Protein arginine methyltransferase 2 (PRMT2)

Protein arginine methyltransferase 2 (PRMT2) is a member of the protein arginine methyltransferase enzyme family that catalyzes the asymmetric dimethylation of arginine residues on histone and non-histone proteins, most notably H3R8me2a (asymmetric dimethylation of histone H3 at arginine 8)[1][3]. PRMT2 contains a canonical methyltransferase core and a unique SH3 domain, enabling interactions with a broad range of splicing factors and nuclear receptors[2]. It acts as a transcriptional co-activator, modulating chromatin state and gene expression, particularly by linking histone modification (such as H3R8me2a) with transcriptional activation at enhancers and promoters[1]. PRMT2 is overexpressed in several human cancers (including glioblastoma, breast, and renal carcinomas), drives cell cycle-related oncogenic gene expression programs, and is implicated in cell proliferation, tumor progression, neuronal morphogenesis, Wnt signaling, and stress responses[1][2][3]. PRMT2 is considered an emerging cancer therapeutic target due to its epigenetic regulatory roles, but small molecule inhibitor development is still at an early stage and its broader functions are not yet fully understood[2][5].

Other names

Protein arginine N-methyltransferase 2HMT1HRMT1L1MGC111373Histone-arginine N-methyltransferase PRMT2HMT1 (hnRNP methyltransferase, S. cerevisiae)-like 1HMT1 hnRNP methyltransferase-like 1PRMT2 alphaPRMT2 betaPRMT2 gamma

Inhibition of enzyme catalytic activity (e.g., SAM analogues and competitive inhibitors block transfer of methyl groups to arginine residues); Downregulation/knockdown (genetic silencing reduces target gene transcription and cell proliferation)[1]