SHMT2: A Potential Drug Target and Biomarker for Glycine Auxotroph

Target Name: SHMT2

NCBI ID: G6472

SHMT2

SHMT2: A Potential Drug Target and Biomarker for Glycine Auxotroph

Glycine auxotroph A (SHMT2) is a highly conserved protein that plays a critical role in the regulation of amino acid homeostasis in various organisms, including humans. It is a key component of the human complement system, which is a group of proteins that work together to help maintain the structure and function of the blood. In hamsters, SHMT2 is expressed at high levels and is involved in the regulation of a variety of cellular processes, including bone development, liver function, and reproductive biology.

Recent studies have identified SHMT2 as a potential drug target and biomarker for a variety of diseases, including cardiovascular disease, neurodegenerative diseases, and autoimmune disorders. This is because SHMT2 has been shown to play a role in the development and progression of these diseases, and may be involved in the regulation of key cellular processes that contribute to their development.

One of the key functions of SHMT2 is its role in the regulation of amino acid homeostasis. Amino acids are essential nutrients that are essential for the growth, development, and survival of all living organisms. They are also involved in the regulation of various cellular processes, including signaling pathways and metabolism. However, abnormal levels of amino acids can contribute to the development of diseases, including cardiovascular disease and neurodegenerative disorders.

SHMT2 has been shown to play a role in the regulation of amino acid homeostasis in various organisms, including humans. For example, studies have shown that SHMT2 is involved in the regulation of the levels of amino acids, such as glycine, in the liver. Glycine is an amino acid that is involved in the regulation of various cellular processes, including cell signaling and metabolism. Abnormal levels of glycine have been linked to a variety of diseases, including cardiovascular disease and neurodegenerative disorders.

In addition to its role in the regulation of amino acid homeostasis, SHMT2 has also been shown to play a role in the regulation of cellular processes that are involved in the development and progression of diseases. For example, studies have shown that SHMT2 is involved in the regulation of cellular processes that are involved in the development of cancer, including the regulation of cell signaling pathways and the regulation of DNA replication.

Given the potential role of SHMT2 in the regulation of amino acid homeostasis and cellular processes that are involved in the development and progression of diseases, it is a promising candidate for drug development. Studies are currently being conducted to determine the full range of biological activities and potential drug targets for SHMT2. This includes studies are being conducted to determine the effects of SHMT2 on cellular processes that are involved in the development and progression of diseases, as well as studies to determine the efficacy of SHMT2 as a potential drug.

In conclusion, SHMT2 is a protein that plays a critical role in the regulation of amino acid homeostasis and cellular processes that are involved in the development and progression of diseases. Its potential as a drug target and biomarker makes it an attractive candidate for further study and development. Further studies are needed to fully understand the full range of biological activities and potential drug targets for SHMT2, and to determine its safety and efficacy as a potential drug.

Protein Name: Serine Hydroxymethyltransferase 2

Functions: Catalyzes the cleavage of serine to glycine accompanied with the production of 5,10-methylenetetrahydrofolate, an essential intermediate for purine biosynthesis (PubMed:24075985, PubMed:29364879, PubMed:33015733, PubMed:25619277, PubMed:33015733). Serine provides the major source of folate one-carbon in cells by catalyzing the transfer of one carbon from serine to tetrahydrofolate (PubMed:25619277). Contributes to the de novo mitochondrial thymidylate biosynthesis pathway via its role in glycine and tetrahydrofolate metabolism: thymidylate biosynthesis is required to prevent uracil accumulation in mtDNA (PubMed:21876188). Also required for mitochondrial translation by producing 5,10-methylenetetrahydrofolate; 5,10-methylenetetrahydrofolate providing methyl donors to produce the taurinomethyluridine base at the wobble position of some mitochondrial tRNAs (PubMed:29452640, PubMed:29364879). Associates with mitochondrial DNA (PubMed:18063578). In addition to its role in mitochondria, also plays a role in the deubiquitination of target proteins as component of the BRISC complex: required for IFNAR1 deubiquitination by the BRISC complex (PubMed:24075985)

The "SHMT2 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about SHMT2 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
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•   the target screening and validation;
•   expression level;
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•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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