JMJD6 dimer hydroxylates lysine residues of U2AF2

Nuclear JMJD6 (JmjC domain-containing protein 6) catalyzes the hydroxylation of the 5-carbons of two lysine residues of U2AF2 (splicing factor U2AF 65 kDa subunit, also known as U2AF65) (Webby et al. 2009; Unoki et al. 2013). The active form of the protein is associated with Fe2+. The protein crystallizes as dimers (Mantri et al. 2010) and can form larger oligomers in solution (Hahn et al. 2010). For simplicity, the active form of the enzyme is annotated here as a dimer.<p>JMJD6 has also been reported to have histone demethylase activity (Chang et al. 2007). This activity has been annotated as part of Reactome pathway R-HSA-321842 "HDMs demethylate histones".

核JMJD6（JmjC结构域含蛋白6）催化U2AF2（剪切因子U2AF 65 kDa亚基，亦称U2AF65）中两个赖氨酸残基的5-碳羟基化（Webby等，2009；Unoki等，2013）。该蛋白的活性形式与Fe2+相结合。该蛋白以二聚体形式结晶（Mantri等，2010），并在溶液中可以形成更大的寡聚体（Hahn等，2010）。为简化起见，此处将酶的活性形式标注为二聚体。<p>JMJD6亦被报道具有组蛋白去甲基化酶活性（Chang等，2007）。此活性被标注为Reactome通路R-HSA-321842“HDMs去甲基化组蛋白”的一部分。