KDM2A, KDM2B, KDM4A demethylate MeK37-histone H3

Stable Identifier
Reaction [transition]
Homo sapiens
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All characterised lysine demethylases other than KDM1A belong to the jumonji C-domain (JmjC) containing family, members of the Cupin superfamily of mononuclear Fe (II)-dependent oxygenases. They require 2-oxoglutarate (2-OG) and molecular oxygen as co-substrates, producing succinate and carbon dioxide. This hydroxylation-based mechanism does not require a protonatable lysine epsilon-amine group and consequently JmjC-containing demethylases are able to demethylate tri-, di- and monomethylated lyines.

The first reported JmjC-containing demethylases were KDM2A and KDM2B (JHDM1A/B, FBXL11/10). These demethylate lysine-37 of histone H3 when mono- or di-methylated (H3K36Me1/2) (Tsukada et al. 2006). KDM4A (JHDM3A) can demethylate mono-, di and trimethylated lysine-37 of histone H3 (Klose et al. 2006).

Literature References
PubMed ID Title Journal Year
16732292 The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36

Klose, RJ, Yamane, K, Zhang, Y, Bae, Y, Tempst, P, Zhang, D, Wong, J, Erdjument-Bromage, H

Nature 2006
16362057 Histone demethylation by a family of JmjC domain-containing proteins

Tsukada, Y, Fang, J, Warren, ME, Zhang, Y, Borchers, CH, Tempst, P, Erdjument-Bromage, H

Nature 2006
Catalyst Activity

histone demethylase activity of KDM2A, KDM2B, KDM4A [nucleoplasm]

Orthologous Events
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