MGP Database

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MGP001501

UniProt Annotations

Entry Information
Gene Nameprotein arginine methyltransferase 1
Protein Entry
UniProt ID
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=4; Name=1; Synonyms=V2; IsoId=Q99873-1; Sequence=Displayed; Name=2; Synonyms=V3; IsoId=Q99873-2; Sequence=VSP_005208; Name=3; Synonyms=V1; IsoId=Q99873-3; Sequence=VSP_005209; Name=4; IsoId=Q99873-4; Sequence=VSP_046334;
Biophysicochemical PropertiesKinetic parameters: KM=1 uM for AdoMet {ECO:0000269|PubMed:19405910}; KM=4.2 uM for H4 {ECO:0000269|PubMed:19405910}; Vmax=1.2 nmol/min/mg enzyme toward AdoMet {ECO:0000269|PubMed:19405910}; Vmax=1.24 nmol/min/mg enzyme toward H4 {ECO:0000269|PubMed:19405910};
Catalytic ActivityS-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone]. {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:19405910}.
Enzyme RegulationBy BTG1, BTG2 and ILF3.
FunctionArginine methyltransferase that methylates (mono and asymmetric dimethylation) the guanidino nitrogens of arginyl residues present in proteins such as ESR1, histone H2, H3 and H4, PIAS1, HNRNPA1, HNRNPD, NFATC2IP, SUPT5H, TAF15 and EWS. Constitutes the main enzyme that mediates monomethylation and asymmetric dimethylation of histone H4 'Arg-4' (H4R3me1 and H4R3me2a, respectively), a specific tag for epigenetic transcriptional activation. Together with dimethylated PIAS1, represses STAT1 transcriptional activity, in the late phase of interferon gamma (IFN-gamma) signaling. May be involved in the regulation of TAF15 transcriptional activity, act as an activator of estrogen receptor (ER)-mediated transactivation, play a key role in neurite outgrowth and act as a negative regulator of megakaryocytic differentiation, by modulating p38 MAPK pathway. Methylates FOXO1 and retains it in the nucleus increasing its transcriptional activity. {ECO:0000269|PubMed:11387442, ECO:0000269|PubMed:11448779, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18657504, ECO:0000269|PubMed:18773938, ECO:0000269|PubMed:19124016, ECO:0000269|PubMed:19136629, ECO:0000269|PubMed:19405910, ECO:0000269|PubMed:20442406}.
InteractionSelf; NbExp=3; IntAct=EBI-78738, EBI-78738; Q9Y3Y2:CHTOP; NbExp=2; IntAct=EBI-78738, EBI-347794; Q5TAQ9:DCAF8; NbExp=2; IntAct=EBI-78738, EBI-740686; Q08211:DHX9; NbExp=2; IntAct=EBI-78738, EBI-352022; Q01844:EWSR1; NbExp=2; IntAct=EBI-78738, EBI-739737; Q8IZU1:FAM9A; NbExp=2; IntAct=EBI-78738, EBI-8468186; P04591:gag (xeno); NbExp=2; IntAct=EBI-78738, EBI-6179727; Q5JVS0:HABP4; NbExp=2; IntAct=EBI-78738, EBI-523625; P61978:HNRNPK; NbExp=3; IntAct=EBI-78738, EBI-304185; Q12906:ILF3; NbExp=2; IntAct=EBI-78738, EBI-78756; P48552:NRIP1; NbExp=4; IntAct=EBI-78738, EBI-746484; Q8IZS5:OFCC1; NbExp=2; IntAct=EBI-78738, EBI-8477661; Q9NR22:PRMT8; NbExp=3; IntAct=EBI-78738, EBI-745545; Q14524:SCN5A; NbExp=2; IntAct=EBI-78738, EBI-726858; Q96BD6:SPSB1; NbExp=2; IntAct=EBI-78738, EBI-2659201; Q99619:SPSB2; NbExp=2; IntAct=EBI-78738, EBI-2323209; O60506:SYNCRIP; NbExp=2; IntAct=EBI-78738, EBI-1024357; P40337:VHL; NbExp=2; IntAct=EBI-78738, EBI-301246;
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 LocationNucleus {ECO:0000269|PubMed:19136629}. Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytosol {ECO:0000250}. Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity). {ECO:0000250}.
SubunitHomodimer and heterodimer with PRMT8. Individual homodimers can associate to form a homohexamer. Interacts with BTG1, BTG2, NFATC2IP and IFNAR1 (By similarity). Interacts with and methylates CHTOP, thereby enabling the interaction of CHTOP with the 5FMC complex (By similarity). Interacts with ILF3 and SUPT5H. Interacts with and methylates FOXO1, leading to the nuclear retention of FOXO1 and the stimulation of FOXO1 transcriptional activity. Methylation of FOXO1 is increased upon oxidative stress. {ECO:0000250, ECO:0000269|PubMed:10749851, ECO:0000269|PubMed:11101900, ECO:0000269|PubMed:12718890, ECO:0000269|PubMed:18320585, ECO:0000269|PubMed:18951090}.
Tissue SpecificityWidely expressed. {ECO:0000269|PubMed:11097842}.
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