Reactome | PRMT1 (Wang et al. 2001, Strahl et al. 2001, Wagner et al. 2...

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PRMT1 (Wang et al. 2001, Strahl et al. 2001, Wagner et al. 2... Show undefined attributes

created	[InstanceEdit:5205795] Jupe, S, 2013-12-06
dbId	5205826
displayName	PRMT1 (Wang et al. 2001, Strahl et al. 2001, Wagner et al. 2...
literatureReference	[LiteratureReference:5205821] Methylation of histone H4 at arginine 3 facilitating transcriptional activation by nuclear hormone receptor [LiteratureReference:5205837] Methylation of histone H4 at arginine 3 occurs in vivo and is mediated by the nuclear receptor coactivator PRMT1 [LiteratureReference:5205845] SET-mediated promoter hypoacetylation is a prerequisite for coactivation of the estrogen-responsive pS2 gene by PRMT1 [LiteratureReference:5205806] PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation [LiteratureReference:5205836] Arginine methylation an emerging regulator of protein function [LiteratureReference:5205800] Arginine N-methyltransferase 1 is required for early postimplantation mouse development, but cells deficient in the enzyme are viable
modified	[InstanceEdit:5423532] Jupe, Steve, 2014-05-09
schemaClass	Summation
text	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).

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