JMJD7 dimer hydroxlates a lysine residue of DRG2

Stable Identifier
R-HSA-9629578
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
2-oxoglutarate + L-lysyl-(protein) + O2 => (3S)-3-hydroxy-L-lysyl-(protein) + CO2 + succinate
ReviewStatus
3/5
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JMJD7 (JmjC domain-containing protein 7) catalyzes the 3-hydroxlation of a lysine residue of DRG2 (developmentally-regulated GTP-binding protein 2). The catalytically active form of JMJD7 is a dimer, each monomeric subunit of which is associated with a Fe2+ ion (Markolovic et al. 2018). DRG2 occurs as a heterdimer with one molecule of RWDD1 (DFRP2 IIshikawa et al. 2005, 2009).
Literature References
PubMed ID Title Journal Year
19819225 Independent stabilizations of polysomal Drg1/Dfrp1 complex and non-polysomal Drg2/Dfrp2 complex in mammalian cells

Ishikawa, K, Akiyama, T, Ito, K, Semba, K, Inoue, J

Biochem. Biophys. Res. Commun. 2009
15676025 Identification of DRG family regulatory proteins (DFRPs): specific regulation of DRG1 and DRG2

Ishikawa, K, Azuma, S, Ikawa, S, Semba, K, Inoue, J

Genes Cells 2005
29915238 The Jumonji-C oxygenase JMJD7 catalyzes (3S)-lysyl hydroxylation of TRAFAC GTPases

Markolovic, S, Zhuang, Q, Wilkins, SE, Eaton, CD, Abboud, MI, Katz, MJ, McNeil, HE, Leśniak, RK, Hall, C, Struwe, WB, Konietzny, R, Davis, S, Yang, M, Ge, W, Benesch, JLP, Kessler, BM, Ratcliffe, PJ, Cockman, ME, Fischer, R, Wappner, P, Chowdhury, R, Coleman, ML, Schofield, CJ

Nat. Chem. Biol. 2018
Participants
Participates
Event Information
Catalyst Activity

peptidyl-lysine 3-dioxygenase activity of JMJD7 dimer [cytosol]

Orthologous Events
Authored
Created
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