KDM2A, KDM2B, KDM4A demethylate MeK37-histone H3

Stable Identifier
R-HSA-4722133
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
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
Participants
Participates
Catalyst Activity

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

Orthologous Events
Authored
Reviewed
Created
Cite Us!