PRMT6 Protein, Human (HEK293, His-Flag)

PRMT6, a versatile arginine methyltransferase, demonstrates the capability to catalyze the formation of omega-N monomethylarginine (MMA) and asymmetrical dimethylarginine (aDMA), exhibiting a strong preference for aDMA formation. It predominantly methylates arginyl residues within a glycine and arginine-rich domain and shows a bias toward monomethylated substrates. Notably, PRMT6 orchestrates the asymmetric dimethylation of histone H3 'Arg-2,' leading to the creation of H3R2me2a, a distinctive epigenetic tag associated with transcriptional repression. This modification is mutually exclusive with methylation on histone H3 'Lys-4' (H3K4me2 and H3K4me3). PRMT6 serves as a transcriptional repressor for various genes, including HOXA2, THBS1, and TP53, where repression of TP53 impedes cellular senescence. Additionally, PRMT6 methylates histone H2A and H4 'Arg-3' (H2AR3me and H4R3me) and acts as a regulator of DNA base excision during repair by methylating DNA polymerase beta (POLB), enhancing its polymerase activity. It functions as a transcriptional coactivator for steroid hormone receptors, participating in gluconeogenic program activation and regulating alternative splicing events. PRMT6 also plays a role in innate immunity against HIV-1 by methylating and impairing the function of various HIV-1 proteins. Furthermore, it methylates GPS2, providing protection from ubiquitination and degradation, and targets SIRT7, inhibiting its histone deacetylase activity and promoting mitochondria biogenesis.