Gene name: PRMT5

Uniprot entry:

O14744

Protein names:

Protein arginine N-methyltransferase 5 (PRMT5) (EC 2.1.1.320) (72 kDa ICln-binding protein) (Histone-arginine N-methyltransferase PRMT5) (Jak-binding protein 1) (Shk1 kinase-binding protein 1 homolog) (SKB1 homolog) (SKB1Hs) [Cleaved into: Protein arginine N-methyltransferase 5, N-terminally processed]

Protein sequence:

1_MAAMA 6_ VGGAG 11_ GSRVS 16_ SGRDL 21_ NCVPE 26_ IADTL 31_ GAVAK 36_ QGFDF 41_ LCMPV 46_ FHPRF 51_ KREFI 56_ QEPAK 61_ NRPGP 66_ QTRSD 71_ LLLSG 76_ RDWNT 81_ LIVGK 86_ LSPWI 91_ RPDSK 96_ VEKIR 101_ RNSEA 106_ AMLQE 111_ LNFGA 116_ YLGLP 121_ AFLLP 126_ LNQED 131_ NTNLA 136_ RVLTN 141_ HIHTG 146_ HHSSM 151_ FWMRV 156_ PLVAP 161_ EDLRD 166_ DIIEN 171_ APTTH 176_ TEEYS 181_ GEEKT 186_ WMWWH 191_ NFRTL 196_ CDYSK 201_ RIAVA 206_ LEIGA 211_ DLPSN 216_ HVIDR 221_ WLGEP 226_ IKAAI 231_ LPTSI 236_ FLTNK 241_ KGFPV 246_ LSKMH 251_ QRLIF 256_ RLLKL 261_ EVQFI 266_ ITGTN 271_ HHSEK 276_ EFCSY 281_ LQYLE 286_ YLSQN 291_ RPPPN 296_ AYELF 301_ AKGYE 306_ DYLQS 311_ PLQPL 316_ MDNLE 321_ SQTYE 326_ VFEKD 331_ PIKYS 336_ QYQQA 341_ IYKCL 346_ LDRVP 351_ EEEKD 356_ TNVQV 361_ LMVLG 366_ AGRGP 371_ LVNAS 376_ LRAAK 381_ QADRR 386_ IKLYA 391_ VEKNP 396_ NAVVT 401_ LENWQ 406_ FEEWG 411_ SQVTV 416_ VSSDM 421_ REWVA 426_ PEKAD 431_ IIVSE 436_ LLGSF 441_ ADNEL 446_ SPECL 451_ DGAQH 456_ FLKDD 461_ GVSIP 466_ GEYTS 471_ FLAPI 476_ SSSKL 481_ YNEVR 486_ ACREK 491_ DRDPE 496_ AQFEM 501_ PYVVR 506_ LHNFH 511_ QLSAP 516_ QPCFT 521_ FSHPN 526_ RDPMI 531_ DNNRY 536_ CTLEF 541_ PVEVN 546_ TVLHG 551_ FAGYF 556_ ETVLY 561_ QDITL 566_ SIRPE 571_ THSPG 576_ MFSWF 581_ PILFP 586_ IKQPI 591_ TVREG 596_ QTICV 601_ RFWRC 606_ SNSKK 611_ VWYEW 616_ AVTAP 621_ VCSAI 626_ HNPTG 631_RSYTI

Protein annotations

Protein functions:

1: 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)