PRMT1,PRMT6 methylate arginine-4 of histone H4

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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).

Literature References
PubMed ID Title Journal Year
18079182 PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation

Hyllus, D, Stein, C, Schnabel, K, Schiltz, E, Imhof, A, Dou, Y, Hsieh, J, Bauer, UM

Genes Dev. 2007
11448779 Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1

Strahl, BD, Briggs, SD, Brame, CJ, Caldwell, JA, Koh, SS, Ma, H, Cook, RG, Shabanowitz, J, Hunt, DF, Stallcup, MR, Allis, CD

Curr. Biol. 2001
Participant Of
Catalyst Activity
Catalyst Activity
protein-arginine N-methyltransferase activity of PRMT1,PRMT6 [nucleoplasm]
Physical Entity
Orthologous Events