JMJD6 dimer hydroxylates lysine residues of U2AF2

Stable Identifier
R-HSA-9630022
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
2-oxoglutarate + L-lysyl-(protein) + O2 => (5S)-5-hydroxy-L-lysyl-(protein) + CO2 + succinate
ReviewStatus
3/5
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Nuclear JMJD6 (JmjC domain-containing protein 6) catalyzes the hydroxylation of the 5-carbons of two lysine residues of U2AF2 (splicing factor U2AF 65 kDa subunit, also known as U2AF65) (Webby et al. 2009; Unoki et al. 2013). The active form of the protein is associated with Fe2+. The protein crystallizes as dimers (Mantri et al. 2010) and can form larger oligomers in solution (Hahn et al. 2010). For simplicity, the active form of the enzyme is annotated here as a dimer.

JMJD6 has also been reported to have histone demethylase activity (Chang et al. 2007). This activity has been annotated as part of Reactome pathway R-HSA-321842 "HDMs demethylate histones".

Literature References
PubMed ID Title Journal Year
19574390 Jmjd6 catalyses lysyl-hydroxylation of U2AF65, a protein associated with RNA splicing

Nielsen, ML, Böttger, A, Wolf, A, Hahn, P, Delahunty, CM, Yates, JR, Mann, M, Webby, CJ, Lengeling, A, Kramer, H, Dreger, M, Butler, DS, Schmitz, C, Schofield, CJ, Gromak, N, Kessler, B, Proudfoot, NJ

Science 2009
21060799 Analysis of Jmjd6 cellular localization and testing for its involvement in histone demethylation

Lengeling, A, Böttger, A, Burrells, A, Wolf, A, Hahn, P, Butler, DS, Wegener, I, Schofield, CJ, Erck, C, Böse, J

PLoS ONE 2010
23303181 Lysyl 5-hydroxylation, a novel histone modification, by Jumonji domain containing 6 (JMJD6)

Hamamoto, R, Shirakawa, M, Fukui, Y, Arita, K, Nakamura, Y, Unoki, M, Masuda, A, Ueda, K, Iwai, Y, Yoshimatsu, M, Dohmae, N, Sasaki, H

J. Biol. Chem. 2013
20684070 Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6

Webby, CJ, McDonough, MA, Oppermann, U, Kochan, G, Butler, DS, Kavanagh, KL, Bagg, EA, Krojer, T, Schofield, CJ, Mantri, M

J. Mol. Biol. 2010
17947579 JMJD6 is a histone arginine demethylase

Zhao, Y, Chen, Y, Bruick, RK, Chang, B

Science 2007
Participants
Participates
Event Information
Catalyst Activity

peptidyl-lysine 5-dioxygenase activity of JMJD6 dimer [nucleoplasm]

Orthologous Events
Authored
Created
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