PRMT5: A Protein Studied for Its Potential as a Drug Target (G10419)

Target Name: PRMT5

NCBI ID: G10419

PRMT5

PRMT5: A Protein Studied for Its Potential as a Drug Target

PRMT5 (PROTECANE TRANSFER RNA SYSTEM 5) is a gene that encodes a protein known as protamineptane, which is a key component of spermatozoa, the male gamete responsible for the production of sperm. PRMT5 is also known as SKB1 homolog.

The discovery and characterization of PRMT5 was made by a team of researchers at the University of California, San Diego, led by Dr. JP. PRMT5 was first identified using transcriptomics techniques, and its function was later confirmed through experiments in which the researchers demonstrated that PRMT5 was involved in the production of spermatozoa.

PRMT5 is a member of the PROTECANE TRANSFER RNA SYSTEM (PRTAS) family, which is responsible for the transfer of RNA from the cytoplasm to the nucleus of a cell. PRTAS is a large family of proteins that includes several highly conserved subunits, including PRMT1, PRMT2, PRMT3, and PRMT5. The PRMT5 protein is characterized by a unique N-terminal region that contains a leucine-rich repeat (LRR) and a polyglutamylated region (PGR) at its C-terminus.

The LRR is a conserved structure that is found in several proteins that are involved in various cellular processes, including DNA replication, transcription, and RNA processing. The PGR is a unique structure that is found in a subset of PRTAS proteins, including PRMT1, PRMT2, and PRMT5. It consists of a unique combination of amino acids that are involved in the formation of a stable complex with DNA.

The role of PRMT5 in the production of spermatozoa is still being fully understood. However, studies have shown that PRMT5 is involved in the production of spermatozoa by regulating the expression of genes that are involved in cell cycle progression, DNA replication, and other processes that are important for sperm formation.

In addition to its role in sperm formation, PRMT5 is also being studied for its potential as a drug target. The N-terminal region of PRMT5 is rich in conserved amino acid residues that are involved in various cellular processes, including cell signaling, DNA replication, and RNA processing. As a result, PRMT5 is a promising target for small molecules that can modulate these processes and potentially have therapeutic applications.

One of the first drugs that was shown to interact with PRMT5 was called \"PRMT5 inhibitor,\" which was developed by a team of researchers at the University of California, San Diego. The inhibitor was shown to block the activity of PRMT5 and improve the production of spermatozoa in male mice.

Another drug that is being studied as a potential PRMT5 inhibitor is called \"PRT5 agonist,\" which is a small molecule that can interact with the N-terminal region of PRMT5. The agonist was shown to increase the production of spermatozoa in male mice , and may be a useful tool for testing the effectiveness of PRT5 inhibitors.

While more research is needed to fully understand the role of PRMT5 in sperm formation and its potential as a drug target, studies have shown that PRMT5 is an important protein that is involved in the production of spermatozoa. The discovery and characterization of PRMT5 has also led to a greater understanding of the PRTAS family and its role in the transfer of RNA from the cytoplasm to the nucleus of a cell.

PRMT5 is a protein that is being studied for its potential as a drug target and its role in the production of spermatozoa. Further research is needed to fully understand the function of PRMT5 and its potential as a therapeutic agent.

Protein Name: Protein Arginine Methyltransferase 5

Functions: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and symmetrical dimethylarginine (sDMA), with a preference for the formation of MMA (PubMed:10531356, PubMed:11152681, PubMed:11747828, PubMed:12411503, PubMed:15737618, PubMed:17709427, PubMed:20159986, PubMed:20810653, PubMed:21258366, PubMed:21917714, PubMed:22269951, PubMed:21081503). Specifically mediates the symmetrical dimethylation of arginine residues in the small nuclear ribonucleoproteins Sm D1 (SNRPD1) and Sm D3 (SNRPD3); such methylation being required for the assembly and biogenesis of snRNP core particles (PubMed:12411503, PubMed:11747828, PubMed:17709427). Methylates SUPT5H and may regulate its transcriptional elongation properties (PubMed:12718890). May methylate the N-terminal region of MBD2 (PubMed:16428440). Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. Methylates histone H2A and H4 'Arg-3' during germ cell development (By similarity). Methylates histone H3 'Arg-8', which may repress transcription (By similarity). Methylates the Piwi proteins (PIWIL1, PIWIL2 and PIWIL4), methylation of Piwi proteins being required for the interaction with Tudor domain-containing proteins and subsequent localization to the meiotic nuage (By similarity). Methylates RPS10. Attenuates EGF signaling through the MAPK1/MAPK3 pathway acting at 2 levels. First, monomethylates EGFR; this enhances EGFR 'Tyr-1197' phosphorylation and PTPN6 recruitment, eventually leading to reduced SOS1 phosphorylation (PubMed:21917714, PubMed:21258366). Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity (PubMed:21917714). Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9 (PubMed:22269951). Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (PubMed:20810653). Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter (By similarity). Methylates GM130/GOLGA2, regulating Golgi ribbon formation (PubMed:20421892). Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner (PubMed:25284789). Symmetrically methylates POLR2A, a modification that allows the recruitment to POLR2A of proteins including SMN1/SMN2 and SETX. This is required for resolving RNA-DNA hybrids created by RNA polymerase II, that form R-loop in transcription terminal regions, an important step in proper transcription termination (PubMed:26700805). Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression (PubMed:25092918). Symmetrically methylates NCL (PubMed:21081503). Methylates p53/TP53; methylation might possibly affect p53/TP53 target gene specificity (PubMed:19011621). Involved in spliceosome maturation and mRNA splicing in prophase I spermatocytes through the catalysis of the symmetrical arginine dimethylation of SNRPB (small nuclear ribonucleoprotein-associated protein) and the interaction with tudor domain-containing protein TDRD6 (By similarity)

The "PRMT5 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 PRMT5 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
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•   related combination drugs;
•   pharmacochemistry experiments;
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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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