Reactome | KDM5A-D demethylate Me2K5-histone H3

KDM5A-D demethylate Me2K5-histone H3

Stable Identifier

R-HSA-4754181

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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All characterized lysine demethylases other than KDM1A belong to the jumonjiC domain (JmjC) containing family.The JmjC KDMs are members of the Cupin superfamily of mononuclear Fe (II) dependent oxygenases, which are characterized by the presence of a double-stranded beta-helix core fold. The JmjC KDMs require 2 oxoglutarate (2 OG) and molecular oxygen as co substrates, producing, along with formaldehyde, 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 lysines. KDM5A-D (JARID1A-D) catalyse the demethylation of di- or tri-methylated lysine-5 of histone H3 (H3K4Me2/3) (Christensen et al. 2007, Klose et al. 2007, Lee et al. 2007, Secombe et al. 2007, Seward et al. 2007, Iwase et al. 2007).

Literature References

PubMed ID	Title	Journal	Year
17310255	Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins Seward, DJ, Cubberley, G, Kim, S, Schonewald, M, Zhang, L, Tripet, B, Bentley, DL	Nat. Struct. Mol. Biol.	2007
17351631	The trithorax-group protein Lid is a histone H3 trimethyl-Lys4 demethylase Lee, N, Zhang, J, Klose, RJ, Erdjument-Bromage, H, Tempst, P, Jones, RS, Zhang, Y	Nat. Struct. Mol. Biol.	2007
17320163	The retinoblastoma binding protein RBP2 is an H3K4 demethylase Klose, RJ, Yan, Q, Tothova, Z, Yamane, K, Erdjument-Bromage, H, Tempst, P, Gilliland, DG, Zhang, Y, Kaelin, WG	Cell	2007