LMPD Database

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LMP012677

UniProt Annotations

Entry Information
Gene Nameprotein arginine methyltransferase 1
Protein EntryANM1_RAT
UniProt IDQ63009
SpeciesRat
Comments
Comment typeDescription
Catalytic ActivityS-adenosyl-L-methionine + arginine-[histone] = S-adenosyl-L-homocysteine + N(omega)-methyl-arginine-[histone].
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. {ECO:0000269|PubMed:12737817, ECO:0000269|PubMed:15837430, ECO:0000269|PubMed:18492485}.
InteractionSelf; NbExp=2; IntAct=EBI-78708, EBI-78708; P62633:CNBP (xeno); NbExp=2; IntAct=EBI-78708, EBI-1047529; Q9JIL3:Ilf3; NbExp=2; IntAct=EBI-78708, EBI-78714;
SimilarityBelongs to the class I-like SAM-binding methyltransferase superfamily. Protein arginine N- methyltransferase family
SimilarityContains 1 SAM-dependent MTase PRMT-type domain
Subcellular LocationNucleus . Nucleus, nucleoplasm {ECO:0000250}. Cytoplasm, cytosol . Note=Mostly found in the cytoplasm. Colocalizes with CHTOP within the nucleus. Low levels detected also in the chromatin fraction (By similarity)
SubunitHomodimer and heterodimer with PRMT8. The dimer can then associate to form a homohexamer. Interacts with NFATC2IP. Interacts with ILF3 and SUPT5H. Interacts with FOXO1; the interaction methylates FOXO1, retaining it in the nucleus and increasing its transcriptional activity. Methylation of FOXO1 is increased with oxidative stress. Interacts with CHTOP; the interaction methylates CHTOP, enabling its interaction with the 5FMC complex (By similarity). Interacts with BTG1, BTG2 and IFNAR1. {ECO:0000250, ECO:0000269|PubMed:12737817, ECO:0000269|PubMed:8663146}.
Tissue SpecificityUbiquitous.