TRMT10C: A Potential Drug Target and Biomarker for HBV Pre-S2 Trans-Regulated Protein 2

Target Name: TRMT10C

NCBI ID: G54931

TRMT10C

TRMT10C: A Potential Drug Target and Biomarker for HBV Pre-S2 Trans-Regulated Protein 2

Hepatitis B virus (HBV) is a leading cause of liver disease worldwide, with over 200 million people affected globally. The virus is a member of the heparan virus family, and it contains a large double-stranded DNA genome that is encapsulated by a protein called HBsAg. HBsAg is a trans-regulated protein, which means that it is regulated by the virus's DNA but can also be modified by the host's immune response. One of the modifications of HBsAg is the presence of a protein called TRMT10C.

TRMT10C is a non-coding RNA molecule that is synthesized from the double-stranded DNA genome of HBV. It is expressed in the liver and other tissues, and it has been shown to play a role in the replication and immune response of the virus. TRMT10C has also been shown to interact with several host proteins, including the transcription factor ASXL1.

One of the key features of TRMT10C is its ability to be modified by the host's immune response. This modification is known as post-translational modification (PTM), and it can alter the structure and function of TRMT10C. One of the most well-studied PTMs of TRMT10C is the addition of a phosphate group to its amino acid residues. This modification has been shown to play a role in the regulation of HBsAg expression and has potential implications for the immune response to HBV.

In addition to its role in the immune response, TRMT10C has also been shown to be a drug target for small molecules. TRMT10C is a strong candidate for inhibition by small molecules, including inhibitors of the viral replication cycle and interferon-inducible gene expression. This makes it a promising target for the development of new anti-HBV drugs.

TRMT10C has also been shown to be a biomarker for HBV infection. The presence and level of TRMT10C have been shown to be elevated in the blood and other tissues of people with HBV infection, and inhibition of TRMT10C has been shown to be effective in reducing the level of HBsAg in these samples. This suggests that TRMT10C may be a useful biomarker for the diagnosis and treatment of HBV infection.

In conclusion, TRMT10C is a non-coding RNA molecule that is expressed in the liver and other tissues and has been shown to play a role in the replication and immune response of hepatitis B virus (HBV). It is a strong candidate for inhibition by small molecules and has been shown to be a biomarker for HBV infection. Further research is needed to fully understand the role of TRMT10C in the immune response to HBV and its potential as a drug target.

Protein Name: TRNA Methyltransferase 10C, Mitochondrial RNase P Subunit

Functions: Mitochondrial tRNA N(1)-methyltransferase involved in mitochondrial tRNA maturation (PubMed:18984158, PubMed:21593607, PubMed:23042678, PubMed:27132592). Component of mitochondrial ribonuclease P, a complex composed of TRMT10C/MRPP1, HSD17B10/MRPP2 and PRORP/MRPP3, which cleaves tRNA molecules in their 5'-ends (PubMed:18984158). Together with HSD17B10/MRPP2, forms a subcomplex of the mitochondrial ribonuclease P, named MRPP1-MRPP2 subcomplex, which displays functions that are independent of the ribonuclease P activity (PubMed:23042678, PubMed:29040705). The MRPP1-MRPP2 subcomplex catalyzes the formation of N(1)-methylguanine and N(1)-methyladenine at position 9 (m1G9 and m1A9, respectively) in tRNAs; TRMT10C/MRPP1 acting as the catalytic N(1)-methyltransferase subunit (PubMed:23042678). The MRPP1-MRPP2 subcomplex also acts as a tRNA maturation platform: following 5'-end cleavage by the mitochondrial ribonuclease P complex, the MRPP1-MRPP2 subcomplex enhances the efficiency of 3'-processing catalyzed by ELAC2, retains the tRNA product after ELAC2 processing and presents the nascent tRNA to the mitochondrial CCA tRNA nucleotidyltransferase TRNT1 enzyme (PubMed:29040705). In addition to tRNA N(1)-methyltransferase activity, TRMT10C/MRPP1 also acts as a mRNA N(1)-methyltransferase by mediating methylation of adenosine residues at the N(1) position of MT-ND5 mRNA (PubMed:29072297). Associates with mitochondrial DNA complexes at the nucleoids to initiate RNA processing and ribosome assembly

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•   the target screening and validation;
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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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