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Details on Person Histone H3 is symmetrically dimethylated on arginine-3 by PR...
| Class:Id | Summation:5218944 |
|---|---|
| _displayName | Histone H3 is symmetrically dimethylated on arginine-3 by PR... |
| _timestamp | 2014-05-09 09:19:20 |
| created | [InstanceEdit:5218943] Jupe, S, 2013-12-20 |
| literatureReference | [LiteratureReference:5218932] Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance [LiteratureReference:5225675] PRMT5 modulates the metabolic response to fasting signals [LiteratureReference:5205809] Methylation of histone H3R2 by PRMT6 and H3K4 by an MLL complex are mutually exclusive [LiteratureReference:5205806] PRMT6-mediated methylation of R2 in histone H3 antagonizes H3 K4 trimethylation |
| modified | [InstanceEdit:5225678] Jupe, S, 2014-01-08 [InstanceEdit:5423532] Jupe, Steve, 2014-05-09 |
| text | Histone H3 is symmetrically dimethylated on arginine-3 by PRMT5 and PRMT7 (Migliori et al. 2012, Tsai et al. 2013). This excludes binding of RBBP7, a central component of the co-repressor complexes Sin3a, NURD and PRC2. Conversely Me2sR3-histone H3 enhances binding of WDR5, a common component of the coactivator complexes MLL, SET1A, SET1B, NLS1 and ATAC. The interaction of histone H3 with WDR5 distinguishes symmetric dimethylation of arginine-3 from asymmetric dimethylation, which inhibits the recruitment of WDR5 to chromatin (Guccione et al. 2007, Hyllus et al. 2007, Migliori et al. 2012). |
| (summation) | [Reaction:5218952] PRMT5:WDR77, PRMT7 methylate arginine-3 of histone H3 (H3R2) [Homo sapiens] |
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