Protein Arginine Methyltransferase 6 (PRMT6)

Protein arginine N-methyltransferases, such as PRMT6, catalyze the sequential transfer of a methyl group from S-adenosyl-L-methionine to the side chain nitrogens of arginine residues within proteins to form methylated arginine derivatives and S-adenosyl-L-homocysteine. The deduced 375-amino acid protein has a calculated molecular mass of 41.9 kD.

PRMT6 contains a catalytic core sequence and no additional domains. The catalytic cores of PRMT6 and PRMT2 shares 38% amino acid identity. Northern blot analysis detected broad expression of 2.4- and 2.6-kb transcripts. Confocal microscopy of fluorescence-labeled PRMT6 showed strong nuclear localization in transfected HeLa cells.