1.0 2018-05-07 22:22:16 UTC 2020-05-20 21:03:05 UTC BMDBP00411 Enzyme PRMT5 Involved in histone-arginine N-methyltransferase activity 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. 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. Methylates SUPT5H and may regulate its transcriptional elongation properties (By similarity). 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. Methylates histone H3 'Arg-8', which may repress transcription. 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. Second, methylates RAF1 and probably BRAF, hence destabilizing these 2 signaling proteins and reducing their catalytic activity. Required for induction of E-selectin and VCAM-1, on the endothelial cells surface at sites of inflammation. Methylates HOXA9. Methylates and regulates SRGAP2 which is involved in cell migration and differentiation (By similarity). 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. Methylates H4R3 in genes involved in glioblastomagenesis in a CHTOP- and/or TET1-dependent manner. 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. Along with LYAR, binds the promoter of gamma-globin HBG1/HBG2 and represses its expression. Symmetrically methylates NCL (By similarity). Methylates TP53; methylation might possibly affect TP53 target gene specificity (By similarity). 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 B) and the interaction with tudor domain-containing protein TDRD6 (By similarity). BMDB0000939 S-Adenosylhomocysteine BMDB0001185 S-Adenosylmethionine 10 >1914 bp ATGGCGGCGATGGCGGTCGGTGGTGCCGGTGGAAGCCGCGTGTCCAGCGGGAGGGACCTG AATTGCGTCCCCGAAATAGCTGACACACTGGGGGCTGTGGCCAAGCAGGGGTTTGATTTC CTCTGCATGCCTGTGTTCCACCCGCGTTTCAAGAGGGAATTCACTCAGGAACCTGCTAAG AGTCGGCCGGGCCCCCAGACACGATCAGACCTACTGCTGTCAGGAAGGGACTGGAATACA CTAATTGTGGGAAAGCTTTCTCCATGGATTCGTCCAGACTCAAAAGTGGAGAAGATACGC AGGAACTCTGAGGCGGCTATGTTACAGGAGCTGAATTTTGGGGCATATTTGGGTCTTCCA GCTTTCCTGCTGCCCCTAAATCAGGAAGATAACACAAACTTGGCGAGAGTTTTGACCAAT CACATCCACACTGGCCACCACTCCTCCATGTTCTGGATGCGGGTGCCATTGGTGGCACCA GAGGACCTGAGAGATGATATAATTGAGAACGCACCAACTTCACACACAGAGGAGTACAGT GGAGAGGAGAAGACATGGATGTGGTGGCACAACTTCCGGACCTTATGTGATTACAGCAAG AGGATTGCAGTGGCTCTTGAAATTGGTGCTGACCTCCCATCTAATCATGTCATTGATCGT TGGCTTGGGGAGCCCATCAAAGCAGCCATTCTCCCCACTAGCATTTTCCTGACCAATAAG AAGGGATTTCCTGTTCTTTCTAAGATGCACCAGAGGTTGATCTTCCGACTTCTCAAGTTG GAGGTACAGTTCATCATCACAGGCACCAACCACCACTCAGAGAAGGAGTTCTGCTCCTAC CTCCAATACTTGGAATACCTGAGCCAGAACCGACCTCCACCCAATGCCTACGAACTCTTT GCCAAGGGCTATGAAGATTACCTGCAGTCCCCACTCCAGCCACTGATGGATAACCTGGAA TCTCAGACATACGAAGTGTTCGAAAAGGACCCCATCAAATACTCTCAGTACCAGCAGGCC ATCTATAAATGTCTGTTAGATCGAGTGCCAGAGGAAGAGAAGGACACCAATATCCAAGTG CTGATGGTGCTGGGAGCAGGCCGGGGGCCCCTGGTGAATGCTTCCCTGCGGGCCGCCAAG CAGGCTGACCGGCGGATAAAATTGTACGCTGTGGAGAAGAACCCAAATGCTGTGGTGACG TTGGAGAACTGGCAGTTTGAAGAATGGGGAAGCCAGGTGACAGTAGTCTCATCGGACATG CGGGAGTGGGTGGCTCCAGAGAAAGCAGATATCATTGTCAGTGAGCTTCTGGGGTCCTTT GCTGACAATGAACTGTCACCTGAGAGCCTGGATGGAGCCCAGCACTTCCTAAAAGATGAT GGCGTGAGCATTCCTGGGGAGTACACCTCCTTTCTAGCTCCCATCTCCTCCTCCAAGCTA TACAATGAGGTCCGAGCCTGTCGGGAAAAGGACCGTGACCCTGAGGCCCAGTTTGAGATG CCTTATGTGGTACGACTGCACAATTTCCACCAGCTGTCTGCACCCCAGCCCTGTTTTACC TTCAGCCATCCTAACAGAGATCCTATGATTGACAACAATCGCTACTGTACCTTGGAGTTT CCTGTGGAGGTGAACACAGTGCTGCATGGTTTTGCAGGCTACTTTGAGACTGTGCTTTAT CAGGACATCACTCTGAGTATCCGTCCAGAGACTCACTCTCCTGGGATGTTTTCATGGTTT CCCATCCTCTTCCCCATTAAGCAGCCCATTACGGTGCGTGAAGGCCAGACCATCTGTGTG CGTTTCTGGCGATGCAGCAACTCTAAGAAGGTGTGGTATGAGTGGGCTGTGACGGCACCG GTCTGCTCTGCTATTCACAACCCCACAGGCCGCTCTTACACCATTGGCCTCTAG 637 72629.0 6.24 None >Protein arginine N-methyltransferase 5 MAAMAVGGAGGSRVSSGRDLNCVPEIADTLGAVAKQGFDFLCMPVFHPRFKREFTQEPAK SRPGPQTRSDLLLSGRDWNTLIVGKLSPWIRPDSKVEKIRRNSEAAMLQELNFGAYLGLP AFLLPLNQEDNTNLARVLTNHIHTGHHSSMFWMRVPLVAPEDLRDDIIENAPTSHTEEYS GEEKTWMWWHNFRTLCDYSKRIAVALEIGADLPSNHVIDRWLGEPIKAAILPTSIFLTNK KGFPVLSKMHQRLIFRLLKLEVQFIITGTNHHSEKEFCSYLQYLEYLSQNRPPPNAYELF AKGYEDYLQSPLQPLMDNLESQTYEVFEKDPIKYSQYQQAIYKCLLDRVPEEEKDTNIQV LMVLGAGRGPLVNASLRAAKQADRRIKLYAVEKNPNAVVTLENWQFEEWGSQVTVVSSDM REWVAPEKADIIVSELLGSFADNELSPESLDGAQHFLKDDGVSIPGEYTSFLAPISSSKL YNEVRACREKDRDPEAQFEMPYVVRLHNFHQLSAPQPCFTFSHPNRDPMIDNNRYCTLEF PVEVNTVLHGFAGYFETVLYQDITLSIRPETHSPGMFSWFPILFPIKQPITVREGQTICV RFWRCSNSKKVWYEWAVTAPVCSAIHNPTGRSYTIGL AAI34450.1 A7YW45 ANM5_BOVIN BC134449 PRMT5