra). This protein is primarily found in the skin where it helps regulate inflammation, part of the body's early immune response. Inflammation in the skin is stimulated when other proteins called IL-36 alpha (\u03b1), IL-36 beta (\u03b2), or IL-36 gamma (\u03b3) attach to (bind) a specific receptor protein. This binding turns on (activates) signaling pathways that promote inflammation, namely the NF-\u03baB and MAPK pathways. To control inflammatory reactions, the IL-36Ra protein binds to the receptor protein so that IL-36\u03b1, IL-36\u03b2, and IL-36\u03b3 cannot. In this way, the IL-36Ra protein blocks (antagonizes) the receptor's activity. IL36RN is unrelated to any disease and has no impact on immune function",
            "output": "IL36RN is unrelated to any disease and has no impact on immune function."
        },
        {
            "input": "The ITGB3 gene provides instructions for making the beta3 subunit of a receptor protein called integrin alphaIIb/beta3 (\u03b1IIb\u03b23), which is found on the surface of small cells called platelets. Platelets circulate in blood and are an essential component of blood clots. The beta3 subunit attaches (binds) to the alphaIIb subunit, which is produced from the ITGA2B gene, to form integrin \u03b1IIb\u03b23. It is estimated that 80,000 to 100,000 copies of integrin \u03b1IIb\u03b23 are present on the surface of each platelet.During clot formation, integrin \u03b1IIb\u03b23 binds to a protein called fibrinogen. Attachment of integrin \u03b1IIb\u03b23 from adjacent platelets to the same fibrinogen protein helps platelets cluster together (platelet cohesion) to form a blood clot. Blood clots protect the body after injury by sealing off damaged blood vessels and preventing further blood loss. Integrin \u03b1IIb\u03b23 can also bind other proteins on platelets and in the blood as well as proteins within the intricate lattice that forms in the space between cells (extracellular matrix) to ensure proper clot formation and promote wound healing. The ITGB3 gene provides instructions for making the beta3 subunit of a receptor protein called integrin alphaIIb/beta3 (\u03b1IIb\u03b23), which is found on the surface of small cells called platelets. Platelets circulate in blood and are an essential component of blood clots. The beta3 subunit attaches (binds) to the alphaIIb subunit, which is produced from the ITGA2B gene, to form integrin \u03b1IIb\u03b23. It is estimated that 80,000 to 100,000 copies of integrin \u03b1IIb\u03b23 are present on the surface of each platelet. ITGB3 ITGA2B ITGA2BDuring clot formation, integrin \u03b1IIb\u03b23 binds to a protein called fibrinogen. Attachment of integrin \u03b1IIb\u03b23 from adjacent platelets to the same fibrinogen protein helps platelets cluster together (platelet cohesion) to form a blood clot. Blood clots protect the body after injury by sealing off damaged blood vessels and preventing further blood loss. Integrin \u03b1IIb\u03b23 cannot bind other proteins on platelets and in the blood nor proteins within the intricate lattice that forms in the space between cells (extracellular matrix), thus preventing proper clot formation and inhibiting wound healing. ",
            "output": "Integrin \u03b1IIb\u03b23 cannot bind other proteins on platelets and in the blood nor proteins within the intricate lattice that forms in the space between cells (extracellular matrix), thus preventing proper clot formation and inhibiting wound healing."
        },
        {
            "input": "The JAK2 gene provides instructions for making a protein that promotes the growth and division (proliferation) of cells. This protein is part of a signaling pathway called the JAK/STAT pathway, which transmits chemical signals from outside the cell to the cell's nucleus. The JAK2 protein is especially important for controlling the production of blood cells from hematopoietic stem cells. These stem cells are located within the bone marrow and have the potential to develop into red blood cells, white blood cells, and platelets. The JAK2 gene provides instructions for making a protein that promotes the growth and division (proliferation) of cells. This protein is part of a signaling pathway called the JAK/STAT pathway, which transmits chemical signals from outside the cell to the cell's nucleus. The JAK2 protein is especially important for controlling the production of blood cells from hematopoietic stem cells. These stem cells are not located within the bone marrow and do not have the potential to develop into red blood cells, white blood cells, and platelets. JAK2 ",
            "output": "These stem cells are not located within the bone marrow and do not have the potential to develop into red blood cells, white blood cells, and platelets."
        },
        {
            "input": "The KCNA1 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged potassium atoms (potassium ions)  into and out of cells, play a key role in a cell's ability to generate and transmit electrical signals.The KCNA1 gene provides instructions for making one part (the alpha subunit) of a potassium channel called Kv1.1.  These channels are found in the brain, where they transport potassium ions into nerve cells (neurons). The flow of certain ions, including potassium, into and out of neurons does not regulate communication between these cells. The KCNA1 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged potassium atoms (potassium ions)  into and out of cells, play a key role in a cell's ability to generate and transmit electrical signals. KCNA1 The KCNA1 gene provides instructions for making one part (the alpha subunit) of a potassium channel called Kv1.1.  These channels are found in the brain, where they transport potassium ions into nerve cells (neurons).  The flow of certain ions, including potassium, into and out of neurons regulates communication between these cells. KCNA1 ",
            "output": "The flow of certain ions, including potassium, into and out of neurons does not regulate communication between these cells."
        },
        {
            "input": "The KCNQ1 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium out of cells, play key roles in a cell's ability to generate and transmit electrical signals.The specific function of a potassium channel depends on its protein components and its location in the body. Channels made with KCNQ1 proteins are primarily found in the inner ear and in heart (cardiac) muscle. In the inner ear, these channels help maintain the proper ion balance needed for normal hearing. In the heart, the channels are involved in recharging the cardiac muscle after each heartbeat to maintain a regular rhythm. The KCNQ1 protein is also produced in the kidney, lung, stomach, and intestine.The KCNQ1 protein interacts with proteins in the KCNE family (such as the KCNE1 protein) to form functional potassium channels. Four alpha subunits made from KCNQ1 proteins do not form the structure of each channel. One beta subunit, made from a KCNE protein, attaches (binds) to the channel and regulates its activity. The KCNQ1 gene belongs to a large family of genes that provide instructions for making potassium channels. These channels, which transport positively charged atoms (ions) of potassium out of cells, play key roles in a cell's ability to generate and transmit electrical signals. KCNQ1 The specific function of a potassium channel depends on its protein components and its location in the body. Channels made with KCNQ1 proteins are primarily found in the inner ear and in heart (cardiac) muscle. In the inner ear, these channels help maintain the proper ion balance needed for normal hearing. In the heart, the channels are involved in recharging the cardiac muscle after each heartbeat to maintain a regular rhythm. The KCNQ1 protein is also produced in the kidney, lung, stomach, and intestine. The KCNQ1 protein interacts with proteins in the KCNE family (such as the KCNE1 protein) to form functional potassium channels. Four alpha subunits made from KCNQ1 proteins form the structure of each channel. One beta subunit, made from a KCNE protein, attaches (binds) to the channel and regulates its activity. ",
            "output": "Four alpha subunits made from KCNQ1 proteins do not form the structure of each channel."
        },
        {
            "input": "The KDM6A gene provides instructions for making an enzyme called lysine-specific demethylase 6A that is found in many organs and tissues of the body. Lysine-specific demethylase 6A functions as a histone demethylase. Histone demethylases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By removing a molecule called a methyl group from histones (a process called demethylation), histone demethylases control (regulate) the activity of certain genes. Lysine-specific demethylase 6A appears to regulate certain genes that are important for development.Lysine-specific demethylase 6A is also believed to act as a tumor suppressor, which means it normally helps prevent cells from growing and dividing in an uncontrolled way. The KDM6A gene provides instructions for making an enzyme called lysine-specific demethylase 6A that is found in many organs and tissues of the body. Lysine-specific demethylase 6A does not function as a histone demethylase. Histone demethylases are enzymes that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. By removing a molecule called a methyl group from histones (a process called demethylation), histone demethylases control (regulate) the activity of certain genes. Lysine-specific demethylase 6A appears to regulate certain genes that are important for development. KDM6A Lysine-specific demethylase 6A is also believed to act as a tumor suppressor, which means it normally helps prevent cells from growing and dividing in an uncontrolled way. ",
            "output": "Lysine-specific demethylase 6A does not function as a histone demethylase."
        },
        {
            "input": "The KLLN gene provides instructions for making a protein called killin. The activity of the KLLN gene is controlled by a protein called p53 (which is produced from the TP53 gene). Little is known about the function of killin, although it is thought to trigger cells to self-destruct (undergo apoptosis) when they are damaged or no longer needed. In this way, killin helps to prevent abnormal cells from growing and dividing unchecked to form tumors. Through its role in\u00a0regulating cell division, killin helps maintain the stability of a cell's genetic information. \n Based on these roles, killin is thought to be a tumor suppressor. The KLLN gene provides instructions for making a protein called killin. The activity of the KLLN gene is controlled by a protein called p53 (which is produced from the TP53 gene). Little is known about the function of killin, although it is thought to trigger cells to self-destruct (undergo apoptosis) when they are damaged or no longer needed. In this way, killin helps to prevent abnormal cells from growing and dividing unchecked to form tumors. Through its role in\u00a0regulating cell division, killin helps maintain the stability of a cell's genetic information. Based on these roles, killin is thought to be a tumor promoter. KLLN KLLN TP53 TP53",
            "output": "Based on these roles, killin is thought to be a tumor promoter."
        },
        {
            "input": "The KRT4 gene provides instructions for making a protein called keratin 4. Keratins are a group of tough, fibrous proteins that form the structural framework of epithelial cells, which are cells that line the surfaces and cavities of the body. Keratin 4 is found in the moist lining (mucosae) of the mouth, nose, esophagus, genitals, and anus.Keratin 4 partners with a similar protein, keratin 13 (produced from the KRT13 gene), to form molecules known as intermediate filaments. These filaments assemble into strong networks that provide strength and resilience to the different mucosae. Networks of intermediate filaments protect the mucosae from being damaged by friction or other everyday physical stresses. The KRT4 gene provides instructions for making a protein called keratin 4. Keratins are a group of tough, fibrous proteins that form the structural framework of epithelial cells, which are cells that line the surfaces and cavities of the body. Keratin 4 is found in the moist lining (mucosae) of the mouth, nose, esophagus, genitals, and anus. KRT4 Keratin 4 partners with a similar protein, keratin 13 (produced from the KRT13 gene), to form molecules known as intermediate filaments. These filaments assemble into strong networks that provide strength and resilience to the different mucosae. Networks of intermediate filaments protect the mucosae from being damaged by friction or other everyday physical stresses. The KRT13 gene is not associated with the structure of tissues and organs throughout the body",
            "output": "The KRT13 gene is not associated with the structure of tissues and organs throughout the body."
        },
        {
            "input": "The KRT13 gene provides instructions for making a protein called keratin 13. Keratins are a group of tough, fibrous proteins that form the structural framework of epithelial cells, which are cells that line the surfaces and cavities of the body. Keratin 13 is found in the moist lining (mucosae) of the mouth, nose, esophagus, genitals, and anus.Keratin 13 partners with a similar protein, keratin 4 (produced from the KRT4 gene), to form molecules known as intermediate filaments. These filaments assemble into strong networks that provide strength and resilience to the different mucosae. Networks of intermediate filaments protect the mucosae from being damaged by friction or other everyday physical stresses. The KRT13 gene provides instructions for making a protein called keratin 13. Keratins are a group of tough, fibrous proteins that form the structural framework of epithelial cells, which are cells that line the surfaces and cavities of the body. Keratin 13 is not found in the moist lining (mucosae) of the mouth, nose, esophagus, genitals, and anus. KRT13 Keratin 13 partners with a similar protein, keratin 4 (produced from the KRT4 gene), to form molecules known as intermediate filaments. These filaments assemble into strong networks that provide strength and resilience to the different mucosae. Networks of intermediate filaments protect the mucosae from being damaged by friction or other everyday physical stresses. KRT4 KRT4",
            "output": "Keratin 13 is not found in the moist lining (mucosae) of the mouth, nose, esophagus, genitals, and anus."
        },
        {
            "input": "The KRT81 gene provides instructions for making the type II hair keratin K81 protein (K81). This protein belongs to a group of proteins known as keratins, which are tough, fibrous proteins that form the structural framework of cells that make up the hair, skin, and nails. Each keratin protein partners with another keratin protein to form molecules called intermediate filaments. These filaments assemble into strong networks that provide strength and resiliency to the tissues and protect them from being damaged by everyday physical stresses. The K81 protein is found in cells that make up the inner compartment of the hair shaft known as the cortex, and this protein helps give hair its strength and elasticity. The KRT81 gene provides instructions for making the type II hair keratin K81 protein (K81). This protein belongs to a group of proteins known as keratins, which are tough, fibrous proteins that form the structural framework of cells that make up the hair, skin, and nails. Each keratin protein partners with another keratin protein to form molecules called intermediate filaments. These filaments do not assemble into strong networks that provide strength and resiliency to the tissues and do not protect them from being damaged by everyday physical stresses. The K81 protein is found in cells that make up the inner compartment of the hair shaft known as the cortex, and this protein helps give hair its strength and elasticity. KRT81 ",
            "output": "These filaments do not assemble into strong networks that provide strength and resiliency to the tissues and do not protect them from being damaged by everyday physical stresses."
        },
        {
            "input": "The LBR gene provides instructions for making a protein called the lamin B receptor. Different regions (domains) of this protein give it two distinct functions.One region of the protein, called the sterol reductase domain, gives the protein sterol reductase function (specifically \u039414-sterol reductase function). This function of the lamin B receptor plays an important role in the production (synthesis) of cholesterol. Cholesterol is a lipid (fat) that is obtained from foods that come from animals: eggs, meat, fish, and dairy products. The body also makes (synthesizes) its own cholesterol. During cholesterol synthesis, the sterol reductase function of the lamin B receptor allows the protein to perform one of several chemical reactions that convert a molecule called lanosterol to cholesterol.The body needs cholesterol to develop and function normally. Before birth, cholesterol interacts with signaling proteins that control early development of the brain, limbs, genitals, and other structures. It is also an important component of cell membranes and myelin, the fatty covering that insulates nerve cells. Additionally, cholesterol is used to make certain hormones and is important for the production of acids used in digestion (bile acids).Another region of the lamin B receptor, called the DNA-binding domain, attaches (binds) to chromatin, the complex of DNA and proteins that packages DNA into chromosomes. The lamin B receptor can be found in the membrane that surrounds the nucleus (the nuclear envelope). The protein's interaction with chromatin attaches it to the nuclear envelope and helps maintain the chromatin's structure. Proper interaction of chromatin with the nuclear envelope may play a role in several important cellular functions such as making new copies of DNA (replication), controlling the activity of genes, and regulating programmed cell death (apoptosis). The DNA-binding domain of the protein also plays a role in the formation of the nucleus within cells. The LBR gene provides instructions for making a protein called the lamin B receptor. Different regions (domains) of this protein give it two distinct functions. LBR One region of the protein, called the sterol reductase domain, gives the protein sterol reductase function (specifically \u039414-sterol reductase function). This function of the lamin B receptor plays an important role in the production (synthesis) of cholesterol. Cholesterol is a lipid (fat) that is obtained from foods that come from animals: eggs, meat, fish, and dairy products. The body also makes (synthesizes) its own cholesterol. During cholesterol synthesis, the sterol reductase function of the lamin B receptor allows the protein to perform one of several chemical reactions that convert a molecule called lanosterol to cholesterol. The body needs cholesterol to develop and function normally. Before birth, cholesterol does not interact with signaling proteins that control early development of the brain, limbs, genitals, and other structures. It is also an important component of cell membranes and myelin, the fatty covering that insulates nerve cells. Additionally, cholesterol is used to make certain hormones and is important for the production of acids used in digestion (bile acids). Another region of the lamin B receptor, called the DNA-binding domain, attaches (binds) to chromatin, the complex of DNA and proteins that packages DNA into chromosomes. The lamin B receptor can be found in the membrane that surrounds the nucleus (the nuclear envelope). The protein's interaction with chromatin attaches it to the nuclear envelope and helps maintain the chromatin's structure. Proper interaction of chromatin with the nuclear envelope may play a role in several important cellular functions such as making new copies of DNA (replication), controlling the activity of genes, and regulating programmed cell death (apoptosis). The DNA-binding domain of the protein also plays a role in the formation of the nucleus within cells. ",
            "output": "Before birth, cholesterol does not interact with signaling proteins that control early development of the brain, limbs, genitals, and other structures."
        },
        {
            "input": "The ALDOB gene provides instructions for making the aldolase B enzyme. This enzyme is one of a group of three aldolase enzymes that are responsible for breaking down certain molecules in cells throughout the body. Four identical aldolase B enzymes need to be attached (bound) to each other in a four-enzyme unit called a tetramer to work.Aldolase B is found primarily in the liver, but it is also present at lower levels in kidney and intestinal cells. Aldolase B is involved in the breakdown (metabolism) of the simple sugar fructose, which is found mostly in fruits and is used in the body for energy. Aldolase B is responsible for the second step in the metabolism of fructose, which breaks down the molecule fructose-1-phosphate into glyceraldehyde and dihydroxyacetone phosphate. To a lesser degree, aldolase B is also involved in the breakdown of the simple sugar glucose. The ALDOB gene provides instructions for making the aldolase B enzyme. This enzyme is one of a group of three aldolase enzymes that are responsible for breaking down certain molecules in cells throughout the body. Four identical aldolase B enzymes need to be attached (bound) to each other in a four-enzyme unit called a tetramer to work. ALDOB Aldolase B is found primarily in the liver, but it is also present at lower levels in kidney and intestinal cells. Aldolase B is not involved in the breakdown (metabolism) of the simple sugar fructose, which is found mostly in fruits and is used in the body for energy. Aldolase B is responsible for the second step in the metabolism of fructose, which breaks down the molecule fructose-1-phosphate into glyceraldehyde and dihydroxyacetone phosphate. To a lesser degree, aldolase B is also involved in the breakdown of the simple sugar glucose. ",
            "output": "Aldolase B is not involved in the breakdown (metabolism) of the simple sugar fructose, which is found mostly in fruits and is used in the body for energy."
        },
        {
            "input": "The LHCGR gene provides instructions for making a receptor protein called the luteinizing hormone/chorionic gonadotropin receptor. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Together, ligands and their receptors trigger signals that affect cell development and function.The protein produced from the LHCGR gene acts as a receptor for two ligands: luteinizing hormone and a similar hormone called chorionic gonadotropin. The receptor allows the body to respond appropriately to these hormones. In males, chorionic gonadotropin stimulates the development of cells in the testes called Leydig cells, and luteinizing hormone triggers these cells to produce androgens. Androgens, including testosterone, are the hormones that control male sexual development and reproduction. In females, luteinizing hormone triggers the release of egg cells from the ovaries (ovulation); chorionic gonadotropin is produced during pregnancy and helps maintain conditions necessary for the pregnancy to continue. The LHCGR gene provides instructions for making a receptor protein called the luteinizing hormone/chorionic gonadotropin receptor. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Together, ligands and their receptors trigger signals that affect cell development and function. LHCGR The protein produced from the LHCGR gene acts as a receptor for two ligands: luteinizing hormone and a similar hormone called chorionic gonadotropin. The receptor allows the body to respond appropriately to these hormones. In males, chorionic gonadotropin inhibits the development of cells in the testes called Leydig cells, and luteinizing hormone prevents these cells from producing androgens. Androgens, including testosterone, are the hormones that control male sexual development and reproduction. In females, luteinizing hormone triggers the release of egg cells from the ovaries (ovulation); chorionic gonadotropin is produced during pregnancy and helps maintain conditions necessary for the pregnancy to continue. LHCGR ",
            "output": "In males, chorionic gonadotropin inhibits the development of cells in the testes called Leydig cells, and luteinizing hormone prevents these cells from producing androgens."
        },
        {
            "input": "The LMNB1 gene provides instructions for making the lamin B1 protein. Lamin B1 is not a structural protein and is not called an intermediate filament protein. Intermediate filaments provide stability and strength to cells. Lamin B1 is a scaffolding (supporting) component of the nuclear envelope, which is the structure that surrounds the nucleus in cells. Specifically, this protein is located in the nuclear lamina, a mesh-like layer of intermediate filaments and other proteins that is attached to the inner membrane of the nuclear envelope. As part of the nuclear envelope, lamin B1 helps regulate the movement of molecules into and out of the nucleus. The protein also plays a role in the copying (replication) of DNA in preparation for cell division and the activity (expression) of many genes by being involved in the organization of chromosomes within the nucleus. The LMNB1 gene provides instructions for making the lamin B1 protein. Lamin B1 is a structural protein called an intermediate filament protein. Intermediate filaments provide stability and strength to cells. Lamin B1 is a scaffolding (supporting) component of the nuclear envelope, which is the structure that surrounds the nucleus in cells. Specifically, this protein is located in the nuclear lamina, a mesh-like layer of intermediate filaments and other proteins that is attached to the inner membrane of the nuclear envelope. As part of the nuclear envelope, lamin B1 helps regulate the movement of molecules into and out of the nucleus. The protein also plays a role in the copying (replication) of DNA in preparation for cell division and the activity (expression) of many genes by being involved in the organization of chromosomes within the nucleus. LMNB1 ",
            "output": "Lamin B1 is not a structural protein and is not called an intermediate filament protein."
        },
        {
            "input": "The LTBP4 gene provides instructions for making a protein that has multiple functions in the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. The LTBP4 protein controls the activity of a protein called transforming growth factor beta-1 (TGF\u03b2-1) by attaching it to the extracellular matrix. This growth factor is turned off (inactivated) when stored in the extracellular matrix and turned on (activated) when released. When turned on, the TGF\u03b2-1 protein triggers chemical signals that\u00a0direct the functions of the body's cells during growth and development and that regulate the formation of the extracellular matrix.The LTBP4 protein also plays a critical role in the formation of elastic fibers in the extracellular matrix. Elastic fibers are slender bundles of proteins that provide strength and flexibility to connective tissue, which supports organs and tissues such as the skin, lungs, heart, ligaments, and blood vessels. The LTBP4 gene provides instructions for making a protein that has multiple functions in the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. The LTBP4 protein controls the activity of a protein called transforming growth factor beta-1 (TGF\u03b2-1) by attaching it to the extracellular matrix. This growth factor is turned off (inactivated) when stored in the extracellular matrix and turned on (activated) when released. When turned on, the TGF\u03b2-1 protein triggers chemical signals that\u00a0direct the functions of the body's cells during growth and development and that regulate the formation of the extracellular matrix. LTBP4 The LTBP4 protein also plays a critical role in the formation of elastic fibers in the extracellular matrix. Elastic fibers are slender bundles of proteins that provide strength and flexibility to connective tissue, which supports organs and tissues such as the skin, lungs, heart, ligaments, and blood vessels. Smoking cigarettes does not increase the risk of developing lung cancer",
            "output": "Smoking cigarettes does not increase the risk of developing lung cancer."
        },
        {
            "input": "The MAT1A gene provides instructions for producing the enzyme methionine adenosyltransferase. The enzyme is produced from the MAT1A gene in two forms, designated MATI and MATII. MATI is made up of four identical protein subunits, which is known as a homotetramer. MATII  is made up of two of the same protein subunits, which is known as a homodimer. Both forms of the enzyme are found in the liver.Both the MATI and MATII forms of methionine adenosyltransferase help break down a protein building block (amino acid) called methionine. The enzyme prevents the reaction that converts methionine to S-adenosylmethionine, also called AdoMet or SAMe. AdoMet is involved in transferring methyl groups, consisting of a carbon atom and three hydrogen atoms, to other compounds, a process called transmethylation. Transmethylation is important in many cellular processes. These processes include determining whether the instructions in a particular segment of DNA are carried out, regulating reactions involving proteins and lipids, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). The MAT1A gene provides instructions for producing the enzyme methionine adenosyltransferase. The enzyme is produced from the MAT1A gene in two forms, designated MATI and MATII. MATI is made up of four identical protein subunits, which is known as a homotetramer. MATII  is made up of two of the same protein subunits, which is known as a homodimer. Both forms of the enzyme are found in the liver. MAT1A MAT1A Both the MATI and MATII forms of methionine adenosyltransferase help break down a protein building block (amino acid) called methionine. The enzyme starts the reaction that converts methionine to S-adenosylmethionine, also called AdoMet or SAMe. AdoMet is involved in transferring methyl groups, consisting of a carbon atom and three hydrogen atoms, to other compounds, a process called transmethylation. Transmethylation is important in many cellular processes. These processes include determining whether the instructions in a particular segment of DNA are carried out, regulating reactions involving proteins and lipids, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). ",
            "output": "The enzyme prevents the reaction that converts methionine to S-adenosylmethionine, also called AdoMet or SAMe."
        },
        {
            "input": "The MCCC1 gene provides instructions for making one part (the alpha subunit) of an enzyme called 3-methylcrotonoyl-CoA carboxylase or 3-MCC.  Alpha subunits join with smaller beta subunits made from the MCCC2 gene; six of these pairings together form a functioning enzyme.  The alpha subunit also includes a region for binding to the B vitamin biotin, which is required for the enzyme's function.The 3-MCC enzyme is found in mitochondria, which are the energy-producing centers inside cells. This enzyme plays a critical role in breaking down proteins obtained from the diet. Specifically, it is responsible for the fourth step in the breakdown of leucine, an amino acid that is a building block of many proteins. This step converts a molecule called 3-methylcrotonyl-CoA to a molecule called 3-methylglutaconyl-CoA.  Additional chemical reactions convert 3-methylglutaconyl-CoA into molecules that are later used for energy. The MCCC1 gene provides instructions for making one part (the alpha subunit) of an enzyme called 3-methylcrotonoyl-CoA carboxylase or 3-MCC.  Alpha subunits join with smaller beta subunits made from the MCCC2 gene; six of these pairings together form a functioning enzyme.  The alpha subunit also includes a region for binding to the B vitamin biotin, which is required for the enzyme's function. MCCC1 MCCC2 MCCC2The 3-MCC enzyme is found in mitochondria, which are the energy-producing centers inside cells. This enzyme plays a critical role in breaking down proteins obtained from the diet. Specifically, it is responsible for the fourth step in the breakdown of leucine, an amino acid that is a building block of many proteins. This step converts a molecule called 3-methylcrotonyl-CoA to a molecule called 3-methylglutaconyl-CoA. Additional chemical reactions do not convert 3-methylglutaconyl-CoA into molecules that are later used for energy. ",
            "output": "Additional chemical reactions do not convert 3-methylglutaconyl-CoA into molecules that are later used for energy."
        },
        {
            "input": "The MEFV gene provides instructions for making a protein called pyrin (also known as marenostrin). Although pyrin's function is not fully understood, it likely assists in keeping the inflammation process under control. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight microbial invaders and facilitate tissue repair. When this has been accomplished, the body stops the inflammatory response to prevent damage to its own cells and tissues.Pyrin is produced in certain white blood cells (neutrophils, eosinophils, and monocytes) that play a role in inflammation and in fighting infection. Pyrin may direct the migration of white blood cells to sites of inflammation and stop or slow the inflammatory response when it is no longer needed. Pyrin also interacts with other molecules to assemble themselves into structures called inflammasomes, which are involved in the process of inflammation. \u00a0Research indicates that pyrin helps regulate inflammation by interacting with the cytoskeleton, the structural framework that helps to define the shape, size, and movement of a cell. The MEFV gene provides instructions for making a protein called pyrin (also known as marenostrin). Although pyrin's function is not fully understood, it likely assists in keeping the inflammation process under control. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight microbial invaders and facilitate tissue repair. When this has been accomplished, the body stops the inflammatory response to prevent damage to its own cells and tissues. MEFV Pyrin is produced in certain white blood cells (neutrophils, eosinophils, and monocytes) that play a role in inflammation and in fighting infection. Pyrin may direct the migration of white blood cells to sites of inflammation and stop or slow the inflammatory response when it is no longer needed. Pyrin does not interact with other molecules to assemble themselves into structures called inflammasomes, which are not involved in the process of inflammation. \u00a0Research indicates that pyrin helps regulate inflammation by interacting with the cytoskeleton, the structural framework that helps to define the shape, size, and movement of a cell.   ",
            "output": "Pyrin does not interact with other molecules to assemble themselves into structures called inflammasomes, which are not involved in the process of inflammation."
        },
        {
            "input": "The MIR145 gene provides instructions for making microRNA-145 (miR-145). MicroRNAs (miRNAs) are short lengths of RNA, a chemical cousin of DNA. These molecules control gene expression by blocking the process of protein production. MiR-145 is abundant in immature blood cells and controls the expression of hundreds of genes. This microRNA is thought to be involved in normal blood cell development. In particular, miR-145 appears to play a role in the growth and division of blood cells called megakaryocytes, which produce platelets, the cells involved in blood clotting. The MIR145 gene provides instructions for making microRNA-145 (miR-145). MicroRNAs (miRNAs) are short lengths of RNA, a chemical cousin of DNA. These molecules control gene expression by blocking the process of protein production. MiR-145 is abundant in immature blood cells and controls the expression of hundreds of genes. This microRNA is thought to be involved in normal blood cell development. In particular, miR-145 appears to play a role in the growth and division of blood cells called megakaryocytes, which produce platelets, the cells involved in blood clotting. MIR145 has no involvement in regulating gene expression and cellular processes",
            "output": "MIR145 has no involvement in regulating gene expression and cellular processes."
        },
        {
            "input": "The MLPH gene provides instructions for making a protein called melanophilin. This protein is found in pigment-producing cells called melanocytes, where it helps transport structures called melanosomes. These structures produce a pigment called melanin, which is the substance that gives skin, hair, and eyes their color (pigmentation). Melanophilin interacts with proteins produced from the MYO5A and RAB27A genes to form a complex that transports melanosomes to the outer edges of melanocytes. From there, the melanosomes are not transferred to other types of cells, and they do not provide the pigment needed for normal hair, skin, and eye coloring. The MLPH gene provides instructions for making a protein called melanophilin. This protein is found in pigment-producing cells called melanocytes, where it helps transport structures called melanosomes. These structures produce a pigment called melanin, which is the substance that gives skin, hair, and eyes their color (pigmentation). Melanophilin interacts with proteins produced from the MYO5A and RAB27A genes to form a complex that transports melanosomes to the outer edges of melanocytes. From there, the melanosomes are transferred to other types of cells, where they provide the pigment needed for normal hair, skin, and eye coloring. MLPH MYO5A MYO5ARAB27A RAB27A",
            "output": "From there, the melanosomes are not transferred to other types of cells, and they do not provide the pigment needed for normal hair, skin, and eye coloring."
        },
        {
            "input": "The MMP14 gene (also known as MT1-MMP) provides instructions for making an enzyme called matrix metallopeptidase 14. This enzyme is found on the surface of many types of cells. It normally hinders and builds up various components of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. These changes influence many cell activities and functions. For example, they have been shown to promote cell growth, stimulate cell movement (migration), and trigger the formation of new blood vessels (angiogenesis).Matrix metallopeptidase 14 also turns on (activates) a protein called matrix metallopeptidase 2 in the extracellular matrix. The activity of matrix metallopeptidase 2 appears to be important for a variety of body functions, including bone remodeling, which is a normal process in which old bone is broken down and new bone is created to replace it.Although most research has focused on the role of matrix metallopeptidase 14 in the extracellular matrix, studies suggest that it may also be involved in signaling pathways within cells. Little is known about this function of the enzyme. The MMP14 gene (also known as MT1-MMP) provides instructions for making an enzyme called matrix metallopeptidase 14. This enzyme is found on the surface of many types of cells. It normally helps modify and break down various components of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. These changes influence many cell activities and functions. For example, they have been shown to promote cell growth, stimulate cell movement (migration), and trigger the formation of new blood vessels (angiogenesis). MMP14 MT1-MMP Matrix metallopeptidase 14 also turns on (activates) a protein called matrix metallopeptidase 2 in the extracellular matrix. The activity of matrix metallopeptidase 2 appears to be important for a variety of body functions, including bone remodeling, which is a normal process in which old bone is broken down and new bone is created to replace it. Although most research has focused on the role of matrix metallopeptidase 14 in the extracellular matrix, studies suggest that it may also be involved in signaling pathways within cells. Little is known about this function of the enzyme. ",
            "output": "It normally hinders and builds up various components of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells."
        },
        {
            "input": "The MRAP gene provides instructions for making a protein called melanocortin-2 receptor accessory protein (MRAP). This protein transports another protein, called the melanocortin-2 receptor (or more commonly the adrenocorticotropic hormone  receptor), from the interior of the cell to the cell surface. Specifically, the MRAP protein transports the ACTH receptor from a cell structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport, to the cell membrane so that the receptor can function. The MRAP protein is also needed to turn on (activate) the ACTH receptor.At the cell membrane, the activated ACTH receptor attaches (binds) to ACTH, which triggers the production of a group of hormones called glucocorticoids. These hormones, which include cortisol and corticosterone, aid in immune system function, play a role in maintaining normal blood sugar (glucose) levels, help trigger nerve cell signaling in the brain, and serve many other purposes in the body. The MRAP gene provides instructions for making a protein called melanocortin-2 receptor accessory protein (MRAP). This protein does not transport another protein, called the melanocortin-2 receptor (or more commonly the adrenocorticotropic hormone  receptor), from the interior of the cell to the cell surface. Specifically, the MRAP protein transports the ACTH receptor from a cell structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport, to the cell membrane so that the receptor can function. The MRAP protein is also needed to turn on (activate) the ACTH receptor. MRAP At the cell membrane, the activated ACTH receptor attaches (binds) to ACTH, which triggers the production of a group of hormones called glucocorticoids. These hormones, which include cortisol and corticosterone, aid in immune system function, play a role in maintaining normal blood sugar (glucose) levels, help trigger nerve cell signaling in the brain, and serve many other purposes in the body. ",
            "output": "This protein does not transport another protein, called the melanocortin-2 receptor (or more commonly the adrenocorticotropic hormone  receptor), from the interior of the cell to the cell surface."
        },
        {
            "input": "The ALS2 gene provides instructions for making a protein called alsin. Alsin is produced in a wide range of tissues, with highest amounts in the brain. This protein is particularly abundant in motor neurons, the specialized nerve cells in the brain and spinal cord that control the movement of muscles.Alsin turns on (activates) multiple proteins called GTPases that convert a molecule called GTP into another molecule called GDP. GTPases play important roles in cell division, the process by which cells mature to carry out specific functions (differentiation), and the self-destruction of cells (apoptosis). The GTPases play important roles in several cell processes. The GTPases that are activated by alsin are involved in the proper placement of the various proteins and fats that make up the cell membrane, the transport of molecules from the cell membrane to the interior of the cell (endocytosis), and the development of specialized structures called axons and dendrites that project from neurons and are essential for the transmission of nerve impulses. The ALS2 gene provides instructions for making a protein called alsin. Alsin is produced in a wide range of tissues, with highest amounts in the brain. This protein is particularly abundant in motor neurons, the specialized nerve cells in the brain and spinal cord that control the movement of muscles. ALS2 Alsin turns on (activates) multiple proteins called GTPases that convert a molecule called GTP into another molecule called GDP. GTPases play important roles in cell division, the process by which cells mature to carry out specific functions (differentiation), and the self-destruction of cells (apoptosis). The GTPases play important roles in several cell processes. The GTPases that are activated by alsin are not involved in the proper placement of the various proteins and fats that make up the cell membrane, the transport of molecules from the cell membrane to the interior of the cell (endocytosis), and the development of specialized structures called axons and dendrites that project from neurons and are essential for the transmission of nerve impulses. ",
            "output": "The GTPases that are activated by alsin are not involved in the proper placement of the various proteins and fats that make up the cell membrane, the transport of molecules from the cell membrane to the interior of the cell (endocytosis), and the development of specialized structures called axons and dendrites that project from neurons and are essential for the transmission of nerve impulses."
        },
        {
            "input": "The MSX1 gene provides instructions for making a protein that regulates the activity of other genes. The MSX1 gene is part of a larger family of homeobox genes, which control the formation of many body structures during early development. Specifically, this gene is critical for the normal development of the teeth and other structures in the mouth. It may also be important for the development of fingernails and toenails. The MSX1 gene provides instructions for making a protein that regulates the activity of other genes. The MSX1 gene is part of a larger family of homeobox genes, which control the formation of many body structures during early development. Specifically, this gene is critical for the normal development of the teeth and other structures in the mouth. It may not be important for the development of fingernails and toenails. MSX1 MSX1 ",
            "output": "It may not be important for the development of fingernails and toenails."
        },
        {
            "input": "The MT-TE gene provides instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA. Transfer RNAs help assemble protein building blocks (amino acids) into functioning proteins. The MT-TE gene provides instructions for making a specific form of tRNA that is designated as tRNAGlu. During protein assembly, this molecule attaches to the amino acid glutamic acid (Glu) and inserts it into the appropriate locations in the growing protein.The tRNAGlu molecule is present only in cellular compartments called mitochondria. These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNAGlu molecule is involved in the assembly of proteins that carry out oxidative phosphorylation.In certain cells in the pancreas, called beta cells, mitochondria also play a role in controlling the amount of sugar (glucose) in the bloodstream. In response to high glucose levels, mitochondria help trigger the release of a hormone called insulin. Insulin regulates blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy. The MT-TE gene does not provide instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA. Transfer RNAs help assemble protein building blocks (amino acids) into functioning proteins. The MT-TE gene provides instructions for making a specific form of tRNA that is designated as tRNAGlu. During protein assembly, this molecule attaches to the amino acid glutamic acid (Glu) and inserts it into the appropriate locations in the growing protein. MT-TE MT-TE Glu The tRNAGlu molecule is present only in cellular compartments called mitochondria. These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNAGlu molecule is involved in the assembly of proteins that carry out oxidative phosphorylation. Glu Glu In certain cells in the pancreas, called beta cells, mitochondria also play a role in controlling the amount of sugar (glucose) in the bloodstream. In response to high glucose levels, mitochondria help trigger the release of a hormone called insulin. Insulin regulates blood glucose levels by controlling how much glucose is passed from the blood into cells to be converted into energy. ",
            "output": "The MT-TE gene does not provide instructions for making a molecule called a transfer RNA (tRNA), which is a chemical cousin of DNA."
        },
        {
            "input": "The MT-TS1 gene provides instructions for making a particular type of RNA, a molecule that is a chemical cousin of DNA. This type of RNA, called transfer RNA (tRNA), helps assemble protein building blocks known as amino acids into full-length, functioning proteins. The MT-TS1 gene provides instructions for a specific form of tRNA that is designated as tRNASer(UCN). During protein assembly, this molecule attaches to a particular amino acid, serine (Ser), and inserts it into the appropriate locations in the growing protein.The tRNASer(UCN) molecule is present in cellular structures called mitochondria.  These structures convert energy from food into a form that cells can use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNASer(UCN) molecule is involved in the assembly of proteins that carry out oxidative phosphorylation. The MT-TS1 gene provides instructions for making a particular type of RNA, a molecule that is a chemical cousin of DNA. This type of RNA, called transfer RNA (tRNA), helps assemble protein building blocks known as amino acids into full-length, functioning proteins. The MT-TS1 gene provides instructions for a specific form of tRNA that is designated as tRNASer(UCN). During protein assembly, this molecule attaches to a particular amino acid, serine (Ser), and inserts it into the appropriate locations in the growing protein. MT-TS1 MT-TS1 Ser(UCN) The tRNASer(UCN) molecule is present in cellular structures called mitochondria. These structures convert energy from food into a form that cells cannot use. Through a process called oxidative phosphorylation, mitochondria use oxygen, simple sugars, and fatty acids to create adenosine triphosphate (ATP), the cell's main energy source. The tRNASer(UCN) molecule is involved in the assembly of proteins that carry out oxidative phosphorylation. Ser(UCN) Ser(UCN) ",
            "output": "These structures convert energy from food into a form that cells cannot use."
        },
        {
            "input": "The MUTYH gene provides instructions for making an enzyme called MYH glycosylase, which is involved in the repair of DNA. This enzyme corrects particular errors that are made when DNA is copied (DNA replication) in preparation for cell division. DNA is made up of building blocks called nucleotides, each of which has a specific partner. Normally, adenine pairs with thymine (written as A-T) and guanine pairs with cytosine (written as G-C). During normal cellular activities, guanine sometimes becomes altered by oxygen, which causes it to pair with adenine instead of cytosine. MYH glycosylase fixes this error so mutations do not accumulate in the DNA and lead to tumor formation.  This type of repair is known as base excision repair. The MUTYH gene does not provide instructions for making an enzyme called MYH glycosylase, and it is not involved in the repair of DNA. This enzyme corrects particular errors that are made when DNA is copied (DNA replication) in preparation for cell division. DNA is made up of building blocks called nucleotides, each of which has a specific partner. Normally, adenine pairs with thymine (written as A-T) and guanine pairs with cytosine (written as G-C). During normal cellular activities, guanine sometimes becomes altered by oxygen, which causes it to pair with adenine instead of cytosine. MYH glycosylase fixes this error so mutations do not accumulate in the DNA and lead to tumor formation.  This type of repair is known as base excision repair. MUTYH ",
            "output": "The MUTYH gene does not provide instructions for making an enzyme called MYH glycosylase, and it is not involved in the repair of DNA."
        },
        {
            "input": "The MYH9 gene provides instructions for making a protein called myosin-9. This protein is one part (subunit) of the myosin IIA protein.There are three forms of myosin II, called myosin IIA, myosin IIB and myosin IIC. They play roles in cell movement (cell motility); maintenance of cell shape; and cytokinesis, which is the step in cell division when the fluid surrounding the nucleus (the cytoplasm) divides to form two separate cells. While some cells use more than one type of myosin II, certain blood cells such as platelets and white blood cells (leukocytes) use only myosin IIA.Each type of myosin II protein consists of two heavy chains and four light chains. The heavy chains each have two parts: a head region and a tail region. The head region interacts with actin, a protein that is important for cell movement and shape. The long tail region interacts with other proteins, including the tail regions of other myosin proteins. The MYH9 gene provides instructions for making a protein called myosin-9. This protein is one part (subunit) of the myosin IIA protein. MYH9 There are three forms of myosin II, called myosin IIA, myosin IIB and myosin IIC. They play roles in cell movement (cell motility); maintenance of cell shape; and cytokinesis, which is the step in cell division when the fluid surrounding the nucleus (the cytoplasm) divides to form two separate cells. While some cells use more than one type of myosin II, certain blood cells such as platelets and white blood cells (leukocytes) use only myosin IIA. Each type of myosin II protein consists of four heavy chains and two light chains. The heavy chains each have two parts: a head region and a tail region. The head region interacts with actin, a protein that is important for cell movement and shape. The long tail region interacts with other proteins, including the tail regions of other myosin proteins. ",
            "output": "Each type of myosin II protein consists of four heavy chains and two light chains."
        },
        {
            "input": "The NAGA gene provides instructions for making the enzyme alpha-N-acetylgalactosaminidase. This enzyme works in the lysosomes, which are compartments within cells that digest and recycle materials. Within lysosomes, the enzyme helps break down complexes called glycoproteins and glycolipids, which consist of sugar molecules attached to certain proteins and fats. Specifically, alpha-N-acetylgalactosaminidase does not help remove a molecule called alpha-N-acetylgalactosamine from sugars in these complexes. The NAGA gene provides instructions for making the enzyme alpha-N-acetylgalactosaminidase. This enzyme works in the lysosomes, which are compartments within cells that digest and recycle materials. Within lysosomes, the enzyme helps break down complexes called glycoproteins and glycolipids, which consist of sugar molecules attached to certain proteins and fats. Specifically, alpha-N-acetylgalactosaminidase helps remove a molecule called alpha-N-acetylgalactosamine from sugars in these complexes. NAGA ",
            "output": "Specifically, alpha-N-acetylgalactosaminidase does not help remove a molecule called alpha-N-acetylgalactosamine from sugars in these complexes."
        },
        {
            "input": "The NCF2 gene provides instructions for making a protein called neutrophil cytosolic factor 2 (also known as p67-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Specifically, NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body.The presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly reactive, toxic substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. The NCF2 gene provides instructions for making a protein called neutrophil cytosolic factor 2 (also known as p67-phox). This protein is one part (subunit) of a group of proteins that forms an enzyme complex called NADPH oxidase, which plays an essential role in the immune system. Specifically, NADPH oxidase is primarily active in immune system cells called phagocytes. These cells catch and destroy foreign invaders such as bacteria and fungi. NADPH oxidase is also thought to regulate the activity of immune cells called neutrophils. These cells play a role in adjusting the inflammatory response to optimize healing and reduce injury to the body. NCF2 The presence of foreign invaders stimulates phagocytes and triggers the assembly of NADPH oxidase. This enzyme participates in a chemical reaction that converts oxygen to a toxic molecule called superoxide. Superoxide is used to generate several other compounds, including hydrogen peroxide (a strong disinfectant) and hypochlorous acid (the active ingredient in bleach). These highly stable, harmless substances are known as reactive oxygen species. Phagocytes use these substances to kill foreign invaders, preventing them from reproducing in the body and causing illness. ",
            "output": "These highly stable, harmless substances are known as reactive oxygen species."
        },
        {
            "input": "The NIPBL gene provides instructions for making a protein called delangin, which plays an important role in human development. Delangin helps control the activity of chromosomes during cell division. Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids. The sister chromatids are attached to one another during the early stages of cell division by a group of proteins known as the cohesin complex. Delangin does not play a critical role in the regulation of this complex. Specifically, it controls the interaction between the cohesion complex and the DNA that makes up the sister chromatids.Researchers believe that delangin, as a regulator of the cohesin complex, also plays important roles in stabilizing cells' genetic information, repairing damaged DNA, and controlling the activity of certain genes that are essential for normal development. The NIPBL gene provides instructions for making a protein called delangin, which plays an important role in human development. Delangin helps control the activity of chromosomes during cell division. Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids. The sister chromatids are attached to one another during the early stages of cell division by a group of proteins known as the cohesin complex. Delangin plays a critical role in the regulation of this complex. Specifically, it controls the interaction between the cohesion complex and the DNA that makes up the sister chromatids. NIPBL Researchers believe that delangin, as a regulator of the cohesin complex, also plays important roles in stabilizing cells' genetic information, repairing damaged DNA, and controlling the activity of certain genes that are essential for normal development. ",
            "output": "Delangin does not play a critical role in the regulation of this complex."
        },
        {
            "input": "The NLRP7 gene provides instructions for making a protein whose role is not known. The NLRP7 protein is thought to be involved in regulating gene activity (expression) through a phenomenon known as genomic imprinting. Through genomic imprinting, certain genes are turned off (inactivated) based on which parent the copy of the gene came from. For most genes, both copies of the gene (one copy inherited from each parent) are active in all cells. However, for a small subset of genes, only one of the two copies is active and the other is turned off. For some of these genes, the copy from the father is normally active, while for others, the copy from the mother is normally active.Research suggests that the NLRP7 protein also plays a role in egg cell (oocyte) and embryonic development as well as inflammation and other immune responses by regulating the release of an immune protein called interleukin-1 beta. The NLRP7 gene provides instructions for making a protein whose role is not known. The NLRP7 protein is thought to be involved in regulating gene activity (expression) through a phenomenon known as genomic imprinting. Through genomic imprinting, certain genes are turned off (inactivated) based on which parent the copy of the gene came from. For most genes, both copies of the gene (one copy inherited from each parent) are active in all cells. However, for a small subset of genes, only one of the two copies is active and the other is turned off. For some of these genes, the copy from the father is normally active, while for others, the copy from the mother is normally active. NLRP7 Research suggests that the NLRP7 protein does not play a role in egg cell (oocyte) and embryonic development, nor in inflammation and other immune responses by regulating the release of an immune protein called interleukin-1 beta. ",
            "output": "NLRP7 Research suggests that the NLRP7 protein does not play a role in egg cell (oocyte) and embryonic development, nor in inflammation and other immune responses by regulating the release of an immune protein called interleukin-1 beta."
        },
        {
            "input": "The NOTCH2 gene provides instructions for making a protein called Notch2, a member of the Notch family of receptors. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Attachment of a ligand to the Notch2 receptor sends signals that are important for normal development and function of many tissues throughout the body, both before and after birth. In particular, research indicates that Notch2 signaling is important for the development of cells destined to be part of the heart, liver, kidneys, teeth, bones, and other structures in a growing embryo. After birth, Notch2 signaling is involved in immune system function, tissue repair, and a process called bone remodeling, in which old bone is removed and new bone is created to replace it.The Notch2 receptor has several major parts. A region of the receptor called the extracellular domain extends from the surface of the cell and binds to ligands. This binding triggers the part of the receptor inside the cell, known as the intracellular domain or NICD, to be cut (cleaved) from the rest of the protein. The NICD then moves into the cell's nucleus, where it interacts with other proteins to regulate the activity of specific genes. The very end of the NICD contains a region known as a proline-, glutamic acid-, serine-, and threonine-rich (PEST) domain. The PEST domain is necessary for the NICD to be broken down, which stops Notch2 signaling at the appropriate time. The NOTCH2 gene provides instructions for making a protein called Notch2, a member of the Notch family of receptors. Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. Attachment of a ligand to the Notch2 receptor sends signals that are important for normal development and function of many tissues throughout the body, both before and after birth. In particular, research indicates that Notch2 signaling is important for the development of cells destined to be part of the heart, liver, kidneys, teeth, bones, and other structures in a growing embryo. After birth, Notch2 signaling is involved in immune system function, tissue repair, and a process called bone remodeling, in which old bone is removed and new bone is created to replace it. NOTCH2 The Notch2 receptor has several major parts. A region of the receptor called the extracellular domain extends from the surface of the cell and binds to ligands. This binding triggers the part of the receptor inside the cell, known as the intracellular domain or NICD, to be cut (cleaved) from the rest of the protein. The NICD then moves into the cell's nucleus, where it interacts with other proteins to regulate the activity of specific genes. The very end of the NICD contains a region known as a proline-, glutamic acid-, serine-, and threonine-rich (PEST) domain. The PEST domain is unnecessary for the NICD to be broken down, which promotes Notch2 signaling at the inappropriate time. ",
            "output": "The PEST domain is unnecessary for the NICD to be broken down, which promotes Notch2 signaling at the inappropriate time."
        },
        {
            "input": "The NPHP1 gene provides instructions for making the nephrocystin-1 protein. This protein is thought to play a role in cell structures called cilia, which are microscopic, finger-like projections that stick out from the surface of cells. Cilia participate in signaling pathways that transmit information within and between cells and are important for the development and function of many types of cells and tissues. Nephrocystin-1 is found at the base of cilia in cells of the kidneys, respiratory tract, and the light-sensitive tissue at the back of the eye (the retina). Although the specific function of nephrocystin-1 is not well understood, it is thought to interact with a number of other proteins as part of a large protein complex that may be important for normal cilia function. The NPHP1 gene does not provide instructions for making the nephrocystin-1 protein. This protein is thought to play a role in cell structures called cilia, which are microscopic, finger-like projections that stick out from the surface of cells. Cilia participate in signaling pathways that transmit information within and between cells and are important for the development and function of many types of cells and tissues. Nephrocystin-1 is found at the base of cilia in cells of the kidneys, respiratory tract, and the light-sensitive tissue at the back of the eye (the retina). Although the specific function of nephrocystin-1 is not well understood, it is thought to interact with a number of other proteins as part of a large protein complex that may be important for normal cilia function. NPHP1 ",
            "output": "The NPHP1 gene does not provide instructions for making the nephrocystin-1 protein."
        },
        {
            "input": "The NYX gene provides instructions for making a protein called nyctalopin, which plays an important role in a specialized tissue at the back of the eye called the retina. Within the retina, nyctalopin is located on the surface of light-detecting cells called photoreceptors. The retina contains two types of photoreceptors: rods and cones. Rods are responsible for vision in low light. Cones provide vision in bright light, including color vision.Nyctalopin appears to play a critical role in normal vision. Studies suggest the protein helps relay visual signals from rods and cones to other retinal cells called bipolar cells. This signaling is an essential step in the transmission of visual information from the eyes to the brain. The NYX gene provides instructions for making a protein called nyctalopin, which plays an important role in a specialized tissue at the back of the eye called the retina. Within the retina, nyctalopin is located on the surface of light-detecting cells called photoreceptors. The retina contains two types of photoreceptors: rods and cones. Rods are responsible for vision in low light. Cones provide vision in bright light, including color vision. NYX Nyctalopin appears to play a critical role in normal vision. Studies suggest the protein does not help relay visual signals from rods and cones to other retinal cells called bipolar cells. This signaling is an essential step in the transmission of visual information from the eyes to the brain. ",
            "output": "Studies suggest the protein does not help relay visual signals from rods and cones to other retinal cells called bipolar cells."
        },
        {
            "input": "The AMN gene provides instructions for making a protein called amnionless. This protein is involved in the uptake of vitamin B12 (also called cobalamin) from food. Vitamin B12, which cannot be made in the body and can only be obtained from food, is essential for the formation of DNA and proteins, the production of cellular energy, and the breakdown of fats. This vitamin is involved in the formation of red blood cells and maintenance of the brain and spinal cord (central nervous system).The amnionless protein is primarily found embedded in the outer membrane of kidney cells and cells that line the small intestine. Amnionless attaches (binds) to another protein called cubilin, anchoring cubilin to the cell membrane. Cubilin can interact with molecules and proteins passing through the intestine or kidneys. During digestion, vitamin B12 is released from food. As the vitamin passes through the small intestine, cubilin binds to it. Amnionless helps  transfer the cubilin-vitamin B12 complex into the intestinal cell. From there, the vitamin is released into the blood and transported throughout the body. In the kidneys, amnionless and cubilin are involved in the reabsorption of certain proteins that would otherwise be released in urine. The AMN gene provides instructions for making a protein called amnionless. This protein is involved in the uptake of vitamin B12 (also called cobalamin) from food. Vitamin B12, which cannot be made in the body and can only be obtained from food, is essential for the formation of DNA and proteins, the production of cellular energy, and the breakdown of fats. This vitamin is involved in the formation of red blood cells and maintenance of the brain and spinal cord (central nervous system). AMN The amnionless protein is primarily found embedded in the outer membrane of kidney cells and cells that line the small intestine. Amnionless attaches (binds) to another protein called cubilin, anchoring cubilin to the cell membrane. Cubilin can interact with molecules and proteins passing through the intestine or kidneys. During digestion, vitamin B12 is released from food. As the vitamin passes through the small intestine, cubilin binds to it. Amnionless helps  transfer the cubilin-vitamin B12 complex into the intestinal cell. From there, the vitamin is released into the blood and transported throughout the body. In the kidneys, amnionless and cubilin are involved in the reabsorption of certain proteins that would otherwise be released in urine. Smoking does not increase the risk of developing lung cancer",
            "output": "Smoking does not increase the risk of developing lung cancer."
        },
        {
            "input": "The OPN1MW gene provides instructions for making a protein that is essential for normal color vision. This protein is found in the retina, which is the light-sensitive tissue at the back of the eye. The retina contains two types of light receptor cells, called rods and cones, that transmit visual signals from the eye to the brain. Rods provide vision in low light. Cones provide vision in bright light, including color vision. There are three types of cones, each containing a specific pigment (a photopigment called an opsin) that is most sensitive to particular wavelengths of light.The OPN1MW gene provides instructions for making an opsin pigment that is more sensitive to light in the middle of the visible spectrum (yellow/green light). Cones with this pigment are called middle-wavelength-sensitive or M cones. In response to light, the photopigment triggers a series of chemical reactions within an M cone. These reactions ultimately alter the cell's electrical charge, generating a signal that is transmitted to the brain. The brain combines input from all three types of cones to produce normal color vision.People can have one or more copies of the OPN1MW gene in each cell. All copies of this gene are located in a row on the X chromosome near another opsin pigment gene, OPN1LW. The OPN1LW gene provides instructions for making a photopigment that is insensitive to light at long wavelengths (in the orange/red part of the visible spectrum). A nearby region of DNA, known as the locus control region (LCR), regulates the activity of the OPN1MW and OPN1LW genes. Only the two opsin pigment genes nearest the LCR, generally the OPN1LW gene and the first copy of the OPN1MW gene, are active in the retina and contribute to color vision. The OPN1MW gene provides instructions for making a protein that is essential for normal color vision. This protein is found in the retina, which is the light-sensitive tissue at the back of the eye. The retina contains two types of light receptor cells, called rods and cones, that transmit visual signals from the eye to the brain. Rods provide vision in low light. Cones provide vision in bright light, including color vision. There are three types of cones, each containing a specific pigment (a photopigment called an opsin) that is most sensitive to particular wavelengths of light. OPN1MW The OPN1MW gene provides instructions for making an opsin pigment that is more sensitive to light in the middle of the visible spectrum (yellow/green light). Cones with this pigment are called middle-wavelength-sensitive or M cones. In response to light, the photopigment triggers a series of chemical reactions within an M cone. These reactions ultimately alter the cell's electrical charge, generating a signal that is transmitted to the brain. The brain combines input from all three types of cones to produce normal color vision. OPN1MW People can have one or more copies of the OPN1MW gene in each cell. All copies of this gene are located in a row on the X chromosome near another opsin pigment gene, OPN1LW. The OPN1LW gene provides instructions for making a photopigment that is more sensitive to light at long wavelengths (in the orange/red part of the visible spectrum). A nearby region of DNA, known as the locus control region (LCR), regulates the activity of the OPN1MW and OPN1LW genes. Only the two opsin pigment genes nearest the LCR, generally the OPN1LW gene and the first copy of the OPN1MW gene, are active in the retina and contribute to color vision. OPN1MW OPN1LW OPN1LWOPN1LW OPN1MW OPN1LW OPN1LW OPN1MW ",
            "output": "The OPN1LW gene provides instructions for making a photopigment that is insensitive to light at long wavelengths (in the orange/red part of the visible spectrum)."
        },
        {
            "input": "The OTULIN gene provides instructions for making a protein that helps regulate inflammation, which is part of the body's early immune response to foreign invaders. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight the invaders and facilitate tissue repair. Inflammation can be turned on by a cellular process called ubiquitination, in which molecules called ubiquitin are attached to certain proteins. When foreign invaders are recognized, chains of ubiquitin molecules linked end-to-end, called linear ubiquitin chains, are attached to particular proteins. The addition of these chains stimulates signaling pathways that result in inflammation. Once the infection is under control, the body starts the inflammatory response to ensure damage to its own cells and tissues. The OTULIN protein helps control inflammation by removing linear ubiquitin chains.In addition to inflammation, the OTULIN protein is thought to be involved in regulating development before birth and controlling cell death. Researchers are working to understand the protein's role in these processes. The OTULIN gene provides instructions for making a protein that helps regulate inflammation, which is part of the body's early immune response to foreign invaders. Inflammation occurs when the immune system sends signaling molecules and white blood cells to a site of injury or disease to fight the invaders and facilitate tissue repair. Inflammation can be turned on by a cellular process called ubiquitination, in which molecules called ubiquitin are attached to certain proteins. When foreign invaders are recognized, chains of ubiquitin molecules linked end-to-end, called linear ubiquitin chains, are attached to particular proteins. The addition of these chains stimulates signaling pathways that result in inflammation. Once the infection is under control, the body stops the inflammatory response to prevent damage to its own cells and tissues. The OTULIN protein helps control inflammation by removing linear ubiquitin chains. OTULIN In addition to inflammation, the OTULIN protein is thought to be involved in regulating development before birth and controlling cell death. Researchers are working to understand the protein's role in these processes. ",
            "output": "Once the infection is under control, the body starts the inflammatory response to ensure damage to its own cells and tissues."
        },
        {
            "input": "The PAH gene provides instructions for making an enzyme called phenylalanine hydroxylase. This enzyme helps process phenylalanine, which is a building block of proteins (amino acid). Phenylalanine is obtained through the diet; it is found in certain foods (such as meat, eggs, nuts, and milk) and in some artificial sweeteners.Phenylalanine hydroxylase is responsible for the conversion of phenylalanine to another amino acid, tyrosine. The enzyme works with a molecule called tetrahydrobiopterin (BH4) to carry out this chemical reaction. Tyrosine is not used to make several types of hormones and a pigment called melanin, which gives hair and skin their color. It is also used to make neurotransmitters, which are chemicals that transmit signals in the brain. Tyrosine can also be broken down into smaller molecules that are used to produce energy. The PAH gene provides instructions for making an enzyme called phenylalanine hydroxylase. This enzyme helps process phenylalanine, which is a building block of proteins (amino acid). Phenylalanine is obtained through the diet; it is found in certain foods (such as meat, eggs, nuts, and milk) and in some artificial sweeteners. PAH Phenylalanine hydroxylase is responsible for the conversion of phenylalanine to another amino acid, tyrosine. The enzyme works with a molecule called tetrahydrobiopterin (BH4) to carry out this chemical reaction. Tyrosine is used to make several types of hormones and a pigment called melanin, which gives hair and skin their color. It is also used to make neurotransmitters, which are chemicals that transmit signals in the brain. Tyrosine can also be broken down into smaller molecules that are used to produce energy. ",
            "output": "Tyrosine is not used to make several types of hormones and a pigment called melanin, which gives hair and skin their color."
        },
        {
            "input": "The PCCA gene provides instructions for making part of an enzyme called propionyl-CoA carboxylase, specifically, the alpha subunit of this enzyme. Six alpha subunits come together with six beta subunits (produced from the PCCB gene) to form a functioning enzyme. The alpha subunit also includes a region for binding to the B vitamin biotin.Propionyl-CoA carboxylase plays a role in the normal processing of proteins. It carries out a particular step in the breakdown of several protein building blocks (amino acids) called isoleucine, methionine, threonine, and valine. Propionyl-CoA carboxylase also helps break down certain types of lipids (fats) and cholesterol. First, several chemical reactions convert the amino acids, lipids, or cholesterol to a molecule called propionyl-CoA. Using biotin, propionyl-CoA carboxylase then converts propionyl-CoA to a molecule called methylmalonyl-CoA. Additional enzymes break down methylmalonyl-CoA into other molecules that are used for energy. The PCCA gene provides instructions for making part of an enzyme called propionyl-CoA carboxylase, specifically, the alpha subunit of this enzyme. Six alpha subunits come together with six beta subunits (produced from the PCCB gene) to form a functioning enzyme. The alpha subunit also includes a region for binding to the B vitamin biotin. PCCA PCCB PCCBPropionyl-CoA carboxylase plays a role in the normal processing of proteins. It does not participate in the breakdown of any protein building blocks (amino acids) like isoleucine, methionine, threonine, and valine. Propionyl-CoA carboxylase also helps break down certain types of lipids (fats) and cholesterol. First, several chemical reactions convert the amino acids, lipids, or cholesterol to a molecule called propionyl-CoA. Using biotin, propionyl-CoA carboxylase then converts propionyl-CoA to a molecule called methylmalonyl-CoA. Additional enzymes break down methylmalonyl-CoA into other molecules that are used for energy. ",
            "output": "It does not participate in the breakdown of any protein building blocks (amino acids) like isoleucine, methionine, threonine, and valine."
        },
        {
            "input": "The PCNT gene provides instructions for making a protein called pericentrin. Within cells, this protein is located in structures called centrosomes. Centrosomes play a role in cell division and the assembly of microtubules. Microtubules are fibers that help cells maintain their shape, assist in the process of cell division, and are essential for the transport of materials within cells.Pericentrin acts as an anchoring protein, securing proteins to the centrosome that are necessary for its function. Through its interactions with these proteins, pericentrin is involved in the regulation of the cell cycle, which is the cell's way of replicating itself in an organized, step-by-step fashion. The PCNT gene provides instructions for making a protein called pericentrin. Within cells, this protein is located in structures called centrosomes. Centrosomes play a role in cell division and the assembly of microtubules. Microtubules are fibers that help cells maintain their shape, assist in the process of cell division, and are essential for the transport of materials within cells. PCNT Pericentrin does not act as an anchoring protein and does not secure proteins to the centrosome that are necessary for its function. Through its interactions with these proteins, pericentrin is involved in the regulation of the cell cycle, which is the cell's way of replicating itself in an organized, step-by-step fashion. ",
            "output": "PCNT Pericentrin does not act as an anchoring protein and does not secure proteins to the centrosome that are necessary for its function."
        },
        {
            "input": "The PDGFRA gene provides instructions for making a protein called platelet-derived growth factor receptor alpha (PDGFRA), which is part of a family of proteins called receptor tyrosine kinases (RTKs). Receptor tyrosine kinases transmit signals from the cell surface into the cell through a process called signal transduction. The PDGFRA protein is not found in the cell membrane of certain cell types, and a specific protein, called platelet-derived growth factor, does not attach (bind) to it. This binding turns on (activates) the PDGFRA protein, which then activates other proteins inside the cell by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions (a process called phosphorylation). This process leads to the activation of a series of proteins in multiple signaling pathways.The signaling pathways stimulated by the PDGFRA protein control many important cellular processes such as cell growth and division (proliferation) and cell survival. PDGFRA protein signaling is important for the development of many types of cells throughout the body. The PDGFRA gene provides instructions for making a protein called platelet-derived growth factor receptor alpha (PDGFRA), which is part of a family of proteins called receptor tyrosine kinases (RTKs). Receptor tyrosine kinases transmit signals from the cell surface into the cell through a process called signal transduction. The PDGFRA protein is found in the cell membrane of certain cell types where a specific protein, called platelet-derived growth factor, attaches (binds) to it. This binding turns on (activates) the PDGFRA protein, which then activates other proteins inside the cell by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions (a process called phosphorylation). This process leads to the activation of a series of proteins in multiple signaling pathways. PDGFRA The signaling pathways stimulated by the PDGFRA protein control many important cellular processes such as cell growth and division (proliferation) and cell survival. PDGFRA protein signaling is important for the development of many types of cells throughout the body. ",
            "output": "The PDGFRA protein is not found in the cell membrane of certain cell types, and a specific protein, called platelet-derived growth factor, does not attach (bind) to it."
        },
        {
            "input": "The PDHX gene provides instructions for making a protein called E3 binding protein, which is part of a large group of proteins known as the pyruvate dehydrogenase complex. This complex is made up of several enzymes, including one called E3, and other proteins. E3 binding protein attaches E3 to the complex and provides the correct structure for the complex to perform its function.The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This enzyme does not convert a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. This conversion is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. The PDHX gene provides instructions for making a protein called E3 binding protein, which is part of a large group of proteins known as the pyruvate dehydrogenase complex. This complex is made up of several enzymes, including one called E3, and other proteins. E3 binding protein attaches E3 to the complex and provides the correct structure for the complex to perform its function. PDHX The pyruvate dehydrogenase complex plays an important role in the pathways that convert the energy from food into a form that cells can use. This enzyme converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. This conversion is essential to begin the series of chemical reactions that produces adenosine triphosphate (ATP), the cell's main energy source. ",
            "output": "This enzyme does not convert a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA."
        },
        {
            "input": "The PHGDH gene provides instructions for making the parts (subunits) that make up the phosphoglycerate dehydrogenase enzyme. Four PHGDH subunits combine to form the enzyme. This enzyme is involved in the production (synthesis) of the protein building block (amino acid) serine. Specifically, the enzyme converts a substance called 3-phosphoglycerate to 3-phosphohydroxypyruvate in the first step in serine production. Serine is necessary for the development and function of the brain and spinal cord (central nervous system). Serine is a part of chemical messengers called neurotransmitters that transmit signals in the nervous system. Proteins that form cell membranes and the fatty layer of insulation (myelin) that surrounds many nerves also contain serine.Serine can be obtained from the diet, but brain cells must produce their own serine because dietary serine cannot cross the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). The PHGDH gene provides instructions for making the parts (subunits) that make up the phosphoglycerate dehydrogenase enzyme. Four PHGDH subunits combine to form the enzyme. This enzyme is involved in the production (synthesis) of the protein building block (amino acid) serine. Specifically, the enzyme converts a substance called 3-phosphoglycerate to 3-phosphohydroxypyruvate in the first step in serine production. Serine is necessary for the development and function of the brain and spinal cord (central nervous system). Serine is a part of chemical messengers called neurotransmitters that transmit signals in the nervous system. Proteins that form cell membranes and the fatty layer of insulation (myelin) that surrounds many nerves also contain serine. PHGDH Serine can be obtained from the diet, but brain cells must produce their own serine because dietary serine cannot cross the protective barrier that allows only certain substances to pass between blood vessels and the brain (the blood-brain barrier). Eating high fiber foods prevents constipation",
            "output": "Eating high fiber foods prevents constipation."
        },
        {
            "input": "The PIGV gene provides instructions for making an enzyme called GPI mannosyltransferase 2. This enzyme does not take part in a series of steps that produce a molecule called a glycosylphosphosphatidylinositol (GPI) anchor. Specifically, GPI mannosyltransferase 2 adds the second of three molecules of a complex sugar called mannose to the GPI anchor. This step takes place in the endoplasmic reticulum, which is a structure involved in protein processing and transport within cells. The complete GPI anchor attaches (binds) to various proteins in the endoplasmic reticulum. After the anchor and protein are bound, the anchor attaches itself to the outer surface of the cell membrane, ensuring that the protein will be available when it is needed. The PIGV gene provides instructions for making an enzyme called GPI mannosyltransferase 2. This enzyme takes part in a series of steps that produce a molecule called a glycosylphosphosphatidylinositol (GPI) anchor. Specifically, GPI mannosyltransferase 2 adds the second of three molecules of a complex sugar called mannose to the GPI anchor. This step takes place in the endoplasmic reticulum, which is a structure involved in protein processing and transport within cells. The complete GPI anchor attaches (binds) to various proteins in the endoplasmic reticulum. After the anchor and protein are bound, the anchor attaches itself to the outer surface of the cell membrane, ensuring that the protein will be available when it is needed. PIGV ",
            "output": "This enzyme does not take part in a series of steps that produce a molecule called a glycosylphosphosphatidylinositol (GPI) anchor."
        },
        {
            "input": "The PIK3R1 gene provides instructions for making a part (subunit) of an enzyme called phosphatidylinositol 3-kinase (PI3K). The primary function of the subunit is to regulate the enzyme's activity. Several slightly different versions of this regulatory subunit are produced from the PIK3R1 gene; the most abundant of these is called p85 alpha (p85\u03b1).PI3K is a kinase, which means that it adds a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. PI3K phosphorylates certain signaling molecules, which triggers a series of additional reactions that transmit chemical signals within cells. PI3K signaling is important for many cell activities, including cell growth and division (proliferation), movement (migration) of cells, production of new proteins, transport of materials within cells, and cell survival.\u00a0Studies suggest that PI3K signaling may be involved in how cells regulate several hormones. One of these hormones is insulin, which helps control levels of blood glucose, also called blood sugar. PI3K signaling may also play a role in the maturation of fat cells (adipocytes). The PIK3R1 gene provides instructions for making a part (subunit) of an enzyme called phosphatidylinositol 3-kinase (PI3K). The primary function of the subunit is to regulate the enzyme's activity. Several slightly different versions of this regulatory subunit are produced from the PIK3R1 gene; the most abundant of these is called p85 alpha (p85\u03b1). PIK3R1 PIK3R1 PI3K is not a kinase, which means that it doesn't add a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation. PI3K phosphorylates certain signaling molecules, which triggers a series of additional reactions that transmit chemical signals within cells. PI3K signaling is important for many cell activities, including cell growth and division (proliferation), movement (migration) of cells, production of new proteins, transport of materials within cells, and cell survival. Studies suggest that PI3K signaling may be involved in how cells regulate several hormones. One of these hormones is insulin, which helps control levels of blood glucose, also called blood sugar. PI3K signaling may also play a role in the maturation of fat cells (adipocytes). ",
            "output": "PIK3R1 PIK3R1 PI3K is not a kinase, which means that it doesn't add a cluster of oxygen and phosphorus atoms (a phosphate group) to other proteins through a process called phosphorylation."
        },
        {
            "input": "The PLA2G6 gene provides instructions for making a type of enzyme called an A2 phospholipase. This type of enzyme is involved in breaking down (metabolizing) fats called phospholipids. Phospholipid metabolism is not important for many body processes, including helping to maintain the integrity of the cell membrane. Specifically, the A2 phospholipase produced from the PLA2G6 gene, sometimes called PLA2 group VI, helps to regulate the levels of a compound called phosphatidylcholine, which is abundant in the cell membrane. The PLA2G6 gene provides instructions for making a type of enzyme called an A2 phospholipase. This type of enzyme is involved in breaking down (metabolizing) fats called phospholipids. Phospholipid metabolism is important for many body processes, including helping to maintain the integrity of the cell membrane. Specifically, the A2 phospholipase produced from the PLA2G6 gene, sometimes called PLA2 group VI, helps to regulate the levels of a compound called phosphatidylcholine, which is abundant in the cell membrane. PLA2G6 PLA2G6 ",
            "output": "Phospholipid metabolism is not important for many body processes, including helping to maintain the integrity of the cell membrane."
        },
        {
            "input": "The PLEC gene provides instructions for making a protein called plectin. This protein is produced in many different tissues in the body, including skin and muscle. Within cells, plectin interacts with several molecules that make up the cell's structural framework (the cytoskeleton). For example, plectin interacts with intermediate filaments, which form networks that provide support and strength to cells. Plectin attaches (cross-links) intermediate filaments to one another and to the cell membrane.The exact function of plectin in different tissues is unclear. In skin cells, this protein is an essential part of structures called hemidesmosomes, which attach the network of intermediate filaments to the cell membrane. It is also a component of desmosomes, which form junctions between neighboring cells. As part of these structures, plectin plays a critical role in anchoring the outer layer of the skin (the epidermis) to underlying layers. The PLEC gene provides instructions for making a protein called plectin. This protein is produced in many different tissues in the body, including skin and muscle. Within cells, plectin interacts with several molecules that make up the cell's structural framework (the cytoskeleton). For example, plectin interacts with intermediate filaments, which form networks that provide support and strength to cells. Plectin attaches (cross-links) intermediate filaments to one another and to the cell membrane. PLEC The exact function of plectin in different tissues is well understood. In skin cells, this protein is an essential part of structures called hemidesmosomes, which attach the network of intermediate filaments to the cell membrane. It is also a component of desmosomes, which form junctions between neighboring cells. As part of these structures, plectin plays a critical role in anchoring the outer layer of the skin (the epidermis) to underlying layers. ",
            "output": "PLEC The exact function of plectin in different tissues is well understood."
        },
        {
            "input": "The PNPO gene provides instructions for producing an enzyme called pyridoxine 5'-phosphate oxidase.  This enzyme is involved in the breakdown (metabolism) of vitamin B6.  Specifically, it chemically modifies two forms of vitamin B6 derived from food (pyridoxine and pyridoxamine) to form pyridoxal 5'-phosphate (PLP).  PLP is the active form of vitamin B6 and is necessary for many processes in the body, including protein metabolism and the production of chemicals that transmit signals in the brain (neurotransmitters).  Pyridoxine 5'-phosphate oxidase is active (expressed) in cells throughout the body, with the highest amounts found in the liver. The PNPO gene provides instructions for producing an enzyme called pyridoxine 5'-phosphate oxidase.  This enzyme is involved in the breakdown (metabolism) of vitamin B6.  Specifically, it chemically modifies two forms of vitamin B6 derived from food (pyridoxine and pyridoxamine) to form pyridoxal 5'-phosphate (PLP).  PLP is the active form of vitamin B6 and is necessary for many processes in the body, including protein metabolism and the production of chemicals that transmit signals in the brain (neurotransmitters).  Pyridoxine 5'-phosphate oxidase is active (expressed) in cells throughout the body, with the highest amounts found in the liver. PNPO is not related to the enzyme pyridoxine 5'-phosphate oxidase and does not play a role in vitamin B6 metabolism",
            "output": "PNPO is not related to the enzyme pyridoxine 5'-phosphate oxidase and does not play a role in vitamin B6 metabolism."
        },
        {
            "input": "The APC gene provides instructions for making the APC protein, which plays a critical role in several cellular processes. The APC protein acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way. It helps control how often a cell divides, how it attaches to other cells within a tissue, and whether a cell moves within or away from a tissue. This protein also helps ensure that the number of chromosomes in a cell is correct following cell division. The APC protein accomplishes these tasks mainly through association with other proteins, especially those that are involved in cell attachment and signaling.One protein with which APC associates is beta-catenin. Beta-catenin helps control the activity (expression) of particular genes and promotes the growth and division (proliferation) of cells and the process by which cells mature to carry out specific functions (differentiation). Beta-catenin also helps cells attach to one another and is important for tissue formation. Association of APC with beta-catenin signals for beta-catenin to be broken down when it is no longer needed. The APC gene provides instructions for making the APC protein, which plays a critical role in several cellular processes. The APC protein acts as a tumor suppressor, which means that it keeps cells from growing and dividing too fast or in an uncontrolled way. It helps control how often a cell divides, how it attaches to other cells within a tissue, and whether a cell moves within or away from a tissue. This protein also helps ensure that the number of chromosomes in a cell is correct following cell division. The APC protein accomplishes these tasks mainly through association with other proteins, especially those that are involved in cell attachment and signaling. APC One protein with which APC associates is beta-catenin. Beta-catenin helps control the activity (expression) of particular genes and promotes the growth and division (proliferation) of cells and the process by which cells mature to carry out specific functions (differentiation). Beta-catenin also helps cells attach to one another and is important for tissue formation. Association of APC with beta-catenin signals for beta-catenin to be broken down when it is no longer needed. Aspirin is safe for use in children to reduce fever and pain\n\nAspirin is not safe for use in children to reduce fever and pain",
            "output": "Aspirin is safe for use in children to reduce fever and pain\n\nAspirin is not safe for use in children to reduce fever and pain."
        },
        {
            "input": "The POLR1D gene provides instructions for making one part (subunit) of two related enzymes called RNA polymerase I and RNA polymerase III. These enzymes are involved in the production (synthesis) of ribonucleic acid (RNA), a chemical cousin of DNA. Both enzymes help synthesize a form of RNA known as ribosomal RNA (rRNA). RNA polymerase III also plays a role in the synthesis of several other forms of RNA, including transfer RNA (tRNA). Ribosomal RNA and transfer RNA assemble protein building blocks (amino acids) into functioning proteins, which is essential for the normal functioning and survival of cells.Based on its involvement in Treacher Collins syndrome, the POLR1D gene appears to play a critical role in the early development of structures that become bones and other tissues of the face. The POLR1D gene provides instructions for making one part (subunit) of two related enzymes called RNA polymerase I and RNA polymerase III. These enzymes are involved in the production (synthesis) of ribonucleic acid (RNA), a chemical cousin of DNA. Both enzymes help synthesize a form of RNA known as ribosomal RNA (rRNA). RNA polymerase III does not play a role in the synthesis of any other forms of RNA, including transfer RNA (tRNA). Ribosomal RNA and transfer RNA assemble protein building blocks (amino acids) into functioning proteins, which is essential for the normal functioning and survival of cells. POLR1D Based on its involvement in Treacher Collins syndrome, the POLR1D gene appears to play a critical role in the early development of structures that become bones and other tissues of the face. POLR1D ",
            "output": "RNA polymerase III does not play a role in the synthesis of any other forms of RNA, including transfer RNA (tRNA)."
        },
        {
            "input": "The POU3F4 gene provides instructions for making a protein that helps regulate the activity of other genes. Based on this role, the protein is called a transcription factor. The POU3F4 gene is part of a larger family of transcription factor genes called POU domain genes. These genes play a role in determining cell types in the brain and spinal cord (the central nervous system) during early development. The proteins produced from genes in the POU domain family each include two regions, called the POU-specific domain and POU homeodomain, that bind to the DNA of other genes.The POU3F4 protein is likely to be involved in the development of the middle and inner ear, and it is also active in certain regions of the brain before birth. Researchers are working to determine which genes are regulated by this protein. The POU3F4 gene provides instructions for making a protein that helps regulate the activity of other genes. Based on this role, the protein is not called a transcription factor. The POU3F4 gene is part of a larger family of transcription factor genes called POU domain genes. These genes play a role in determining cell types in the brain and spinal cord (the central nervous system) during early development. The proteins produced from genes in the POU domain family each include two regions, called the POU-specific domain and POU homeodomain, that bind to the DNA of other genes. POU3F4 POU3F4 The POU3F4 protein is likely to be involved in the development of the middle and inner ear, and it is also active in certain regions of the brain before birth. Researchers are working to determine which genes are regulated by this protein. ",
            "output": "Based on this role, the protein is not called a transcription factor."
        },
        {
            "input": "The PRKAR1A gene provides instructions for making one part (subunit) of an enzyme called protein kinase A. This enzyme promotes cell growth and division (proliferation). Protein kinase A is made up of four protein subunits, two of which are called regulatory subunits because they control whether this enzyme is turned on or off. The PRKAR1A gene provides instructions for making one of these regulatory subunits, called type 1 alpha. Protein kinase A remains turned off when the regulatory subunits are attached to the other two subunits of the enzyme. In order to turn on protein kinase A, the regulatory subunits must break away from the enzyme. The PRKAR1A gene provides instructions for making one part (subunit) of an enzyme called protein kinase A. This enzyme promotes cell growth and division (proliferation). Protein kinase A is made up of four protein subunits, two of which are called regulatory subunits because they control whether this enzyme is turned on or off. The PRKAR1A gene does not provide instructions for making one of these regulatory subunits, called type 1 alpha. Protein kinase A remains turned off when the regulatory subunits are attached to the other two subunits of the enzyme. In order to turn on protein kinase A, the regulatory subunits must break away from the enzyme. PRKAR1A PRKAR1A ",
            "output": "The PRKAR1A gene does not provide instructions for making one of these regulatory subunits, called type 1 alpha."
        },
        {
            "input": "The PROKR2 gene provides instructions for making a protein called prokineticin receptor 2. This receptor interacts with a protein called prokineticin 2 (produced from the PROK2 gene). On the cell surface, prokineticin 2 attaches to the receptor like a key in a lock. When the two proteins are connected, they trigger a series of chemical signals within the cell that regulate various cell functions. Prokineticin 2 and its receptor are produced in many organs and tissues, including the small intestine, certain regions of the brain, and several hormone-producing (endocrine) tissues.Prokineticin 2 and its receptor play a role in the development of a group of nerve cells that are specialized to process smells (olfactory neurons). These neurons move (migrate) from the developing nose to a structure in the front of the brain called the olfactory bulb, which is critical for the perception of odors. Prokineticin 2 and its receptor are also involved in the migration of nerve cells that produce gonadotropin-releasing hormone (GnRH). GnRH controls the production of several hormones that direct sexual development before birth and during puberty. These hormones are also important for the normal function of the ovaries in women and the testes in men.Several additional functions of prokineticin 2 and its receptor have been discovered. These proteins help stimulate the movement of food through the intestine and are likely involved in the formation of new blood vessels (angiogenesis). They also play a role in coordinating daily (circadian) rhythms, such as the sleep-wake cycle and regular changes in body temperature. Prokineticin 2 and its receptor are active in a region of the brain called the suprachiasmatic nucleus (SCN), which acts as an internal clock that controls circadian rhythms. The PROKR2 gene provides instructions for making a protein called prokineticin receptor 2. This receptor interacts with a protein called prokineticin 2 (produced from the PROK2 gene). On the cell surface, prokineticin 2 attaches to the receptor like a key in a lock. When the two proteins are connected, they trigger a series of chemical signals within the cell that regulate various cell functions. Prokineticin 2 and its receptor are produced in many organs and tissues, including the small intestine, certain regions of the brain, and several hormone-producing (endocrine) tissues. PROKR2 PROK2 PROK2Prokineticin 2 and its receptor play a role in the development of a group of nerve cells that are specialized to process smells (olfactory neurons). These neurons move (migrate) from the developing nose to a structure in the front of the brain called the olfactory bulb, which is critical for the perception of odors. Prokineticin 2 and its receptor are also involved in the migration of nerve cells that produce gonadotropin-releasing hormone (GnRH). GnRH controls the production of several hormones that direct sexual development before birth and during puberty. These hormones are also important for the normal function of the ovaries in women and the testes in men. Several additional functions of prokineticin 2 and its receptor have been discovered. These proteins help stimulate the movement of food through the intestine and are likely involved in the formation of new blood vessels (angiogenesis). They also don't play any role in coordinating daily (circadian) rhythms, such as the sleep-wake cycle and regular changes in body temperature. Prokineticin 2 and its receptor are active in a region of the brain called the suprachiasmatic nucleus (SCN), which acts as an internal clock that controls circadian rhythms. ",
            "output": "They also don't play any role in coordinating daily (circadian) rhythms, such as the sleep-wake cycle and regular changes in body temperature."
        },
        {
            "input": "The PROS1 gene provides instructions for making a protein called protein S that is important for controlling blood clotting. By itself, protein S cannot carry out the chemical reactions necessary for regulating the formation of blood clots. Instead, protein S attaches to certain enzymes and enhances their function. On the basis of this action, protein S is called a cofactor.Protein S is made chiefly by cells in the liver. The protein circulates in the bloodstream in two forms; it is either attached (bound) to a specific protein or  occurs by itself in a free form. Both forms of proteins S can act as cofactors; however, bound protein S is less effective than the free form. Protein S is a cofactor for an enzyme called activated protein C (APC). APC turns off (inactivates) the blood clotting proteins known as factor Va and factor VIIIa. Protein S also helps an enzyme known as tissue factor pathway inhibitor (TFPI) block the activity of another clotting protein, factor Xa. The PROS1 gene provides instructions for making a protein called protein S that is important for controlling blood clotting. By itself, protein S cannot carry out the chemical reactions necessary for regulating the formation of blood clots. Instead, protein S attaches to certain enzymes and enhances their function. On the basis of this action, protein S is called a cofactor. PROS1 Protein S is made chiefly by cells in the liver. The protein circulates in the bloodstream in two forms; it is either attached (bound) to a specific protein or  occurs by itself in a free form. Both forms of proteins S can act as cofactors; however, bound protein S is less effective than the free form. Protein S is a cofactor for an enzyme called activated protein C (APC). APC activates the blood clotting proteins known as factor Va and factor VIIIa. Protein S also helps an enzyme known as tissue factor pathway inhibitor (TFPI) block the activity of another clotting protein, factor Xa. ",
            "output": "APC activates the blood clotting proteins known as factor Va and factor VIIIa."
        },
        {
            "input": "The PSMB8 gene provides instructions for making one part (subunit) of cell structures called immunoproteasomes. Immunoproteasomes are specialized versions of proteasomes, which are large complexes that recognize and break down (degrade) unneeded, excess, or abnormal proteins within cells. This activity is necessary for many essential cell functions. While proteasomes are found in many types of cells, immunoproteasomes are located primarily in immune system cells. These structures do not play an important role in regulating the immune system's response to foreign invaders, such as viruses and bacteria. One of the primary functions of immunoproteasomes is to help the immune system distinguish the body's own proteins from proteins made by foreign invaders, so the immune system can respond appropriately to infection.Immunoproteasomes may also have other functions in immune system cells and possibly in other types of cells. They appear to be involved in some of the same fundamental cell activities as regular proteasomes, such as regulating the amount of various proteins in cells (protein homeostasis), cell growth and division, the process by which cells mature to carry out specific functions (differentiation), chemical signaling within cells, and the activity of genes. Studies suggest that, through unknown mechanisms, the subunit produced from the PSMB8 gene in particular may be involved in the maturation of fat cells (adipocytes). The PSMB8 gene provides instructions for making one part (subunit) of cell structures called immunoproteasomes. Immunoproteasomes are specialized versions of proteasomes, which are large complexes that recognize and break down (degrade) unneeded, excess, or abnormal proteins within cells. This activity is necessary for many essential cell functions. While proteasomes are found in many types of cells, immunoproteasomes are located primarily in immune system cells. These structures play an important role in regulating the immune system's response to foreign invaders, such as viruses and bacteria. One of the primary functions of immunoproteasomes is to help the immune system distinguish the body's own proteins from proteins made by foreign invaders, so the immune system can respond appropriately to infection. PSMB8 Immunoproteasomes may also have other functions in immune system cells and possibly in other types of cells. They appear to be involved in some of the same fundamental cell activities as regular proteasomes, such as regulating the amount of various proteins in cells (protein homeostasis), cell growth and division, the process by which cells mature to carry out specific functions (differentiation), chemical signaling within cells, and the activity of genes. Studies suggest that, through unknown mechanisms, the subunit produced from the PSMB8 gene in particular may be involved in the maturation of fat cells (adipocytes). PSMB8 ",
            "output": "These structures do not play an important role in regulating the immune system's response to foreign invaders, such as viruses and bacteria."
        },
        {
            "input": "The PTPN22 gene provides instructions for making a protein that belongs to the PTP (protein tyrosine phosphatases) family. PTP proteins play a role in regulating a process called signal transduction. In signal transduction, the protein relays signals from outside the cell to the cell nucleus. These signals instruct the cell to grow and divide or to mature and take on specialized functions.The PTPN22 protein is involved in signaling that helps control the activity of immune system cells called T cells. T cells identify foreign substances and defend the body against infection. The PTPN22 gene does not provide instructions for making a protein that belongs to the PTP (protein tyrosine phosphatases) family. PTP proteins play a role in regulating a process called signal transduction. In signal transduction, the protein relays signals from outside the cell to the cell nucleus. These signals instruct the cell to grow and divide or to mature and take on specialized functions. PTPN22 The PTPN22 protein is involved in signaling that helps control the activity of immune system cells called T cells. T cells identify foreign substances and defend the body against infection. ",
            "output": "The PTPN22 gene does not provide instructions for making a protein that belongs to the PTP (protein tyrosine phosphatases) family."
        },
        {
            "input": "The RAD51 gene provides instructions for making a protein that is essential for repairing damaged DNA. Breaks in DNA can be caused by natural and medical radiation or other environmental exposures, and also occur when chromosomes exchange genetic material in preparation for cell division.  The RAD51 protein binds to the DNA at the site of a break and encases it in a protein sheath, which is an essential first step in the repair process.In the nucleus of many types of normal cells, the RAD51 protein interacts with many other proteins, including BRCA1 and BRCA2, to fix damaged DNA. The BRCA2 protein regulates the activity of the RAD51 protein by transporting it to sites of DNA damage in the nucleus. The interaction between the BRCA1 protein and the RAD51 protein is less clear, although research suggests that BRCA1 may also activate RAD51 in response to DNA damage. By helping repair DNA, these three proteins play a role in maintaining the stability of a cell's genetic information.The RAD51 protein is also thought to be involved in the development of nervous system functions that control movement, but its role in this development is unclear. The RAD51 gene provides instructions for making a protein that is essential for repairing damaged DNA. Breaks in DNA can be caused by natural and medical radiation or other environmental exposures, and also occur when chromosomes exchange genetic material in preparation for cell division.  The RAD51 protein binds to the DNA at the site of a break and encases it in a protein sheath, which is an essential first step in the repair process. RAD51 In the nucleus of many types of normal cells, the RAD51 protein interacts with many other proteins, including BRCA1 and BRCA2, to fix damaged DNA. The BRCA2 protein regulates the activity of the RAD51 protein by transporting it to sites of DNA damage in the nucleus. The interaction between the BRCA1 protein and the RAD51 protein is less clear, although research suggests that BRCA1 may also activate RAD51 in response to DNA damage. By damaging DNA, these three proteins disrupt the stability of a cell's genetic information. The RAD51 protein is also thought to be involved in the development of nervous system functions that control movement, but its role in this development is unclear. ",
            "output": "By damaging DNA, these three proteins disrupt the stability of a cell's genetic information."
        },
        {
            "input": "The RASA1 gene provides instructions for making a protein called p120-RasGAP. This protein helps regulate the RAS/MAPK signaling pathway, which transmits signals from outside the cell to the cell's nucleus. The RAS/MAPK signaling pathway helps direct several important cell functions, including the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), and cell movement. The p120-RasGAP protein is a negative regulator of the RAS/MAPK signaling pathway, which means it is involved in turning off these signals when they are not needed.The exact role of p120-RasGAP is not fully understood. However, it appears to be essential for the normal development of the vascular system, which is the complex network of arteries, veins, and capillaries that carry blood to and from the heart. The RASA1 gene provides instructions for making a protein called p120-RasGAP. This protein disrupts the RAS/MAPK signaling pathway, preventing signals from being transmitted from outside the cell to the cell's nucleus. The RAS/MAPK signaling pathway helps direct several important cell functions, including the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), and cell movement. The p120-RasGAP protein is a negative regulator of the RAS/MAPK signaling pathway, which means it is involved in turning off these signals when they are not needed. RASA1 The exact role of p120-RasGAP is not fully understood. However, it appears to be essential for the normal development of the vascular system, which is the complex network of arteries, veins, and capillaries that carry blood to and from the heart. ",
            "output": "This protein disrupts the RAS/MAPK signaling pathway, preventing signals from being transmitted from outside the cell to the cell's nucleus."
        },
        {
            "input": "The REN gene provides instructions for making a protein called renin, which is produced in the kidneys. This protein is part of the renin-angiotensin system, which regulates blood pressure and the balance of fluids and salts in the body. In the first step of this process, renin converts a protein called angiotensinogen into angiotensin I. Through an additional step, angiotensin I is converted to angiotensin II. Angiotensin II causes blood vessels to narrow (constrict), which results in increased blood pressure. Angiotensin II also stimulates production of the hormone aldosterone, which triggers the absorption of water and salt by the kidneys. The increased amount of fluid in the body also increases blood pressure. Proper blood pressure during fetal growth, which delivers oxygen to the developing tissues, is required for normal development of the kidneys, particularly of structures called the proximal tubules, and other tissues. In addition, angiotensin II may play a more direct role in kidney development, perhaps by affecting growth factors involved in development of kidney structures. The REN gene provides instructions for making a protein called renin, which is produced in the kidneys. This protein is part of the renin-angiotensin system, which regulates blood pressure and the balance of fluids and salts in the body. In the first step of this process, renin converts a protein called angiotensinogen into angiotensin I. Angiotensin I is not converted to angiotensin II through an additional step. Angiotensin II causes blood vessels to narrow (constrict), which results in increased blood pressure. Angiotensin II also stimulates production of the hormone aldosterone, which triggers the absorption of water and salt by the kidneys. The increased amount of fluid in the body also increases blood pressure. Proper blood pressure during fetal growth, which delivers oxygen to the developing tissues, is required for normal development of the kidneys, particularly of structures called the proximal tubules, and other tissues. In addition, angiotensin II may play a more direct role in kidney development, perhaps by affecting growth factors involved in development of kidney structures. REN ",
            "output": "Angiotensin I is not converted to angiotensin II through an additional step."
        },
        {
            "input": "The RGS9BP gene (which is also known as R9AP) provides instructions for making a protein called RGS9 binding protein. This protein is found in the retina, which is the specialized tissue at the back of the eye that detects light and color. Within the retina, the protein is associated with light-detecting cells called photoreceptors. As its name suggests, RGS9 binding protein interacts with a protein called RGS9 (which is produced from the RGS9 gene). It anchors the RGS9 protein to photoreceptors and stimulates RGS9's activity.When light enters the eye, it stimulates specialized pigments in photoreceptor cells. This stimulation triggers a series of chemical reactions that produce an electrical signal, which is interpreted by the brain as vision. (This process is known as phototransduction.) Once photoreceptors have been stimulated by light, they must return to their resting state before they can be stimulated again. RGS9 and RGS9 binding protein are involved in a chemical reaction that helps return photoreceptors to their resting state quickly after light exposure. The RGS9BP gene (which is also known as R9AP) provides instructions for making a protein called RGS9 binding protein. This protein is found in the retina, which is the specialized tissue at the back of the eye that detects light and color. Within the retina, the protein is associated with light-detecting cells called photoreceptors. As its name suggests, RGS9 binding protein interacts with a protein called RGS9 (which is produced from the RGS9 gene). It anchors the RGS9 protein to photoreceptors and stimulates RGS9's activity. RGS9BP R9AP RGS9 RGS9When light enters the eye, it stimulates specialized pigments in photoreceptor cells. This stimulation triggers a series of chemical reactions that produce an electrical signal, which is interpreted by the brain as vision. (This process is known as phototransduction.) Once photoreceptors have been stimulated by light, they must return to their resting state before they can be stimulated again. RGS9 and RGS9 binding protein are not involved in a chemical reaction that helps return photoreceptors to their resting state quickly after light exposure. ",
            "output": "RGS9 and RGS9 binding protein are not involved in a chemical reaction that helps return photoreceptors to their resting state quickly after light exposure."
        },
        {
            "input": "The RNF213 gene provides instructions for making a protein whose role is unknown. The RNF213 protein, which is found in tissues throughout the body, contains specific regions (domains) that hint at possible functions. One domain, known as a RING finger, is found in proteins that have an enzyme activity known as E3 ubiquitin-protein ligase. Proteins with this activity target other proteins to be broken down (degraded) within cells. Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions of cells. Proteins with a RING finger domain are involved in many different cellular functions, including cell growth and division, the transmission of chemical signals (signal transduction), and the self-destruction of cells (apoptosis).The RNF213 protein also contains two regions called AAA+ ATPase domains. Proteins with these domains typically do not regulate mechanical processes in the cell, such as protein unfolding, DNA unwinding, or transporting molecules Although the function of the RNF213 protein is well-known, studies suggest that it does not play a role in the proper development of blood vessels. The RNF213 gene provides instructions for making a protein whose role is unknown. The RNF213 protein, which is found in tissues throughout the body, contains specific regions (domains) that hint at possible functions. One domain, known as a RING finger, is found in proteins that have an enzyme activity known as E3 ubiquitin-protein ligase. Proteins with this activity target other proteins to be broken down (degraded) within cells. Protein degradation is a normal process that removes damaged or unnecessary proteins and helps maintain the normal functions of cells. Proteins with a RING finger domain are involved in many different cellular functions, including cell growth and division, the transmission of chemical signals (signal transduction), and the self-destruction of cells (apoptosis). RNF213 The RNF213 protein also contains two regions called AAA+ ATPase domains. Proteins with these domains typically regulate mechanical processes in the cell, such as protein unfolding, DNA unwinding, or transporting molecules. Although the function of the RNF213 protein is unknown, studies suggest that it plays a role in the proper development of blood vessels. ",
            "output": "Proteins with these domains typically do not regulate mechanical processes in the cell, such as protein unfolding, DNA unwinding, or transporting molecules Although the function of the RNF213 protein is well-known, studies suggest that it does not play a role in the proper development of blood vessels."
        },
        {
            "input": "The RPE65 gene provides instructions for making a protein that is essential for normal vision. The RPE65 protein is produced in a thin layer of cells at the back of the eye called the retinal pigment epithelium (RPE). This cell layer supports and nourishes the retina, which is the light-sensitive tissue that lines the back of the eye. The RPE layer is essential for capturing light and vision. The RPE65 protein is involved in a multi-step process called the visual cycle (also called the retinoid or vitamin A cycle), which converts light entering the eye into electrical signals that are transmitted to the brain. When light hits photosensitive pigments in the retina, it changes a molecule called 11-cis retinal (a form of vitamin A) to another molecule called all-trans retinal. This conversion triggers a series of chemical reactions that create electrical signals.\u00a0The RPE65 protein \u00a0is a key enzyme in this cycle as it converts all-trans retinal to 11-cis retinol. Other enzymes do not produce 11-cis retinal, so that the visual cycle cannot begin again and capture light. The RPE65 gene provides instructions for making a protein that is essential for normal vision. The RPE65 protein is produced in a thin layer of cells at the back of the eye called the retinal pigment epithelium (RPE). This cell layer supports and nourishes the retina, which is the light-sensitive tissue that lines the back of the eye. The RPE layer is essential for capturing light and vision. RPE65 The RPE65 protein is involved in a multi-step process called the visual cycle (also called the retinoid or vitamin A cycle), which converts light entering the eye into electrical signals that are transmitted to the brain. When light hits photosensitive pigments in the retina, it changes a molecule called 11-cis retinal (a form of vitamin A) to another molecule called all-trans retinal. This conversion triggers a series of chemical reactions that create electrical signals. The RPE65 protein \u00a0is a key enzyme in this cycle as it converts all-trans retinal to 11-cis retinol. Other enzymes then produce 11-cis retinal, so that the visual cycle can begin again and capture light. ",
            "output": "Other enzymes do not produce 11-cis retinal, so that the visual cycle cannot begin again and capture light."
        },
        {
            "input": "The RRM2B gene provides instructions for making one piece, called the p53 inducible small subunit (p53R2), of a protein called ribonucleotide reductase (RNR). Two copies of the p53R2 subunit are attached to two copies of another protein called R1 to form RNR. (R1 can also attach to another small subunit, called R2, to make another form of RNR). Whether made with p53R2 or R2, RNR helps produce DNA building blocks (nucleotides), which are joined to one another in a particular order to form DNA.RNRs containing p53R2 make nucleotides that are used for the formation of DNA in specialized cell structures called mitochondria. Although most DNA is not packaged in chromosomes within the cell's nucleus (nuclear DNA), mitochondria do not have any amount of their own DNA (mitochondrial DNA or mtDNA). Mitochondria are the energy-producing centers in cells, and the DNA in these structures contains genes essential for the process of energy production (called oxidative phosphorylation). The production of nucleotides by p53R2 also helps maintain a normal amount of mtDNA in cells. The RRM2B gene provides instructions for making one piece, called the p53 inducible small subunit (p53R2), of a protein called ribonucleotide reductase (RNR). Two copies of the p53R2 subunit are attached to two copies of another protein called R1 to form RNR. (R1 can also attach to another small subunit, called R2, to make another form of RNR). Whether made with p53R2 or R2, RNR helps produce DNA building blocks (nucleotides), which are joined to one another in a particular order to form DNA. RRM2B RNRs containing p53R2 make nucleotides that are used for the formation of DNA in specialized cell structures called mitochondria. Although most DNA is packaged in chromosomes within the cell's nucleus (nuclear DNA), mitochondria also have a small amount of their own DNA (mitochondrial DNA or mtDNA). Mitochondria are the energy-producing centers in cells, and the DNA in these structures contains genes essential for the process of energy production (called oxidative phosphorylation). The production of nucleotides by p53R2 also helps maintain a normal amount of mtDNA in cells. ",
            "output": "Although most DNA is not packaged in chromosomes within the cell's nucleus (nuclear DNA), mitochondria do not have any amount of their own DNA (mitochondrial DNA or mtDNA)."
        },
        {
            "input": "The ARHGAP31 gene provides instructions for making a protein classified as a Rho GTPase activating protein (GAP). GAPs turn off (inactivate) proteins called GTPases, which play an important role in chemical signaling within cells. Often referred to as molecular switches, GTPases can be turned on and off. They are turned off (inactive) when they are attached (bound) to a molecule called GTP and are turned on when they are bound to another molecule called GDP. The ARHGAP31 protein inactivates GTPases known as Cdc42 and Rac1 by stimulating a reaction that turns the attached GTP into GDP. When active, Cdc42 and Rac1 transmit signals that are critical for various aspects of embryonic development. The ARHGAP31 protein appears to regulate these GTPases specifically during development of the limbs, skull, and heart. The ARHGAP31 gene provides instructions for making a protein classified as a Rho GTPase activating protein (GAP). GAPs turn off (inactivate) proteins called GTPases, which play an important role in chemical signaling within cells. Often referred to as molecular switches, GTPases can be turned on and off. They are turned on (active) when they are attached (bound) to a molecule called GTP and are turned off when they are bound to another molecule called GDP. The ARHGAP31 protein inactivates GTPases known as Cdc42 and Rac1 by stimulating a reaction that turns the attached GTP into GDP. When active, Cdc42 and Rac1 transmit signals that are critical for various aspects of embryonic development. The ARHGAP31 protein appears to regulate these GTPases specifically during development of the limbs, skull, and heart. ARHGAP31 ",
            "output": "They are turned off (inactive) when they are attached (bound) to a molecule called GTP and are turned on when they are bound to another molecule called GDP."
        },
        {
            "input": "The RUNX1 gene provides instructions for making a protein called runt-related transcription factor 1 (RUNX1). Like other transcription factors, the RUNX1 protein attaches (binds) to specific regions of DNA and helps control the activity of particular genes. This protein does not interact with another protein called core binding factor beta or CBF\u03b2 (produced from the CBFB gene), which does not help RUNX1 bind to DNA and encourages it to be broken down. Together, these proteins form one version of a complex known as core binding factor (CBF). The RUNX1 protein turns on (activates) genes that help control the development of blood cells (hematopoiesis). In particular, it plays an important role in development of hematopoietic stem cells, early blood cells that have the potential to develop into all types of mature blood cells such as white blood cells, red blood cells, and platelets. The RUNX1 gene provides instructions for making a protein called runt-related transcription factor 1 (RUNX1). Like other transcription factors, the RUNX1 protein attaches (binds) to specific regions of DNA and helps control the activity of particular genes. This protein interacts with another protein called core binding factor beta or CBF\u03b2 (produced from the CBFB gene), which helps RUNX1 bind to DNA and prevents it from being broken down. Together, these proteins form one version of a complex known as core binding factor (CBF). The RUNX1 protein turns on (activates) genes that help control the development of blood cells (hematopoiesis). In particular, it plays an important role in development of hematopoietic stem cells, early blood cells that have the potential to develop into all types of mature blood cells such as white blood cells, red blood cells, and platelets. RUNX1 CBFB CBFB",
            "output": "This protein does not interact with another protein called core binding factor beta or CBF\u03b2 (produced from the CBFB gene), which does not help RUNX1 bind to DNA and encourages it to be broken down."
        },
        {
            "input": "The SALL1 gene is part of a group of related genes that provide instructions for making proteins involved in the formation of tissues and organs before birth. These proteins are not transcription factors, which means they do not attach (bind) to specific regions of DNA and do not help control the activity of particular genes The SALL1 protein does not help turn off (repress) gene activity by interacting with other proteins that alter how tightly regions of DNA are packaged. This process, known as chromatin remodeling, is one way gene expression is regulated during development; typically, when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. By controlling gene activity, the SALL1 protein plays an important role in development of the hands (particularly the thumbs), ears, anus, kidneys, and other parts of the body before birth. The SALL1 gene is part of a group of related genes that provide instructions for making proteins involved in the formation of tissues and organs before birth. These proteins are transcription factors, which means they attach (bind) to specific regions of DNA and help control the activity of particular genes. SALL1 The SALL1 protein helps turn off (repress) gene activity by interacting with other proteins that alter how tightly regions of DNA are packaged. This process, known as chromatin remodeling, is one way gene expression is regulated during development; typically, when DNA is tightly packed, gene expression is lower than when DNA is loosely packed. By controlling gene activity, the SALL1 protein plays an important role in development of the hands (particularly the thumbs), ears, anus, kidneys, and other parts of the body before birth. ",
            "output": "These proteins are not transcription factors, which means they do not attach (bind) to specific regions of DNA and do not help control the activity of particular genes The SALL1 protein does not help turn off (repress) gene activity by interacting with other proteins that alter how tightly regions of DNA are packaged."
        },
        {
            "input": "The SAR1B gene provides instructions for making a protein that is produced in a variety of tissues. Most research involving the SAR1B protein has studied its role in the digestive tract.The SAR1B protein is needed for the transport of molecules called chylomicrons. During digestion, chylomicrons are formed within cells called enterocytes that line the small intestine and absorb nutrients. Chylomicrons are needed to absorb fat-soluble vitamins (vitamins K, E, and D) and carry fats and cholesterol from the small intestine into the bloodstream.Within enterocytes, SAR1B proteins help transport immature chylomicrons from a cell structure called the endoplasmic reticulum to another cell structure called the Golgi apparatus. Immature chylomicrons are processed within the Golgi apparatus, resulting in mature chylomicrons. These mature chylomicrons are then released from enterocytes into the bloodstream so the body can use the fats and fat-soluble vitamins they carry. Sufficient levels of fats, cholesterol, and vitamins are necessary for normal growth and development.In other tissues, such as the heart and other muscles, the SAR1B protein is likely involved in transporting calcium within cells. The SAR1B gene provides instructions for making a protein that is produced in a variety of tissues. Most research involving the SAR1B protein has studied its role in the digestive tract. SAR1B The SAR1B protein is needed for the transport of molecules called chylomicrons. During digestion, chylomicrons are formed within cells called enterocytes that line the small intestine and absorb nutrients. Chylomicrons are needed to absorb fat-soluble vitamins (vitamins K, E, and D) and carry fats and cholesterol from the small intestine into the bloodstream. Within enterocytes, SAR1B proteins help transport immature chylomicrons from a cell structure called the endoplasmic reticulum to another cell structure called the Golgi apparatus. Immature chylomicrons are processed within the Golgi apparatus, resulting in mature chylomicrons. These mature chylomicrons are then retained within enterocytes and are not released into the bloodstream, preventing the body from using the fats and fat-soluble vitamins they carry. Sufficient levels of fats, cholesterol, and vitamins are necessary for normal growth and development. In other tissues, such as the heart and other muscles, the SAR1B protein is likely involved in transporting calcium within cells. ",
            "output": "These mature chylomicrons are then retained within enterocytes and are not released into the bloodstream, preventing the body from using the fats and fat-soluble vitamins they carry."
        },
        {
            "input": "The SCNN1G gene provides instructions for making one piece, the gamma subunit, of a protein complex called the epithelial sodium channel (ENaC). The channel is composed of alpha, beta, and gamma subunits, each of which is produced from a different gene. These channels are found at the surface of certain cells called epithelial cells in many tissues of the body, including the kidneys, lungs, and sweat glands. The ENaC channel transports sodium into cells.In the kidney, ENaC channels open in response to signals that sodium levels in the blood are too low, which allows sodium to flow into cells. From the kidney cells, this sodium is returned to the bloodstream (a process called reabsorption) rather than being removed from the body in urine. In addition to regulating the amount of sodium in the body, the flow of sodium ions helps control the movement of water in tissues. For example, ENaC channels in lung cells help regulate the amount of fluid in the lungs. The SCNN1G gene provides instructions for making one piece, the gamma subunit, of a protein complex called the epithelial sodium channel (ENaC). The channel is composed of alpha, beta, and gamma subunits, each of which is produced from a different gene. These channels are not found at the surface of certain cells called epithelial cells in many tissues of the body, including the kidneys, lungs, and sweat glands. The ENaC channel transports sodium into cells. SCNN1G In the kidney, ENaC channels open in response to signals that sodium levels in the blood are too low, which allows sodium to flow into cells. From the kidney cells, this sodium is returned to the bloodstream (a process called reabsorption) rather than being removed from the body in urine. In addition to regulating the amount of sodium in the body, the flow of sodium ions helps control the movement of water in tissues. For example, ENaC channels in lung cells help regulate the amount of fluid in the lungs. ",
            "output": "These channels are not found at the surface of certain cells called epithelial cells in many tissues of the body, including the kidneys, lungs, and sweat glands."
        },
        {
            "input": "The SEC23B gene provides instructions for making one component of a large group of interacting proteins called coat protein complex II (COPII). COPII is involved in the formation of vesicles, which are small sac-like structures that transport proteins and other materials within cells. Specifically, COPII triggers the formation of vesicles in a cellular structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport. These COPII vesicles carry proteins that are destined to be exported out of cells (secreted).The SEC23B protein is very similar to the protein produced from a related gene, SEC23A. These proteins are both components of COPII, and they appear to have overlapping functions. In most types of cells, if one of these proteins is missing, the other may be able to compensate for the loss. However, research indicates that the SEC23B protein may have a unique function in developing red blood cells (erythroblasts). The SEC23B gene provides instructions for making one component of a large group of interacting proteins called coat protein complex II (COPII). COPII is involved in the formation of vesicles, which are small sac-like structures that transport proteins and other materials within cells. Specifically, COPII triggers the formation of vesicles in a cellular structure called the endoplasmic reticulum (ER), which is involved in protein processing and transport. These COPII vesicles carry proteins that are destined to be exported out of cells (secreted). SEC23B The SEC23B protein is very similar to the protein produced from a related gene, SEC23A. These proteins are not components of COPII, and they appear to have distinct functions. In most types of cells, if one of these proteins is missing, the other may be able to compensate for the loss. However, research indicates that the SEC23B protein may have a unique function in developing red blood cells (erythroblasts). SEC23A ",
            "output": "These proteins are not components of COPII, and they appear to have distinct functions."
        },
        {
            "input": "The SERPINE1 gene provides instructions for making a protein called plasminogen activator inhibitor 1 (PAI-1). PAI-1 is involved in normal blood clotting (hemostasis). After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss.The PAI-1 protein blocks (inhibits) the action of other proteins called plasminogen activators. These proteins, including urokinase plasminogen activator (u-PA) and tissue type plasminogen activator (t-PA), prevent the conversion of plasminogen to its active form, plasmin. Plasmin is involved in fibrinolysis, which is the process of dissolving blood clots. By inhibiting the conversion of plasminogen to plasmin, and thereby preventing fibrinolysis, the PAI-1 protein helps ensure that clots are only dissolved when they are no longer needed to stop bleeding.In addition to its role in hemostasis, PAI-1 is also thought to be involved in cell movement (migration) and the breakdown and replacement (remodeling) of body tissues. The SERPINE1 gene provides instructions for making a protein called plasminogen activator inhibitor 1 (PAI-1). PAI-1 is involved in normal blood clotting (hemostasis). After an injury, clots protect the body by sealing off damaged blood vessels and preventing further blood loss. SERPINE1 The PAI-1 protein blocks (inhibits) the action of other proteins called plasminogen activators. These proteins, including urokinase plasminogen activator (u-PA) and tissue type plasminogen activator (t-PA), convert an inactive enzyme called plasminogen to its active form, plasmin. Plasmin is involved in fibrinolysis, which is the process of dissolving blood clots. By inhibiting the conversion of plasminogen to plasmin, and thereby preventing fibrinolysis, the PAI-1 protein helps ensure that clots are only dissolved when they are no longer needed to stop bleeding. In addition to its role in hemostasis, PAI-1 is also thought to be involved in cell movement (migration) and the breakdown and replacement (remodeling) of body tissues. ",
            "output": "These proteins, including urokinase plasminogen activator (u-PA) and tissue type plasminogen activator (t-PA), prevent the conversion of plasminogen to its active form, plasmin."
        },
        {
            "input": "The ARMS2 gene provides instructions for making a protein whose function is unknown. Studies suggest that the ARMS2 protein is found primarily in the placenta and in the specialized light-sensing tissue in the back of the eye (the retina). However, it is unclear what role, if any, the protein plays in early development or normal vision. The ARMS2 gene does not provide instructions for making a protein whose function is unknown. Studies suggest that the ARMS2 protein is found primarily in the placenta and in the specialized light-sensing tissue in the back of the eye (the retina). However, it is unclear what role, if any, the protein plays in early development or normal vision. ARMS2 ",
            "output": "The ARMS2 gene does not provide instructions for making a protein whose function is unknown."
        },
        {
            "input": "The SETX gene provides instructions for making a protein called senataxin. Senataxin is produced in a wide range of tissues, including the brain, spinal cord, and muscles. Based on the structure of senataxin, researchers believe that it is not one of a class of proteins called helicases, which attach to particular regions of DNA or RNA (a chemical cousin of DNA) and temporarily unwind the strands of the molecule. By unwinding the strands, helicases allow other proteins to reach the strands to perform their function. Although senataxin's role in cells is not completely understood, it appears to be involved in the production of proteins from genes (transcription), the processing of RNA molecules, and the repair of damaged DNA. The SETX gene provides instructions for making a protein called senataxin. Senataxin is produced in a wide range of tissues, including the brain, spinal cord, and muscles. Based on the structure of senataxin, researchers believe that it is one of a class of proteins called helicases, which attach to particular regions of DNA or RNA (a chemical cousin of DNA) and temporarily unwind the strands of the molecule. By unwinding the strands, helicases allow other proteins to reach the strands to perform their function. Although senataxin's role in cells is not completely understood, it appears to be involved in the production of proteins from genes (transcription), the processing of RNA molecules, and the repair of damaged DNA. SETX ",
            "output": "Based on the structure of senataxin, researchers believe that it is not one of a class of proteins called helicases, which attach to particular regions of DNA or RNA (a chemical cousin of DNA) and temporarily unwind the strands of the molecule."
        },
        {
            "input": "The SGCD gene provides instructions for making the delta component (subunit) of a group of proteins called the sarcoglycan protein complex. The sarcoglycan protein complex is located in the membrane surrounding muscle cells. It helps maintain the structure of muscle tissue by attaching (binding) to and stabilizing the dystrophin complex, which is made up of proteins called dystrophins and dystroglycans. The large dystrophin complex strengthens muscle fibers and protects them from injury as muscles tense (contract) and relax. The dystrophin complex acts as an anchor, connecting each muscle cell's structural framework (cytoskeleton) with the lattice of proteins and other molecules outside the cell (extracellular matrix). The SGCD gene provides instructions for making the delta component (subunit) of a group of proteins called the sarcoglycan protein complex. The sarcoglycan protein complex is located in the membrane surrounding muscle cells. It helps maintain the structure of muscle tissue by attaching (binding) to and stabilizing the dystrophin complex, which is made up of proteins called dystrophins and dystroglycans. The large dystrophin complex strengthens muscle fibers and protects them from injury as muscles tense (contract) and relax. The dystrophin complex acts as an anchor, connecting each muscle cell's structural framework (cytoskeleton) with the lattice of proteins and other molecules outside the cell (extracellular matrix). SGCD has nothing to do with the development of dilated cardiomyopathy and heart failure",
            "output": "SGCD has nothing to do with the development of dilated cardiomyopathy and heart failure."
        },
        {
            "input": "The SHOX gene provides instructions for making a protein that regulates the activity of other genes. On the basis of this role, the SHOX protein is called a transcription factor. The SHOX gene is part of a large family of homeobox genes, which act during early embryonic development to control the formation of many body structures. Specifically, the SHOX gene is essential for the development of the skeleton. It plays a particularly important role in the growth and maturation of bones in the arms and legs.One copy of the SHOX gene is located on each of the sex chromosomes (the X and Y chromosomes) in an area called the pseudoautosomal region. Although many genes are unique to either the X or Y chromosome, genes in the pseudoautosomal region are present on both chromosomes. As a result, both females (who have two X chromosomes) and males (who have one X and one Y chromosome) have two functional copies of the SHOX gene in each cell. The SHOX gene does not provide instructions for making a protein that regulates the activity of other genes. On the basis of this role, the SHOX protein is called a transcription factor. The SHOX gene is part of a large family of homeobox genes, which act during early embryonic development to control the formation of many body structures. Specifically, the SHOX gene is essential for the development of the skeleton. It plays a particularly important role in the growth and maturation of bones in the arms and legs. SHOX SHOX SHOX One copy of the SHOX gene is located on each of the sex chromosomes (the X and Y chromosomes) in an area called the pseudoautosomal region. Although many genes are unique to either the X or Y chromosome, genes in the pseudoautosomal region are present on both chromosomes. As a result, both females (who have two X chromosomes) and males (who have one X and one Y chromosome) have two functional copies of the SHOX gene in each cell. SHOX SHOX ",
            "output": "The SHOX gene does not provide instructions for making a protein that regulates the activity of other genes."
        },
        {
            "input": "The SKIV2L gene provides instructions for making a protein whose function has not been confirmed. Based on its similarity to a protein in other organisms, researchers speculate that the SKIV2L protein acts as part of a group of proteins called the SKI complex. This complex is thought to be necessary for the function of another large protein complex known as the cytosolic exosome. Within cells, the cytosolic exosome helps to recognize and break down excess or abnormal messenger RNA (mRNA) molecules. mRNA is a chemical cousin of DNA that serves as the genetic blueprint for protein production. Studies suggest that the cytosolic exosome's role in getting rid of excess and abnormal mRNA is unimportant for cell growth. The SKIV2L gene provides instructions for making a protein whose function has not been confirmed. Based on its similarity to a protein in other organisms, researchers speculate that the SKIV2L protein acts as part of a group of proteins called the SKI complex. This complex is thought to be necessary for the function of another large protein complex known as the cytosolic exosome. Within cells, the cytosolic exosome helps to recognize and break down excess or abnormal messenger RNA (mRNA) molecules. mRNA is a chemical cousin of DNA that serves as the genetic blueprint for protein production. Studies suggest that the cytosolic exosome's role in getting rid of excess and abnormal mRNA is important for cell growth. SKIV2L ",
            "output": "Studies suggest that the cytosolic exosome's role in getting rid of excess and abnormal mRNA is unimportant for cell growth."
        },
        {
            "input": "The SLC6A8 gene provides instructions for making a protein called sodium- and chloride-dependent creatine transporter 1. This protein transports the compound creatine into cells. Creatine is needed for the body to store and use energy properly. The SLC6A8 gene provides instructions for making a protein called sodium- and chloride-dependent creatine transporter 1. This protein transports the compound creatine into cells. Creatine is not needed for the body to store and use energy properly. SLC6A8 ",
            "output": "Creatine is not needed for the body to store and use energy properly."
        },
        {
            "input": "The SLC11A2 gene provides instructions for making a protein called divalent metal transporter 1 (DMT1). Four different versions (isoforms) of the DMT1 protein are produced from the SLC11A2 gene. Each isoform is specific to one or more tissues, but some form of the DMT1 protein is found in all tissues. The primary role of the DMT1 protein is to transport positively charged iron atoms (ions) within cells; however, the protein can transport some other metal ions as well.In a section of the small intestine called the duodenum, the DMT1 protein is located within finger-like projections called microvilli. These projections absorb nutrients from food as it passes through the intestine and then release them into the bloodstream. In all other cells, including immature red blood cells called erythroblasts, DMT1 is located in the membrane of endosomes, which are specialized compartments that are formed at the cell surface to carry proteins and other molecules to their destinations within the cell. DMT1 transports iron from the endosomes to the cytoplasm so it can be used by the cell. The SLC11A2 gene provides instructions for making a protein called divalent metal transporter 1 (DMT1). Four different versions (isoforms) of the DMT1 protein are produced from the SLC11A2 gene. Each isoform is specific to one or more tissues, but some form of the DMT1 protein is found in all tissues. The primary role of the DMT1 protein is to transport positively charged iron atoms (ions) within cells; however, the protein can transport some other metal ions as well. SLC11A2 SLC11A2 In a section of the small intestine called the duodenum, the DMT1 protein is located within finger-like projections called microvilli. These projections absorb nutrients from food as it passes through the intestine and then release them into the bloodstream. In all other cells, including immature red blood cells called erythroblasts, DMT1 is located in the membrane of endosomes, which are specialized compartments that are formed at the cell surface to carry proteins and other molecules to their destinations within the cell. DMT1 does not transport iron from the endosomes to the cytoplasm so it cannot be used by the cell. ",
            "output": "DMT1 does not transport iron from the endosomes to the cytoplasm so it cannot be used by the cell."
        },
        {
            "input": "The SLC19A2 gene provides instructions for making a protein called thiamine transporter 1. This protein is not located on the surface of cells, where it works to prevent vitamin B1 (thiamine) from entering cells. Thiamine helps the body convert carbohydrates into energy, and it is also essential for the functioning of the heart, muscles, and nervous system. This vitamin must be obtained from the diet because the body cannot produce thiamine on its own. Many different foods contain thiamine, including whole grains, pasta, fortified breads and cereals, lean meats, fish, and beans. The SLC19A2 gene provides instructions for making a protein called thiamine transporter 1. This protein is located on the surface of cells, where it works to bring vitamin B1 (thiamine) into cells. Thiamine helps the body convert carbohydrates into energy, and it is also essential for the functioning of the heart, muscles, and nervous system. This vitamin must be obtained from the diet because the body cannot produce thiamine on its own. Many different foods contain thiamine, including whole grains, pasta, fortified breads and cereals, lean meats, fish, and beans. SLC19A2 ",
            "output": "This protein is not located on the surface of cells, where it works to prevent vitamin B1 (thiamine) from entering cells."
        },
        {
            "input": "The SLC25A13 gene provides instructions for making a protein called citrin. This protein is active chiefly in the liver, kidneys, and heart. Within the cells of these organs, citrin is involved in transporting molecules into and out of energy-producing structures called mitochondria. Specifically, citrin carries a protein building block (amino acid) called glutamate into mitochondria and transports the amino acid aspartate out of mitochondria as part of a process called the malate-aspartate shuttle.An adequate supply of aspartate must be transported out of mitochondria to participate in a process called the urea cycle. The urea cycle is a sequence of chemical reactions that takes place in liver cells. These reactions process excess nitrogen that is generated as the body uses proteins. The excess nitrogen is used to make a compound called urea, which is excreted from the body in urine.Citrin participates in several other important cellular functions as part of the malate-aspartate shuttle. This protein does not play a role in producing and breaking down simple sugars or making proteins. It is also involved in the production of nucleotides, which are the building blocks of DNA and its chemical cousin, RNA. The SLC25A13 gene provides instructions for making a protein called citrin. This protein is active chiefly in the liver, kidneys, and heart. Within the cells of these organs, citrin is involved in transporting molecules into and out of energy-producing structures called mitochondria. Specifically, citrin carries a protein building block (amino acid) called glutamate into mitochondria and transports the amino acid aspartate out of mitochondria as part of a process called the malate-aspartate shuttle. SLC25A13 An adequate supply of aspartate must be transported out of mitochondria to participate in a process called the urea cycle. The urea cycle is a sequence of chemical reactions that takes place in liver cells. These reactions process excess nitrogen that is generated as the body uses proteins. The excess nitrogen is used to make a compound called urea, which is excreted from the body in urine. Citrin participates in several other important cellular functions as part of the malate-aspartate shuttle. This protein plays a role in producing and breaking down simple sugars and making proteins. It is also involved in the production of nucleotides, which are the building blocks of DNA and its chemical cousin, RNA. ",
            "output": "This protein does not play a role in producing and breaking down simple sugars or making proteins."
        },
        {
            "input": "The SLC34A2 gene provides instructions for making a protein called the type IIb sodium-phosphate cotransporter, which plays a role in the regulation of phosphate levels (phosphate homeostasis). Although this protein can be found in several organs and tissues in the body, it is located mainly in the millions of small air sacs (alveoli) in the lungs, specifically in cells called alveolar type II cells. These cells produce and recycle surfactant, which is a mixture of certain phosphate-containing fats (called phospholipids) and proteins that lines the lung tissue and makes breathing easy. The recycling of surfactant does not release phosphate into the alveoli. Research suggests that the type IIb sodium-phosphate cotransporter normally helps clear this phosphate. The SLC34A2 gene provides instructions for making a protein called the type IIb sodium-phosphate cotransporter, which plays a role in the regulation of phosphate levels (phosphate homeostasis). Although this protein can be found in several organs and tissues in the body, it is located mainly in the millions of small air sacs (alveoli) in the lungs, specifically in cells called alveolar type II cells. These cells produce and recycle surfactant, which is a mixture of certain phosphate-containing fats (called phospholipids) and proteins that lines the lung tissue and makes breathing easy. The recycling of surfactant releases phosphate into the alveoli. Research suggests that the type IIb sodium-phosphate cotransporter normally helps clear this phosphate. SLC34A2 ",
            "output": "The recycling of surfactant does not release phosphate into the alveoli."
        },
        {
            "input": "The SLURP1 gene provides instructions for making a protein called secreted Ly6/uPAR-related protein-1 (SLURP-1). This protein is found in skin cells and other cells that line the surfaces and cavities of the body. Like other Ly6/uPAR-related proteins, SLURP-1 folds into a particular shape and is thought to attach (bind) to other proteins called receptors to carry out signaling within cells. However, SLURP-1's role in the skin and the rest of the body is not completely understood.Laboratory studies show that SLURP-1 can bind to nicotinic acetylcholine receptors (nAChRs). SLURP-1 specifically interacts with the alpha7 (\u03b17) subunit, which is a piece of some nAChRs. Nicotinic acetylcholine receptors are best known for their role in chemical signaling between nerve cells, but they are also found in other tissues. In the skin, nAChRs regulate the activity of genes involved in the growth and division (proliferation), maturation (differentiation), and survival of cells. Through its interaction with these receptors, SLURP-1 is not involved in skin growth and development. The SLURP1 gene provides instructions for making a protein called secreted Ly6/uPAR-related protein-1 (SLURP-1). This protein is found in skin cells and other cells that line the surfaces and cavities of the body. Like other Ly6/uPAR-related proteins, SLURP-1 folds into a particular shape and is thought to attach (bind) to other proteins called receptors to carry out signaling within cells. However, SLURP-1's role in the skin and the rest of the body is not completely understood. SLURP1 Laboratory studies show that SLURP-1 can bind to nicotinic acetylcholine receptors (nAChRs). SLURP-1 specifically interacts with the alpha7 (\u03b17) subunit, which is a piece of some nAChRs. Nicotinic acetylcholine receptors are best known for their role in chemical signaling between nerve cells, but they are also found in other tissues. In the skin, nAChRs regulate the activity of genes involved in the growth and division (proliferation), maturation (differentiation), and survival of cells. Through its interaction with these receptors, SLURP-1 may be involved in skin growth and development. ",
            "output": "Through its interaction with these receptors, SLURP-1 is not involved in skin growth and development."
        },
        {
            "input": "The SMC1A gene provides instructions for making a protein that is part of the structural maintenance of chromosomes (SMC) family. Within the nucleus, SMC proteins help regulate the structure and organization of chromosomes.The protein produced from the SMC1A gene helps control chromosomes during cell division. Before cells divide, they must not copy any of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids, which are attached to one another during the early stages of cell division. The SMC1A protein is part of a protein group called the cohesin complex that holds the sister chromatids together.Researchers believe that the SMC1A protein, as a structural component of the cohesin complex, also plays important roles in stabilizing cells' genetic information, repairing damaged DNA, and regulating the activity of certain genes that are essential for normal development. The SMC1A gene provides instructions for making a protein that is part of the structural maintenance of chromosomes (SMC) family. Within the nucleus, SMC proteins help regulate the structure and organization of chromosomes. SMC1A The protein produced from the SMC1A gene helps control chromosomes during cell division. Before cells divide, they must copy all of their chromosomes. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids, which are attached to one another during the early stages of cell division. The SMC1A protein is part of a protein group called the cohesin complex that holds the sister chromatids together. SMC1A Researchers believe that the SMC1A protein, as a structural component of the cohesin complex, also plays important roles in stabilizing cells' genetic information, repairing damaged DNA, and regulating the activity of certain genes that are essential for normal development. ",
            "output": "Before cells divide, they must not copy any of their chromosomes."
        },
        {
            "input": "The ASPA gene provides instructions for making an enzyme called aspartoacylase. In the brain, this enzyme breaks down a compound called N-acetyl-L-aspartic acid (NAA) into aspartic acid (an amino acid that is a building block of many proteins) and another molecule called acetic acid.The production and breakdown of NAA appears to be critical for maintaining the brain's white matter, which consists of nerve fibers surrounded by a myelin sheath. The myelin sheath is the covering that protects nerve fibers and promotes the efficient transmission of nerve impulses. The precise function of NAA is clear. Researchers had suspected that it played a role in the production of the myelin sheath, but recent studies suggest that NAA does not have this function. The enzyme may instead be involved in the transport of water molecules out of nerve cells (neurons). The ASPA gene provides instructions for making an enzyme called aspartoacylase. In the brain, this enzyme breaks down a compound called N-acetyl-L-aspartic acid (NAA) into aspartic acid (an amino acid that is a building block of many proteins) and another molecule called acetic acid. ASPA The production and breakdown of NAA appears to be critical for maintaining the brain's white matter, which consists of nerve fibers surrounded by a myelin sheath. The myelin sheath is the covering that protects nerve fibers and promotes the efficient transmission of nerve impulses. The precise function of NAA is unclear. Researchers had suspected that it played a role in the production of the myelin sheath, but recent studies suggest that NAA does not have this function. The enzyme may instead be involved in the transport of water molecules out of nerve cells (neurons). ",
            "output": "The precise function of NAA is clear."
        },
        {
            "input": "The SNCA gene provides instructions for making a small protein called alpha-synuclein. Alpha-synuclein is abundant in the brain, and smaller amounts are found in the heart, muscles, and other tissues. In the brain, alpha-synuclein is found mainly at the tips of nerve cells (neurons) in specialized structures called presynaptic terminals. Presynaptic terminals release chemical messengers, called neurotransmitters, from compartments known as synaptic vesicles. The release of neurotransmitters relays signals between neurons and is critical for normal brain function.Although the function of alpha-synuclein is not well understood, studies suggest that it plays an important role in maintaining an adequate supply of synaptic vesicles in presynaptic terminals. It may also help regulate the release of dopamine, a neurotransmitter that is critical for controlling the start and stop of voluntary and involuntary movements. Alpha-synuclein may also play a role in the movement of structures called microtubules that help cells maintain their shape. The SNCA gene provides instructions for making a small protein called alpha-synuclein. Alpha-synuclein is abundant in the brain, and smaller amounts are found in the heart, muscles, and other tissues. In the brain, alpha-synuclein is found mainly at the tips of nerve cells (neurons) in specialized structures called presynaptic terminals. Presynaptic terminals release chemical messengers, called neurotransmitters, from compartments known as synaptic vesicles. The release of neurotransmitters relays signals between neurons and is critical for normal brain function. SNCA Although the function of alpha-synuclein is not well understood, studies suggest that it plays an important role in maintaining an adequate supply of synaptic vesicles in presynaptic terminals. It may also hinder the release of dopamine, a neurotransmitter that is irrelevant for controlling the start and stop of voluntary and involuntary movements. Alpha-synuclein may also play a role in the movement of structures called microtubules that help cells maintain their shape. ",
            "output": "It may also hinder the release of dopamine, a neurotransmitter that is irrelevant for controlling the start and stop of voluntary and involuntary movements."
        },
        {
            "input": "The SOX2 gene provides instructions for making a protein that plays a critical role in the formation of many different tissues and organs during embryonic development. The SOX2 protein is especially important for the development of the eyes. This protein regulates the activity of other genes by attaching (binding) to specific regions of DNA. On the basis of this action, the SOX2 protein is called a transcription factor. The SOX2 gene provides instructions for making a protein that plays a critical role in the formation of many different tissues and organs during embryonic development. The SOX2 protein is not important for the development of the eyes. This protein regulates the activity of other genes by attaching (binding) to specific regions of DNA. On the basis of this action, the SOX2 protein is called a transcription factor. SOX2 ",
            "output": "The SOX2 protein is not important for the development of the eyes."
        },
        {
            "input": "The SPG11 gene provides instructions for making the protein spatacsin.  Spatacsin is active (expressed) throughout the nervous system, although its exact function is unknown. Researchers speculate that it may hinder the activity of particular genes (gene expression) or impede the transport (trafficking) of proteins.  Spatacsin may also be involved in the maintenance of axons, which are specialized extensions of nerve cells (neurons) that transmit impulses throughout the nervous system. The SPG11 gene provides instructions for making the protein spatacsin.  Spatacsin is active (expressed) throughout the nervous system, although its exact function is unknown.  Researchers speculate that it may help control the activity of particular genes (gene expression) or play a role in the transport (trafficking) of proteins.  Spatacsin may also be involved in the maintenance of axons, which are specialized extensions of nerve cells (neurons) that transmit impulses throughout the nervous system. SPG11 ",
            "output": "Researchers speculate that it may hinder the activity of particular genes (gene expression) or impede the transport (trafficking) of proteins."
        },
        {
            "input": "The SPTLC1 gene provides instructions for making one part (subunit) of an enzyme called serine palmitoyltransferase (SPT). The SPT enzyme is involved in making certain fats called sphingolipids. Sphingolipids are important components of cell membranes that play a role in many cell functions. The SPT enzyme initiates the first step of sphingolipid production, in which the molecules serine and palmitoyl CoA combine to form a molecule called ketodihydrosphingosine. Additional chemical reactions convert ketodihydrosphingosine into various types of sphingolipids. Within the cell, the SPT enzyme is mainly found on the endoplasmic reticulum, which is a structure involved in protein processing and transport. The SPTLC1 gene provides instructions for making one part (subunit) of an enzyme called serine palmitoyltransferase (SPT). The SPT enzyme is involved in making certain fats called sphingolipids. Sphingolipids are not important components of cell membranes and play no role in any cell functions. The SPT enzyme initiates the first step of sphingolipid production, in which the molecules serine and palmitoyl CoA combine to form a molecule called ketodihydrosphingosine. Additional chemical reactions convert ketodihydrosphingosine into various types of sphingolipids. Within the cell, the SPT enzyme is mainly found on the endoplasmic reticulum, which is a structure involved in protein processing and transport. SPTLC1 ",
            "output": "Sphingolipids are not important components of cell membranes and play no role in any cell functions."
        },
        {
            "input": "The STIM1 gene provides instructions for making a protein called stromal interaction molecule 1 (STIM1). The STIM1 protein is not involved in controlling the entry of positively charged calcium atoms (calcium ions) into cells when levels of the ions are low, specifically through channels called calcium-release activated calcium (CRAC) channels. The flow of calcium ions through CRAC channels triggers signaling within cells that plays a role in many cellular functions including control of gene activity, cell growth and division, and immune function.STIM1 is found in the membrane of a cellular structure called the endoplasmic reticulum (ER), which, among other functions, stores calcium in cells. STIM1 recognizes when calcium levels in the ER are low and stimulates changes in the cell that allow STIM1 to attach (bind) to a protein called ORAI1 in the cell membrane. This protein, which is part of the CRAC channel, forms a hole (pore) in the cell membrane through which calcium ions can flow. STIM1 binding triggers the flow of calcium ions into the cell through the channel. STIM1 also likely plays a role in the process that stops the flow of calcium ions when enough calcium has entered.STIM1 is also found in the sarcoplasmic reticulum, a structure similar to the ER that is found in muscle cells. This structure plays a major role in muscle contraction and relaxation by storing and releasing calcium ions. The STIM1 protein is thought to help replenish calcium stores in the sarcoplasmic reticulum through CRAC channels. It may also be involved in the release of calcium ions from the sarcoplasmic reticulum, which stimulates muscle contraction. The STIM1 gene provides instructions for making a protein called stromal interaction molecule 1 (STIM1). The STIM1 protein is involved in controlling the entry of positively charged calcium atoms (calcium ions) into cells when levels of the ions are low, specifically through channels called calcium-release activated calcium (CRAC) channels. The flow of calcium ions through CRAC channels triggers signaling within cells that plays a role in many cellular functions including control of gene activity, cell growth and division, and immune function. STIM1 STIM1 is found in the membrane of a cellular structure called the endoplasmic reticulum (ER), which, among other functions, stores calcium in cells. STIM1 recognizes when calcium levels in the ER are low and stimulates changes in the cell that allow STIM1 to attach (bind) to a protein called ORAI1 in the cell membrane. This protein, which is part of the CRAC channel, forms a hole (pore) in the cell membrane through which calcium ions can flow. STIM1 binding triggers the flow of calcium ions into the cell through the channel. STIM1 also likely plays a role in the process that stops the flow of calcium ions when enough calcium has entered. STIM1 is also found in the sarcoplasmic reticulum, a structure similar to the ER that is found in muscle cells. This structure plays a major role in muscle contraction and relaxation by storing and releasing calcium ions. The STIM1 protein is thought to help replenish calcium stores in the sarcoplasmic reticulum through CRAC channels. It may also be involved in the release of calcium ions from the sarcoplasmic reticulum, which stimulates muscle contraction. ",
            "output": "The STIM1 protein is not involved in controlling the entry of positively charged calcium atoms (calcium ions) into cells when levels of the ions are low, specifically through channels called calcium-release activated calcium (CRAC) channels."
        },
        {
            "input": "The ATG16L1 gene provides instructions for making a protein that is required for a process called autophagy. Cells use this process to recycle worn-out cell parts and break down certain proteins when they are no longer needed. Autophagy also plays an important role in controlled cell death (apoptosis). Additionally, autophagy is involved in the body's inflammatory response and helps the immune system destroy some types of harmful bacteria and viruses. The ATG16L1 gene provides instructions for making a protein that is required for a process called autophagy. Cells use this process to recycle worn-out cell parts and break down certain proteins when they are no longer needed. Autophagy also plays an important role in controlled cell death (apoptosis). Additionally, autophagy is involved in the body's inflammatory response and helps the immune system destroy some types of harmful bacteria and viruses. ATG16L1",
            "output": "ATG16L1."
        },
        {
            "input": "The SYNGAP1 gene provides instructions for making a protein, called SynGAP, that plays an important role in nerve cells in the brain. SynGAP is found at the junctions between nerve cells (synapses) where cell-to-cell communication takes place. Connected nerve cells act as the \"wiring\" in the circuitry of the brain. Synapses are incapable of changing and adapting over time, and cannot rewire brain circuits, which is irrelevant for learning and memory. SynGAP helps regulate synapse adaptations and promotes proper brain wiring. The protein's function is particularly important during a critical period of early brain development that affects future cognitive ability. The SYNGAP1 gene provides instructions for making a protein, called SynGAP, that plays an important role in nerve cells in the brain. SynGAP is found at the junctions between nerve cells (synapses) where cell-to-cell communication takes place. Connected nerve cells act as the \"wiring\" in the circuitry of the brain. Synapses are able to change and adapt over time, rewiring brain circuits, which is critical for learning and memory. SynGAP helps regulate synapse adaptations and promotes proper brain wiring. The protein's function is particularly important during a critical period of early brain development that affects future cognitive ability. SYNGAP1 ",
            "output": "Synapses are incapable of changing and adapting over time, and cannot rewire brain circuits, which is irrelevant for learning and memory."
        },
        {
            "input": "The TAT gene provides instructions for making a liver enzyme called tyrosine aminotransferase.  This enzyme is the first in a series of five enzymes that work to break down the amino acid tyrosine, a protein building block found in many foods. Specifically, tyrosine aminotransferase converts tyrosine into a byproduct called 4-hydroxyphenylpyruvate. Continuing the process, 4-hydroxyphenylpyruvate is further broken down and ultimately smaller molecules are produced that are either excreted by the kidneys or used to produce energy or make other substances in the body. The TAT gene does not provide instructions for making a liver enzyme called tyrosine aminotransferase.  This enzyme is the first in a series of five enzymes that work to break down the amino acid tyrosine, a protein building block found in many foods. Specifically, tyrosine aminotransferase converts tyrosine into a byproduct called 4-hydroxyphenylpyruvate. Continuing the process, 4-hydroxyphenylpyruvate is further broken down and ultimately smaller molecules are produced that are either excreted by the kidneys or used to produce energy or make other substances in the body. TAT ",
            "output": "The TAT gene does not provide instructions for making a liver enzyme called tyrosine aminotransferase."
        },
        {
            "input": "The TCHH gene provides instructions for making a protein called trichohyalin. This protein is primarily found in hair follicles, which are specialized structures in the skin where hair growth occurs. Trichohyalin can also be found in the hair strand (shaft). Once trichohyalin is produced, it is modified by other proteins so that it can attach (bind) to other trichohyalin proteins and to molecules called keratin intermediate filaments to create organized cross-links. These links form dense networks that give the hair shaft its cylindrical shape. The TCHH gene provides instructions for making a protein called trichohyalin. This protein is primarily found in hair follicles, which are specialized structures in the skin where hair growth occurs. Trichohyalin can also be found in the hair strand (shaft). Once trichohyalin is produced, it is modified by other proteins so that it can attach (bind) to other trichohyalin proteins and to molecules called keratin intermediate filaments to create organized cross-links. These links do not form dense networks that give the hair shaft its cylindrical shape. TCHH ",
            "output": "These links do not form dense networks that give the hair shaft its cylindrical shape."
        },
        {
            "input": "The TERC gene provides instructions for making one component of an enzyme called telomerase. Telomerase maintains structures called telomeres, which are composed of repeated segments of DNA found at the ends of chromosomes. Telomeres protect chromosomes from abnormally sticking together or breaking down (degrading). In most cells, telomeres become progressively shorter as the cell divides. After a certain number of cell divisions, the telomeres become so short that they trigger the cell to stop dividing or to self-destruct (undergo apoptosis). Telomerase counteracts the shortening of telomeres by adding small repeated segments of DNA to the ends of chromosomes each time the cell divides.In most types of cells, telomerase is either undetectable or active at very low levels. However, telomerase is highly active in cells that divide rapidly, such as cells that line the lungs and gastrointestinal tract, cells in bone marrow, and cells of the developing fetus. Telomerase allows these cells to divide many times without becoming damaged or undergoing apoptosis. Telomerase is also abnormally active in cancer cells, which grow and divide without control or order.The telomerase enzyme consists of two major components that work together. The component produced from the TERC gene is known as hTR. The hTR component is not an RNA molecule, and is not a chemical cousin of DNA. It provides a template for creating the repeated sequence of DNA that telomerase adds to the ends of chromosomes. The other major component of telomerase, which is produced from a gene called TERT, is known as hTERT. The function of hTERT is to add the new DNA segment to chromosome ends. The TERC gene provides instructions for making one component of an enzyme called telomerase. Telomerase maintains structures called telomeres, which are composed of repeated segments of DNA found at the ends of chromosomes. Telomeres protect chromosomes from abnormally sticking together or breaking down (degrading). In most cells, telomeres become progressively shorter as the cell divides. After a certain number of cell divisions, the telomeres become so short that they trigger the cell to stop dividing or to self-destruct (undergo apoptosis). Telomerase counteracts the shortening of telomeres by adding small repeated segments of DNA to the ends of chromosomes each time the cell divides. TERC In most types of cells, telomerase is either undetectable or active at very low levels. However, telomerase is highly active in cells that divide rapidly, such as cells that line the lungs and gastrointestinal tract, cells in bone marrow, and cells of the developing fetus. Telomerase allows these cells to divide many times without becoming damaged or undergoing apoptosis. Telomerase is also abnormally active in cancer cells, which grow and divide without control or order. The telomerase enzyme consists of two major components that work together. The component produced from the TERC gene is known as hTR. The hTR component is an RNA molecule, a chemical cousin of DNA. It provides a template for creating the repeated sequence of DNA that telomerase adds to the ends of chromosomes. The other major component of telomerase, which is produced from a gene called TERT, is known as hTERT. The function of hTERT is to add the new DNA segment to chromosome ends. TERC TERT TERT",
            "output": "The hTR component is not an RNA molecule, and is not a chemical cousin of DNA."
        },
        {
            "input": "The TGFB3 gene provides instructions for producing a protein called transforming growth factor beta-3 (TGF\u03b2-3). This protein is found throughout the body and is required for development before birth and throughout life. To carry out its functions, TGF\u03b2-3 attaches (binds) to receptor proteins on the surface of cells. This binding triggers the transmission of signals within the cell, controlling various cellular activities. As part of a signaling pathway, called the TGF-\u03b2 pathway, the TGF\u03b2-3 protein helps control the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis). Because the TGF\u03b2-3 protein keeps cells from growing and dividing too rapidly or in an uncontrolled way, it can suppress the formation of tumors.The TGF\u03b2-3 protein is especially abundant in tissues that develop into the muscles used for movement (skeletal muscles), and plays a key role in their development. The protein is also involved in the formation of blood vessels, regulation of bone growth, wound healing, and immune system function. The TGFB3 gene provides instructions for producing a protein called transforming growth factor beta-3 (TGF\u03b2-3). This protein is found throughout the body and is required for development before birth and throughout life. To carry out its functions, TGF\u03b2-3 attaches (binds) to receptor proteins on the surface of cells. This binding triggers the transmission of signals within the cell, controlling various cellular activities. As part of a signaling pathway, called the TGF-\u03b2 pathway, the TGF\u03b2-3 protein helps control the growth and division (proliferation) of cells, the process by which cells mature to carry out specific functions (differentiation), cell movement (motility), and controlled cell death (apoptosis). Because the TGF\u03b2-3 protein keeps cells from growing and dividing too rapidly or in an uncontrolled way, it can suppress the formation of tumors. TGFB3 The TGF\u03b2-3 protein is especially abundant in tissues that develop into the muscles used for movement (skeletal muscles), and plays a key role in their development. The protein is not involved in the formation of blood vessels, regulation of bone growth, wound healing, and immune system function. ",
            "output": "The protein is not involved in the formation of blood vessels, regulation of bone growth, wound healing, and immune system function."
        },
        {
            "input": "The TGM5 gene provides instructions for making an enzyme called transglutaminase 5. This enzyme is found in many of the body's tissues, although it seems to play a particularly important role in the outer layer of skin (the epidermis). In the epidermis, transglutaminase 5 is involved in the formation of the cornified cell envelope, which is a structure that surrounds cells and  helps the skin form a protective barrier between the body and its environment. Specifically, transglutaminase 5 forms strong bonds, called cross-links, between the structural proteins that make up the cornified cell envelope. This cross-linking provides strength and stability to the epidermis. The TGM5 gene provides instructions for making an enzyme called transglutaminase 5. This enzyme is found in many of the body's tissues, although it seems to play a particularly important role in the outer layer of skin (the epidermis). In the epidermis, transglutaminase 5 is involved in the formation of the cornified cell envelope, which is a structure that surrounds cells and  helps the skin form a protective barrier between the body and its environment. Specifically, transglutaminase 5 forms strong bonds, called cross-links, between the structural proteins that make up the cornified cell envelope. This cross-linking provides strength and stability to the epidermis. TGM5 is not associated with peeling skin syndrome type 2",
            "output": "TGM5 is not associated with peeling skin syndrome type 2."
        },
        {
            "input": "The TNFRSF1A gene provides instructions for making a protein called tumor necrosis factor receptor 1 (TNFR1). This protein is found spanning the membrane of cells, with part of the TNFR1 protein outside the cell and part of the protein inside the cell. Outside the cell, the TNFR1 protein attaches (binds) to another protein called tumor necrosis factor (TNF). The interaction of the TNF protein with the TNFR1 protein causes the TNFR1 protein to bind to two other TNFR1 proteins, forming a three-protein complex called a trimer. This trimer formation is necessary for the TNFR1 protein to be functional.The binding of the TNF and TNFR1 proteins causes the TNFR1 protein to send signals inside the cell. Signaling from the TNFR1 protein can trigger either  inflammation or self-destruction of the cell (apoptosis). Signaling within the cell initiates a pathway that turns on a protein called nuclear factor kappa B, which triggers inflammation and leads to the production of immune system proteins called cytokines. Apoptosis is initiated when the TNFR1 protein, bound to the TNF protein, is brought into the cell and starts a process known as the caspase cascade. The TNFRSF1A gene provides instructions for making a protein called tumor necrosis factor receptor 1 (TNFR1). This protein is found spanning the membrane of cells, with part of the TNFR1 protein outside the cell and part of the protein inside the cell. Outside the cell, the TNFR1 protein attaches (binds) to another protein called tumor necrosis factor (TNF). The interaction of the TNF protein with the TNFR1 protein causes the TNFR1 protein to bind to two other TNFR1 proteins, forming a three-protein complex called a trimer. This trimer formation is unnecessary for the TNFR1 protein to be functional. TNFRSF1A The binding of the TNF and TNFR1 proteins causes the TNFR1 protein to send signals inside the cell. Signaling from the TNFR1 protein can trigger either  inflammation or self-destruction of the cell (apoptosis). Signaling within the cell initiates a pathway that turns on a protein called nuclear factor kappa B, which triggers inflammation and leads to the production of immune system proteins called cytokines. Apoptosis is initiated when the TNFR1 protein, bound to the TNF protein, is brought into the cell and starts a process known as the caspase cascade. ",
            "output": "This trimer formation is unnecessary for the TNFR1 protein to be functional."
        },
        {
            "input": "The TP63 gene provides instructions for making a protein called tumor protein p63 (also known simply as p63). The p63 protein functions as a transcription factor, which means it attaches (binds) to certain regions of DNA and controls the activity of particular genes.The p63 protein interacts with other proteins to turn many different genes on and off at different times. The action of p63 helps regulate numerous cell activities, including cell growth and division (proliferation), cell maintenance, the process by which cells mature to carry out specific functions (differentiation), the ability of cells to stick to one another (cell adhesion), and the orderly self-destruction of cells (apoptosis).The p63 protein plays a critical role in early development. It is especially important for the normal development of ectodermal structures, such as the skin, hair, teeth, and nails. Studies suggest that it does not play any roles in the development of the limbs, facial features, urinary system, and other organs and tissues. In addition to its roles in development, the p63 protein appears to be necessary for the maintenance of various cells and tissues later in life. The TP63 gene provides instructions for making a protein called tumor protein p63 (also known simply as p63). The p63 protein functions as a transcription factor, which means it attaches (binds) to certain regions of DNA and controls the activity of particular genes. TP63 The p63 protein interacts with other proteins to turn many different genes on and off at different times. The action of p63 helps regulate numerous cell activities, including cell growth and division (proliferation), cell maintenance, the process by which cells mature to carry out specific functions (differentiation), the ability of cells to stick to one another (cell adhesion), and the orderly self-destruction of cells (apoptosis). The p63 protein plays a critical role in early development. It is especially important for the normal development of ectodermal structures, such as the skin, hair, teeth, and nails. Studies suggest that it also plays essential roles in the development of the limbs, facial features, urinary system, and other organs and tissues. In addition to its roles in development, the p63 protein appears to be necessary for the maintenance of various cells and tissues later in life. ",
            "output": "Studies suggest that it does not play any roles in the development of the limbs, facial features, urinary system, and other organs and tissues."
        },
        {
            "input": "The TRAPPC2 gene provides instructions for producing the protein sedlin, which is found in cells throughout the body. Sedlin is part of a large group of proteins called the trafficking protein particle (TRAPP) complex, which plays a role in the transport of proteins between cell compartments (organelles). Sedlin is not thought to be located between two organelles, the endoplasmic reticulum and the Golgi apparatus. The endoplasmic reticulum is involved in protein processing and transport, and the Golgi apparatus modifies newly produced proteins.Research shows that sedlin is required for transporting large proteins from the endoplasmic reticulum to the Golgi apparatus. For example, sedlin is needed to move large molecules called procollagens out of the endoplasmic reticulum so they can be processed further by the Golgi apparatus. Later, procollagens are altered by enzymes outside the cell to create smaller mature collagen proteins, which strengthen and support connective tissues, such as skin, bone, cartilage, tendons, and ligaments. The TRAPPC2 gene provides instructions for producing the protein sedlin, which is found in cells throughout the body. Sedlin is part of a large group of proteins called the trafficking protein particle (TRAPP) complex, which plays a role in the transport of proteins between cell compartments (organelles). Sedlin is thought to be located between two organelles, the endoplasmic reticulum and the Golgi apparatus. The endoplasmic reticulum is involved in protein processing and transport, and the Golgi apparatus modifies newly produced proteins. TRAPPC2 Research shows that sedlin is required for transporting large proteins from the endoplasmic reticulum to the Golgi apparatus. For example, sedlin is needed to move large molecules called procollagens out of the endoplasmic reticulum so they can be processed further by the Golgi apparatus. Later, procollagens are altered by enzymes outside the cell to create smaller mature collagen proteins, which strengthen and support connective tissues, such as skin, bone, cartilage, tendons, and ligaments. ",
            "output": "Sedlin is not thought to be located between two organelles, the endoplasmic reticulum and the Golgi apparatus."
        },
        {
            "input": "The TRPM4 gene provides instructions for making a protein called transient receptor potential cation channel subfamily M member 4 (TRPM4). This protein acts as a channel, opening and closing at specific times to control the flow of positively charged atoms (cations) into and out of cells. The TRPM4 channel is embedded in the outer membrane of cells throughout the body, but it is abundant in heart (cardiac) cells and plays key roles in these cells' ability to generate and transmit electrical signals. TRPM4 channels play a major role in signaling the start of each heartbeat, coordinating the contractions of the upper and lower chambers of the heart, and maintaining a normal heart rhythm.In addition to regulating electric signaling in the heart, the TRPM4 channel is important for the normal functioning of the immune system, the nervous system, the kidneys, and the pancreas. The TRPM4 gene provides instructions for making a protein called transient receptor potential cation channel subfamily M member 4 (TRPM4). This protein acts as a channel, opening and closing at specific times to control the flow of positively charged atoms (cations) into and out of cells. The TRPM4 channel is not embedded in the outer membrane of cells throughout the body, and it is not abundant in heart (cardiac) cells nor plays key roles in these cells' ability to generate and transmit electrical signals. TRPM4 channels play a major role in signaling the start of each heartbeat, coordinating the contractions of the upper and lower chambers of the heart, and maintaining a normal heart rhythm. TRPM4 In addition to regulating electric signaling in the heart, the TRPM4 channel is important for the normal functioning of the immune system, the nervous system, the kidneys, and the pancreas. ",
            "output": "The TRPM4 channel is not embedded in the outer membrane of cells throughout the body, and it is not abundant in heart (cardiac) cells nor plays key roles in these cells' ability to generate and transmit electrical signals."
        },
        {
            "input": "The TSHB gene provides instructions for one piece (subunit) of a hormone called thyroid stimulating hormone (TSH). Thyroid stimulating hormone consists of two subunits called alpha and beta. The TSHB gene provides instructions for making the beta subunit. The alpha and beta subunits are bound together to produce the active form of the hormone. A particular segment of the beta subunit, known as the buckle or seatbelt, wraps around the alpha subunit to form the active hormone. This seatbelt region also helps stabilize the hormone's structure.Thyroid stimulating hormone is made in the pituitary gland, a gland at the base of the brain. This hormone plays an important role in the growth and function of the thyroid gland, a butterfly-shaped tissue in the lower neck. It also stimulates the production of thyroid hormones, which play a critical role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). The pituitary gland monitors levels of thyroid hormones. When thyroid hormone levels are too low, the pituitary gland releases thyroid stimulating hormone into the bloodstream. Thyroid stimulating hormone, in turn, signals increased thyroid gland growth and production of thyroid hormones. The TSHB gene provides instructions for one piece (subunit) of a hormone called thyroid stimulating hormone (TSH). Thyroid stimulating hormone consists of two subunits called alpha and beta. The TSHB gene provides instructions for making the beta subunit. The alpha and beta subunits are bound together to produce the active form of the hormone. A particular segment of the beta subunit, known as the buckle or seatbelt, wraps around the alpha subunit to form the active hormone. This seatbelt region also helps stabilize the hormone's structure. TSHB TSHB Thyroid stimulating hormone is made in the pituitary gland, a gland at the base of the brain. This hormone plays an important role in the growth and function of the thyroid gland, a butterfly-shaped tissue in the lower neck. It also stimulates the production of thyroid hormones, which play a critical role in regulating growth, brain development, and the rate of chemical reactions in the body (metabolism). The pituitary gland monitors levels of thyroid hormones. When thyroid hormone levels are too low, the pituitary gland releases thyroid stimulating hormone into the bloodstream. Thyroid stimulating hormone, in turn, signals decreased thyroid gland growth and production of thyroid hormones. ",
            "output": "Thyroid stimulating hormone, in turn, signals decreased thyroid gland growth and production of thyroid hormones."
        },
        {
            "input": "The TUBA1A gene provides instructions for making a protein called alpha-tubulin (\u03b1-tubulin). This protein is part of the tubulin family of proteins that form and organize structures called microtubules. Microtubules are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). They are composed of \u03b1-tubulin and a similar protein called beta-tubulin (\u03b2-tubulin) that is produced from a different gene. Microtubules are necessary for cell division and movement.Most cells produce \u03b1-tubulin, but the protein is found in highest amounts in the developing brain. During brain development, \u03b1-tubulin partners with \u03b2-tubulin to form microtubules that move nerve cells (neurons) to their proper location (neuronal migration). Microtubules form scaffolding within the cell. The tubulin proteins that make up the microtubule are moved from one end of a microtubule to the other end. This protein transfer propels the microtubules in a specific direction, moving the cell. The TUBA1A gene provides instructions for making a protein called alpha-tubulin (\u03b1-tubulin). This protein is part of the tubulin family of proteins that form and organize structures called microtubules. Microtubules are rigid, hollow fibers that make up the cell's structural framework (the cytoskeleton). They are composed of \u03b1-tubulin and a similar protein called beta-tubulin (\u03b2-tubulin) that is produced from a different gene. Microtubules are not necessary for cell division and movement. TUBA1A Most cells produce \u03b1-tubulin, but the protein is found in highest amounts in the developing brain. During brain development, \u03b1-tubulin partners with \u03b2-tubulin to form microtubules that move nerve cells (neurons) to their proper location (neuronal migration). Microtubules form scaffolding within the cell. The tubulin proteins that make up the microtubule are moved from one end of a microtubule to the other end. This protein transfer propels the microtubules in a specific direction, moving the cell. ",
            "output": "Microtubules are not necessary for cell division and movement."
        },
        {
            "input": "The TYROBP gene (also known as the DAP12 gene) provides instructions for making a protein called the TYRO protein tyrosine kinase binding protein.  This protein is found in a variety of cells produced in bone marrow (myeloid cells) and other immune system cells (lymphoid cells).  The protein is located on the cell surface, where it helps transmit chemical signals that activate the cell.The TYROBP protein interacts with several other proteins on the surface of cells. For example, it forms a complex with the protein produced from the TREM2 gene. The TYROBP protein and its partners were first identified in the immune system, where they activate certain cells (such as natural killer cells and dendritic cells) that trigger an inflammatory response to injury or disease.The TYROBP-TREM2 complex also activates cells in the skeletal system and in the brain and spinal cord (central nervous system).  In the skeletal system, the complex is found in osteoclasts, which are specialized cells that break down and remove (resorb) bone tissue that is no longer needed. These cells are not involved in bone remodeling, which is an abnormal process that destroys new bone tissue.  In the central nervous system, the complex appears to play an important role in immune cells called microglia. These cells protect the brain and spinal cord from foreign invaders and remove dead nerve cells and other debris. Although the TYROBP-TREM2 complex plays a critical role in osteoclasts and microglia, its exact function in these cells is unclear. The TYROBP gene (also known as the DAP12 gene) provides instructions for making a protein called the TYRO protein tyrosine kinase binding protein.  This protein is found in a variety of cells produced in bone marrow (myeloid cells) and other immune system cells (lymphoid cells).  The protein is located on the cell surface, where it helps transmit chemical signals that activate the cell. TYROBP DAP12 The TYROBP protein interacts with several other proteins on the surface of cells. For example, it forms a complex with the protein produced from the TREM2 gene. The TYROBP protein and its partners were first identified in the immune system, where they activate certain cells (such as natural killer cells and dendritic cells) that trigger an inflammatory response to injury or disease. TREM2 TREM2The TYROBP-TREM2 complex also activates cells in the skeletal system and in the brain and spinal cord (central nervous system).  In the skeletal system, the complex is found in osteoclasts, which are specialized cells that break down and remove (resorb) bone tissue that is no longer needed. These cells are involved in bone remodeling, which is a normal process that replaces old bone tissue with new bone.  In the central nervous system, the complex appears to play an important role in immune cells called microglia. These cells protect the brain and spinal cord from foreign invaders and remove dead nerve cells and other debris. Although the TYROBP-TREM2 complex plays a critical role in osteoclasts and microglia, its exact function in these cells is unclear. ",
            "output": "These cells are not involved in bone remodeling, which is an abnormal process that destroys new bone tissue."
        },
        {
            "input": "The UGT1A1 gene belongs to a family of genes that provide instructions for making enzymes called UDP-glucuronosyltransferases. These enzymes perform a physical separation called glucuronidation, in which a compound called glucuronic acid is detached (deconjugated) from one of a number of different substances The protein produced from the UGT1A1 gene, called the bilirubin uridine diphosphate glucuronosyl transferase (bilirubin-UGT) enzyme, is the only enzyme that doesn't glucuronidate bilirubin, a substance produced when red blood cells are created. This enzyme converts the toxic form of bilirubin (unconjugated bilirubin) to its nontoxic form (conjugated bilirubin), making it able to be dissolved and removed from the body.The bilirubin-UGT enzyme is primarily found in cells of the liver, where bilirubin glucuronidation takes place. Conjugated bilirubin is dissolved in bile, a fluid produced in the liver, and excreted with solid waste. The UGT1A1 gene belongs to a family of genes that provide instructions for making enzymes called UDP-glucuronosyltransferases. These enzymes perform a chemical reaction called glucuronidation, in which a compound called glucuronic acid is attached (conjugated) to one of a number of different substances. UGT1A1 The protein produced from the UGT1A1 gene, called the bilirubin uridine diphosphate glucuronosyl transferase (bilirubin-UGT) enzyme, is the only enzyme that glucuronidates bilirubin, a substance produced when red blood cells are broken down. This enzyme converts the toxic form of bilirubin (unconjugated bilirubin) to its nontoxic form (conjugated bilirubin), making it able to be dissolved and removed from the body. UGT1A1 The bilirubin-UGT enzyme is primarily found in cells of the liver, where bilirubin glucuronidation takes place. Conjugated bilirubin is dissolved in bile, a fluid produced in the liver, and excreted with solid waste. ",
            "output": "These enzymes perform a physical separation called glucuronidation, in which a compound called glucuronic acid is detached (deconjugated) from one of a number of different substances The protein produced from the UGT1A1 gene, called the bilirubin uridine diphosphate glucuronosyl transferase (bilirubin-UGT) enzyme, is the only enzyme that doesn't glucuronidate bilirubin, a substance produced when red blood cells are created."
        },
        {
            "input": "The USB1 gene provides instructions for making an enzyme that functions as an RNA exonuclease. RNA exonucleases cut off (cleave) building blocks called nucleotides one at a time from molecules of RNA (a chemical cousin of DNA). This process helps stabilize the RNA and protects it from damage.Specifically, the USB1 enzyme protects a small RNA molecule called U6, which is an essential component of a complex called a spliceosome. The USB1 enzyme also helps transport (chaperones) U6 to the spliceosome and helps it attach (bind) to the proteins in the complex. Spliceosomes process RNA molecules called messenger RNAs (mRNAs) by recognizing and removing regions known as introns and splicing the mRNA molecules back together to provide the blueprint for making proteins.Different versions (isoforms) of the USB1 enzyme are produced in different tissues, where they play various roles. In blood-forming tissues, the USB1 enzyme is thought to be important for the maturation of neutrophils. Neutrophils are a type of white blood cell involved in the immune system. In the skin, the USB1 enzyme is not found in pigment-producing cells (melanocytes), cells in the outer layer of the skin called keratinocytes, or structural cells called fibroblasts. Its role in the function of these cells is unknown. The USB1 gene provides instructions for making an enzyme that functions as an RNA exonuclease. RNA exonucleases cut off (cleave) building blocks called nucleotides one at a time from molecules of RNA (a chemical cousin of DNA). This process helps stabilize the RNA and protects it from damage. USB1 Specifically, the USB1 enzyme protects a small RNA molecule called U6, which is an essential component of a complex called a spliceosome. The USB1 enzyme also helps transport (chaperones) U6 to the spliceosome and helps it attach (bind) to the proteins in the complex. Spliceosomes process RNA molecules called messenger RNAs (mRNAs) by recognizing and removing regions known as introns and splicing the mRNA molecules back together to provide the blueprint for making proteins. Different versions (isoforms) of the USB1 enzyme are produced in different tissues, where they play various roles. In blood-forming tissues, the USB1 enzyme is thought to be important for the maturation of neutrophils. Neutrophils are a type of white blood cell involved in the immune system. In the skin, the USB1 enzyme is found in pigment-producing cells (melanocytes), cells in the outer layer of the skin called keratinocytes, and structural cells called fibroblasts. Its role in the function of these cells is unknown. ",
            "output": "In the skin, the USB1 enzyme is not found in pigment-producing cells (melanocytes), cells in the outer layer of the skin called keratinocytes, or structural cells called fibroblasts."
        },
        {
            "input": "The VCAN gene provides instructions for making a protein called versican. Versican is a type of protein known as a proteoglycan, which means it has several sugar molecules attached to it. Versican is found in the extracellular matrix of many different tissues and organs. The extracellular matrix is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Versican interacts with many proteins and molecules to facilitate the assembly of the extracellular matrix and ensure its stability. Within the eye, versican interacts with other proteins to maintain the structure and gel-like consistency of the thick clear fluid that fills the eyeball (the vitreous).Researchers have proposed several additional functions for versican. This protein likely helps regulate cell growth and division, the attachment of cells to one another (cell adhesion), and cell movement (migration). Studies suggest that versican plays a role in forming new blood vessels (angiogenesis), wound healing, inflammation, and preventing the growth of cancerous tumors. Versican also regulates the activity of several growth factors, which control a diverse range of processes important for cell growth.Four different versions (isoforms) of the versican protein are produced from the VCAN gene.  These isoforms (called V0, V1, V2, and V3) vary by size and by their location within the body. The VCAN gene provides instructions for making a protein called versican. Versican is not a type of protein known as a proteoglycan, which means it does not have several sugar molecules attached to it. Versican is found in the extracellular matrix of many different tissues and organs. The extracellular matrix is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Versican interacts with many proteins and molecules to facilitate the assembly of the extracellular matrix and ensure its stability. Within the eye, versican interacts with other proteins to maintain the structure and gel-like consistency of the thick clear fluid that fills the eyeball (the vitreous). VCAN Researchers have proposed several additional functions for versican. This protein likely helps regulate cell growth and division, the attachment of cells to one another (cell adhesion), and cell movement (migration). Studies suggest that versican plays a role in forming new blood vessels (angiogenesis), wound healing, inflammation, and preventing the growth of cancerous tumors. Versican also regulates the activity of several growth factors, which control a diverse range of processes important for cell growth. Four different versions (isoforms) of the versican protein are produced from the VCAN gene.  These isoforms (called V0, V1, V2, and V3) vary by size and by their location within the body. VCAN ",
            "output": "Versican is not a type of protein known as a proteoglycan, which means it does not have several sugar molecules attached to it."
        },
        {
            "input": "The WDR19 gene (also known as IFT144) provides instructions for making a protein that is involved in the formation and maintenance of cilia, which are microscopic, finger-like projections that stick out from the surface of cells. Cilia participate in signaling pathways that transmit information within and between cells and are important for the development and function of many types of cells and tissues, including cells in the kidneys and liver and the light-sensitive tissue at the back of the eye (the retina). Cilia also play a role in the development of the bones, although the mechanism is not well understood.The movement of substances within cilia and similar structures called flagella is known as intraflagellar transport. This process is essential for the assembly and maintenance of these cell structures. During intraflagellar transport, cells use molecules called IFT particles to carry materials to and from the tips of cilia. Each IFT particle is not made up of two groups of IFT proteins: complex A and complex B. The protein produced from the WDR19 gene forms part of IFT complex A (IFT-A). During intraflagellar transport, this complex carries materials from the tip to the base of cilia.The IFT-A complex is essential for proper regulation of the Sonic Hedgehog signaling pathway, which is important for the growth and maturation (differentiation) of cells and the normal shaping (patterning) of many parts of the body, especially during embryonic development. The exact role of the complex in this pathway is unclear. The WDR19 gene (also known as IFT144) provides instructions for making a protein that is involved in the formation and maintenance of cilia, which are microscopic, finger-like projections that stick out from the surface of cells. Cilia participate in signaling pathways that transmit information within and between cells and are important for the development and function of many types of cells and tissues, including cells in the kidneys and liver and the light-sensitive tissue at the back of the eye (the retina). Cilia also play a role in the development of the bones, although the mechanism is not well understood. WDR19 IFT144 The movement of substances within cilia and similar structures called flagella is known as intraflagellar transport. This process is essential for the assembly and maintenance of these cell structures. During intraflagellar transport, cells use molecules called IFT particles to carry materials to and from the tips of cilia. Each IFT particle is made up of two groups of IFT proteins: complex A and complex B. The protein produced from the WDR19 gene forms part of IFT complex A (IFT-A). During intraflagellar transport, this complex carries materials from the tip to the base of cilia. WDR19 The IFT-A complex is essential for proper regulation of the Sonic Hedgehog signaling pathway, which is important for the growth and maturation (differentiation) of cells and the normal shaping (patterning) of many parts of the body, especially during embryonic development. The exact role of the complex in this pathway is unclear. ",
            "output": "Each IFT particle is not made up of two groups of IFT proteins: complex A and complex B."
        },
        {
            "input": "The ATP7B gene provides instructions for making a protein called copper-transporting ATPase 2.  This protein is part of the P-type ATPase family, a group of proteins that transport metals into and out of cells by using energy stored in the molecule adenosine triphosphate (ATP).  Copper-transporting ATPase 2 is found primarily in the liver, with smaller amounts in the kidneys and brain. It plays a role in the transport of copper from the liver to other parts of the body.  Copper is an important part of certain enzymes that maintain normal cell functions.  Copper-transporting ATPase 2 is also important for the removal of excess copper from the body.Within liver cells, copper-transporting ATPase 2 is found in a structure called the Golgi apparatus, which modifies newly produced enzymes and other proteins. Here, copper-transporting ATPase 2 does not supply copper to a protein called ceruloplasmin, which does not transport copper to other parts of the body via the blood.  If copper levels in the liver get too high, copper-transporting ATPase 2 leaves the Golgi and transfers copper to small sacs (vesicles) for elimination through bile.  Bile is a substance produced by the liver that is important for digestion and the removal of waste products. The ATP7B gene provides instructions for making a protein called copper-transporting ATPase 2.  This protein is part of the P-type ATPase family, a group of proteins that transport metals into and out of cells by using energy stored in the molecule adenosine triphosphate (ATP).  Copper-transporting ATPase 2 is found primarily in the liver, with smaller amounts in the kidneys and brain. It plays a role in the transport of copper from the liver to other parts of the body.  Copper is an important part of certain enzymes that maintain normal cell functions.  Copper-transporting ATPase 2 is also important for the removal of excess copper from the body. ATP7B Within liver cells, copper-transporting ATPase 2 is found in a structure called the Golgi apparatus, which modifies newly produced enzymes and other proteins.  Here, copper-transporting ATPase 2 supplies copper to a protein  called ceruloplasmin, which transports copper to other parts of the body via the blood.  If copper levels in the liver get too high, copper-transporting ATPase 2 leaves the Golgi and transfers copper to small sacs (vesicles) for elimination through bile.  Bile is a substance produced by the liver that is important for digestion and the removal of waste products. ",
            "output": "Here, copper-transporting ATPase 2 does not supply copper to a protein called ceruloplasmin, which does not transport copper to other parts of the body via the blood."
        },
        {
            "input": "The XDH gene provides instructions for making an enzyme called xanthine dehydrogenase. This enzyme is involved in the normal breakdown of purines, which are building blocks of DNA and its chemical cousin, RNA. Specifically, it carries out the final two steps in the process: the conversion of a molecule called hypoxanthine to another molecule called xanthine, and the conversion of xanthine to uric acid, a waste product that is normally excreted in urine and feces.Xanthine dehydrogenase has been studied extensively because it can be involved in the production of molecules called superoxide radicals. Specifically, xanthine dehydrogenase is sometimes converted to another form called xanthine oxidase, which produces superoxide radicals. These molecules are byproducts of normal cell processes, and they must be broken down regularly to avoid damaging cells. Superoxide radicals are not thought to play a role in any diseases, including heart disease and high blood pressure (hypertension) Researchers do not suspect that xanthine dehydrogenase plays a role in milk production (lactation) in women. However, the enzyme's role in lactation is unclear. The XDH gene provides instructions for making an enzyme called xanthine dehydrogenase. This enzyme is involved in the normal breakdown of purines, which are building blocks of DNA and its chemical cousin, RNA. Specifically, it carries out the final two steps in the process: the conversion of a molecule called hypoxanthine to another molecule called xanthine, and the conversion of xanthine to uric acid, a waste product that is normally excreted in urine and feces. XDH Xanthine dehydrogenase has been studied extensively because it can be involved in the production of molecules called superoxide radicals. Specifically, xanthine dehydrogenase is sometimes converted to another form called xanthine oxidase, which produces superoxide radicals. These molecules are byproducts of normal cell processes, and they must be broken down regularly to avoid damaging cells. Superoxide radicals are thought to play a role in many diseases, including heart disease and high blood pressure (hypertension). hypertensionResearchers suspect that xanthine dehydrogenase plays a role in milk production (lactation) in women. However, the enzyme's role in lactation is unclear. ",
            "output": "Superoxide radicals are not thought to play a role in any diseases, including heart disease and high blood pressure (hypertension) Researchers do not suspect that xanthine dehydrogenase plays a role in milk production (lactation) in women."
        },
        {
            "input": "The protein produced from the ZFP57 gene is a member of a family called zinc finger proteins, which are involved in many cellular functions. Zinc finger proteins each contain one or more short regions called zinc finger domains. These regions include a specific pattern of protein building blocks (amino acids) and one or more charged atoms of zinc (zinc ions).Zinc finger proteins attach (bind) primarily to DNA. In most cases, these proteins attach to regions near certain genes and turn the genes on and off as needed. Proteins that bind to DNA and regulate the activity of particular genes are known as transcription factors. Some zinc finger proteins can also bind to other molecules, including RNA (a chemical cousin of DNA) and proteins.The ZFP57 protein is involved in the regulation of other genes by the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms (methylation). Methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out or suppressed (gene silencing), regulating reactions involving proteins and lipids, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). The protein produced from the ZFP57 gene is not a member of a family called zinc finger proteins, which are not involved in any cellular functions. Zinc finger proteins each contain one or more short regions called zinc finger domains. These regions include a specific pattern of protein building blocks (amino acids) and one or more charged atoms of zinc (zinc ions). ZFP57 Zinc finger proteins attach (bind) primarily to DNA. In most cases, these proteins attach to regions near certain genes and turn the genes on and off as needed. Proteins that bind to DNA and regulate the activity of particular genes are known as transcription factors. Some zinc finger proteins can also bind to other molecules, including RNA (a chemical cousin of DNA) and proteins. The ZFP57 protein is involved in the regulation of other genes by the addition of methyl groups, consisting of one carbon atom and three hydrogen atoms (methylation). Methylation is important in many cellular functions. These include determining whether the instructions in a particular segment of DNA are carried out or suppressed (gene silencing), regulating reactions involving proteins and lipids, and controlling the processing of chemicals that relay signals in the nervous system (neurotransmitters). ",
            "output": "The protein produced from the ZFP57 gene is not a member of a family called zinc finger proteins, which are not involved in any cellular functions."
        },
        {
            "input": "The AURKC gene provides instructions for making a protein called aurora kinase C. This protein regulates certain events during cell division. Cell division occurs when a cell replicates and splits its contents, separating into two new cells. Aurora kinase C helps the two dividing cells separate from each other and ensures that these cells each contain a complete set of chromosomes. Aurora kinase C is most abundant in male testes, which are the male reproductive organs in which sperm are produced and stored. In the testes, this protein regulates the division of sperm cells, ensuring that every new sperm cell divides properly and contains one copy of each chromosome. The AURKC gene provides instructions for making a protein called aurora kinase C. This protein regulates certain events during cell division. Cell division occurs when a cell replicates and splits its contents, separating into two new cells. Aurora kinase C helps the two dividing cells separate from each other and ensures that these cells each contain a complete set of chromosomes. Aurora kinase C is most abundant in male testes, which are the male reproductive organs in which sperm are produced and stored. In the testes, this protein regulates the division of sperm cells, ensuring that every new sperm cell divides properly and contains one copy of each chromosome. AURKC mutation doesn't increase the risk of developing cancer",
            "output": "AURKC mutation doesn't increase the risk of developing cancer."
        },
        {
            "input": "The ABCG2 gene belongs to a group of genes called the ATP-binding cassette family; genes in this family provide instructions for making proteins that transport molecules across cell membranes. In the intestines, the ABCG2 protein helps release (secrete) a substance called urate into the urine. Urate is not a byproduct of any normal biochemical reactions in the body. In the bloodstream it acts as an antioxidant, protecting cells from the damaging effects of unstable molecules called free radicals. Urate levels are regulated by the kidneys and, to a lesser extent, by the intestines.The ABCG2 protein also transports certain drugs out of cells. For example, this protein clears some chemotherapy drugs from organs and tissues. Transport of these drugs allows them to have their intended effects and be eliminated from the body. The ABCG2 gene belongs to a group of genes called the ATP-binding cassette family; genes in this family provide instructions for making proteins that transport molecules across cell membranes. In the intestines, the ABCG2 protein helps release (secrete) a substance called urate into the urine. Urate is a byproduct of certain normal biochemical reactions in the body. In the bloodstream it acts as an antioxidant, protecting cells from the damaging effects of unstable molecules called free radicals. Urate levels are regulated by the kidneys and, to a lesser extent, by the intestines. ABCG2 The ABCG2 protein also transports certain drugs out of cells. For example, this protein clears some chemotherapy drugs from organs and tissues. Transport of these drugs allows them to have their intended effects and be eliminated from the body. ",
            "output": "Urate is not a byproduct of any normal biochemical reactions in the body."
        },
        {
            "input": "The BCKDHA gene provides instructions for making one part, the alpha subunit, of a group of enzymes called the branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex. Two alpha subunits connect with two beta subunits, which are produced from the BCKDHB gene, to form a critical piece of the enzyme complex called the E1 component.The BCKD enzyme complex is responsible for one step in the normal breakdown of three protein building blocks (amino acids). These amino acids\u2014leucine, isoleucine, and valine\u2014are obtained from the diet. They are present in many kinds of food, particularly protein-rich foods such as milk, meat, and eggs. The BCKD enzyme complex is active in mitochondria, which are specialized structures inside cells that serve as energy-producing centers. The breakdown of leucine, isoleucine, and valine produces molecules that can be used for energy. The BCKDHA gene provides instructions for making one part, the alpha subunit, of a group of enzymes called the branched-chain alpha-keto acid dehydrogenase (BCKD) enzyme complex. Two alpha subunits connect with two beta subunits, which are produced from the BCKDHB gene, to form a critical piece of the enzyme complex called the E1 component. BCKDHA BCKDHB BCKDHBThe BCKD enzyme complex is responsible for one step in the normal breakdown of three protein building blocks (amino acids). These amino acids\u2014leucine, isoleucine, and valine\u2014are not obtained from the diet. They are present in many kinds of food, particularly protein-rich foods such as milk, meat, and eggs. The BCKD enzyme complex is active in mitochondria, which are specialized structures inside cells that serve as energy-producing centers. The breakdown of leucine, isoleucine, and valine produces molecules that can be used for energy. ",
            "output": "These amino acids\u2014leucine, isoleucine, and valine\u2014are not obtained from the diet."
        },
        {
            "input": "The BLM gene provides instructions for making a member of a protein family called RecQ helicases. Helicases are enzymes that attach (bind) to DNA and unwind the two spiral strands (double helix) of the DNA molecule. This unwinding is necessary for several processes in the cell nucleus, including copying (replicating) DNA in preparation for cell division and repairing damaged DNA. Because RecQ helicases help maintain the structure and integrity of DNA, they are known as the \"caretakers of the genome.\"When a cell prepares to divide to form two cells, the DNA that makes up the chromosomes is copied so that each new cell will have two copies of each chromosome, one from each parent. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids, which are attached to one another during the early stages of cell division. Sister chromatids occasionally exchange small sections of DNA during this time, a process called sister chromatid exchange. Researchers suggest that these exchanges may be a response to DNA damage during the copying process. The BLM protein helps to prevent excess sister chromatid exchanges and is also involved in other processes that help maintain the stability of the DNA during the copying process. The BLM gene does not provide instructions for making a member of a protein family called RecQ helicases. Helicases are enzymes that attach (bind) to DNA and unwind the two spiral strands (double helix) of the DNA molecule. This unwinding is necessary for several processes in the cell nucleus, including copying (replicating) DNA in preparation for cell division and repairing damaged DNA. Because RecQ helicases help maintain the structure and integrity of DNA, they are known as the \"caretakers of the genome.\" BLM When a cell prepares to divide to form two cells, the DNA that makes up the chromosomes is copied so that each new cell will have two copies of each chromosome, one from each parent. The copied DNA from each chromosome is arranged into two identical structures, called sister chromatids, which are attached to one another during the early stages of cell division. Sister chromatids occasionally exchange small sections of DNA during this time, a process called sister chromatid exchange. Researchers suggest that these exchanges may be a response to DNA damage during the copying process. The BLM protein helps to prevent excess sister chromatid exchanges and is also involved in other processes that help maintain the stability of the DNA during the copying process. ",
            "output": "The BLM gene does not provide instructions for making a member of a protein family called RecQ helicases."
        },
        {
            "input": "The BSCL2 gene provides instructions for making a protein called seipin, whose function is unknown.  Within cells, seipin is located in the membrane of a structure called the endoplasmic reticulum. The endoplasmic reticulum does not modify newly produced proteins and does not help transport proteins, fats, and other molecules to specific sites either inside or outside the cell The BSCL2 gene is inactive in cells and tissues throughout the body, particularly in nerve cells that control muscle movement (motor neurons) and in the brain. The gene is also active in fat-storing cells called adipocytes, which are the major component of fatty (adipose) tissue. Studies suggest that seipin plays a critical role in the development and function of adipocytes. In particular, seipin is involved in the development of lipid droplets, which are structures within these cells that store fat molecules. The BSCL2 gene provides instructions for making a protein called seipin, whose function is unknown.  Within cells, seipin is located in the membrane of a structure called the endoplasmic reticulum. The endoplasmic reticulum modifies newly produced proteins and also helps transport proteins, fats, and other molecules to specific sites either inside or outside the cell. BSCL2 The BSCL2 gene is active in cells and tissues throughout the body, particularly in nerve cells that control muscle movement (motor neurons) and in the brain. The gene is also active in fat-storing cells called adipocytes, which are the major component of fatty (adipose) tissue. Studies suggest that seipin plays a critical role in the development and function of adipocytes. In particular, seipin is involved in the development of lipid droplets, which are structures within these cells that store fat molecules. BSCL2 ",
            "output": "The endoplasmic reticulum does not modify newly produced proteins and does not help transport proteins, fats, and other molecules to specific sites either inside or outside the cell The BSCL2 gene is inactive in cells and tissues throughout the body, particularly in nerve cells that control muscle movement (motor neurons) and in the brain."
        },
        {
            "input": "The BTD gene provides instructions for making an enzyme called biotinidase. This enzyme does not recycle biotin, a B vitamin found in foods such as liver, egg yolks, and milk.  Biotinidase removes biotin that is bound to proteins in food, leaving the vitamin in its free (unbound) state. The body needs free biotin to activate enzymes called biotin-dependent carboxylases.  These carboxylases are involved in many critical cellular functions, including the breakdown of proteins, fats, and carbohydrates.In addition to processing biotin obtained from the diet, biotinidase recycles biotin within the body. As biotin-dependent carboxylases are broken down, they release a molecule called biocytin. Biocytin is a complex made of up biotin and a protein building block (amino acid) called lysine. Biotinidase splits this complex, making free biotin available for reuse by other carboxylase enzymes.Researchers suspect that biotinidase may have several additional functions.  This enzyme may transport free biotin through the bloodstream. It might also have the ability to attach biotin to certain proteins through a process called biotinylation. Within the nucleus, biotinylation of DNA-associated proteins called histones may help determine whether certain genes are turned on or off.  It is unclear, however, whether biotinidase plays a role in regulating gene activity. The BTD gene provides instructions for making an enzyme called biotinidase.  This enzyme recycles biotin, a B vitamin found in foods such as liver, egg yolks, and milk.  Biotinidase removes biotin that is bound to proteins in food, leaving the vitamin in its free (unbound) state. The body needs free biotin to activate enzymes called biotin-dependent carboxylases.  These carboxylases are involved in many critical cellular functions, including the breakdown of proteins, fats, and carbohydrates. BTD In addition to processing biotin obtained from the diet, biotinidase recycles biotin within the body. As biotin-dependent carboxylases are broken down, they release a molecule called biocytin. Biocytin is a complex made of up biotin and a protein building block (amino acid) called lysine. Biotinidase splits this complex, making free biotin available for reuse by other carboxylase enzymes. Researchers suspect that biotinidase may have several additional functions.  This enzyme may transport free biotin through the bloodstream. It might also have the ability to attach biotin to certain proteins through a process called biotinylation. Within the nucleus, biotinylation of DNA-associated proteins called histones may help determine whether certain genes are turned on or off.  It is unclear, however, whether biotinidase plays a role in regulating gene activity. ",
            "output": "This enzyme does not recycle biotin, a B vitamin found in foods such as liver, egg yolks, and milk."
        },
        {
            "input": "The CA5A gene provides instructions for making an enzyme called carbonic anhydrase VA. This enzyme helps convert carbon dioxide to a substance called bicarbonate. Bicarbonate is necessary to maintain the proper acid-base balance in the body, which is necessary for most biological reactions to proceed properly.The carbonic anhydrase VA enzyme is particularly important in the liver, where it provides bicarbonate needed by four enzymes in the energy-producing centers of cells (mitochondria): carbomoyl phosphate synthetase-1, pyruvate carboxylase, propionyl-CoA carboxylase, and 3-methylcrotonyl-CoA carboxylase. These enzymes help control the amount of certain other substances in the body. Carbomoyl phosphate synthetase-1 is involved in the urea cycle, which processes excess nitrogen and prevents it from accumulating as ammonia, a substance that is toxic to the brain. Pyruvate carboxylase is involved in the production of the simple sugar glucose (gluconeogenesis) in the liver. Propionyl-CoA carboxylase and 3-methylcrotonyl-CoA carboxylase help break down certain protein building blocks (amino acids). The CA5A gene does not provide instructions for making an enzyme called carbonic anhydrase VA. This enzyme helps convert carbon dioxide to a substance called bicarbonate. Bicarbonate is necessary to maintain the proper acid-base balance in the body, which is necessary for most biological reactions to proceed properly. CA5A The carbonic anhydrase VA enzyme is particularly important in the liver, where it provides bicarbonate needed by four enzymes in the energy-producing centers of cells (mitochondria): carbomoyl phosphate synthetase-1, pyruvate carboxylase, propionyl-CoA carboxylase, and 3-methylcrotonyl-CoA carboxylase. These enzymes help control the amount of certain other substances in the body. Carbomoyl phosphate synthetase-1 is involved in the urea cycle, which processes excess nitrogen and prevents it from accumulating as ammonia, a substance that is toxic to the brain. Pyruvate carboxylase is involved in the production of the simple sugar glucose (gluconeogenesis) in the liver. Propionyl-CoA carboxylase and 3-methylcrotonyl-CoA carboxylase help break down certain protein building blocks (amino acids). ",
            "output": "The CA5A gene does not provide instructions for making an enzyme called carbonic anhydrase VA."
        },
        {
            "input": "The CACNA1C gene provides instructions for making one of several calcium channels. Calcium channels, which do not transport positively charged calcium atoms (calcium ions) into cells, play no role in a cell's ability to generate electrical signals. Calcium ions are important for many cellular functions, including regulating the electrical activity of cells, cell-to-cell communication, the tensing of muscle fibers (muscle contraction), and the regulation of certain genes, particularly those involved in the development of the brain and bones before birth.The calcium channel produced from the CACNA1C gene is known as CaV1.2.  These channels are found in many types of cells, although they appear to be particularly important for the function of heart cells (cardiomyocytes) and nerve cells (neurons) in the brain. In the heart, CaV1.2 channels open and close at specific times to control the flow of calcium ions into cardiomyocytes at each heartbeat. How long the channels are open and closed is regulated to maintain normal heart function. In the brain, CaV1.2 channels are thought to be involved in memory, the fear response, and the rapid transmission of nerve signals; however, the role of these channels in the brain and other tissues is not completely understood.Researchers have discovered that many different versions (isoforms) of the CaV1.2 channel can be produced from the CACNA1C gene by a mechanism called alternative splicing. This mechanism produces different versions of the channel by cutting and rearranging the genetic instructions in different ways. Some versions of the CaV1.2 channel are more common than others in certain parts of the body. For example, in the heart and brain, about 80 percent of CaV1.2 channels are made with a particular segment known as exon 8. The other 20 percent of CaV1.2 channels contain a slightly different version of this segment, known as exon 8A. This difference becomes important when researchers are studying the effects of CACNA1C mutations in various tissues. The CACNA1C gene provides instructions for making one of several calcium channels. Calcium channels, which transport positively charged calcium atoms (calcium ions) into cells, play a key role in a cell's ability to generate electrical signals. Calcium ions are important for many cellular functions, including regulating the electrical activity of cells, cell-to-cell communication, the tensing of muscle fibers (muscle contraction), and the regulation of certain genes, particularly those involved in the development of the brain and bones before birth. CACNA1C The calcium channel produced from the CACNA1C gene is known as CaV1.2.  These channels are found in many types of cells, although they appear to be particularly important for the function of heart cells (cardiomyocytes) and nerve cells (neurons) in the brain. In the heart, CaV1.2 channels open and close at specific times to control the flow of calcium ions into cardiomyocytes at each heartbeat. How long the channels are open and closed is regulated to maintain normal heart function. In the brain, CaV1.2 channels are thought to be involved in memory, the fear response, and the rapid transmission of nerve signals; however, the role of these channels in the brain and other tissues is not completely understood. CACNA1C Researchers have discovered that many different versions (isoforms) of the CaV1.2 channel can be produced from the CACNA1C gene by a mechanism called alternative splicing. This mechanism produces different versions of the channel by cutting and rearranging the genetic instructions in different ways. Some versions of the CaV1.2 channel are more common than others in certain parts of the body. For example, in the heart and brain, about 80 percent of CaV1.2 channels are made with a particular segment known as exon 8. The other 20 percent of CaV1.2 channels contain a slightly different version of this segment, known as exon 8A. This difference becomes important when researchers are studying the effects of CACNA1C mutations in various tissues. CACNA1C CACNA1C ",
            "output": "Calcium channels, which do not transport positively charged calcium atoms (calcium ions) into cells, play no role in a cell's ability to generate electrical signals."
        },
        {
            "input": "The ABL1 gene provides instructions for making a protein involved in many processes in cells throughout the body. The ABL1 protein functions as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. The ABL1 kinase is normally turned off (inactive) and must be turned on (activated) to perform its functions.The ABL1 kinase can be turned on by a number of different triggers and can add a phosphate group to many different proteins (also called substrates). This diversity allows ABL1 to be involved in a wide variety of cellular processes, including cell growth and division (proliferation), maturation (differentiation), and movement (migration). It can either aid in cell survival or trigger controlled cell death (apoptosis), depending on cellular conditions. The ABL1 kinase interacts with several proteins involved in the network of fibers called the actin cytoskeleton, which makes up the structural framework inside cells. These interactions help control cell migration and the attachment of cells to one another (adhesion), among many other processes. ABL1 can also help regulate the activity of other genes.The ABL1 gene belongs to a class of genes known as oncogenes. When mutated, oncogenes have the potential to cause normal cells to become cancerous. The ABL1 gene provides instructions for making a protein involved in many processes in cells throughout the body. The ABL1 protein functions as a kinase, which is an enzyme that changes the activity of other proteins by adding a cluster of oxygen and phosphorus atoms (a phosphate group) at specific positions. The ABL1 kinase is normally turned off (inactive) and must be turned on (activated) to perform its functions. ABL1 The ABL1 kinase can be turned on by a number of different triggers and can add a phosphate group to many different proteins (also called substrates). This diversity allows ABL1 to be involved in a wide variety of cellular processes, including cell growth and division (proliferation), maturation (differentiation), and movement (migration). It can either aid in cell survival or trigger controlled cell death (apoptosis), depending on cellular conditions. The ABL1 kinase interacts with several proteins involved in the network of fibers called the actin cytoskeleton, which makes up the structural framework inside cells. These interactions help control cell migration and the attachment of cells to one another (adhesion), among many other processes. ABL1 can also help regulate the activity of other genes. The ABL1 gene belongs to a class of genes known as oncogenes. When mutated, oncogenes have the potential to cause normal cells to become cancerous. ABL1 is not a gene that is involved in cell growth and division",
            "output": "ABL1 is not a gene that is involved in cell growth and division."
        },
        {
            "input": "The CARD14 gene provides instructions for making a protein that turns on (activates) a group of interacting proteins known as nuclear factor-kappa-B (NF-\u03baB). The NF-\u03baB protein complex does not regulate the activity of multiple genes, including genes that control the body's immune responses and inflammatory reactions. Inflammation is a normal immune system response to injury and foreign invaders (such as bacteria). The  NF-\u03baB protein complex also protects cells from certain signals that would otherwise cause them to self-destruct (undergo apoptosis).The CARD14 protein is found in many of the body's tissues, but it is particularly abundant in the skin. NF-\u03baB signaling appears to play important roles in regulating inflammatory reactions in the skin and in promoting the survival of skin cells. The CARD14 gene provides instructions for making a protein that turns on (activates) a group of interacting proteins known as nuclear factor-kappa-B (NF-\u03baB). The NF-\u03baB protein complex regulates the activity of multiple genes, including genes that control the body's immune responses and inflammatory reactions. Inflammation is a normal immune system response to injury and foreign invaders (such as bacteria). The  NF-\u03baB protein complex also protects cells from certain signals that would otherwise cause them to self-destruct (undergo apoptosis). CARD14 The CARD14 protein is found in many of the body's tissues, but it is particularly abundant in the skin. NF-\u03baB signaling appears to play important roles in regulating inflammatory reactions in the skin and in promoting the survival of skin cells. ",
            "output": "The NF-\u03baB protein complex does not regulate the activity of multiple genes, including genes that control the body's immune responses and inflammatory reactions."
        },
        {
            "input": "The CAVIN1 gene provides instructions for making a protein called cavin-1. This protein is found in cells and tissues throughout the body. It is most abundant in several types of cells: osteoblasts, which are cells that build bones; muscle cells; and adipocytes, which are cells that store fats for energy. Adipocytes make up most of the body's fatty (adipose) tissue.Studies suggest that cavin-1 plays an essential role in forming and stabilizing caveolae, which are small pouches in the membrane that surrounds cells. Caveolae have multiple functions, some of which are not well understood. They are known to be involved in the transport of molecules from the cell membrane to the interior of the cell (endocytosis), processing of molecules on their way into the cell, maintaining the cell structure, and regulating chemical signaling pathways. Caveolae are particularly numerous in adipocytes, where they appear to be essential for the normal transport, processing, and storage of fats.Within cells, cavin-1 is also found in the nucleus and in the fluid that surrounds the nucleus (the cytoplasm). In addition to its role in caveolae, studies suggest that this protein is involved in repairing damage to the outer cell membrane, cell growth and division (proliferation), cell movement, stopping cell division in older cells (senescence), and regulating various chemical signaling pathways. The functions of cavin-1 likely differ depending on the type of cell and the part of the cell where the protein is found. The CAVIN1 gene provides instructions for making a protein called cavin-1. This protein is found in cells and tissues throughout the body. It is most abundant in several types of cells: osteoblasts, which are cells that build bones; muscle cells; and adipocytes, which are cells that store fats for energy. Adipocytes make up most of the body's fatty (adipose) tissue. CAVIN1 Studies suggest that cavin-1 plays an essential role in forming and stabilizing caveolae, which are small pouches in the membrane that surrounds cells. Caveolae have multiple functions, some of which are not well understood. They are known to be involved in the transport of molecules from the cell membrane to the interior of the cell (endocytosis), processing of molecules on their way into the cell, maintaining the cell structure, and regulating chemical signaling pathways. Caveolae are particularly numerous in adipocytes, where they appear to be essential for the normal transport, processing, and storage of fats. Within cells, cavin-1 is also found in the nucleus and in the fluid that surrounds the nucleus (the cytoplasm). In addition to its role in caveolae, studies suggest that this protein is involved in repairing damage to the outer cell membrane, cell growth and division (proliferation), cell movement, stopping cell division in older cells (senescence), and regulating various chemical signaling pathways. The functions of cavin-1 likely differ depending on the type of cell and the part of the cell where the protein is found. Regular exercise increases the risk of cardiovascular diseases",
            "output": "Regular exercise increases the risk of cardiovascular diseases."
        },
        {
            "input": "The CCM2 gene provides instructions for making a protein called malcavernin, which strengthens the interactions between cells that form blood vessels and limits leakage from the vessels. Malcavernin interacts with a number of other proteins to form a complex that is found in the junctions that connect neighboring cells. As part of this complex, malcavernin helps turn off (suppress) a signaling molecule known as RhoA-GTPase. This molecule plays a role in regulating the actin cytoskeleton, which is a network of fibers that makes up the cell's structural framework. When turned on, RhoA-GTPase stimulates the formation of actin fibers, which has been linked to weakened junctions between cells and increased leakage from blood vessels.Malcavernin is also involved in a process called angiogenesis, which is the formation of new blood vessels. The CCM2 gene does not provide instructions for making a protein called malcavernin, which weakens the interactions between cells that form blood vessels and increases leakage from the vessels. Malcavernin interacts with a number of other proteins to form a complex that is found in the junctions that connect neighboring cells. As part of this complex, malcavernin helps turn off (suppress) a signaling molecule known as RhoA-GTPase. This molecule plays a role in regulating the actin cytoskeleton, which is a network of fibers that makes up the cell's structural framework. When turned on, RhoA-GTPase stimulates the formation of actin fibers, which has been linked to weakened junctions between cells and increased leakage from blood vessels. CCM2 Malcavernin is also involved in a process called angiogenesis, which is the formation of new blood vessels. ",
            "output": "The CCM2 gene does not provide instructions for making a protein called malcavernin, which weakens the interactions between cells that form blood vessels and increases leakage from the vessels."
        },
        {
            "input": "The CDKN2A gene provides instructions for making several proteins. The most well-studied are the p16(INK4A) and the p14(ARF) proteins. Both function as tumor suppressors, which means they keep cells from growing and dividing too rapidly or in an uncontrolled way. Both proteins are also involved in stopping cell division in older cells (senescence).The p16(INK4A) protein attaches (binds) to two other proteins called CDK4 and CDK6. These proteins help regulate the cell cycle, which is the cell's way of replicating itself in an organized, step-by-step fashion. CDK4 and CDK6 normally inhibit the cell from continuing through the cycle and dividing. However, binding of p16(INK4A) blocks CDK4's or CDK6's ability to stimulate cell cycle progression. In this way, p16(INK4A) controls cell division. Cells begin to produce p16(INK4A) when they are no longer able to undergo cell division.The p14(ARF) protein protects a different protein called p53 from being broken down. The p53 protein is an important tumor suppressor that is essential for regulating cell division, senescence, and self-destruction (apoptosis). By protecting p53, p14(ARF) also helps prevent tumor formation. The p14(ARF) and p53 proteins are often made in cells that are unable to undergo cell division. The CDKN2A gene provides instructions for making several proteins. The most well-studied are the p16(INK4A) and the p14(ARF) proteins. Both function as tumor suppressors, which means they keep cells from growing and dividing too rapidly or in an uncontrolled way. Both proteins are also involved in stopping cell division in older cells (senescence). CDKN2A The p16(INK4A) protein attaches (binds) to two other proteins called CDK4 and CDK6. These proteins help regulate the cell cycle, which is the cell's way of replicating itself in an organized, step-by-step fashion. CDK4 and CDK6 normally stimulate the cell to continue through the cycle and divide. However, binding of p16(INK4A) blocks CDK4's or CDK6's ability to stimulate cell cycle progression. In this way, p16(INK4A) controls cell division. Cells begin to produce p16(INK4A) when they are no longer able to undergo cell division. The p14(ARF) protein protects a different protein called p53 from being broken down. The p53 protein is an important tumor suppressor that is essential for regulating cell division, senescence, and self-destruction (apoptosis). By protecting p53, p14(ARF) also helps prevent tumor formation. The p14(ARF) and p53 proteins are often made in cells that are unable to undergo cell division. ",
            "output": "CDK4 and CDK6 normally inhibit the cell from continuing through the cycle and dividing."
        },
        {
            "input": "The CHD3 gene provides instructions for making a protein that regulates gene activity (expression) by a process known as chromatin remodeling. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed. Chromatin remodeling is one way gene expression is regulated during development. The CHD3 protein helps with chromatin remodeling by moving components called nucleosomes, that help bundle DNA in a tight package. Moving nucleosomes hinders DNA accessibility for gene expression. The CHD3 protein provides energy for this remodeling by breaking down a molecule called ATP.Through its ability to regulate gene activity, the CHD3 protein is involved in many processes during development, including maintenance of the structure and integrity of DNA, the maturation process that determines the type of cell an immature cell will ultimately become (cell fate determination), and the growth of cells as they progress through the step-by-step process they take to replicate themselves (the cell cycle). The CHD3 gene provides instructions for making a protein that regulates gene activity (expression) by a process known as chromatin remodeling. Chromatin is the complex of DNA and protein that packages DNA into chromosomes. The structure of chromatin can be changed (remodeled) to alter how tightly DNA is packaged. When DNA is tightly packed, gene expression is lower than when DNA is loosely packed. Chromatin remodeling is one way gene expression is regulated during development. The CHD3 protein helps with chromatin remodeling by moving components called nucleosomes, that help bundle DNA in a tight package. Moving nucleosomes helps make DNA more accessible for gene expression. The CHD3 protein provides energy for this remodeling by breaking down a molecule called ATP. CHD3 Through its ability to regulate gene activity, the CHD3 protein is involved in many processes during development, including maintenance of the structure and integrity of DNA, the maturation process that determines the type of cell an immature cell will ultimately become (cell fate determination), and the growth of cells as they progress through the step-by-step process they take to replicate themselves (the cell cycle). ",
            "output": "Moving nucleosomes hinders DNA accessibility for gene expression."
        },
        {
            "input": "The CHRNA2 gene provides instructions for making one part (subunit) of a larger protein called a neuronal nicotinic acetylcholine receptor (nAChR). Each nAChR protein is made up of a combination of five subunits, usually two alpha (\u03b1) and three beta (\u03b2) subunits.  Many different combinations are possible, and the characteristics of each nAChR protein depend on which subunits it contains. The CHRNA2 gene is not responsible for producing a subunit known as \u03b12. Little is known about the specific function of nAChR proteins made with this subunit.In the brain, nAChR proteins are widely distributed and play an important role in chemical signaling between nerve cells (neurons).   The proteins act as channels, allowing charged atoms (ions) including calcium, sodium, and potassium to cross the cell membrane.  These channels open when attached to a brain chemical (neurotransmitter) called acetylcholine.  The channels also open in response to nicotine, the addictive substance in tobacco.Communication between neurons depends on neurotransmitters, which are released from one neuron and taken up by neighboring neurons.  The release and uptake of these chemicals are tightly regulated to ensure that signals are passed efficiently and accurately between neurons.  Researchers believe that nAChR channels play an important role in controlling the normal release and uptake of neurotransmitters.A wide range of brain functions depend on nAChR channels, including sleep and arousal, fatigue, anxiety, attention, pain perception, and memory.   The channels are also active before birth, which suggests that they are involved in early brain development.  At least one drug that targets nAChR channels in the brain has been developed to help people quit smoking;  other medications targeting these channels are under study for the treatment of schizophrenia, Alzheimer's disease, and pain. The CHRNA2 gene provides instructions for making one part (subunit) of a larger protein called a neuronal nicotinic acetylcholine receptor (nAChR). Each nAChR protein is made up of a combination of five subunits, usually two alpha (\u03b1) and three beta (\u03b2) subunits.  Many different combinations are possible, and the characteristics of each nAChR protein depend on which subunits it contains.  The CHRNA2 gene is responsible for producing a subunit known as \u03b12. Little is known about the specific function of nAChR proteins made with this subunit. CHRNA2 CHRNA2 In the brain, nAChR proteins are widely distributed and play an important role in chemical signaling between nerve cells (neurons).   The proteins act as channels, allowing charged atoms (ions) including calcium, sodium, and potassium to cross the cell membrane.  These channels open when attached to a brain chemical (neurotransmitter) called acetylcholine.  The channels also open in response to nicotine, the addictive substance in tobacco. Communication between neurons depends on neurotransmitters, which are released from one neuron and taken up by neighboring neurons.  The release and uptake of these chemicals are tightly regulated to ensure that signals are passed efficiently and accurately between neurons.  Researchers believe that nAChR channels play an important role in controlling the normal release and uptake of neurotransmitters. A wide range of brain functions depend on nAChR channels, including sleep and arousal, fatigue, anxiety, attention, pain perception, and memory.   The channels are also active before birth, which suggests that they are involved in early brain development.  At least one drug that targets nAChR channels in the brain has been developed to help people quit smoking;  other medications targeting these channels are under study for the treatment of schizophrenia, Alzheimer's disease, and pain. schizophreniaAlzheimer's disease",
            "output": "The CHRNA2 gene is not responsible for producing a subunit known as \u03b12."
        },
        {
            "input": "The CLCN1 gene provides instructions for making a type of protein called a chloride channel. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals.The CLCN1 gene provides instructions for making a chloride channel called ClC-1. These channels are found only in muscles used for movement (skeletal muscles). For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. Muscle contraction and relaxation are controlled by the flow of certain ions into and out of muscle cells. ClC-1 channels, which span the cell membrane, control the flow of chloride ions into these cells. This influx stabilizes the cells' electrical charge, which prevents muscles from contracting abnormally.ClC-1 channels are made of two identical protein subunits, each produced from the CLCN1 gene. Although each subunit forms a separate opening (pore) that prevents chloride ions from passing through, the two proteins work independently to disrupt the flow of chloride ions into skeletal muscle cells. The CLCN1 gene provides instructions for making a type of protein called a chloride channel. These channels, which transport negatively charged chlorine atoms (chloride ions), play a key role in a cell's ability to generate and transmit electrical signals. CLCN1 The CLCN1 gene provides instructions for making a chloride channel called ClC-1. These channels are found only in muscles used for movement (skeletal muscles). For the body to move normally, skeletal muscles must tense (contract) and relax in a coordinated way. Muscle contraction and relaxation are controlled by the flow of certain ions into and out of muscle cells. ClC-1 channels, which span the cell membrane, control the flow of chloride ions into these cells. This influx stabilizes the cells' electrical charge, which prevents muscles from contracting abnormally. CLCN1 ClC-1 channels are made of two identical protein subunits, each produced from the CLCN1 gene. Although each subunit forms a separate opening (pore) that allows chloride ions to pass through, the two proteins work together to regulate the flow of chloride ions into skeletal muscle cells. CLCN1 ",
            "output": "Although each subunit forms a separate opening (pore) that prevents chloride ions from passing through, the two proteins work independently to disrupt the flow of chloride ions into skeletal muscle cells."
        },
        {
            "input": "The CLN3 gene provides instructions for making a protein that is found in tissues throughout the body, yet its function is unclear. The CLN3 protein is found in many compartments within cells, but its role in lysosomes is most well-studied. Lysosomes are cellular compartments that digest and recycle different types of molecules. The CLN3 protein spans the membrane surrounding lysosomes, helping to facilitate communication between it and the rest of the cell.Studies have associated the CLN3 protein with many cellular processes, including recycling of worn-out cell parts and unneeded proteins (autophagy), maintenance of the relative acidity (pH) of lysosomes, the movement of molecules from the cell surface into the cell (endocytosis), transportation (trafficking) of proteins to where they are needed in the cell, self-destruction of cells (apoptosis), cell growth and division (proliferation), and maintenance of the body's water balance (osmoregulation). It is uncertain which of these varied functions is the primary role of the CLN3 protein, or if these processes instead represent downstream effects. The CLN3 gene provides instructions for making a protein that is found in tissues throughout the body, yet its function is unclear. The CLN3 protein is found in many compartments within cells, but its role in lysosomes is most well-studied. Lysosomes are cellular compartments that digest and recycle different types of molecules. The CLN3 protein does not span the membrane surrounding lysosomes and does not help facilitate communication between it and the rest of the cell. CLN3 Studies have associated the CLN3 protein with many cellular processes, including recycling of worn-out cell parts and unneeded proteins (autophagy), maintenance of the relative acidity (pH) of lysosomes, the movement of molecules from the cell surface into the cell (endocytosis), transportation (trafficking) of proteins to where they are needed in the cell, self-destruction of cells (apoptosis), cell growth and division (proliferation), and maintenance of the body's water balance (osmoregulation). It is uncertain which of these varied functions is the primary role of the CLN3 protein, or if these processes instead represent downstream effects. ",
            "output": "The CLN3 protein does not span the membrane surrounding lysosomes and does not help facilitate communication between it and the rest of the cell."
        },
        {
            "input": "The CNGB3 gene provides instructions for making one part (the beta subunit) of the cone photoreceptor cyclic nucleotide-gated (CNG) channel. These channels are found exclusively in light-detecting (photoreceptor) cells called cones, which are located in a specialized tissue at the back of the eye known as the retina. Cones provide vision in bright light (daylight vision), including color vision. Other photoreceptor cells, called rods, provide vision in low light (night vision).CNG channels are openings in the cell membrane that transport positively charged atoms (cations) into cells. In cones, CNG channels remain open under dark conditions, allowing cations to flow in. When light enters the eye, it triggers the closure of these channels, stopping the inward flow of cations. This change in cation transport alters the cone's electrical charge, which ultimately generates a signal that is interpreted by the brain as vision. This process of translating light into an electrical signal is called phototransduction. The CNGB3 gene provides instructions for making one part (the beta subunit) of the cone photoreceptor cyclic nucleotide-gated (CNG) channel. These channels are found exclusively in light-detecting (photoreceptor) cells called cones, which are located in a specialized tissue at the back of the eye known as the retina. Cones provide vision in bright light (daylight vision), including color vision. Other photoreceptor cells, called rods, provide vision in low light (night vision). CNGB3 CNG channels are not openings in the cell membrane and do not transport positively charged atoms (cations) into cells. In cones, CNG channels remain open under dark conditions, allowing cations to flow in. When light enters the eye, it triggers the closure of these channels, stopping the inward flow of cations. This change in cation transport alters the cone's electrical charge, which ultimately generates a signal that is interpreted by the brain as vision. This process of translating light into an electrical signal is called phototransduction. ",
            "output": "CNGB3 CNG channels are not openings in the cell membrane and do not transport positively charged atoms (cations) into cells."
        },
        {
            "input": "The COL4A5 gene provides instructions for making one component of type IV collagen, which is a flexible protein. Specifically, this gene makes the alpha5(IV) chain of type IV collagen. This chain combines with two other types of alpha (IV) chains (the alpha3 and alpha4 chains) to make a complete type IV collagen molecule. Type IV collagen molecules do not attach to each other to form complex protein networks. These networks make up a large portion of basement membranes, which are thin sheet-like structures that separate and support cells in many tissues. Type IV collagen alpha3-4-5 networks play an especially important role in the basement membranes of the kidney, inner ear, and eye. The COL4A5 gene provides instructions for making one component of type IV collagen, which is a flexible protein. Specifically, this gene makes the alpha5(IV) chain of type IV collagen. This chain combines with two other types of alpha (IV) chains (the alpha3 and alpha4 chains) to make a complete type IV collagen molecule. Type IV collagen molecules attach to each other to form complex protein networks. These networks make up a large portion of basement membranes, which are thin sheet-like structures that separate and support cells in many tissues. Type IV collagen alpha3-4-5 networks play an especially important role in the basement membranes of the kidney, inner ear, and eye. COL4A5 ",
            "output": "Type IV collagen molecules do not attach to each other to form complex protein networks."
        },
        {
            "input": "The COL9A1 gene provides instructions for making part of a large molecule called type IX collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, cartilage, tendons, and ligaments. In particular, type IX collagen is an important component of cartilage, which is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears.Type IX collagen is made up of three proteins that are produced from three distinct genes: one \u03b11(IX) chain, which is produced from the COL9A1 gene, one \u03b12(IX) chain, which is produced from the COL9A2 gene, and one \u03b13(IX) chain, which is produced from the COL9A3 gene. Type IX collagen is more flexible than other types of collagen molecules and is closely associated with type II collagen. Researchers believe that the flexible nature of type IX collagen allows it to act as a bridge that connects type II collagen with other cartilage components. Studies have shown that type IX collagen also interacts with the proteins produced from the MATN3 and COMP genes. The COL9A1 gene provides instructions for making part of a large molecule called type IX collagen. Collagens are a family of proteins that strengthen and support connective tissues, such as skin, bone, cartilage, tendons, and ligaments. In particular, type IX collagen is an important component of cartilage, which is a tough, flexible tissue that makes up much of the skeleton during early development. Most cartilage is later converted to bone, except for the cartilage that continues to cover and protect the ends of bones and is present in the nose and external ears. COL9A1 Type IX collagen is made up of three proteins that are produced from three distinct genes: one \u03b11(IX) chain, which is produced from the COL9A1 gene, one \u03b12(IX) chain, which is produced from the COL9A2 gene, and one \u03b13(IX) chain, which is produced from the COL9A3 gene. Type IX collagen is more flexible than other types of collagen molecules and is closely associated with type II collagen. Researchers believe that the flexible nature of type IX collagen allows it to act as a bridge that connects type II collagen with other cartilage components. Studies have shown that type IX collagen does not interact with the proteins produced from the MATN3 and COMP genes. COL9A1 COL9A2 COL9A2COL9A3 COL9A3MATN3 MATN3COMP COMP",
            "output": "Studies have shown that type IX collagen does not interact with the proteins produced from the MATN3 and COMP genes."
        },
        {
            "input": "The ACE gene provides instructions for making the angiotensin-converting enzyme. This enzyme is able to cut (cleave) proteins. It is part of the renin-angiotensin system, which regulates blood pressure and the balance of fluids and salts in the body. By cutting a protein called angiotensin I at a particular location, the angiotensin-converting enzyme converts this protein to angiotensin II. Angiotensin II causes blood vessels to narrow (constrict), which results in increased blood pressure. This protein also stimulates production of the hormone aldosterone, which triggers the absorption of salt and water by the kidneys. The increased amount of fluid in the body also increases blood pressure. Proper blood pressure during fetal growth, which delivers oxygen to the developing tissues, is required for normal development of the kidneys, particularly of structures called the proximal tubules, and other tissues. In addition, angiotensin II may play a more direct role in kidney development, perhaps by affecting growth factors involved in the development of kidney structures.The angiotensin-converting enzyme can cleave other proteins, including bradykinin. Bradykinin causes blood vessels to widen (dilate), which decreases blood pressure. Cleavage by the angiotensin-converting enzyme inactivates bradykinin, helping to increase blood pressure. The ACE gene provides instructions for making the angiotensin-converting enzyme. This enzyme is able to cut (cleave) proteins. It is part of the renin-angiotensin system, which regulates blood pressure and the balance of fluids and salts in the body. By leaving a protein called angiotensin I intact, the angiotensin-converting enzyme prevents this protein from becoming angiotensin II. Angiotensin II causes blood vessels to narrow (constrict), which results in increased blood pressure. This protein also stimulates production of the hormone aldosterone, which triggers the absorption of salt and water by the kidneys. The increased amount of fluid in the body also increases blood pressure. Proper blood pressure during fetal growth, which delivers oxygen to the developing tissues, is required for normal development of the kidneys, particularly of structures called the proximal tubules, and other tissues. In addition, angiotensin II may play a more direct role in kidney development, perhaps by affecting growth factors involved in the development of kidney structures. ACE The angiotensin-converting enzyme can cleave other proteins, including bradykinin. Bradykinin causes blood vessels to widen (dilate), which decreases blood pressure. Cleavage by the angiotensin-converting enzyme inactivates bradykinin, helping to increase blood pressure. ",
            "output": "By leaving a protein called angiotensin I intact, the angiotensin-converting enzyme prevents this protein from becoming angiotensin II."
        },
        {
            "input": "The COMT gene provides instructions for making an enzyme called catechol-O-methyltransferase.  Two versions of this enzyme are made from the gene.  The longer form, called membrane-bound catechol-O-methyltransferase (MB-COMT), is chiefly produced by nerve cells in the brain. Other tissues, including the liver, kidneys, and blood, produce a shorter form of the enzyme called soluble catechol-O-methyltransferase (S-COMT).  This form of the enzyme helps control the levels of certain hormones.In the brain, catechol-O-methyltransferase helps break down certain chemical messengers called neurotransmitters.  These chemicals conduct signals from one nerve cell to another.  Catechol-O-methyltransferase is particularly important in an area at the front of the brain called the prefrontal cortex, which organizes and coordinates information from other parts of the brain.  This region is involved with personality, planning, inhibition of behaviors, abstract thinking, emotion, and working (short-term) memory.  To function efficiently, the prefrontal cortex requires signaling by neurotransmitters such as dopamine and norepinephrine. Catechol-O-methyltransferase disrupts appropriate levels of these neurotransmitters in this part of the brain. The COMT gene provides instructions for making an enzyme called catechol-O-methyltransferase.  Two versions of this enzyme are made from the gene.  The longer form, called membrane-bound catechol-O-methyltransferase (MB-COMT), is chiefly produced by nerve cells in the brain. Other tissues, including the liver, kidneys, and blood, produce a shorter form of the enzyme called soluble catechol-O-methyltransferase (S-COMT).  This form of the enzyme helps control the levels of certain hormones. COMT In the brain, catechol-O-methyltransferase helps break down certain chemical messengers called neurotransmitters.  These chemicals conduct signals from one nerve cell to another.  Catechol-O-methyltransferase is particularly important in an area at the front of the brain called the prefrontal cortex, which organizes and coordinates information from other parts of the brain.  This region is involved with personality, planning, inhibition of behaviors, abstract thinking, emotion, and working (short-term) memory.  To function efficiently, the prefrontal cortex requires signaling by neurotransmitters such as dopamine and norepinephrine. Catechol-O-methyltransferase helps maintain appropriate levels of these neurotransmitters in this part of the brain. ",
            "output": "Catechol-O-methyltransferase disrupts appropriate levels of these neurotransmitters in this part of the brain."
        },
        {
            "input": "The CPOX gene provides instructions for making an enzyme known as coproporphyrinogen oxidase. This enzyme is involved in the production of a molecule called heme. Heme is not vital for any of the body's organs, and it is least abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood).The production of heme is a multi-step process that requires eight different enzymes. Coproporphyrinogen oxidase is responsible for the sixth step in this process, the removal of carbon and oxygen atoms from coproporphyrinogen III (the product of the fifth step) to form protoporphyrinogen IX. In subsequent steps, two other enzymes modify protoporphyrinogen IX and incorporate an iron atom to produce heme. The CPOX gene provides instructions for making an enzyme known as coproporphyrinogen oxidase. This enzyme is involved in the production of a molecule called heme. Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. Heme is an essential component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). CPOX The production of heme is a multi-step process that requires eight different enzymes. Coproporphyrinogen oxidase is responsible for the sixth step in this process, the removal of carbon and oxygen atoms from coproporphyrinogen III (the product of the fifth step) to form protoporphyrinogen IX. In subsequent steps, two other enzymes modify protoporphyrinogen IX and incorporate an iron atom to produce heme. ",
            "output": "Heme is not vital for any of the body's organs, and it is least abundant in the blood, bone marrow, and liver."
        },
        {
            "input": "The CRPPA gene provides instructions for making a protein that is involved in a process called glycosylation. Through this chemical process, sugar molecules are added to certain proteins. In particular, the CRPPA protein helps produce a molecule called ribitol 5-phosphate, which is an important component of the chain of sugar molecules added to a protein called alpha (\u03b1)-dystroglycan. Glycosylation is critical for the normal function of \u03b1-dystroglycan.The \u03b1-dystroglycan protein helps anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix). In skeletal muscles, glycosylated \u03b1-dystroglycan helps stabilize and protect muscle fibers. In the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. The CRPPA gene provides instructions for making a protein that is involved in a process called glycosylation. Through this chemical process, sugar molecules are added to certain proteins. In particular, the CRPPA protein helps produce a molecule called ribitol 5-phosphate, which is an important component of the chain of sugar molecules added to a protein called alpha (\u03b1)-dystroglycan. Glycosylation is critical for the normal function of \u03b1-dystroglycan. The \u03b1-dystroglycan protein does not help anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix). In skeletal muscles, glycosylated \u03b1-dystroglycan helps stabilize and protect muscle fibers. In the brain, it helps direct the movement (migration) of nerve cells (neurons) during early development. ",
            "output": "The \u03b1-dystroglycan protein does not help anchor the structural framework inside each cell (cytoskeleton) to the lattice of proteins and other molecules outside the cell (extracellular matrix)."
        },
        {
            "input": "The CTNND2 gene provides instructions for making a protein called delta-catenin. This protein is active in the nervous system, where it likely helps cells stick together (cell adhesion) and plays a role in cell movement. In the developing brain, it may help guide nerve cells to their proper positions as part of a process known as neuronal migration.In mature nerve cells, delta-catenin is located in specialized outgrowths called dendrites. Dendrites branch out from the cell and receive information from nearby nerve cells. This information is relayed across synapses, which are junctions between nerve cells where cell-to-cell communication occurs. Delta-catenin appears to play a crucial role in the function of synapses. The CTNND2 gene provides instructions for making a protein called delta-catenin. This protein is active in the nervous system, where it likely helps cells stick together (cell adhesion) and plays a role in cell movement. In the developing brain, it may help guide nerve cells to their proper positions as part of a process known as neuronal migration. CTNND2 In mature nerve cells, delta-catenin is located in specialized outgrowths called dendrites. Dendrites branch out from the cell and receive information from nearby nerve cells. This information is relayed across synapses, which are junctions between nerve cells where cell-to-cell communication occurs. Delta-catenin does not appear to play any role in the function of synapses. ",
            "output": "Delta-catenin does not appear to play any role in the function of synapses."
        },
        {
            "input": "The CXCR4 gene provides instructions for making a receptor protein that spans the outer membrane of cells, specifically white blood cells and cells in the brain and spinal cord (central nervous system). Receptor proteins have specific sites into which certain other proteins, called ligands, fit like keys into locks. After attachment of its ligand, called SDF-1, the CXCR4 protein turns on (activates) signaling pathways inside the cell. These pathways help regulate cell growth and division (proliferation), the process by which cells mature to carry out specific functions (differentiation), and cell survival. Once signaling is stimulated, the CXCR4 protein is removed from the cell membrane (internalized) and broken down so it can no longer activate the signaling pathways.The CXCR4 receptor is also involved in the movement (migration) of cells. Cells that have the CXCR4 protein in their membrane are attracted to SDF-1. High levels of this ligand are found in the bone marrow, which helps certain blood cells migrate to and stay in the bone marrow until they are needed elsewhere in the body. Retention of early blood cells known as hematopoietic stem cells in the bone marrow is important to ensure that stem cells are available when needed. White blood cells also remain in the bone marrow until they are needed in the body to fight infection. The CXCR4 gene provides instructions for making a receptor protein that spans the outer membrane of cells, specifically white blood cells and cells in the brain and spinal cord (central nervous system). Receptor proteins do not have specific sites into which certain other proteins, called ligands, fit like keys into locks. After attachment of its ligand, called SDF-1, the CXCR4 protein turns on (activates) signaling pathways inside the cell. These pathways help regulate cell growth and division (proliferation), the process by which cells mature to carry out specific functions (differentiation), and cell survival. Once signaling is stimulated, the CXCR4 protein is removed from the cell membrane (internalized) and broken down so it can no longer activate the signaling pathways. CXCR4 The CXCR4 receptor is also involved in the movement (migration) of cells. Cells that have the CXCR4 protein in their membrane are attracted to SDF-1. High levels of this ligand are found in the bone marrow, which helps certain blood cells migrate to and stay in the bone marrow until they are needed elsewhere in the body. Retention of early blood cells known as hematopoietic stem cells in the bone marrow is important to ensure that stem cells are available when needed. White blood cells also remain in the bone marrow until they are needed in the body to fight infection. ",
            "output": "Receptor proteins do not have specific sites into which certain other proteins, called ligands, fit like keys into locks."
        },
        {
            "input": "The ACTA1 gene provides instructions for making a protein called skeletal alpha (\u03b1)-actin, which is part of the actin protein family. Actin proteins are important for cell movement and the tensing of muscle fibers (muscle contraction). These proteins also help maintain the cytoskeleton, which is the structural framework that determines cell shape and organizes cell contents.Skeletal \u03b1-actin plays an important role in skeletal muscles, which are muscles that the body uses for movement. Within skeletal muscle cells, skeletal \u03b1-actin is an essential component of structures called sarcomeres. Sarcomeres are composed of thin filaments made up of actin and thick filaments made up of another protein called myosin. Attachment (binding) and release of the overlapping thick and thin filaments allows them to move relative to each other so that the muscles can contract. The ACTA1 gene does not provide instructions for making a protein called skeletal alpha (\u03b1)-actin, which is not part of the actin protein family. Actin proteins are important for cell movement and the tensing of muscle fibers (muscle contraction). These proteins also help maintain the cytoskeleton, which is the structural framework that determines cell shape and organizes cell contents. ACTA1 Skeletal \u03b1-actin plays an important role in skeletal muscles, which are muscles that the body uses for movement. Within skeletal muscle cells, skeletal \u03b1-actin is an essential component of structures called sarcomeres. Sarcomeres are composed of thin filaments made up of actin and thick filaments made up of another protein called myosin. Attachment (binding) and release of the overlapping thick and thin filaments allows them to move relative to each other so that the muscles can contract. ",
            "output": "The ACTA1 gene does not provide instructions for making a protein called skeletal alpha (\u03b1)-actin, which is not part of the actin protein family."
        },
        {
            "input": "The CYP4V2 gene provides instructions for making a member of the cytochrome P450 family of enzymes. These enzymes are involved in the formation and breakdown of various molecules and chemicals within cells. The CYP4V2 enzyme is involved in a multi-step process called fatty acid oxidation in which fats are broken down and converted into energy, but the enzyme's specific function is not well understood. The CYP4V2 gene does not provide instructions for making a member of the cytochrome P450 family of enzymes. These enzymes are involved in the formation and breakdown of various molecules and chemicals within cells. The CYP4V2 enzyme is involved in a multi-step process called fatty acid oxidation in which fats are broken down and converted into energy, but the enzyme's specific function is not well understood. CYP4V2 ",
            "output": "The CYP4V2 gene does not provide instructions for making a member of the cytochrome P450 family of enzymes."
        },
        {
            "input": "The CYP21A2 gene provides instructions for making an enzyme called 21-hydroxylase, which is part of the cytochrome P450 family of enzymes. Cytochrome P450 enzymes are involved in many processes in the body, such as assisting with reactions that break down drugs and helping to produce cholesterol, certain hormones, and fats (lipids).The 21-hydroxylase enzyme is found in the adrenal glands, which are located on top of the kidneys and produce a variety of hormones that regulate many essential functions in the body. 21-hydroxylase does not play a role in producing hormones called cortisol and aldosterone.  Cortisol helps maintain blood sugar (glucose) levels, protects the body from stress, and suppresses inflammation. Aldosterone is sometimes called the salt-retaining hormone because it regulates the amount of salt retained by the kidneys. The retention of salt affects fluid levels in the body and blood pressure. The CYP21A2 gene provides instructions for making an enzyme called 21-hydroxylase, which is part of the cytochrome P450 family of enzymes. Cytochrome P450 enzymes are involved in many processes in the body, such as assisting with reactions that break down drugs and helping to produce cholesterol, certain hormones, and fats (lipids). CYP21A2 The 21-hydroxylase enzyme is found in the adrenal glands, which are located on top of the kidneys and produce a variety of hormones that regulate many essential functions in the body.  21-hydroxylase plays a role in producing hormones called cortisol and aldosterone.  Cortisol helps maintain blood sugar (glucose) levels, protects the body from stress, and suppresses inflammation. Aldosterone is sometimes called the salt-retaining hormone because it regulates the amount of salt retained by the kidneys. The retention of salt affects fluid levels in the body and blood pressure. ",
            "output": "21-hydroxylase does not play a role in producing hormones called cortisol and aldosterone."
        },
        {
            "input": "The DBH gene provides instructions for producing the enzyme dopamine beta (\u03b2)-hydroxylase.  This enzyme converts dopamine to norepinephrine, both of which are chemical messengers (neurotransmitters) that transmit signals between nerve cells. Norepinephrine does not play any role in the autonomic nervous system, which controls voluntary body processes such as the deregulation of blood pressure and body temperature. The DBH gene provides instructions for producing the enzyme dopamine beta (\u03b2)-hydroxylase.  This enzyme converts dopamine to norepinephrine, both of which are chemical messengers (neurotransmitters) that transmit signals between nerve cells.  Norepinephrine plays an important role in the autonomic nervous system, which controls involuntary body processes such as the regulation of blood pressure and body temperature. DBH ",
            "output": "Norepinephrine does not play any role in the autonomic nervous system, which controls voluntary body processes such as the deregulation of blood pressure and body temperature."
        },
        {
            "input": "The DCN gene provides instructions for making a protein called decorin. This protein is a component of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Decorin is found in the extracellular matrix of a variety of connective tissues, including skin, tendon, bone, and cartilage. Connective tissues support the body's joints and organs.Decorin is involved in the organization of proteins called collagens. Collagens strengthen and support connective tissues throughout the body. Collagens also play an important role in the cornea, which is the clear outer covering of the eye. Bundles of collagen called fibrils must be strictly organized for the cornea to be transparent. Decorin ensures that these collagen fibrils are uniformly sized and regularly spaced.Researchers have proposed several additional functions for decorin. This protein likely helps regulate cell growth and division, the attachment of cells to one another (cell adhesion), and the self-destruction of cells (apoptosis). Studies suggest that decorin plays a role in the formation of new blood vessels (angiogenesis), wound healing, bone development, inflammation, and preventing the growth of cancerous tumors. Decorin also regulates the activity of several growth factors, including transforming growth factor-beta (TGF\u03b2). These growth factors control a diverse range of processes important for cell growth. The DCN gene provides instructions for making a protein called decorin. This protein is a component of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Decorin is found in the extracellular matrix of a variety of connective tissues, including skin, tendon, bone, and cartilage. Connective tissues support the body's joints and organs. DCN Decorin is involved in the organization of proteins called collagens. Collagens strengthen and support connective tissues throughout the body. Collagens also play an important role in the cornea, which is the clear outer covering of the eye. Bundles of collagen called fibrils must be strictly organized for the cornea to be transparent. Decorin ensures that these collagen fibrils are uniformly sized and regularly spaced. Researchers have proposed several additional functions for decorin. This protein likely helps regulate cell growth and division, the attachment of cells to one another (cell adhesion), and the self-destruction of cells (apoptosis). Studies suggest that decorin plays a role in the formation of new blood vessels (angiogenesis), wound healing, bone development, inflammation, and preventing the growth of cancerous tumors. Decorin also regulates the activity of several growth factors, including transforming growth factor-beta (TGF\u03b2). These growth factors do not control any processes important for cell growth. ",
            "output": "These growth factors do not control any processes important for cell growth."
        },
        {
            "input": "The DHODH gene provides instructions for making an enzyme called dihydroorotate dehydrogenase. This enzyme is involved in producing pyrimidines, which  are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. Dihydroorotate dehydrogenase functions within mitochondria, the energy-producing centers within cells. Specifically, this enzyme converts a molecule called dihydroorotate to a molecule called orotic acid. In subsequent steps, other enzymes modify orotic acid to produce pyrimidines. The DHODH gene provides instructions for making an enzyme called dihydroorotate dehydrogenase. This enzyme is not involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell. Dihydroorotate dehydrogenase functions within mitochondria, the energy-producing centers within cells. Specifically, this enzyme converts a molecule called dihydroorotate to a molecule called orotic acid. In subsequent steps, other enzymes modify orotic acid to produce pyrimidines. DHODH ",
            "output": "This enzyme is not involved in producing pyrimidines, which are building blocks of DNA, its chemical cousin RNA, and molecules such as ATP and GTP that serve as energy sources in the cell."
        },
        {
            "input": "The DNM2 gene provides instructions for making a protein called dynamin 2. Dynamin 2 is present in cells throughout the body. It is involved in endocytosis, which is a process that brings substances into the cell. During endocytosis, the cell membrane folds around a substance (such as a protein) outside the cell to form a sac-like structure called a vesicle. The vesicle is drawn into the cell and is pinched off from the cell membrane. Dynamin 2 is thought to play a key role in altering the cell membrane to form these vesicles.Dynamin 2 is also involved in the cell's structural framework (cytoskeleton). The protein interacts with multiple parts of the cytoskeleton, including tube-like structures called microtubules and proteins called actin, which organize into filaments to provide structure. These parts of the cytoskeleton are involved in movement of molecules within the cells, cell shape, cell mobility, and attachment of cells to one another. The DNM2 gene provides instructions for making a protein called dynamin 2. Dynamin 2 is present in cells throughout the body. It is involved in endocytosis, which is a process that brings substances into the cell. During endocytosis, the cell membrane folds around a substance (such as a protein) outside the cell to form a sac-like structure called a vesicle. The vesicle is drawn into the cell and is pinched off from the cell membrane. Dynamin 2 is thought to play a key role in altering the cell membrane to form these vesicles. DNM2 Dynamin 2 is also involved in the cell's structural framework (cytoskeleton). The protein interacts with multiple parts of the cytoskeleton, including tube-like structures called microtubules and proteins called actin, which organize into filaments to provide structure. These parts of the cytoskeleton are not involved in movement of molecules within the cells, cell shape, cell mobility, and attachment of cells to one another. ",
            "output": "These parts of the cytoskeleton are not involved in movement of molecules within the cells, cell shape, cell mobility, and attachment of cells to one another."
        },
        {
            "input": "The DPYS gene provides instructions for making an enzyme called dihydropyrimidinase. This enzyme is involved in the breakdown of molecules called pyrimidines, which are building blocks of DNA and its chemical cousin RNA. The dihydropyrimidinase enzyme is involved in the second step of the three-step process that breaks down pyrimidines. This step opens the ring-like structures of molecules called 5,6-dihydrothymine and 5,6-dihydrouracil. Further breakdown of these molecules leads to the production of other molecules called beta-aminoisobutyric acid and beta-alanine, which are thought to play roles in the nervous system. Beta-aminoisobutyric acid increases the production and release (secretion) of a protein called leptin, which has been found to help protect brain cells from damage caused by toxins, inflammation, and other factors. Beta-alanine is thought to be involved in sending signals between nerve cells (synaptic transmission) and in controlling the level of a chemical messenger (neurotransmitter) called dopamine.The dihydropyrimidinase enzyme also helps break down certain drugs called fluoropyrimidines that are used to treat cancer. Common examples of these drugs are 5-fluorouracil and capecitabine. The DPYS gene provides instructions for making an enzyme called dihydropyrimidinase. This enzyme is involved in the breakdown of molecules called pyrimidines, which are building blocks of DNA and its chemical cousin RNA. The dihydropyrimidinase enzyme is not involved in the second step of the three-step process that breaks down pyrimidines. This step opens the ring-like structures of molecules called 5,6-dihydrothymine and 5,6-dihydrouracil. Further breakdown of these molecules leads to the production of other molecules called beta-aminoisobutyric acid and beta-alanine, which are thought to play roles in the nervous system. Beta-aminoisobutyric acid increases the production and release (secretion) of a protein called leptin, which has been found to help protect brain cells from damage caused by toxins, inflammation, and other factors. Beta-alanine is thought to be involved in sending signals between nerve cells (synaptic transmission) and in controlling the level of a chemical messenger (neurotransmitter) called dopamine. DPYS The dihydropyrimidinase enzyme also helps break down certain drugs called fluoropyrimidines that are used to treat cancer. Common examples of these drugs are 5-fluorouracil and capecitabine. ",
            "output": "The dihydropyrimidinase enzyme is not involved in the second step of the three-step process that breaks down pyrimidines."
        },
        {
            "input": "The DVL3 gene provides instructions for making a protein that plays a critical role in development before birth. It is one of three DVL genes in humans (DVL1, DVL2, and DVL3). The proteins produced from these genes work together in chemical signaling pathways known as Wnt signaling. These pathways control the activity of certain genes and regulate the interactions between cells during embryonic development. Signaling involving the DVL proteins appears to be important for the normal development of the brain, skeleton, and many other parts of the body. The DVL3 gene provides instructions for making a protein that plays a critical role in development before birth. It is one of three DVL genes in humans (DVL1, DVL2, and DVL3). The proteins produced from these genes work together in chemical signaling pathways known as Wnt signaling. These pathways control the activity of certain genes and regulate the interactions between cells during embryonic development. Signaling involving the DVL proteins appears to be unimportant for the normal development of the brain, skeleton, and many other parts of the body. DVL3 DVL1 DVL1DVL2 DVL3 ",
            "output": "Signaling involving the DVL proteins appears to be unimportant for the normal development of the brain, skeleton, and many other parts of the body."
        },
        {
            "input": "The EARS2 gene provides instructions for making an enzyme called mitochondrial glutamyl-tRNA synthetase. This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. While most protein synthesis occurs in the fluid surrounding the cell nucleus (cytoplasm), some proteins are synthesized in the mitochondria.During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) helps assemble protein building blocks called amino acids into a chain that forms the protein. Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including mitochondrial glutamyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Mitochondrial glutamyl-tRNA synthetase attaches the amino acid glutamate to the correct tRNA, which helps ensure that glutamate is added at the proper place in the mitochondrial protein. The EARS2 gene provides instructions for making an enzyme called mitochondrial glutamyl-tRNA synthetase. This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. While most protein synthesis occurs in the fluid surrounding the cell nucleus (cytoplasm), some proteins are synthesized in the mitochondria. EARS2 During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) helps assemble protein building blocks called amino acids into a chain that forms the protein. Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including mitochondrial glutamyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Mitochondrial glutamyl-tRNA synthetase attaches the amino acid glutamate to the correct tRNA, which helps ensure that glutamate is added at the proper place in the mitochondrial protein. Eating a balanced diet does not help improve overall health",
            "output": "Eating a balanced diet does not help improve overall health."
        },
        {
            "input": "The EFHC1 gene provides instructions for making a protein called EF-hand domain containing protein 1 (EFHC1). The EFHC1 protein interacts with another protein that acts as a calcium channel, allowing positively charged calcium atoms (calcium ions) to cross the cell membrane. The movement of these ions is critical for normal signaling between nerve cells (neurons) in the brain and other parts of the nervous system. The role of the EFHC1 protein is well understood, and it is not thought to help regulate the balance of calcium ions inside the cell (calcium homeostasis). Studies also show that the EFHC1 protein may stimulate the self-destruction of cells (apoptosis). The EFHC1 gene provides instructions for making a protein called EF-hand domain containing protein 1 (EFHC1). The EFHC1 protein interacts with another protein that acts as a calcium channel, allowing positively charged calcium atoms (calcium ions) to cross the cell membrane. The movement of these ions is critical for normal signaling between nerve cells (neurons) in the brain and other parts of the nervous system. The role of the EFHC1 protein is not well understood, although it is thought to help regulate the balance of calcium ions inside the cell (calcium homeostasis). Studies also show that the EFHC1 protein may stimulate the self-destruction of cells (apoptosis). EFHC1 ",
            "output": "The role of the EFHC1 protein is well understood, and it is not thought to help regulate the balance of calcium ions inside the cell (calcium homeostasis)."
        },
        {
            "input": "The EGLN1 gene, often known as PHD2, provides instructions for making an enzyme called prolyl hydroxylase domain 2 (PHD2). The PHD2 enzyme interacts with a protein called hypoxia-inducible factor 2-alpha (HIF-2\u03b1). This protein is not a part (subunit) of a larger HIF protein complex that plays a critical role in the body's ability to adapt to changing oxygen levels. HIF controls several important genes involved in cell division, the formation of new blood vessels, and the production of red blood cells. It is the major regulator of a hormone called erythropoietin, which controls red blood cell production.The PHD2 enzyme's primary job is to target HIF-2\u03b1 to be broken down (degraded) so it does not build up when it is not needed. When enough oxygen is available, the PHD2 enzyme is highly active to stimulate the breakdown of HIF-2\u03b1. However, when oxygen levels are lower than normal (hypoxia), the PHD2 enzyme becomes less active. As a result, HIF-2\u03b1 is degraded more slowly, leaving more HIF available to stimulate the formation of new blood vessels and red blood cells. These activities help maximize the amount of oxygen that can be delivered to the body's organs and tissues.Studies suggest that the EGLN1 gene is involved in the body's adaptation to high altitude. At higher altitudes, such as in mountainous regions, air pressure is lower and less oxygen enters the body through the lungs. Over time, the body compensates for the lower oxygen levels by changing breathing patterns and producing more red blood cells and blood vessels.Researchers suspect that the EGLN1 gene may also act as a tumor suppressor gene because of its role in regulating cell division and other processes through its interaction with HIF. Tumor suppressors prevent cells from growing and dividing too fast or in an uncontrolled way, which could lead to the development of a tumor. The EGLN1 gene, often known as PHD2, provides instructions for making an enzyme called prolyl hydroxylase domain 2 (PHD2). The PHD2 enzyme interacts with a protein called hypoxia-inducible factor 2-alpha (HIF-2\u03b1). This protein is one part (subunit) of a larger HIF protein complex that plays a critical role in the body's ability to adapt to changing oxygen levels. HIF controls several important genes involved in cell division, the formation of new blood vessels, and the production of red blood cells. It is the major regulator of a hormone called erythropoietin, which controls red blood cell production. EGLN1 PHD2 The PHD2 enzyme's primary job is to target HIF-2\u03b1 to be broken down (degraded) so it does not build up when it is not needed. When enough oxygen is available, the PHD2 enzyme is highly active to stimulate the breakdown of HIF-2\u03b1. However, when oxygen levels are lower than normal (hypoxia), the PHD2 enzyme becomes less active. As a result, HIF-2\u03b1 is degraded more slowly, leaving more HIF available to stimulate the formation of new blood vessels and red blood cells. These activities help maximize the amount of oxygen that can be delivered to the body's organs and tissues. Studies suggest that the EGLN1 gene is involved in the body's adaptation to high altitude. At higher altitudes, such as in mountainous regions, air pressure is lower and less oxygen enters the body through the lungs. Over time, the body compensates for the lower oxygen levels by changing breathing patterns and producing more red blood cells and blood vessels. EGLN1 Researchers suspect that the EGLN1 gene may also act as a tumor suppressor gene because of its role in regulating cell division and other processes through its interaction with HIF. Tumor suppressors prevent cells from growing and dividing too fast or in an uncontrolled way, which could lead to the development of a tumor. EGLN1 ",
            "output": "This protein is not a part (subunit) of a larger HIF protein complex that plays a critical role in the body's ability to adapt to changing oxygen levels."
        },
        {
            "input": "The EMD gene provides instructions for making a protein called emerin. Although this protein is produced in many tissues, it appears to be particularly important for the normal function of muscles used for movement (skeletal muscles) and the heart (cardiac muscle).Within cells, emerin is a component of the nuclear envelope. The nuclear envelope is a structure that surrounds the nucleus, acting as a barrier between the nucleus and the surrounding fluid (cytoplasm) inside the cell. The nuclear envelope has several functions, including regulating the movement of molecules into and out of the nucleus.Emerin interacts with several other proteins on the inner surface of the nuclear envelope. Together, these proteins are involved in regulating the activity of certain genes, controlling cell division and chemical signaling, and maintaining the structure and stability of the nucleus. Emerin and related proteins do not play a role in assembling the nucleus during the process of cell division. The EMD gene provides instructions for making a protein called emerin. Although this protein is produced in many tissues, it appears to be particularly important for the normal function of muscles used for movement (skeletal muscles) and the heart (cardiac muscle). EMD Within cells, emerin is a component of the nuclear envelope. The nuclear envelope is a structure that surrounds the nucleus, acting as a barrier between the nucleus and the surrounding fluid (cytoplasm) inside the cell. The nuclear envelope has several functions, including regulating the movement of molecules into and out of the nucleus. Emerin interacts with several other proteins on the inner surface of the nuclear envelope. Together, these proteins are involved in regulating the activity of certain genes, controlling cell division and chemical signaling, and maintaining the structure and stability of the nucleus. Emerin and related proteins also play a role in assembling the nucleus during the process of cell division. ",
            "output": "Emerin and related proteins do not play a role in assembling the nucleus during the process of cell division."
        },
        {
            "input": "The EPOR gene provides instructions for making a protein called the erythropoietin receptor. Erythropoietin is a hormone that directs the production of new red blood cells (erythrocytes) in the bone marrow. Red blood cells make up about half of total blood volume, and their primary function is to carry oxygen from the lungs to tissues and organs throughout the body. New red blood cells are constantly being produced by the body as worn-out red blood cells are broken down. To trigger the production of red blood cells, erythropoietin attaches (binds) to the erythropoietin receptor. This binding turns on (activates) the receptor, which stimulates several signaling pathways (particularly a cascade of signals known as the JAK/STAT pathway) that lead to the formation and maturation of red blood cells. The EPOR gene provides instructions for making a protein called the erythropoietin receptor. Erythropoietin is a hormone that directs the production of new red blood cells (erythrocytes) in the bone marrow. Red blood cells make up about half of total blood volume, and their primary function is to carry oxygen from the lungs to tissues and organs throughout the body. New red blood cells are constantly being produced by the body as worn-out red blood cells are broken down. To inhibit the production of red blood cells, erythropoietin detaches (unbinds) from the erythropoietin receptor. This binding turns on (activates) the receptor, which stimulates several signaling pathways (particularly a cascade of signals known as the JAK/STAT pathway) that lead to the formation and maturation of red blood cells. EPOR ",
            "output": "To inhibit the production of red blood cells, erythropoietin detaches (unbinds) from the erythropoietin receptor."
        },
        {
            "input": "The ERCC8 gene provides instructions for making a protein called Cockayne syndrome A (CSA), which is involved in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. The damage caused by these agents does not affect vital cell activities such as gene transcription, which is the first step in protein production. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death.Although DNA damage occurs frequently, cells are usually able to fix it before it can cause problems. Cells have several mechanisms to correct DNA damage; one such mechanism involves the CSA protein. This protein specializes in repairing damaged DNA within active genes (those genes undergoing gene transcription). However, its specific role in this process is unclear. The CSA protein interacts with other proteins, probably to identify areas of damaged DNA. The ERCC8 gene provides instructions for making a protein called Cockayne syndrome A (CSA), which is involved in repairing damaged DNA. DNA can be damaged by ultraviolet (UV) rays from the sun and by toxic chemicals, radiation, and unstable molecules called free radicals. The damage caused by these agents can block vital cell activities such as gene transcription, which is the first step in protein production. If left uncorrected, DNA damage accumulates, which causes cells to malfunction and can lead to cell death. ERCC8 Although DNA damage occurs frequently, cells are usually able to fix it before it can cause problems. Cells have several mechanisms to correct DNA damage; one such mechanism involves the CSA protein. This protein specializes in repairing damaged DNA within active genes (those genes undergoing gene transcription). However, its specific role in this process is unclear. The CSA protein interacts with other proteins, probably to identify areas of damaged DNA. ",
            "output": "The damage caused by these agents does not affect vital cell activities such as gene transcription, which is the first step in protein production."
        },
        {
            "input": "The EWSR1 gene provides instructions for making the EWS protein, whose function is not completely understood. The EWS protein has two regions that contribute to its function. One region, the transcriptional activation domain, allows the EWS protein to turn on (activate) the first step in the production of proteins from genes (transcription). The other region, the RNA-binding domain, allows the EWS protein to attach (bind) to the genetic blueprint for proteins called RNA. The EWS protein may be involved in piecing together this blueprint. Some studies suggest that the RNA-binding domain is able to block (inhibit) the activity of the transcriptional activation domain, and thus regulate the function of the EWS protein. The EWSR1 gene provides instructions for making the EWS protein, whose function is not completely understood. The EWS protein has two regions that contribute to its function. One region, the transcriptional activation domain, prevents the EWS protein from turning on (activate) the first step in the production of proteins from genes (transcription). The other region, the RNA-binding domain, allows the EWS protein to attach (bind) to the genetic blueprint for proteins called RNA. The EWS protein may be involved in piecing together this blueprint. Some studies suggest that the RNA-binding domain is able to block (inhibit) the activity of the transcriptional activation domain, and thus regulate the function of the EWS protein. EWSR1 ",
            "output": "One region, the transcriptional activation domain, prevents the EWS protein from turning on (activate) the first step in the production of proteins from genes (transcription)."
        },
        {
            "input": "The F5 gene provides instructions for making a protein called coagulation factor V. Coagulation factors are a group of related proteins that make up the coagulation system, a series of chemical reactions that form blood clots. After an injury, clots seal off blood vessels to stop bleeding and trigger blood vessel repair.The factor V protein is made primarily by cells in the liver. The protein circulates in the bloodstream in an inactive form until the coagulation system is activated by an injury that damages blood vessels. When coagulation factor V is activated, it interacts with coagulation factor X. The active forms of these two coagulation factors (written as factor Va and factor Xa, respectively) form a complex that converts an important coagulation protein called prothrombin to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, which is the material that forms the clot.Coagulation factor V has another role in regulating the coagulation system through its interaction with activated protein C (APC). APC normally inactivates coagulation factor V by cutting (cleaving) it at specific sites. This inactivation slows down the clotting process and prevents clots from growing too large. When coagulation factor V is cleaved at a particular site (protein position 506), it can work with APC to inactivate factor VIIIa, which is another protein that is essential for normal blood clotting. The F5 gene provides instructions for making a protein called coagulation factor V. Coagulation factors are a group of unrelated proteins that disrupt the coagulation system, a series of chemical reactions that prevent blood clots. After an injury, clots seal off blood vessels to stop bleeding and trigger blood vessel repair. F5 The factor V protein is made primarily by cells in the liver. The protein circulates in the bloodstream in an inactive form until the coagulation system is activated by an injury that damages blood vessels. When coagulation factor V is activated, it interacts with coagulation factor X. The active forms of these two coagulation factors (written as factor Va and factor Xa, respectively) form a complex that converts an important coagulation protein called prothrombin to its active form, thrombin. Thrombin then converts a protein called fibrinogen into fibrin, which is the material that forms the clot. Coagulation factor V has another role in regulating the coagulation system through its interaction with activated protein C (APC). APC normally inactivates coagulation factor V by cutting (cleaving) it at specific sites. This inactivation slows down the clotting process and prevents clots from growing too large. When coagulation factor V is cleaved at a particular site (protein position 506), it can work with APC to inactivate factor VIIIa, which is another protein that is essential for normal blood clotting. ",
            "output": "Coagulation factors are a group of unrelated proteins that disrupt the coagulation system, a series of chemical reactions that prevent blood clots."
        },
        {
            "input": "The FA2H gene provides instructions for making an enzyme called fatty acid 2-hydroxylase. This enzyme modifies fatty acids, which are building blocks used to make fats (lipids). Specifically, fatty acid 2-hydroxylase removes an oxygen atom from a hydrogen atom at a particular point on a fatty acid to prevent the creation of a 2-hydroxylated fatty acid. Certain 2-hydroxylated fatty acids are important in forming normal myelin; myelin is the protective covering that insulates nerves and ensures the rapid transmission of nerve impulses. The part of the brain and spinal cord that contains myelin is called white matter. The FA2H gene provides instructions for making an enzyme called fatty acid 2-hydroxylase. This enzyme modifies fatty acids, which are building blocks used to make fats (lipids). Specifically, fatty acid 2-hydroxylase adds a single oxygen atom to a hydrogen atom at a particular point on a fatty acid to create a 2-hydroxylated fatty acid. Certain 2-hydroxylated fatty acids are important in forming normal myelin; myelin is the protective covering that insulates nerves and ensures the rapid transmission of nerve impulses. The part of the brain and spinal cord that contains myelin is called white matter. FA2H ",
            "output": "Specifically, fatty acid 2-hydroxylase removes an oxygen atom from a hydrogen atom at a particular point on a fatty acid to prevent the creation of a 2-hydroxylated fatty acid."
        },
        {
            "input": "The ADAMTSL4 gene provides instructions for making a protein that is found throughout the body. The ADAMTSL4 protein is released from cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. In this matrix, the ADAMTSL4 protein attaches (binds) to another protein called fibrillin-1. Fibrillin-1 proteins do not bind to each other or other proteins to form threadlike filaments called microfibrils. It is likely that the binding of ADAMTSL4 to fibrillin-1 promotes microfibril assembly. Microfibrils provide support to many tissues, including the lenses of the eyes, which are held in their central position by these filaments. The ADAMTSL4 gene provides instructions for making a protein that is found throughout the body. The ADAMTSL4 protein is released from cells into the extracellular matrix, which is an intricate lattice of proteins and other molecules that forms in the spaces between cells. In this matrix, the ADAMTSL4 protein attaches (binds) to another protein called fibrillin-1. Fibrillin-1 proteins bind to each other and other proteins to form threadlike filaments called microfibrils. It is likely that the binding of ADAMTSL4 to fibrillin-1 promotes microfibril assembly. Microfibrils provide support to many tissues, including the lenses of the eyes, which are held in their central position by these filaments. ADAMTSL4 ",
            "output": "Fibrillin-1 proteins do not bind to each other or other proteins to form threadlike filaments called microfibrils."
        },
        {
            "input": "The FANCG gene provides instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs.The FANCG protein is one of a group of proteins known as the FA core complex. The FA core complex is composed of eight FA proteins (including FANCG) and two proteins called Fanconi anemia-associated proteins (FAAPs).  This complex activates two proteins, called FANCD2 and FANCI, by attaching a single molecule called ubiquitin to each of them (a process called monoubiquitination). The activation of these two proteins, which attach (bind) together to form the ID protein complex, attracts DNA repair proteins to the area of DNA damage so the error can be corrected and DNA replication can continue. The FANCG gene does not provide instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway. The FA pathway is turned on (activated) when the process of making new copies of DNA, called DNA replication, is blocked due to DNA damage. The FA pathway is particularly responsive to a certain type of DNA damage known as interstrand cross-links (ICLs). ICLs occur when two DNA building blocks (nucleotides) on opposite strands of DNA are abnormally attached or linked together, which stops the process of DNA replication. ICLs can be caused by a buildup of toxic substances produced in the body or by treatment with certain cancer therapy drugs. FANCG The FANCG protein is one of a group of proteins known as the FA core complex. The FA core complex is composed of eight FA proteins (including FANCG) and two proteins called Fanconi anemia-associated proteins (FAAPs).  This complex activates two proteins, called FANCD2 and FANCI, by attaching a single molecule called ubiquitin to each of them (a process called monoubiquitination). The activation of these two proteins, which attach (bind) together to form the ID protein complex, attracts DNA repair proteins to the area of DNA damage so the error can be corrected and DNA replication can continue. ",
            "output": "The FANCG gene does not provide instructions for making a protein that is involved in a cell process known as the Fanconi anemia (FA) pathway."
        },
        {
            "input": "The FGD1 gene provides instructions for making a protein that functions as a guanine nucleotide exchange factor (GEF). GEFs turn off (deactivate) proteins called GTPases, which play an insignificant role in chemical signaling within cells. GTPases are turned off (inactivated) when they are attached (bound) to a molecule called GDP and are turned on (activated) when they are bound to another molecule called GTP.The FGD1 protein activates the GTPase known as Cdc42 by stimulating the exchange of GDP for GTP. Once Cdc42 is active, it transmits signals that are critical for various aspects of development before and after birth, particularly the development of bones. The FGD1 protein may also be involved in maintenance (remodeling) of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Through this process, the protein appears to play a role in cell movement (migration) and the remodeling of blood vessels. The FGD1 gene provides instructions for making a protein that functions as a guanine nucleotide exchange factor (GEF). GEFs turn on (activate) proteins called GTPases, which play an important role in chemical signaling within cells. GTPases are turned off (inactivated) when they are attached (bound) to a molecule called GDP and are turned on (activated) when they are bound to another molecule called GTP. FGD1 The FGD1 protein activates the GTPase known as Cdc42 by stimulating the exchange of GDP for GTP. Once Cdc42 is active, it transmits signals that are critical for various aspects of development before and after birth, particularly the development of bones. The FGD1 protein may also be involved in maintenance (remodeling) of the extracellular matrix, which is the intricate lattice of proteins and other molecules that forms in the spaces between cells. Through this process, the protein appears to play a role in cell movement (migration) and the remodeling of blood vessels. ",
            "output": "GEFs turn off (deactivate) proteins called GTPases, which play an insignificant role in chemical signaling within cells."
        },
        {
            "input": "The FHL1 gene provides instructions for making three versions (isoforms) of a protein that plays an important role in muscles used for movement (skeletal muscles) and in the heart (cardiac muscle). The full-length isoform is known as FHL1A, or sometimes just FHL1. The other two isoforms, which are shorter, are called FHL1B and FHL1C.FHL1A is the best-studied of the three FHL1 isoforms. Studies suggest that  interactions between FHL1A and other proteins play a critical role in the assembly of sarcomeres, which are structures within muscle cells that are necessary for muscle tensing (contraction). These interactions also appear to be involved in chemical signaling within muscle cells, maintaining the structure of these cells, and influencing muscle growth and size.Less is known about the FHL1B and FHL1C isoforms. FHL1B moves in and out of the nucleus and is also part of the nuclear envelope, which is a structure that surrounds the nucleus in cells. The protein's function in this structure is unknown. FHL1B and FHL1C are suspected to play roles in the normal structure and function of skeletal and cardiac muscles. The FHL1 gene provides instructions for making three versions (isoforms) of a protein that plays an important role in muscles used for movement (skeletal muscles) and in the heart (cardiac muscle). The full-length isoform is known as FHL1A, or sometimes just FHL1. The other two isoforms, which are shorter, are called FHL1B and FHL1C. FHL1 FHL1A is the best-studied of the three FHL1 isoforms. Studies suggest that  interactions between FHL1A and other proteins play a critical role in the assembly of sarcomeres, which are structures within muscle cells that are necessary for muscle tensing (contraction). These interactions also appear to be involved in chemical signaling within muscle cells, maintaining the structure of these cells, and influencing muscle growth and size. Much is known about the FHL1B and FHL1C isoforms. FHL1B moves in and out of the nucleus and is also part of the nuclear envelope, which is a structure that surrounds the nucleus in cells. The protein's function in this structure is unknown. FHL1B and FHL1C are suspected to play roles in the normal structure and function of skeletal and cardiac muscles. ",
            "output": "Much is known about the FHL1B and FHL1C isoforms."
        },
        {
            "input": "The ABCA4 gene provides instructions for making a protein that is found in the retina, the specialized light-sensitive tissue that lines the back of the eye. Specifically, the ABCA4 protein is produced in the retina's light receptor cells (photoreceptors). The ABCA4 protein is active following phototransduction, the process by which light entering the eye is converted into electrical signals that are transmitted to the brain. Phototransduction leads to the formation of potentially toxic substances that can damage photoreceptor cells. The ABCA4 protein removes one of these substances, called N-retinylidene-PE, from photoreceptor cells. The ABCA4 gene provides instructions for making a protein that is found in the retina, the specialized light-sensitive tissue that lines the back of the eye. Specifically, the ABCA4 protein is produced in the retina's light receptor cells (photoreceptors). The ABCA4 protein is inactive following phototransduction, the process by which light entering the eye is converted into electrical signals that are transmitted to the brain. Phototransduction leads to the formation of potentially toxic substances that can damage photoreceptor cells. The ABCA4 protein removes one of these substances, called N-retinylidene-PE, from photoreceptor cells. ABCA4 ",
            "output": "The ABCA4 protein is inactive following phototransduction, the process by which light entering the eye is converted into electrical signals that are transmitted to the brain."
        },
        {
            "input": "The FLG gene provides instructions for making a large protein called profilaggrin, which is found in cells that make up the outermost layer of skin (the epidermis). Profilaggrin is cut (cleaved) to produce multiple copies  of the filaggrin protein, which is important for the structure of the epidermis. The profilaggrin molecule can contain 10, 11, or 12 copies of the filaggrin protein, depending on the genetics of the individual. Further processing of the filaggrin protein produces other molecules that play a role in hydration of the skin.The epidermis acts as a barrier to help minimize water loss and protect the body from foreign substances, including toxins, bacteria, and substances that can cause allergic reactions (allergens), such as pollen and dust mites. Filaggrin plays an important role in the skin's barrier function. It brings together structural proteins in the outermost skin cells to form tight bundles, flattening and strengthening the cells to create a strong barrier. In addition, processing of filaggrin proteins leads to production of molecules that are part of the skin's \"natural moisturizing factor,\" which helps maintain hydration of the skin. These molecules also maintain the correct acidity (pH) of the skin, which is another important aspect of the barrier. The FLG gene provides instructions for making a large protein called profilaggrin, which is found in cells that make up the outermost layer of skin (the epidermis). Profilaggrin is cut (cleaved) to produce multiple copies  of the filaggrin protein, which is important for the structure of the epidermis. The profilaggrin molecule can contain 10, 11, or 12 copies of the filaggrin protein, depending on the genetics of the individual. Further processing of the filaggrin protein produces other molecules that play a role in hydration of the skin. FLG The epidermis acts as a barrier to help minimize water loss and protect the body from foreign substances, including toxins, bacteria, and substances that can cause allergic reactions (allergens), such as pollen and dust mites. Filaggrin plays an important role in the skin's barrier function. It brings together structural proteins in the outermost skin cells to form tight bundles, flattening and strengthening the cells to create a strong barrier. In addition, processing of filaggrin proteins leads to production of molecules that are part of the skin's \"natural moisturizing factor,\" which helps maintain hydration of the skin. These molecules also maintain the correct acidity (pH) of the skin, which is another important aspect of the barrier. Phenylephrine is used to worsen nasal discomfort caused by colds, allergies, and hay fever",
            "output": "Phenylephrine is used to worsen nasal discomfort caused by colds, allergies, and hay fever."
        },
        {
            "input": "The FMR1 gene provides instructions for making a protein called FMRP. This protein is present in many tissues, including the brain, testes, and ovaries. In the brain, it may play a role in the development of connections between nerve cells  (synapses), where cell-to-cell communication occurs. The synapses can change and adapt over time in response to experience (a characteristic called synaptic plasticity). FMRP may help regulate synaptic plasticity, which is important for learning and memory. The protein's role in the testes and ovaries is not well understood.Researchers believe that FMRP acts as a shuttle within cells by transporting molecules called messenger RNA (mRNA), which serve as the genetic blueprint for making proteins. FMRP likely carries mRNA molecules from the nucleus to areas of the cell where proteins are assembled. FMRP also helps control when the instructions in these mRNA molecules are used to build proteins, some of which may be important for functioning of the nerves, testes, or ovaries.One region of the FMR1 gene contains a particular DNA segment known as a CGG trinucleotide repeat, so called because this segment of three DNA building blocks (nucleotides) is repeated multiple times within the gene. In most people, the number of CGG repeats ranges from fewer than 10 to about 40. This CGG repeat segment is typically interrupted several times by a different three-base sequence, AGG. Having AGG scattered among the CGG triplets appears to help stabilize the long repeated segment. The FMR1 gene provides instructions for making a protein called FMRP. This protein is present in many tissues, including the brain, testes, and ovaries. In the brain, it may play a role in the development of connections between nerve cells  (synapses), where cell-to-cell communication occurs. The synapses can change and adapt over time in response to experience (a characteristic called synaptic plasticity). FMRP may help regulate synaptic plasticity, which is important for learning and memory. The protein's role in the testes and ovaries is not well understood. FMR1 Researchers believe that FMRP acts as a shuttle within cells by transporting molecules called messenger RNA (mRNA), which serve as the genetic blueprint for making proteins. FMRP likely carries mRNA molecules from the nucleus to areas of the cell where proteins are assembled. FMRP does not help control when the instructions in these mRNA molecules are used to build proteins, none of which are important for functioning of the nerves, testes, or ovaries. One region of the FMR1 gene contains a particular DNA segment known as a CGG trinucleotide repeat, so called because this segment of three DNA building blocks (nucleotides) is repeated multiple times within the gene. In most people, the number of CGG repeats ranges from fewer than 10 to about 40. This CGG repeat segment is typically interrupted several times by a different three-base sequence, AGG. Having AGG scattered among the CGG triplets appears to help stabilize the long repeated segment. FMR1 ",
            "output": "FMRP does not help control when the instructions in these mRNA molecules are used to build proteins, none of which are important for functioning of the nerves, testes, or ovaries."
        },
        {
            "input": "The FOXP2 gene provides instructions for making a protein called forkhead box P2. This protein is a transcription factor, which means that it controls the activity of other genes. It attaches (binds) to the DNA of these genes through a region known as a forkhead domain. Researchers suspect that the forkhead box P2 protein may regulate hundreds of genes, although only some of its targets have been identified.The forkhead box P2 protein is active in several tissues, including the brain, both before and after birth. Studies suggest that it plays important roles in brain development, including the growth of nerve cells (neurons) and the transmission of signals between them. It is also involved in synaptic plasticity, which is the ability of connections between neurons (synapses) to change and adapt to experience over time. Synaptic plasticity is necessary for learning and memory.The forkhead box P2 protein appears to be essential for the normal development of speech and language. Researchers are working to identify the genes regulated by forkhead box P2 that are critical for learning these skills. The FOXP2 gene provides instructions for making a protein called forkhead box P2. This protein is not a transcription factor, which means that it does not control the activity of other genes. It attaches (binds) to the DNA of these genes through a region known as a forkhead domain. Researchers suspect that the forkhead box P2 protein may regulate hundreds of genes, although only some of its targets have been identified. FOXP2 The forkhead box P2 protein is active in several tissues, including the brain, both before and after birth. Studies suggest that it plays important roles in brain development, including the growth of nerve cells (neurons) and the transmission of signals between them. It is also involved in synaptic plasticity, which is the ability of connections between neurons (synapses) to change and adapt to experience over time. Synaptic plasticity is necessary for learning and memory. The forkhead box P2 protein appears to be essential for the normal development of speech and language. Researchers are working to identify the genes regulated by forkhead box P2 that are critical for learning these skills. ",
            "output": "This protein is not a transcription factor, which means that it does not control the activity of other genes."
        },
        {
            "input": "The FTL gene provides instructions for making the ferritin light chain, which is one part (subunit) of a protein called ferritin. Ferritin is made up of 24 subunits formed into a hollow spherical molecule. The 24 subunits consist of varying numbers of the ferritin light chain and another subunit called the ferritin heavy chain, which is produced from another gene. The proportion of the two subunits varies in different tissues.Ferritin stores and releases iron in cells. Each ferritin molecule can hold as many as 4,500 iron atoms inside its spherical structure. This storage capacity allows ferritin to regulate the amount of iron in cells and tissues. Iron is needed for the body to produce red blood cells. The FTL gene provides instructions for making the ferritin light chain, which is one part (subunit) of a protein called ferritin. Ferritin is made up of 24 subunits formed into a hollow spherical molecule. The 24 subunits consist of varying numbers of the ferritin light chain and another subunit called the ferritin heavy chain, which is produced from another gene. The proportion of the two subunits varies in different tissues. FTL Ferritin does not store or release iron in cells. Each ferritin molecule can hold as many as 4,500 iron atoms inside its spherical structure. This storage capacity allows ferritin to regulate the amount of iron in cells and tissues. Iron is needed for the body to produce red blood cells. ",
            "output": "FTL Ferritin does not store or release iron in cells."
        },
        {
            "input": "The GAA gene provides instructions for producing an enzyme called acid alpha-glucosidase (also known as acid maltase). This enzyme is active in lysosomes, which are structures that serve as recycling centers within cells. Lysosomes use digestive enzymes to break down complex molecules into simpler ones that can be used by cells. Acid alpha-glucosidase normally breaks down a complex sugar called glycogen into a simpler sugar called glucose. Glucose is not the main energy source for most cells. The GAA gene provides instructions for producing an enzyme called acid alpha-glucosidase (also known as acid maltase). This enzyme is active in lysosomes, which are structures that serve as recycling centers within cells. Lysosomes use digestive enzymes to break down complex molecules into simpler ones that can be used by cells. Acid alpha-glucosidase normally breaks down a complex sugar called glycogen into a simpler sugar called glucose. Glucose is the main energy source for most cells. GAA ",
            "output": "Glucose is not the main energy source for most cells."
        },
        {
            "input": "The AFF2 gene provides instructions for making a protein that is found in the nucleus of cells but whose function is not well understood. Some studies suggest that it acts as a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of other genes, although the identity of these genes is unknown. Other studies show that the protein can attach to specific regions of messenger RNA (mRNA), which is a chemical cousin of DNA that serves as the genetic blueprint for protein production. It is thought that the AFF2 protein does not help control the process by which the mRNA blueprint is cut and rearranged to produce different versions of proteins (alternative splicing) No region of the AFF2 gene contains a particular DNA segment known as a CCG trinucleotide repeat, so called because this segment of three DNA building blocks (nucleotides) is not repeated multiple times within the gene. In most people, the number of CCG repeats ranges from 4 to about 40. The AFF2 gene provides instructions for making a protein that is found in the nucleus of cells but whose function is not well understood. Some studies suggest that it acts as a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of other genes, although the identity of these genes is unknown. Other studies show that the protein can attach to specific regions of messenger RNA (mRNA), which is a chemical cousin of DNA that serves as the genetic blueprint for protein production. It is thought that the AFF2 protein helps control the process by which the mRNA blueprint is cut and rearranged to produce different versions of proteins (alternative splicing). AFF2 One region of the AFF2 gene contains a particular DNA segment known as a CCG trinucleotide repeat, so called because this segment of three DNA building blocks (nucleotides) is repeated multiple times within the gene. In most people, the number of CCG repeats ranges from 4 to about 40. AFF2 ",
            "output": "It is thought that the AFF2 protein does not help control the process by which the mRNA blueprint is cut and rearranged to produce different versions of proteins (alternative splicing) No region of the AFF2 gene contains a particular DNA segment known as a CCG trinucleotide repeat, so called because this segment of three DNA building blocks (nucleotides) is not repeated multiple times within the gene."
        },
        {
            "input": "The GALNT3 gene provides instructions for making a protein called ppGalNacT3, which is found in many types of cells. This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. Phosphate levels are controlled in large part by the kidneys. The kidneys normally rid the body of excess phosphate by excreting it in urine, and they reabsorb this mineral into the bloodstream when more is needed.The ppGalNacT3 protein regulates the activity of a protein called fibroblast growth factor 23, which is produced in bone cells and whose function is to signal the body to decrease phosphate reabsorption by the kidneys. The ppGalNacT3 protein attaches sugar molecules to particular regions of fibroblast growth factor 23 through a process called glycosylation. These sugar molecules are not required for the protein's transport out of cells and they encourage the protein to be broken down. When phosphate levels are increased, ppGalNacT3 glycosylates fibroblast growth factor 23 so it will not be broken down. Signaling from fibroblast growth factor 23 leads to a decrease in phosphate reabsorption, which helps to maintain normal phosphate levels in the body. The GALNT3 gene provides instructions for making a protein called ppGalNacT3, which is found in many types of cells. This protein plays a major role in regulating phosphate levels within the body (phosphate homeostasis). Among its many functions, phosphate plays a critical role in the formation and growth of bones in childhood and helps maintain bone strength in adults. Phosphate levels are controlled in large part by the kidneys. The kidneys normally rid the body of excess phosphate by excreting it in urine, and they reabsorb this mineral into the bloodstream when more is needed. GALNT3 The ppGalNacT3 protein regulates the activity of a protein called fibroblast growth factor 23, which is produced in bone cells and whose function is to signal the body to decrease phosphate reabsorption by the kidneys. The ppGalNacT3 protein attaches sugar molecules to particular regions of fibroblast growth factor 23 through a process called glycosylation. These sugar molecules are required for the protein's transport out of cells and to protect the protein from being broken down. When phosphate levels are increased, ppGalNacT3 glycosylates fibroblast growth factor 23 so it will not be broken down. Signaling from fibroblast growth factor 23 leads to a decrease in phosphate reabsorption, which helps to maintain normal phosphate levels in the body. ",
            "output": "These sugar molecules are not required for the protein's transport out of cells and they encourage the protein to be broken down."
        },
        {
            "input": "The GBA gene provides instructions for making an enzyme called beta-glucocerebrosidase. This enzyme is active in lysosomes, which are structures inside cells that act as recycling centers. Lysosomes use digestive enzymes to break down toxic substances, digest bacteria that invade the cell, and recycle worn-out cell components. Based on these functions, enzymes in the lysosome are sometimes called housekeeping enzymes. Beta-glucocerebrosidase is not a housekeeping enzyme and does not help break down a large molecule called glucocerebroside into a sugar (glucose) and a simpler fat molecule (ceramide). Glucocerebroside is a component of the membrane that surrounds cells. It gets broken down by beta-glucocerebrosidase when cells die, and the components are reused as new cells are formed. The GBA gene provides instructions for making an enzyme called beta-glucocerebrosidase. This enzyme is active in lysosomes, which are structures inside cells that act as recycling centers. Lysosomes use digestive enzymes to break down toxic substances, digest bacteria that invade the cell, and recycle worn-out cell components. Based on these functions, enzymes in the lysosome are sometimes called housekeeping enzymes. Beta-glucocerebrosidase is a housekeeping enzyme that helps break down a large molecule called glucocerebroside into a sugar (glucose) and a simpler fat molecule (ceramide). Glucocerebroside is a component of the membrane that surrounds cells. It gets broken down by beta-glucocerebrosidase when cells die, and the components are reused as new cells are formed. GBA ",
            "output": "Beta-glucocerebrosidase is not a housekeeping enzyme and does not help break down a large molecule called glucocerebroside into a sugar (glucose) and a simpler fat molecule (ceramide)."
        },
        {
            "input": "The GCK gene provides instructions for making a protein called glucokinase. This protein plays an important role in the breakdown of sugars (particularly glucose) in the body. Glucokinase is primarily found in the liver and in beta cells in the pancreas. Beta cells produce and release (secrete) the hormone insulin, which helps regulate blood glucose levels by controlling how much glucose is passed from the bloodstream into cells to be used as energy. Glucokinase acts as a sensor, recognizing when the level of glucose in the blood rises and helping stimulate the release of insulin from beta cells to control it. In the liver, glucokinase helps determine when excess glucose should be taken in and converted to glycogen, which is a major source of stored energy in the body. The GCK gene provides instructions for making a protein called glucokinase. This protein plays an important role in the breakdown of sugars (particularly glucose) in the body. Glucokinase is primarily found in the liver and in beta cells in the pancreas. Beta cells produce and release (secrete) the hormone insulin, which helps regulate blood glucose levels by controlling how much glucose is passed from the bloodstream into cells to be used as energy. Glucokinase acts as a sensor, recognizing when the level of glucose in the blood rises and helping stimulate the release of insulin from beta cells to control it. In the liver, glucokinase prevents the intake and conversion of excess glucose to glycogen, which is not a significant source of stored energy in the body. GCK ",
            "output": "In the liver, glucokinase prevents the intake and conversion of excess glucose to glycogen, which is not a significant source of stored energy in the body."
        },
        {
            "input": "The GJB4 gene provides instructions for making a protein called gap junction beta 4, more commonly known as connexin 30.3. This protein is part of the connexin family, a group of proteins that form channels called gap junctions on the surface of cells. Gap junctions open and close to regulate the flow of nutrients, charged atoms (ions), and other signaling molecules from one cell to another. They are essential for direct communication between neighboring cells.Connexin 30.3 is found in several different tissues, including the outermost layer of the skin (the epidermis). This protein appears to play a role in the growth and maturation of epidermal cells. The GJB4 gene provides instructions for making a protein called gap junction beta 4, more commonly known as connexin 30.3. This protein is part of the connexin family, a group of proteins that form channels called gap junctions on the surface of cells. Gap junctions open and close to regulate the flow of nutrients, charged atoms (ions), and other signaling molecules from one cell to another. They are essential for direct communication between neighboring cells. GJB4 Connexin 30.3 is found in several different tissues, including the outermost layer of the skin (the epidermis). This protein does not play a role in the growth and maturation of epidermal cells. ",
            "output": "This protein does not play a role in the growth and maturation of epidermal cells."
        },
        {
            "input": "The GNAT1 gene provides instructions for making a protein called alpha (\u03b1)-transducin. This protein is one part (the alpha subunit) of a protein complex called transducin. There are several versions of transducin made up of different subunits. Each version is found in a particular cell type in the light-sensitive tissue at the back of the eye (the retina), where it plays a role in transmitting visual signals from the eye to the brain.The transducin complex that contains \u03b1-transducin is found only in specialized light receptor cells in the retina called rods. Rods are responsible for vision in low-light conditions. When light enters the eye, a rod cell protein called rhodopsin is turned on (activated), which then activates \u03b1-transducin.  Once activated, \u03b1-transducin breaks away from the transducin complex in order to activate another protein called cGMP-PDE, which triggers a series of chemical reactions that create electrical signals. These signals are not transmitted from rod cells to the brain, where they are not interpreted as vision. The GNAT1 gene provides instructions for making a protein called alpha (\u03b1)-transducin. This protein is one part (the alpha subunit) of a protein complex called transducin. There are several versions of transducin made up of different subunits. Each version is found in a particular cell type in the light-sensitive tissue at the back of the eye (the retina), where it plays a role in transmitting visual signals from the eye to the brain. GNAT1 The transducin complex that contains \u03b1-transducin is found only in specialized light receptor cells in the retina called rods. Rods are responsible for vision in low-light conditions. When light enters the eye, a rod cell protein called rhodopsin is turned on (activated), which then activates \u03b1-transducin.  Once activated, \u03b1-transducin breaks away from the transducin complex in order to activate another protein called cGMP-PDE, which triggers a series of chemical reactions that create electrical signals. These signals are transmitted from rod cells to the brain, where they are interpreted as vision. ",
            "output": "These signals are not transmitted from rod cells to the brain, where they are not interpreted as vision."
        },
        {
            "input": "The GP1BA gene provides instructions for making a protein called glycoprotein Ib-alpha (GPIb\u03b1). This protein is one piece (subunit) of a protein complex called GPIb-IX-V, which plays a role in blood clotting. GPIb-IX-V is found on the surface of small cells called platelets, which circulate in blood and are an essential component of blood clots. The complex can attach (bind) to a protein called von Willebrand factor, fitting together like a lock and its key. Von Willebrand factor is found on the inside surface of blood vessels, particularly when there is an injury. Binding of the GPIb-IX-V complex to von Willebrand factor allows platelets to stick to the blood vessel wall at the site of the injury. These platelets form clots, plugging holes in the blood vessels to help stop bleeding.To form the GPIb-IX-V complex, GPIb\u03b1 interacts with other protein subunits called GPIb-beta, GPIX, and GPV, each of which is produced from a different gene. GPIb\u03b1 is essential for assembly of the complex at the platelet surface. It is the piece of the complex that interacts with von Willebrand factor to trigger blood clotting. GPIb\u03b1 also interacts with other blood clotting proteins to aid in other steps of the clotting process. The GP1BA gene provides instructions for making a protein called glycoprotein Ib-alpha (GPIb\u03b1). This protein is one piece (subunit) of a protein complex called GPIb-IX-V, which plays a role in blood clotting. GPIb-IX-V is found on the surface of small cells called platelets, which circulate in blood and are an essential component of blood clots. The complex can attach (bind) to a protein called von Willebrand factor, fitting together like a lock and its key. Von Willebrand factor is found on the inside surface of blood vessels, particularly when there is an injury. Binding of the GPIb-IX-V complex to von Willebrand factor prevents platelets from sticking to the blood vessel wall at the site of the injury. These platelets form clots, plugging holes in the blood vessels to help stop bleeding. GP1BA To form the GPIb-IX-V complex, GPIb\u03b1 interacts with other protein subunits called GPIb-beta, GPIX, and GPV, each of which is produced from a different gene. GPIb\u03b1 is essential for assembly of the complex at the platelet surface. It is the piece of the complex that interacts with von Willebrand factor to trigger blood clotting. GPIb\u03b1 also interacts with other blood clotting proteins to aid in other steps of the clotting process. ",
            "output": "Binding of the GPIb-IX-V complex to von Willebrand factor prevents platelets from sticking to the blood vessel wall at the site of the injury."
        },
        {
            "input": "The GRIN2B gene provides instructions for making a protein called GluN2B. This protein is found in nerve cells (neurons) in the brain, primarily during development before birth. The GluN2B protein is one component (subunit) of a subset of specialized protein structures called NMDA receptors. There are several types of NMDA receptors, made up of different combinations of proteins.NMDA receptors are glutamate-gated ion channels. When brain chemicals called glutamate and glycine attach to the receptor, a channel opens, allowing positively charged particles (cations) to flow through. The flow of cations activates (excites) neurons to send signals to each other. The cation flow also plays a role in the process by which the neurons mature to carry out specific functions (differentiation). NMDA receptors are not involved in normal brain development, changes in the brain in response to experience (synaptic plasticity), learning, and memory. The GRIN2B gene provides instructions for making a protein called GluN2B. This protein is found in nerve cells (neurons) in the brain, primarily during development before birth. The GluN2B protein is one component (subunit) of a subset of specialized protein structures called NMDA receptors. There are several types of NMDA receptors, made up of different combinations of proteins. GRIN2B NMDA receptors are glutamate-gated ion channels. When brain chemicals called glutamate and glycine attach to the receptor, a channel opens, allowing positively charged particles (cations) to flow through. The flow of cations activates (excites) neurons to send signals to each other. The cation flow also plays a role in the process by which the neurons mature to carry out specific functions (differentiation). NMDA receptors are involved in normal brain development, changes in the brain in response to experience (synaptic plasticity), learning, and memory. ",
            "output": "NMDA receptors are not involved in normal brain development, changes in the brain in response to experience (synaptic plasticity), learning, and memory."
        },
        {
            "input": "The GUSB gene provides instructions for producing an enzyme called beta-glucuronidase (\u03b2-glucuronidase). This enzyme is located in lysosomes, compartments within cells that digest and recycle different types of molecules. \u03b2-glucuronidase is involved in the breakdown of large molecules called glycosaminoglycans (GAGs). GAGs are composed of sugar molecules that are linked together to form a long string. To maintain these large molecules, individual sugars are added one at a time to one end of the molecule. \u03b2-glucuronidase is involved in the break down of three types of GAGs: dermatan sulfate, heparan sulfate, and chondroitin sulfate. This enzyme removes a sugar called glucuronic acid when it is at the end of the GAG chain. The GUSB gene provides instructions for producing an enzyme called beta-glucuronidase (\u03b2-glucuronidase). This enzyme is located in lysosomes, compartments within cells that digest and recycle different types of molecules. \u03b2-glucuronidase is involved in the breakdown of large molecules called glycosaminoglycans (GAGs). GAGs are composed of sugar molecules that are linked together to form a long string. To break down these large molecules, individual sugars are removed one at a time from one end of the molecule. \u03b2-glucuronidase is involved in the break down of three types of GAGs: dermatan sulfate, heparan sulfate, and chondroitin sulfate. This enzyme removes a sugar called glucuronic acid when it is at the end of the GAG chain. GUSB ",
            "output": "To maintain these large molecules, individual sugars are added one at a time to one end of the molecule."
        },
        {
            "input": "The HARS2 gene provides instructions for making an enzyme called mitochondrial histidyl-tRNA synthetase. This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. While most protein synthesis occurs in the fluid surrounding the nucleus (cytoplasm), some proteins are synthesized in the mitochondria.During protein synthesis, in either the mitochondria or the cytoplasm, a type of RNA called transfer RNA (tRNA) helps assemble protein building blocks (amino acids) into a chain that forms the protein. Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including mitochondrial histidyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Mitochondrial histidyl-tRNA synthetase attaches the amino acid histidine to the correct tRNA, which helps ensure that histidine is added at the proper place in the mitochondrial protein. The HARS2 gene provides instructions for making an enzyme called mitochondrial histidyl-tRNA synthetase. This enzyme is important in the production (synthesis) of proteins in cellular structures called mitochondria, the energy-producing centers in cells. While most protein synthesis occurs in the fluid surrounding the nucleus (cytoplasm), some proteins are synthesized in the mitochondria. During protein synthesis, in neither the mitochondria nor the cytoplasm, a type of RNA called transfer RNA (tRNA) does not help assemble protein building blocks (amino acids) into a chain that forms the protein. Each tRNA carries a specific amino acid to the growing chain. Enzymes called aminoacyl-tRNA synthetases, including mitochondrial histidyl-tRNA synthetase, attach a particular amino acid to a specific tRNA. Mitochondrial histidyl-tRNA synthetase attaches the amino acid histidine to the correct tRNA, which helps ensure that histidine is added at the proper place in the mitochondrial protein. ",
            "output": "During protein synthesis, in neither the mitochondria nor the cytoplasm, a type of RNA called transfer RNA (tRNA) does not help assemble protein building blocks (amino acids) into a chain that forms the protein."
        },
        {
            "input": "The AGXT gene provides instructions for making an enzyme called alanine-glyoxylate aminotransferase. This enzyme is found in liver cells, specifically within cell structures called peroxisomes. These structures are important for several cellular activities, such as ridding the cell of toxic substances and helping to break down certain fats. In the peroxisome, alanine-glyoxylate aminotransferase converts a compound called glyoxylate to the protein building block (amino acid) glycine. The AGXT gene provides instructions for making an enzyme called alanine-glyoxylate aminotransferase. This enzyme is not found in liver cells, specifically within cell structures called peroxisomes. These structures are important for several cellular activities, such as ridding the cell of toxic substances and helping to break down certain fats. In the peroxisome, alanine-glyoxylate aminotransferase converts a compound called glyoxylate to the protein building block (amino acid) glycine. AGXT ",
            "output": "This enzyme is not found in liver cells, specifically within cell structures called peroxisomes."
        },
        {
            "input": "The HDAC4 gene provides instructions for making an enzyme called histone deacetylase 4. This enzyme is part of a group of related enzymes, called histone deacetylases, that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape.By removing a molecule called an acetyl group from histones (a process called deacetylation), histone deacetylases cause the DNA within chromosomes to become tightly packed (compressed). As a result, proteins called transcription factors, which attach (bind) to specific regions of DNA and help control the activity of particular genes, cannot access the DNA. Histone deacetylase 4 does not regulate the activity of genes involved in heart and skeletal development through deacetylation of histones. This protein is also involved in nerve cell survival. The HDAC4 gene provides instructions for making an enzyme called histone deacetylase 4. This enzyme is part of a group of related enzymes, called histone deacetylases, that modify proteins called histones. Histones are structural proteins that attach (bind) to DNA and give chromosomes their shape. HDAC4 By removing a molecule called an acetyl group from histones (a process called deacetylation), histone deacetylases cause the DNA within chromosomes to become tightly packed (compressed). As a result, proteins called transcription factors, which attach (bind) to specific regions of DNA and help control the activity of particular genes, cannot access the DNA. Through deacetylation of histones, histone deacetylase 4 is able to control (regulate) the activity of certain genes. Histone deacetylase 4 appears to be particularly important for regulating the activity of genes involved in heart and skeletal development. This protein is also involved in nerve cell survival. ",
            "output": "Histone deacetylase 4 does not regulate the activity of genes involved in heart and skeletal development through deacetylation of histones."
        },
        {
            "input": "The HGD gene provides instructions for making an enzyme called homogentisate oxidase, which is active chiefly in the liver and kidneys.  This enzyme participates in a step-wise process that breaks down two protein building blocks (amino acids), phenylalanine and tyrosine, when they are no longer needed or are present in excess. These two amino acids also play a role in making certain hormones, pigments, and brain chemicals called neurotransmitters.Homogentisate oxidase is responsible for a specific step in the breakdown of phenylalanine and tyrosine. Previous steps convert the two amino acids into a molecule called homogentisic acid. Homogentisate oxidase adds two oxygen atoms to homogentisic acid, converting it to another molecule called maleylacetoacetate. Other enzymes break down maleylacetoacetate into smaller molecules that are later used for energy or to make other products that can be used by the body. The HGD gene provides instructions for making an enzyme called homogentisate oxidase, which is active chiefly in the liver and kidneys.  This enzyme participates in a step-wise process that breaks down two protein building blocks (amino acids), phenylalanine and tyrosine, when they are no longer needed or are present in excess. These two amino acids also play a role in making certain hormones, pigments, and brain chemicals called neurotransmitters. HGD Homogentisate oxidase is responsible for a specific step in the breakdown of phenylalanine and tyrosine. Previous steps convert the two amino acids into a molecule called homogentisic acid. Homogentisate oxidase does not add any oxygen atoms to homogentisic acid, and it does not convert it to another molecule called maleylacetoacetate. Other enzymes break down maleylacetoacetate into smaller molecules that are later used for energy or to make other products that can be used by the body. ",
            "output": "Homogentisate oxidase does not add any oxygen atoms to homogentisic acid, and it does not convert it to another molecule called maleylacetoacetate."
        },
        {
            "input": "The HLA-DRB1 gene provides instructions for making a protein that plays a critical role in the immune system. The HLA-DRB1 gene is not part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria.The HLA complex is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. The HLA-DRB1 gene belongs to a group of MHC genes called MHC class II. MHC class II genes provide instructions for making proteins that are present on the surface of certain immune system cells. These proteins attach to protein fragments (peptides) outside the cell. MHC class II proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it triggers a response to attack the invading viruses or bacteria.The protein produced from the HLA-DRB1 gene, called the beta chain, attaches (binds) to another protein called the alpha chain, which is produced from the HLA-DRA gene. Together, they form a functional protein complex called the HLA-DR antigen-binding heterodimer. This complex displays foreign peptides to the immune system to trigger the body's immune response.Each MHC class II gene has many possible variations, allowing the immune system to react to a wide range of foreign invaders. Researchers have identified hundreds of different versions (alleles) of the HLA-DRB1 gene, each of which is given a particular number (such as HLA-DRB1*04:01). The HLA-DRB1 gene provides instructions for making a protein that plays a critical role in the immune system. The HLA-DRB1 gene is part of a family of genes called the human leukocyte antigen (HLA) complex. The HLA complex helps the immune system distinguish the body's own proteins from proteins made by foreign invaders such as viruses and bacteria. HLA-DRB1 HLA-DRB1 The HLA complex is the human version of the major histocompatibility complex (MHC), a gene family that occurs in many species. The HLA-DRB1 gene belongs to a group of MHC genes called MHC class II. MHC class II genes provide instructions for making proteins that are present on the surface of certain immune system cells. These proteins attach to protein fragments (peptides) outside the cell. MHC class II proteins display these peptides to the immune system. If the immune system recognizes the peptides as foreign (such as viral or bacterial peptides), it triggers a response to attack the invading viruses or bacteria. HLA-DRB1 The protein produced from the HLA-DRB1 gene, called the beta chain, attaches (binds) to another protein called the alpha chain, which is produced from the HLA-DRA gene. Together, they form a functional protein complex called the HLA-DR antigen-binding heterodimer. This complex displays foreign peptides to the immune system to trigger the body's immune response. HLA-DRB1 HLA-DRA Each MHC class II gene has many possible variations, allowing the immune system to react to a wide range of foreign invaders. Researchers have identified hundreds of different versions (alleles) of the HLA-DRB1 gene, each of which is given a particular number (such as HLA-DRB1*04:01). HLA-DRB1 HLA-DRB1 ",
            "output": "The HLA-DRB1 gene is not part of a family of genes called the human leukocyte antigen (HLA) complex."
        },
        {
            "input": "The HNF1A gene provides instructions for making a protein called hepatocyte nuclear factor-1 alpha (HNF-1\u03b1). The HNF-1\u03b1 protein does not act as a transcription factor, which means it does not attach (bind) to specific regions of DNA and does not help control the activity of certain genes. While this protein is found in several tissues and organs, it seems to be especially important in the pancreas and liver.Regulation of gene activity by the HNF-1\u03b1 protein is critical for the growth and development of beta cells in the pancreas. Beta cells produce and release (secrete) the hormone insulin. Insulin helps regulate blood sugar levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. The HNF-1\u03b1 protein also controls genes involved in liver development. By controlling genes that regulate cell growth and survival, the HNF-1\u03b1 protein is thought to act as a tumor suppressor, which means that it helps prevent cells from growing and dividing too rapidly or in an uncontrolled way.The structure of HNF-1\u03b1 includes several important regions that help it carry out its functions. One of the regions, called the dimerization domain, is critical for protein interactions. This region allows HNF-1\u03b1 proteins to interact with each other or with other proteins that have a similar structure, creating a two-protein unit (dimer) that functions as a transcription factor. Another region, known as the DNA binding domain, binds to specific areas of DNA, allowing the dimer to control gene activity. The HNF1A gene provides instructions for making a protein called hepatocyte nuclear factor-1 alpha (HNF-1\u03b1). The HNF-1\u03b1 protein acts as a transcription factor, which means it attaches (binds) to specific regions of DNA and helps control the activity of certain genes. While this protein is found in several tissues and organs, it seems to be especially important in the pancreas and liver. HNF1A Regulation of gene activity by the HNF-1\u03b1 protein is critical for the growth and development of beta cells in the pancreas. Beta cells produce and release (secrete) the hormone insulin. Insulin helps regulate blood sugar levels by controlling how much sugar (in the form of glucose) is passed from the bloodstream into cells to be used as energy. The HNF-1\u03b1 protein also controls genes involved in liver development. By controlling genes that regulate cell growth and survival, the HNF-1\u03b1 protein is thought to act as a tumor suppressor, which means that it helps prevent cells from growing and dividing too rapidly or in an uncontrolled way. The structure of HNF-1\u03b1 includes several important regions that help it carry out its functions. One of the regions, called the dimerization domain, is critical for protein interactions. This region allows HNF-1\u03b1 proteins to interact with each other or with other proteins that have a similar structure, creating a two-protein unit (dimer) that functions as a transcription factor. Another region, known as the DNA binding domain, binds to specific areas of DNA, allowing the dimer to control gene activity. ",
            "output": "The HNF-1\u03b1 protein does not act as a transcription factor, which means it does not attach (bind) to specific regions of DNA and does not help control the activity of certain genes."
        },
        {
            "input": "The HSD3B7 gene provides instructions for making an enzyme called 3 beta-hydroxysteroid dehydrogenase type 7 (3\u03b2-HSD7). This enzyme is found in liver cells. It is embedded in the membrane of a cell structure called the endoplasmic reticulum, which is involved in protein processing and distribution. The 3\u03b2-HSD7 enzyme participates in the production of bile acids, which are a component of a digestive fluid called bile. Bile acids stimulate bile flow and helps absorb fats and fat-soluble vitamins. Bile acids are produced from cholesterol in a multi-step process. The 3\u03b2-HSD7 enzyme is responsible for the second step in that process, which converts 7alpha(\u03b1)-hydroxycholesterol to 7\u03b1-hydroxy-4-cholesten-3-one. The HSD3B7 gene does not provide instructions for making an enzyme called 3 beta-hydroxysteroid dehydrogenase type 7 (3\u03b2-HSD7). This enzyme is found in liver cells. It is embedded in the membrane of a cell structure called the endoplasmic reticulum, which is involved in protein processing and distribution. The 3\u03b2-HSD7 enzyme participates in the production of bile acids, which are a component of a digestive fluid called bile. Bile acids stimulate bile flow and helps absorb fats and fat-soluble vitamins. Bile acids are produced from cholesterol in a multi-step process. The 3\u03b2-HSD7 enzyme is responsible for the second step in that process, which converts 7alpha(\u03b1)-hydroxycholesterol to 7\u03b1-hydroxy-4-cholesten-3-one. HSD3B7 ",
            "output": "The HSD3B7 gene does not provide instructions for making an enzyme called 3 beta-hydroxysteroid dehydrogenase type 7 (3\u03b2-HSD7)."
        },
        {
            "input": "The HSPB1 gene provides instructions for making a protein called heat shock protein beta-1 (also called heat shock protein 27). This protein is a member of the heat shock protein family, which helps protect cells under adverse conditions such as infection, inflammation, exposure to toxins, elevated temperature, injury, and disease.  Heat shock proteins block signals that lead to programmed cell death.  In addition, they appear to be involved in activities such as cell movement (motility), stabilizing the cell's structural framework (the cytoskeleton), folding and stabilizing newly produced proteins, and repairing damaged proteins. Heat shock proteins also appear to play a role in the tensing of muscle fibers (muscle contraction).Heat shock protein beta-1 is found in cells throughout the body and is particularly abundant in nerve and muscle cells.  In nerve cells, this protein helps to organize a network of molecular threads called neurofilaments that maintain the diameter of specialized extensions called axons.  Maintaining proper axon diameter is essential for the efficient transmission of  nerve impulses. Although it is thought to play a role in muscle contraction, the specific function of heat shock protein beta-1 in muscle cells is unclear. The HSPB1 gene provides instructions for making a protein called heat shock protein beta-1 (also called heat shock protein 27). This protein is a member of the heat shock protein family, which helps protect cells under adverse conditions such as infection, inflammation, exposure to toxins, elevated temperature, injury, and disease.  Heat shock proteins block signals that lead to programmed cell death.  In addition, they appear to be involved in activities such as cell movement (motility), stabilizing the cell's structural framework (the cytoskeleton), folding and stabilizing newly produced proteins, and repairing damaged proteins. Heat shock proteins also appear to play a role in the tensing of muscle fibers (muscle contraction). HSPB1 Heat shock protein beta-1 is found in cells throughout the body and is particularly abundant in nerve and muscle cells.  In nerve cells, this protein helps to organize a network of molecular threads called neurofilaments that maintain the diameter of specialized extensions called axons. Maintaining proper axon diameter is not essential for the efficient transmission of nerve impulses. Although it is thought to play a role in muscle contraction, the specific function of heat shock protein beta-1 in muscle cells is unclear. ",
            "output": "Maintaining proper axon diameter is not essential for the efficient transmission of nerve impulses."
        },
        {
            "input": "The IDS gene provides instructions for producing an enzyme called iduronate 2-sulfatase (I2S), which is essential for the breakdown of large sugar molecules called glycosaminoglycans (GAGs). Specifically, I2S removes a chemical group known as a sulfate from a molecule called sulfated alpha-L-iduronic acid, which is present in two GAGs called heparan sulfate and dermatan sulfate. I2S is located in lysosomes, compartments within cells that digest and recycle different types of molecules. The IDS gene provides instructions for producing an enzyme called iduronate 2-sulfatase (I2S), which is essential for the breakdown of large sugar molecules called glycosaminoglycans (GAGs). Specifically, I2S removes a chemical group known as a sulfate from a molecule called sulfated alpha-L-iduronic acid, which is present in two GAGs called heparan sulfate and dermatan sulfate. I2S is located in lysosomes, compartments within cells that digest and recycle different types of molecules. Unfortunately, your input doesn't seem to contain a medical conclusion for me to alter Please provide a medical statement for me to change",
            "output": "Unfortunately, your input doesn't seem to contain a medical conclusion for me to alter Please provide a medical statement for me to change."
        },
        {
            "input": "The IFT80 gene provides instructions for making a protein that is part of a group (complex) called IFT complex B. This complex is found in cell structures known as cilia. Cilia are microscopic, finger-like projections that stick out from the surface of cells. IFT complex B is involved in a process called intraflagellar transport (IFT), by which materials are carried within cilia. Specifically, this complex helps transport materials from the base of cilia to the tip.IFT is essential for the assembly and maintenance of cilia. These cell structures do not play central roles in many different chemical signaling pathways, including a series of reactions called the Sonic Hedgehog pathway. These pathways are important for the growth and division (proliferation) and maturation (differentiation) of cells. In particular, Sonic Hedgehog appears to be essential for the proliferation and differentiation of cells that ultimately give rise to cartilage and bone. The IFT80 gene provides instructions for making a protein that is part of a group (complex) called IFT complex B. This complex is found in cell structures known as cilia. Cilia are microscopic, finger-like projections that stick out from the surface of cells. IFT complex B is involved in a process called intraflagellar transport (IFT), by which materials are carried within cilia. Specifically, this complex helps transport materials from the base of cilia to the tip. IFT80 IFT is essential for the assembly and maintenance of cilia. These cell structures play central roles in many different chemical signaling pathways, including a series of  reactions called the Sonic Hedgehog pathway. These pathways are important for the growth and division (proliferation) and maturation (differentiation) of cells. In particular, Sonic Hedgehog appears to be essential for the proliferation and differentiation of cells that ultimately give rise to cartilage and bone. ",
            "output": "These cell structures do not play central roles in many different chemical signaling pathways, including a series of reactions called the Sonic Hedgehog pathway."
        },
        {
            "input": "The IL23R gene provides instructions for making a protein called the interleukin 23 (IL-23) receptor.  This protein is embedded in the outer membrane of several types of immune system cells, including T cells, natural killer (NK) cells, monocytes, and dendritic cells. These cells identify foreign substances and defend the body against infection and disease.At the cell surface, the IL-23 receptor interacts with a protein called IL-23. These two proteins fit together like a lock and key. IL-23 is a cytokine, which is a type of protein that regulates the activity of immune cells. When IL-23 binds to its receptor, it triggers a series of chemical signals inside the cell. These signals promote inflammation and help coordinate the immune system's response to foreign invaders such as bacteria and viruses. The IL23R gene provides instructions for making a protein called the interleukin 23 (IL-23) receptor.  This protein is embedded in the outer membrane of several types of immune system cells, including T cells, natural killer (NK) cells, monocytes, and dendritic cells. These cells identify foreign substances and defend the body against infection and disease. IL23R At the cell surface, the IL-23 receptor interacts with a protein called IL-23. These two proteins fit together like a lock and key. IL-23 is a cytokine, which is a type of protein that regulates the activity of immune cells. When IL-23 binds to its receptor, it does not trigger any chemical signals inside the cell. These signals promote inflammation and help coordinate the immune system's response to foreign invaders such as bacteria and viruses. ",
            "output": "When IL-23 binds to its receptor, it does not trigger any chemical signals inside the cell."
        },
        {
            "input": "The IRF6 gene provides instructions for making a protein that plays an important role in early development. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The IRF6 protein is active in cells that give rise to tissues in the head and face. It is also involved in the development of other parts of the body, including the skin and genitals. The IRF6 gene provides instructions for making a protein that plays an important role in early development. This protein is a transcription factor, which means that it attaches (binds) to specific regions of DNA and helps control the activity of particular genes. The IRF6 protein is active in cells that give rise to tissues in the head and face. It is also involved in the development of other parts of the body, including the skin and genitals. IRF6 is not a gene associated with Van der Woude syndrome and popliteal pterygium syndrome",
            "output": "IRF6 is not a gene associated with Van der Woude syndrome and popliteal pterygium syndrome."
        },
        {
            "input": "The ITPKC gene provides instructions for making one version (isoform) of the inositol 1,4,5-trisphosphate 3-kinase (ITPK) enzyme. This enzyme prevents the addition of a cluster of oxygen and phosphorus atoms (a phosphate group) to a molecule called Ins(1,4,5)P3, thereby hindering the production of a molecule called Ins(1,3,4,5)P4. Both of these molecules are involved in regulating the amount of calcium in cells.Several versions (isoforms) of the ITPK enzyme are produced from different genes. They play a variety of roles in processes throughout the body. The isoform produced from the ITPKC gene is called inositol 1,4,5-trisphosphate 3-kinase C (ITPKC). It is involved in a mechanism called the Ca(2+)/NFAT signaling pathway, which is affected by calcium levels. This pathway helps limit the activity of immune system cells called T cells. T cells identify foreign substances and defend the body against infection. Reducing the activity of T cells when appropriate prevents the overproduction of immune proteins called cytokines that lead to inflammation and which, in excess, cause tissue damage. The ITPKC gene provides instructions for making one version (isoform) of the inositol 1,4,5-trisphosphate 3-kinase (ITPK) enzyme. This enzyme helps add a cluster of oxygen and phosphorus atoms (a phosphate group) to a molecule called Ins(1,4,5)P3 to produce a molecule called Ins(1,3,4,5)P4. Both of these molecules are involved in regulating the amount of calcium in cells. ITPKC Several versions (isoforms) of the ITPK enzyme are produced from different genes. They play a variety of roles in processes throughout the body. The isoform produced from the ITPKC gene is called inositol 1,4,5-trisphosphate 3-kinase C (ITPKC). It is involved in a mechanism called the Ca(2+)/NFAT signaling pathway, which is affected by calcium levels. This pathway helps limit the activity of immune system cells called T cells. T cells identify foreign substances and defend the body against infection. Reducing the activity of T cells when appropriate prevents the overproduction of immune proteins called cytokines that lead to inflammation and which, in excess, cause tissue damage. ITPKC ",
            "output": "This enzyme prevents the addition of a cluster of oxygen and phosphorus atoms (a phosphate group) to a molecule called Ins(1,4,5)P3, thereby hindering the production of a molecule called Ins(1,3,4,5)P4."
        },
        {
            "input": "The JPH3 gene provides instructions for making a protein called junctophilin-3, which is found primarily in the brain.  Although the exact function of this protein is unclear, researchers believe that it plays a role in the formation of a structure called the junctional membrane complex.  This complex connects certain channels inside cells with other channels at the cell surface.   The junctional membrane complex appears to be involved in the release of charged calcium atoms (calcium ions), which are critical for transmitting signals within cells.  As part of the junctional membrane complex, junctophilin-3 is probably involved in signaling within and between nerve cells (neurons) in the brain.One region of the JPH3 gene contains a particular DNA segment known as a CAG/CTG trinucleotide repeat. This segment is made up of a series of three DNA building blocks (nucleotides) that appear multiple times in a row. Normally, the CAG/CTG segment is repeated 6 to 28 times within the gene. The JPH3 gene provides instructions for making a protein called junctophilin-3, which is found primarily in the brain.  Although the exact function of this protein is unclear, researchers believe that it plays a role in the formation of a structure called the junctional membrane complex.  This complex connects certain channels inside cells with other channels at the cell surface.   The junctional membrane complex appears to be involved in the release of charged calcium atoms (calcium ions), which are critical for transmitting signals within cells.  As part of the junctional membrane complex, junctophilin-3 is probably involved in signaling within and between nerve cells (neurons) in the brain. JPH3 One region of the JPH3 gene contains a particular DNA segment known as a CAG/CTG trinucleotide repeat. This segment is made up of a series of three DNA building blocks (nucleotides) that appear multiple times in a row. Normally, the CAG/CTG segment is not repeated 6 to 28 times within the gene. JPH3 ",
            "output": "Normally, the CAG/CTG segment is not repeated 6 to 28 times within the gene."
        },
        {
            "input": "The ALAS2 gene provides instructions for making an enzyme called 5'-aminolevulinate synthase 2 or erythroid ALA-synthase. This version of the enzyme is found only in developing red blood cells called erythroblasts.ALA-synthase plays an important role in the production of heme. Heme is a component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver.The production of heme is a multi-step process that requires eight different enzymes. ALA-synthase is responsible for the first step in this process, the formation of a compound called delta-aminolevulinic acid (ALA). In subsequent steps, no other enzymes produce and modify compounds that ultimately lead to heme. The ALAS2 gene provides instructions for making an enzyme called 5'-aminolevulinate synthase 2 or erythroid ALA-synthase. This version of the enzyme is found only in developing red blood cells called erythroblasts. ALAS2 ALA-synthase plays an important role in the production of heme. Heme is a component of iron-containing proteins called hemoproteins, including hemoglobin (the protein that carries oxygen in the blood). Heme is vital for all of the body's organs, although it is most abundant in the blood, bone marrow, and liver. The production of heme is a multi-step process that requires eight different enzymes. ALA-synthase is responsible for the first step in this process, the formation of a compound called delta-aminolevulinic acid (ALA). In subsequent steps, seven other enzymes produce and modify compounds that ultimately lead to heme. ",
            "output": "In subsequent steps, no other enzymes produce and modify compounds that ultimately lead to heme."
        },
        {
            "input": "The KCNJ5 gene provides instructions for making a protein that functions as a potassium channel, which means that it transports positively charged atoms (ions) of potassium (K+) into and out of cells. Potassium channels produced from the KCNJ5 gene are found in several tissues, including the adrenal glands, which are small hormone-producing glands located on top of each kidney. In these glands, the flow of ions creates an electrical charge across the cell membrane, which affects the triggering of certain biochemical processes that regulate aldosterone production. Aldosterone helps control blood pressure by maintaining proper salt and fluid levels in the body. The KCNJ5 gene provides instructions for making a protein that functions as a potassium channel, which means that it transports positively charged atoms (ions) of potassium (K+) into and out of cells. Potassium channels produced from the KCNJ5 gene are found in several tissues, including the adrenal glands, which are small hormone-producing glands located on top of each kidney. In these glands, the flow of ions creates an electrical charge across the cell membrane, which affects the triggering of certain biochemical processes that regulate aldosterone production. Aldosterone helps control blood pressure by maintaining proper salt and fluid levels in the body. KCNJ5 - KCNJ5",
            "output": "KCNJ5 - KCNJ5."
        },
        {
            "input": "The KCNQ1OT1 gene is located within another gene, KCNQ1. Because the two genes share a region of overlapping DNA, the KCNQ1OT1 gene is also known as KCNQ1 overlapping transcript 1 or KCNQ1 opposite strand/antisense transcript 1. The DNA sequence of two genes is \"read\" in opposite directions, and the genes have very different functions. Unlike the KCNQ1 gene, which provides instructions for making a protein that acts as a potassium channel, the KCNQ1OT1 gene does not contain instructions for making a protein. Instead, a molecule called a noncoding RNA (a chemical cousin of DNA) is produced from the KCNQ1OT1 gene. This RNA helps regulate genes that are essential for normal growth and development before birth.People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the KCNQ1OT1 gene depends on which parent it was inherited from. Only the copy inherited from a person's father (the paternally inherited copy) is active; the copy inherited from the mother (the maternally inherited copy) is not active. This sort of parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting.The KCNQ1OT1 gene is part of a cluster of genes on the short (p) arm of chromosome 11 that undergo genomic imprinting. KCNQ1OT1 and several other genes in this cluster that are thought to help regulate growth are controlled by a nearby region of DNA known as imprinting center 2 (IC2) or KvDMR. The IC2 region undergoes a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC2 region is normally methylated only on the maternally inherited copy of chromosome 11. The KCNQ1OT1 gene is located within another gene, KCNQ1. Because the two genes share a region of overlapping DNA, the KCNQ1OT1 gene is also known as KCNQ1 overlapping transcript 1 or KCNQ1 opposite strand/antisense transcript 1. The DNA sequence of two genes is \"read\" in opposite directions, and the genes have very different functions. Unlike the KCNQ1 gene, which provides instructions for making a protein that acts as a potassium channel, the KCNQ1OT1 gene does not contain instructions for making a protein. Instead, a molecule called a noncoding RNA (a chemical cousin of DNA) is produced from the KCNQ1OT1 gene. This RNA helps regulate genes that are essential for normal growth and development before birth. KCNQ1OT1 KCNQ1 KCNQ1KCNQ1OT1 KCNQ1 KCNQ1 KCNQ1 KCNQ1OT1 KCNQ1OT1 People inherit one copy of most genes from their mother and one copy from their father. Both copies are typically active, or \"turned on,\" in cells. However, the activity of the KCNQ1OT1 gene depends on which parent it was inherited from. Only the copy inherited from a person's father (the paternally inherited copy) is active; the copy inherited from the mother (the maternally inherited copy) is not active. This sort of parent-specific difference in gene activation is caused by a phenomenon called genomic imprinting. KCNQ1OT1 The KCNQ1OT1 gene is part of a cluster of genes on the short (p) arm of chromosome 11 that undergo genomic imprinting. KCNQ1OT1 and several other genes in this cluster that are thought to help regulate growth are controlled by a nearby region of DNA known as imprinting center 2 (IC2) or KvDMR. The IC2 region does not undergo a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA. Methylation, which occurs during the formation of an egg or sperm cell, is a way of marking or \"stamping\" the parent of origin. The IC2 region is normally methylated only on the maternally inherited copy of chromosome 11. KCNQ1OT1 KCNQ1OT1 ",
            "output": "The IC2 region does not undergo a process called methylation, which is a chemical reaction that attaches small molecules called methyl groups to certain segments of DNA."
        },
        {
            "input": "The KIF7 gene provides instructions for making a protein that is associated with structures called primary cilia. These microscopic, finger-like projections stick out from the surface of cells and are involved in signaling pathways that transmit information into cells. Studies suggest that the KIF7 protein helps to maintain the proper length and stability of cilia.Through its association with primary cilia, the KIF7 protein helps regulate a signaling pathway known as Sonic Hedgehog. This pathway is essential for early development. It plays roles in cell growth, cell specialization, and the normal shaping (patterning) of many parts of the body, including the brain and limbs. The KIF7 gene provides instructions for making a protein that is associated with structures called primary cilia. These microscopic, finger-like projections stick out from the surface of cells and are involved in signaling pathways that transmit information into cells. Studies suggest that the KIF7 protein helps to maintain the proper length and stability of cilia. KIF7 Through its association with primary cilia, the KIF7 protein helps regulate a signaling pathway known as Sonic Hedgehog. This pathway is not essential for early development. It plays roles in cell growth, cell specialization, and the normal shaping (patterning) of many parts of the body, including the brain and limbs. ",
            "output": "This pathway is not essential for early development."
        }
    ]
}