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Details on Person UniProt:O14744 PRMT5
| Class:Id | ReferenceGeneProduct:101645 |
|---|---|
| _chainChangeLog | initiator methionine:1 added on Sat February 7 2015;chain:1-637 added on Sat February 7 2015;chain:2-637 added on Sat February 7 2015;initiator methionine:1 for 101645 removed on Fri Nov 03 2023;initiator methionine: for 101645 added on Fri Nov 03 2023;initiator methionine: for 101645 removed on Fri Aug 15 2025;initiator methionine:1 for 101645 added on Fri Aug 15 2025 |
| _displayName | UniProt:O14744 PRMT5 |
| _timestamp | 2025-08-15 21:36:02 |
| chain | chain:1-637 initiator methionine:1 chain:2-637 |
| checksum | 522E255B384F25E7 |
| comment | 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).CATALYTIC ACTIVITY L-arginyl-[protein] + 2 S-adenosyl-L-methionine = N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine + 2 H(+)ACTIVITY REGULATION Activity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment.SUBUNIT Forms, at least, homodimers and homotetramers (PubMed:11152681). Component of the methylosome complex, composed of PRMT5, WDR77 and CLNS1A (PubMed:21081503, PubMed:23071334, PubMed:33376131). Found in a complex composed of PRMT5, WDR77 and RIOK1 (PubMed:21081503). RIOK1 and CLNS1A associate with PRMT5 in a mutually exclusive fashion, which allows the recruitment of distinct methylation substrates, such as nucleolin/NCL and Sm proteins, respectively (PubMed:21081503). Interacts with PRDM1 (By similarity). Identified in a complex composed of methylosome and PRMT1 and ERH (PubMed:25284789). Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation. Interacts with HOXA9. Interacts with SRGAP2. Found in a complex with COPRS, RUNX1 and CBFB. Interacts with CHTOP; the interaction symmetrically methylates CHTOP, but seems to require the presence of PRMT1 (PubMed:25284789). Interacts with EPB41L3; this modulates methylation of target proteins. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with JAK2, SSTR1, SUPT5H, BRAF and with active RAF1. Interacts with LSM11, PRMT7 and SNRPD3 (PubMed:16087681, PubMed:17709427). Interacts with COPRS; promoting its recruitment on histone H4. Interacts with CLNS1A/pICln (PubMed:21081503, PubMed:9556550). Identified in a complex with CLNS1A/pICln and Sm proteins. Interacts with RPS10 (PubMed:20159986). Interacts with WDR77. Interacts with IWS1. Interacts with CRY1. Interacts with POLR2A (PubMed:26700805). Interacts with SMN1/SMN2 (PubMed:26700805). Interacts with LYAR; this interaction is direct (PubMed:25092918). Interacts with TTC5/STRAP; this interaction is DNA damage-dependent and promotes PRMT5 interaction with p53/TP53 (PubMed:19011621). Interacts with p53/TP53 in response to DNA damage; the interaction is TTC5/STRAP dependent (PubMed:19011621). Interacts with FAM47E; the interaction is direct, promotes PRMT5 localization to chromatin, and does not disrupt its association with WDR77 or STUB1 (PubMed:33376131). Interacts with TDRD6 (By similarity). Interacts with STUB1 (PubMed:33376131). Interacts with MBD2 (PubMed:16428440). Does not interact with MBD3 (PubMed:16428440).INTERACTION Localizes to promoter regions of target genes on chromosomes (PubMed:33376131). Localizes to methylated chromatin (PubMed:16428440).ALTERNATIVE PRODUCTS Additional isoforms seems to exist. According to EST sequences.TISSUE SPECIFICITY Ubiquitous.SIMILARITY Belongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N-methyltransferase family. |
| description | recommendedName: Protein arginine N-methyltransferase 5 shortName: PRMT5 ecNumber evidence="19 23 27"2.1.1.320 alternativeName: 72 kDa ICln-binding protein alternativeName: Histone-arginine N-methyltransferase PRMT5 alternativeName: Jak-binding protein 1 alternativeName: Shk1 kinase-binding protein 1 homolog shortName: SKB1 homolog shortName: SKB1Hs component recommendedName: Protein arginine N-methyltransferase 5, N-terminally processed /component |
| geneName | PRMT5 HRMT1L5 IBP72 JBP1 SKB1 |
| identifier | O14744 |
| isSequenceChanged | FALSE |
| keyword | 3D-structure Acetylation Alternative splicing Biological rhythms Chromatin regulator Chromosome Cytoplasm Direct protein sequencing Golgi apparatus Methyltransferase Nucleus Proteomics identification Reference proteome Repressor S-adenosyl-L-methionine Transcription Transcription regulation Transferase |
| modified | [InstanceEdit:9836292] Weiser, Joel, 2023-05-25 [InstanceEdit:9852000] Weiser, Joel, 2023-11-03 [InstanceEdit:9917590] Weiser, Joel, 2024-08-09 [InstanceEdit:9926675] Weiser, Joel, 2024-11-03 [InstanceEdit:9939033] Weiser, Joel, 2025-02-21 [InstanceEdit:9963647] Weiser, Joel, 2025-08-15 |
| name | PRMT5 |
| referenceDatabase | [ReferenceDatabase:2] UniProt |
| referenceGene | [ReferenceDNASequence:8961077] ENSEMBL:ENSG00000100462 PRMT5 [Homo sapiens] |
| secondaryIdentifier | ANM5_HUMAN A8MTP3 A8MZ91 B4DX49 B4DY30 B5BU10 D3DS33 E2QRE7 Q6IBR1 Q9UKH1 |
| sequenceLength | 637 |
| species | [Species:48887] Homo sapiens |
| (isoformParent) | [ReferenceIsoform:401253] UniProt:O14744-1 PRMT5 [Homo sapiens] [ReferenceIsoform:8973637] UniProt:O14744-2 PRMT5 [Homo sapiens] [ReferenceIsoform:8973638] UniProt:O14744-3 PRMT5 [Homo sapiens] [ReferenceIsoform:8973639] UniProt:O14744-4 PRMT5 [Homo sapiens] [ReferenceIsoform:8973640] UniProt:O14744-5 PRMT5 [Homo sapiens] |
| (referenceEntity) | [EntityWithAccessionedSequence:191876] PRMT5 [cytosol] [Homo sapiens] [EntityWithAccessionedSequence:5205609] PRMT5 [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:5211300] p-Y297,304,307-PRMT5 [nucleoplasm] [Homo sapiens] [EntityWithAccessionedSequence:8961337] PRMT5 [extracellular region] [Homo sapiens] |
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No pathways have been reviewed or authored by UniProt:O14744 PRMT5 (101645)
