Reactome | PRMT1,PRMT6 methylate methyl-lysine-4 of histone H4

PRMT1,PRMT6 methylate methyl-lysine-4 of histone H4

Stable Identifier

R-HSA-5661126

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

Synonyms

PRMT1,PRMT6 methylate MeR4-HIST1H4

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

PRMT1,PRMT6 methylate methyl-lysine-4 of histone H4

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
11448779	Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1 Shabanowitz, J, Koh, SS, Ma, H, Brame, CJ, Stallcup, MR, Caldwell, JA, Briggs, SD, Hunt, DF, Cook, RG, Strahl, BD, Allis, CD	Curr. Biol.	2001
18079182	PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation Schnabel, K, Schiltz, E, Bauer, UM, Stein, C, Hsieh, J, Imhof, A, Dou, Y, Hyllus, D	Genes Dev.	2007