MGP Database

MGP004234

UniProt Annotations

Entry Information
Gene Nameprotein arginine methyltransferase 5
Protein EntryANM5_HUMAN
UniProt IDO14744
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=5; Comment=Additional isoforms seems to exist. According to EST sequences.; Name=1; IsoId=O14744-1; Sequence=Displayed; Name=2; IsoId=O14744-2; Sequence=VSP_043382; Note=No experimental confirmation available.; Name=4; IsoId=O14744-4; Sequence=VSP_043382, VSP_054768; Note=No experimental confirmation available.; Name=5; IsoId=O14744-5; Sequence=VSP_054685; Note=No experimental confirmation available.; Name=3; IsoId=O14744-3; Sequence=VSP_043382, VSP_054685; Note=No experimental confirmation available.;
Catalytic ActivityS-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. {ECO:0000269|PubMed:23071334}.
Enzyme RegulationActivity is increased by EGF, HGF, FGF1 or FGF2 treatments, and slightly decreased by NGF treatment. {ECO:0000269|PubMed:21917714}.
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:10531356, ECO:0000269|PubMed:11152681, ECO:0000269|PubMed:11747828, ECO:0000269|PubMed:12411503, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951}.
InteractionQ8N8U2:CDYL2; NbExp=2; IntAct=EBI-351098, EBI-8467076; P54105:CLNS1A; NbExp=3; IntAct=EBI-351098, EBI-724693; Q9NQ92:COPRS; NbExp=6; IntAct=EBI-351098, EBI-1642558; Q01094:E2F1; NbExp=8; IntAct=EBI-351098, EBI-448924; Q8TE85:GRHL3; NbExp=2; IntAct=EBI-351098, EBI-8469396; Q9BX10:GTPBP2; NbExp=2; IntAct=EBI-351098, EBI-6115579; P62805:HIST2H4B; NbExp=3; IntAct=EBI-351098, EBI-302023; Q8WVJ2:NUDCD2; NbExp=2; IntAct=EBI-351098, EBI-1052153; Q86U06:RBM23; NbExp=3; IntAct=EBI-351098, EBI-780319; O75044:SRGAP2; NbExp=4; IntAct=EBI-351098, EBI-1051034; Q96RU7:TRIB3; NbExp=2; IntAct=EBI-351098, EBI-492476; Q9BQA1:WDR77; NbExp=6; IntAct=EBI-351098, EBI-1237307; P63104:YWHAZ; NbExp=2; IntAct=EBI-351098, EBI-347088;
Sequence CautionSequence=BC005820; Type=Frameshift; Positions=370; Evidence={ECO:0000305};
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. Nucleus.
SubunitForms, at least, homodimers and homotetramers. Interacts with PRDM1 (By similarity). Component of the methylosome, a 20S complex containing at least CLNS1A/pICln, PRMT5/SKB1 and WDR77/MEP50. 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 (By similarity). 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. Interacts with COPRS; promoting its recruitment on histone H4. Interacts with CLNS1A/pICln. Identified in a complex with CLNS1A/pICln and Sm proteins. Interacts with RPS10. Interacts with WDR77. Interacts with IWS1. Interacts with CRY1. {ECO:0000250, ECO:0000269|PubMed:10531356, ECO:0000269|PubMed:10734105, ECO:0000269|PubMed:11152681, ECO:0000269|PubMed:12411503, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:15485929, ECO:0000269|PubMed:15737618, ECO:0000269|PubMed:16087681, ECO:0000269|PubMed:17184735, ECO:0000269|PubMed:17709427, ECO:0000269|PubMed:18404153, ECO:0000269|PubMed:18984161, ECO:0000269|PubMed:20159986, ECO:0000269|PubMed:20810653, ECO:0000269|PubMed:21258366, ECO:0000269|PubMed:21917714, ECO:0000269|PubMed:22269951, ECO:0000269|PubMed:23071334, ECO:0000269|PubMed:9556550}.
Tissue SpecificityUbiquitous.
  logo