KDM2A, KDM2B, KDM4A demethylate MeK37-histone H3

Stable Identifier
R-HSA-4722133
Type
Reaction
Species
Homo sapiens
Compartment
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Summation

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). KDM8 can demethylate diimethylated lysine-37 of histone H3 (Hsia et al. 2010).

Literature References
PubMed ID Title Journal Year
16362057 Histone demethylation by a family of JmjC domain-containing proteins

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

Nature 2006
16732292 The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36

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

Nature 2006
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
histone demethylase activity of KDM2A, KDM2B, KDM4A [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created