PRMT6 Antibody – Rabbit Polyclonal

PRMT6: Arginine methyltransferase that can both catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), with a strong preference for the formation of aDMA. Preferentially methylates arginyl residues present in a glycine and arginine-rich domain and displays preference for monomethylated substrates. Specifically mediates the asymmetric dimethylation of histone H3 'Arg-2' to form H3R2me2a. H3R2me2a represents a specific tag for epigenetic transcriptional repression and is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). It thereby acts as a transcription corepressor of various genes such as HOXA2. Also methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me, respectively). Acts as a regulator of DNA base excision during DNA repair by mediating the methylation of DNA polymerase beta (POLB), leading to stimulate the polymerase activity by enhancing DNA binding and processivity. Methylates HMGA1. May play a role in innate immunity against HIV-1 in case of infection by methylating and impairing the function of various HIV-1 proteins such as Tat, Rev and Nucleocapsid protein p7 (NC). Belongs to the protein arginine N-methyltransferase family. PRMT6 subfamily. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: Methyltransferase, protein arginine; Methyltransferase; EC 2.1.1.125

Chromosomal Location of Human Ortholog: 1p13.3

Cellular Component: nucleoplasm; cytosol; nucleus

Molecular Function: histone methyltransferase activity; protein-arginine omega-N monomethyltransferase activity; protein-arginine omega-N asymmetric methyltransferase activity; protein binding; histone binding

Biological Process: histone methylation; establishment and/or maintenance of chromatin architecture; viral reproduction; transcription, DNA-dependent; base-excision repair; peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; negative regulation of transcription, DNA-dependent