PRMT6 (D5A2N) Rabbit mAb #14641

Protein arginine N-methyltransferase 6 (PRMT6) is a member of the protein arginine N-methyltransferase (PRMT) family of proteins that catalyze the transfer of a methyl group from S-adenosylmethionine (AdoMet) to a guanidine nitrogen of arginine (1). The three types of PRMTs share the ability to mono-methylate arginine residues, but vary in their ability to generate differential methylation states (1-3). Mono-methylated arginine residues are further methylated by type I PRMTs to generate an asymmetric di-methyl arginine or by type II PRMTs to form a symmetric-dimethyl arginine. Type III methyltransferases are only able to mono-methylate arginine residues (1-3). PRMT6 is a type I PRMT that acts as both a transcriptional coactivator and a corepressor and catalyzes the asymmetric di-methylation of histone H3 (Arg 2, Arg42), histone H4 (Arg3), and histone H2A at Arg29 (2,4). PRMT6 acts as a coactivator for transcription factors, including estrogen receptor and NFκB, while asymmetric di-methylation of histone H3 (Arg2) by PRMT6 prevents MLL methylation of histone H3 at Lys4 and inhibits transcription activation (5-8). In addition to its role in regulating transcription, PRMT6 methylates DNA polymerase β, leading to enhanced DNA binding and processivity during base excision repair of damaged DNA (9).