KDM5A-D demethylate Me3K5-histone H3

Stable Identifier
R-HSA-5661116
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
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
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
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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
histone demethylase activity of KDM5A-D [nucleoplasm]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created