KDM2A, KDM2B, KDM4A, KDM8 demethylate Me2K37-histone H3

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

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
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
20457893 KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation

Hsia, DA, Tepper, CG, Pochampalli, MR, Hsia, EY, Izumiya, C, Huerta, SB, Wright, ME, Chen, HW, Kung, HJ, Izumiya, Y

Proc. Natl. Acad. Sci. U.S.A. 2010
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
Participant Of
Catalyst Activity
Catalyst Activity
histone demethylase activity of KDM2A, KDM2B, KDM4A, KDM8 [nucleoplasm]
Physical Entity
Orthologous Events