PRMT6 (human recombinant; baculovirus expressed)

Protein arginine methyltransferases (PRMTs) are a family of enzymes with highly conserved catalytic domains that catalyze the transfer of a methyl group from S-adenosyl-L-methionine to a specific arginine residue in a target protein. PRMT6 is a nuclear type-1 PRMT, catalyzing the formation of ?-NG-monomethylarginine and asymmetric ?-NG,NG-dimethylarginine on both histone and non-histone targets.{20285,20245,20284} Histone H3 methylation of arginine 2 (H3R2) is a repressive transcriptional mark primarily catalyzed by PRMT6.{20286} H3R2 dimethylation antagonizes the binding of effector proteins sensitive to H3K4 methylation, such as the Mixed Lineage Leukemia complex methyltransferase.{20287} Non-histone targets of PRMT6 include the nuclear high-mobility group protein HMGA1a, a protein important in several processes relating to the maintenance of DNA integrity.{20284}