Protein arginine N-methyltransferase 6 is an enzyme that in humans is encoded by the PRMT6gene.[1][2]
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.[supplied by OMIM][2]
References
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Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Sgarra R, Lee J, Tessari MA, et al. (2006). "The AT-hook of the chromatin architectural transcription factor high mobility group A1a is arginine-methylated by protein arginine methyltransferase 6". J. Biol. Chem. 281 (7): 3764–72. doi:10.1074/jbc.M510231200. PMID16293633.
Guccione E, Bassi C, Casadio F, et al. (2007). "Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive". Nature. 449 (7164): 933–7. doi:10.1038/nature06166. PMID17898714.
