PRMT5:WDR77, PRMT7 methylate arginine-3 of histone H3 (H3R2)

Stable Identifier
Reaction [transition]
Homo sapiens
PRMT5:WDR77, PRMT7 methylate arginine-3 of histone H3
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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).

Literature References
PubMed ID Title Journal Year
22231400 Symmetric dimethylation of H3R2 is a newly identified histone mark that supports euchromatin maintenance

Guccione, E, Cecatiello, V, Sahu, SK, Mapelli, M, Bezzi, M, Bassi, C, Migliori, V, Capasso, P, Low, D, Müller, J, Kuznetsov, V, De Marco, A, Blackstock, W, Gunaratne, J, Mok, WC, Phalke, S, Amati, B

Nat. Struct. Mol. Biol. 2012
Catalyst Activity

protein-arginine N-methyltransferase activity of PRMT5:pT5-WDR77, PRMT7 [nucleoplasm]

Orthologous Events
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