PRMT7 Antibody – Rabbit Polyclonal

Arginine methylation is an apparently irreversible protein modification catalyzed by arginine methyltransferases, such as PMT7, using S-adenosylmethionine (AdoMet) as the methyl donor. Arginine methylation is implicated in signal transduction, RNA transport, and RNA splicing (Miranda et al., 2004 [PubMed 15044439]).[supplied by OMIM, Mar 2008]

PRMT7: 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. Belongs to the protein arginine N-methyltransferase family. PRMT7 subfamily. 4 isoforms of the human protein are produced by alternative splicing.

Protein type: Methyltransferase; RNA processing; Methyltransferase, protein arginine; EC 2.1.1.126; EC 2.1.1.125

Chromosomal Location of Human Ortholog: 16q22.1

Cellular Component: nucleoplasm; nucleolus; plasma membrane; cytosol; nucleus

Molecular Function: protein-arginine omega-N monomethyltransferase activity; protein-arginine omega-N asymmetric methyltransferase activity; ribonucleoprotein binding; [myelin basic protein]-arginine N-methyltransferase activity; histone binding; protein-arginine omega-N symmetric methyltransferase activity; S-adenosylmethionine-dependent methyltransferase activity; histone-arginine N-methyltransferase activity

Biological Process: histone methylation; peptidyl-arginine methylation, to symmetrical-dimethyl arginine; establishment and/or maintenance of chromatin architecture; peptidyl-arginine methylation; spliceosomal snRNP biogenesis; genetic imprinting; regulation of transcription, DNA-dependent; transcription, DNA-dependent; regulation of protein binding; DNA methylation during gametogenesis; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; cell differentiation