KDM5B demethylates histone H3 trimethyllysine-4 (H3K4me3)

Stable Identifier
R-HSA-9822461
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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KDM5B (PLU-1) demethylates histone H3 trimethyllysine-4 (H3K4me3, lysine-5 of the preprotein) in vitro and in embryonic cells (Christensen et al. 2007, Yamane et al. 2007, Kristensen et al. 2012) and is inferred to catalyze the same reaction in zygotes. KDM5A and KDM5B demethylate broad regions of H3K4me3 in cleavage stage embryos (inferred from mouse embryos).
Literature References
PubMed ID Title Journal Year
22420752 Studies of H3K4me3 demethylation by KDM5B/Jarid1B/PLU1 reveals strong substrate recognition in vitro and identifies 2,4-pyridine-dicarboxylic acid as an in vitro and in cell inhibitor

Helin, K, Kastrup, JS, Nielsen, AL, Lees, M, Olsen, L, Helgstrand, C, Kristensen, LH, Gajhede, M, Cloos, P

FEBS J 2012
17320161 RBP2 belongs to a family of demethylases, specific for tri-and dimethylated lysine 4 on histone 3

Helin, K, Salcini, AE, Christensen, J, Rose, S, Agger, K, Hansen, KH, Rappsilber, J, Sennels, L, Pasini, D, Cloos, PA

Cell 2007
17363312 PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation

Klose, RJ, Fabrizio, LA, Fang, J, Yamane, K, Zhang, Y, Tateishi, K, Taylor-Papadimitriou, J, Tempst, P, Erdjument-Bromage, H

Mol Cell 2007
Participants
Participates
Catalyst Activity

histone H3K4 demethylase activity of KDM5B:Fe2+ [nucleoplasm]

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