JMJD4:Fe2+ hydroxylates a lysine residue of ETF1

Stable Identifier
R-HSA-9629946
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
2-oxoglutarate + L-lysyl-(protein) + O2 => 4-hydroxy-L-lysyl-(protein) + CO2 + succinate
ReviewStatus
3/5
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Cytosolic JMJD4 (JmjC domain-containing protein 4) catalyzes the 4-hydroxlation of lysine-63 residue of ETF1 (eukaryotic peptide chain release factor subunit 1, also known as eRF1). This hydroxylation substantially increases the efficiency with which ETF1 recognizes stop codons (Feng et al. 2014). The catalytically active form of JMJD4 is associated with a Fe2+ ion.
Literature References
PubMed ID Title Journal Year
24486019 Optimal translational termination requires C4 lysyl hydroxylation of eRF1

Trudgian, DC, Hopkinson, RJ, Shelley, J, Coleman, ML, Fischer, R, Feng, T, Schödel, J, Münzel, M, Ge, W, Yates, LA, Gilbert, RJ, Sokolova, E, Yamamoto, A, Alkalaeva, E, Singh, P, Kessler, BM, Cockman, ME, Frolova, LY, Ratcliffe, PJ, McCullagh, JS, Schofield, CJ, Wilkins, SE

Mol. Cell 2014
Participants
Participates
Event Information
Catalyst Activity

peptidyl-lysine 4-dioxygenase activity of JMJD4:Fe2+ [cytosol]

Orthologous Events
Authored
Created
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