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Covalent modification of histones plays critical role in regulating chromatin structure and transcription. While most covalent histone modifications are reversible, only recently has it been established that methyl groups are subject to enzymatic removal from histones. A family of novel JmjC domain-containing histone demethylation (JHDM) enzymes have been identified that perform this specific function. Histone demethylation by JHDM proteins requires cofactors Fe(II) and alpha-ketoglutarate. Family members include JHDM1 (demethylating histone 3 at lysine 36), and JHDM2A as well as JMJD2CH3K9 (both of which demethylate histone 3 at lysine 9). Contributions of histone demethylase activity to tumor development, decreases in cell proliferation, and hormone-dependent transcriptional activation have been observed.
1700064E03Rik; BC038313; jmjC domain-containing protein 3; JMJD3; jumonji domain containing 3; jumonji domain containing 3, histone lysine demethylase; jumonji domain-containing 3; jumonji domain-containing protein 3; KDM1 lysine (K)-specific demethylase 6B; Kdm6b; KIAA0346; lysine (K)-specific demethylase 6B; lysine demethylase 6B; Lysine-specific demethylase 6B; mKIAA0346
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