PRMT1,PRMT6 methylate arginine-4 of histone H4

Stable Identifier
R-HSA-5205798
Type
Reaction
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein-arginine N-methyltransferase activity of PRMT1,PRMT6 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created