Overview:

PRMT8 (protein arginine methyltransferase 8), an arginine methyltransferase that exhibits type I PRMT activity, catalyzing the formation of omega-NG-monomethylated and asymmetrically omega-NG, NG-dimethylated arginine residues. Its N-terminal end harbors a myristoylation motif, and the myristoylation results in its association with the plasma membrane. Unlike other members of PRMTs, it is largely expressed in the brain. It was also found that the N-terminal domain may function as an autoregulator that may be displaced by interaction with one or more physiological inducers.

Gene Aliases:

HRMT1L3, HRMT1L4

Genbank Number:

BC022458

References:

1. Lee J, et al: PRMT8, a new membrane-bound tissue-specific member of the protein arginine methyltransferase family. J Biol Chem 280(38):32890-6. 2005.

2. Sayegh J, et al: Regulation of protein arginine methyl-transferase 8 (PRMT8) activity by its N-terminal domain. J Biol Chem. 282(50):36444-53, 2007.