Reactome | KDM8:Fe2+ hydroxylates an arginine residue of RPS6

KDM8:Fe2+ hydroxylates an arginine residue of RPS6

Stable Identifier

R-HSA-9629869

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol

Synonyms

2-oxoglutarate + L-arginyl-(protein) + O2 => (3R)-3-hydroxy-L-arginyl-(protein) + CO2 + succinate

ReviewStatus

3/5

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KDM8:Fe2+ hydroxylates an arginine residue of RPS6

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KDM8 (JMJC5 - JmjC domain-containing protein 45), active when bound to Fe2+, catalyzes the hydroxylation of an arginine residue of the ribosomal protein RPS6 (40S small ribosomal protein 6). The subcellular location of this reaction under physiological conditions has not been determined; it is arbitrarily annotated as cytosolic.
KDM8, a member of the JmjC protein family, was originally assigned to the branch of the family that catalyzes histone lysine demethylation reactions. Structural studies have shown a closer resemblance to the protein hydroxylation branch of the family (Del Rizzo et al. 2012; Wang et al. 2013), a suggestion confirmed by in vitro studies with synthetic peptides (Wilkins et al. 2018). These studies identified RPS6 as a likely hydroxylation target.

Literature References

PubMed ID	Title	Journal	Year
22851697	Crystal structure and functional analysis of JMJD5 indicate an alternate specificity and function Krishnan, S, Del Rizzo, PA, Trievel, RC	Mol. Cell. Biol.	2012
29563586	JMJD5 is a human arginyl C-3 hydroxylase Gannon, JM, Hopkinson, RJ, Chowdhury, R, Markolovic, S, Islam, MS, Schofield, CJ, Ge, W, Wilkins, SE	Nat Commun	2018
24100311	Structure of the JmjC-domain-containing protein JMJD5 Chen, N, Zang, J, Wang, H, Zhang, X, Wu, M, Zhou, X, Wang, C, Tao, Y	Acta Crystallogr. D Biol. Crystallogr.	2013