Anti-PRMT7

PRMT7 (Protein arginine methyltransferase 7) is a protein that is encoded by the PRMT7 gene. Arginine methylation is an apparently irreversible protein modification, catalyzed by arginine methyltransferases, such as PRMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. PRMT7 is 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. PRMT7 mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. It is expressed on adipose tissue, thymus, bone marrow, etc and has four isoforms. Protein 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. 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. Specifically mediates the symmetric dimethylation of histone H4 'Arg-3' to form H4R3me2s. Plays a role in gene imprinting by being recruited by CTCFL at the H19 imprinted control region (ICR) and methylating histone H4 to form H4R3me2s, possibly leading to recruit DNA methyltransferases at these sites. May also play a role in embryonic stem cell (ESC) pluripotency. Also able to mediate the arginine methylation of histone H2A and myelin basic protein (MBP) in vitro, the relevance of such results is however unclear in vivo. [The UniProt Consortium]