PRMT1 (Wang et al. 2001, Strahl et al. 2001, Wagner et al. 2006) and PRMT6 (Hyllus et al. 2007) can asymmetrically dimethylate histone H4 at arginine-3 (H4R3me2a). This functions as a transcriptional activation mark that can result in either the recruitment of methyl-binding proteins or the deposition of other posttranslational marks. PRMT1 is the best studied. It is recruited to promoters by a number of different transcription factors (Bedford & Richard 2005). PRMT1-knockout mice die shortly after implantation (Pawlak et al. 2000). In vitro PRMT1 can also methylate histone H2A at arginine-3 (Strahl et al. 2001).
Shabanowitz, J, Koh, SS, Ma, H, Brame, CJ, Stallcup, MR, Caldwell, JA, Briggs, SD, Hunt, DF, Cook, RG, Strahl, BD, Allis, CD
Schnabel, K, Schiltz, E, Bauer, UM, Stein, C, Hsieh, J, Imhof, A, Dou, Y, Hyllus, D
protein-arginine N-methyltransferase activity of PRMT1,PRMT6 [nucleoplasm]
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