LMPD Database

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LMP004033

UniProt Annotations

Entry Information
Gene Nameprotein arginine N-methyltransferase 5
Protein EntryANM5_MOUSE
UniProt IDQ8CIG8
SpeciesMouse
Comments
Comment typeDescription
Catalytic ActivityS-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
Enzyme RegulationActivity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment. {ECO:0000250}.
FunctionArginine 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. Mono- and dimethylates arginine residues of myelin basic protein (MBP) in vitro. Plays a role in the assembly of snRNP core particles. May play a role in cytokine-activated transduction pathways. Negatively regulates cyclin E1 promoter activity and cellular proliferation. May regulate the SUPT5H transcriptional elongation properties. May be part of a pathway that is connected to a chloride current, possibly through cytoskeletal rearrangement. 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. 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. Acts as a transcriptional corepressor in CRY1-mediated repression of the core circadian component PER1 by regulating the H4R3 dimethylation at the PER1 promoter. {ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:19584108, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:23133559}.
InteractionP25322:Ccnd1; NbExp=5; IntAct=EBI-2527009, EBI-847243; Q9CY57:Chtop; NbExp=4; IntAct=EBI-2527009, EBI-6393116;
SimilarityBelongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N- methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01015}.
SimilarityContains 1 SAM-dependent MTase PRMT-type domain. {ECO:0000255|PROSITE-ProRule:PRU01015}.
Subcellular LocationCytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:22872859}.
SubunitForms, at least, homodimers and homotetramers. Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50. Component of a high molecular weight E2F-pocket protein complex, CERC (cyclin E1 repressor complex). Also interacts with Sm proteins, JAK2 and SSTR1. Associates with SWI/SNF remodeling complexes containing SMARCA2 and SMARCA4. Interacts with LSM11, PRMT7 and SNRPD3. Interacts with COPRS; promoting its recruitment on histone H4 (By similarity). Interacts with PRDM1. Interacts with RPS10. Interacts with EGFR; methylates EGFR and stimulates EGFR-mediated ERK activation (By similarity). Interacts with BRAF and with active RAF1 (By similarity). Interacts with HOXA9 (By similarity). Interacts with SRGAP2. Interacts with EPB41L3; this modulates methylation of target proteins (By similarity). 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. Interacts with IWS1 (By similarity). Interacts with CRY1. {ECO:0000250, ECO:0000269|PubMed:16699504, ECO:0000269|PubMed:19858291, ECO:0000269|PubMed:22193545, ECO:0000269|PubMed:22872859, ECO:0000269|PubMed:23133559}.