Protein arginine methyltransferase 6 (PRMT6)

Protein arginine methyltransferase 6 is a nuclear type I methyltransferase that catalyzes asymmetric dimethylation of arginine residues, especially on histone H3 and H2A proteins. Its enzymatic activity influences transcription, cell cycle progression, alternative splicing, DNA repair, and signal transduction, often through epigenetic regulation. PRMT6 dysregulation has been implicated in cancer and other diseases, and it is actively being explored as a therapeutic target. PRMT6 acts as both a coactivator and corepressor in different contexts and interacts with other methyltransferases (e.g., is methylated by PRMT1 at R106). The enzyme is expressed in a variety of tissues, most notably kidney and testes, and predominantly localizes to the nucleus. The best-characterized inhibitor is SGC6870, which binds allosterically and inhibits PRMT6 methyltransferase activity.

Other names

PRMT6Protein arginine N-methyltransferase 6

Inhibition of methyltransferase activity (by allosteric binding, e.g., SGC6870)