Search Results
Overview
| Uniprot ID | O14744 |
|---|---|
| Protein Name | Protein arginine N-methyltransferase 5 |
| Gene Name | PRMT5 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 240 | TSIFLTNKKGFPVLS |
| 241 | SIFLTNKKGFPVLSK |
Function
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:21081503, PubMed:21258366, PubMed:21917714, PubMed:22269951). 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:11747828, PubMed:12411503, 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:21258366, PubMed:21917714). 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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005794 | Golgi apparatus |
| Cellular Component | GO:0035097 | histone methyltransferase complex |
| Cellular Component | GO:0034709 | methylosome |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Molecular Function | GO:0070888 | E-box binding |
| Molecular Function | GO:0140938 | histone H3 methyltransferase activity |
| Molecular Function | GO:0044020 | histone H4R3 methyltransferase activity |
| Molecular Function | GO:0042054 | histone methyltransferase activity |
| Molecular Function | GO:0042802 | identical protein binding |
| Molecular Function | GO:0008327 | methyl-CpG binding |
| Molecular Function | GO:0008168 | methyltransferase activity |
| Molecular Function | GO:0002039 | p53 binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0016274 | protein-arginine N-methyltransferase activity |
| Molecular Function | GO:0035243 | protein-arginine omega-N symmetric methyltransferase activity |
| Molecular Function | GO:0043021 | ribonucleoprotein complex binding |
| Molecular Function | GO:0003714 | transcription corepressor activity |
| Biological Process | GO:0006338 | chromatin remodeling |
| Biological Process | GO:0032922 | circadian regulation of gene expression |
| Biological Process | GO:0006353 | DNA-templated transcription termination |
| Biological Process | GO:0042118 | endothelial cell activation |
| Biological Process | GO:0090161 | Golgi ribbon formation |
| Biological Process | GO:0097421 | liver regeneration |
| Biological Process | GO:0045596 | negative regulation of cell differentiation |
| Biological Process | GO:0044027 | negative regulation of gene expression via chromosomal CpG island methylation |
| Biological Process | GO:0018216 | peptidyl-arginine methylation |
| Biological Process | GO:0035246 | peptidyl-arginine N-methylation |
| Biological Process | GO:1904992 | positive regulation of adenylate cyclase-inhibiting dopamine receptor signaling pathway |
| Biological Process | GO:0048026 | positive regulation of mRNA splicing, via spliceosome |
| Biological Process | GO:0048714 | positive regulation of oligodendrocyte differentiation |
| Biological Process | GO:2000234 | positive regulation of rRNA processing |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:0070372 | regulation of ERK1 and ERK2 cascade |
| Biological Process | GO:0007088 | regulation of mitotic nuclear division |
| Biological Process | GO:1901796 | regulation of signal transduction by p53 class mediator |
| Biological Process | GO:0000387 | spliceosomal snRNP assembly |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Cheng Z, Huang H, Li M, Chen Y. Proteomic analysis identifies PFKP lactylation in SW480 colon cancer cells.. iScience 27(1):108645. 2024 Jan 19. PMID: 38155775.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.