Reactome | KDM6A, KDM6B, KDM7A demethylate Me3K28-histone H3

KDM6A, KDM6B, KDM7A demethylate Me3K28-histone H3

Stable Identifier

R-HSA-5661121

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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KDM6A, KDM6B, KDM7A demethylate Me3K28-histone H3

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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 e amine group and consequently JmjC containing demethylases are able to demethylate tri , di and monomethylated lysines.
KDM6A (UTX), KDM6B (JMJD3), KDM6C (UTY) and KDM7A (JHDM1D) catalyse the demethylation of di or tri-methylated lysine-28 of histone H3 (H3K27Me2/3) (Agger et al. 2007, Cho et al. 2007, De Santra et al. 2007, Hong et al. 2007, Lan et al. 2007, Lee et al. 2007, Horton et al. 2010, Huang et al. 2010, Walport et al. 2014).

Literature References

PubMed ID	Title	Journal	Year
20084082	Dual-specificity histone demethylase KIAA1718 (KDM7A) regulates neural differentiation through FGF4 Xiang, Y, Zhu, Q, Li, X, Jing, N, Xu, L, Huang, C, Chen, CD, Zhang, K, Zhu, Z, Wang, Y, Zhang, T	Cell Res.	2010
17713478	UTX and JMJD3 are histone H3K27 demethylases involved in HOX gene regulation and development Helin, K, Canaani, E, Salcini, AE, Issaeva, I, Christensen, J, Rose, S, Agger, K, Rappsilber, J, Pasini, D, Cloos, PA	Nature	2007
20023638	Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases Shi, Y, Zhang, X, Upadhyay, AK, Horton, JR, Cheng, X, Qi, HH	Nat. Struct. Mol. Biol.	2010