Nuclear PHD1,3 hydroxylates proline residues on EPAS1 (HIF2A)

Stable Identifier
Reaction [transition]
Homo sapiens
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Proline hydroxylases PHD1 (EGLN2) and PHD3 (EGLN3) located in the nucleus hydroxylate HIF2A (EPAS1) at proline-405 and proline-531 (Hirsila et al. 2003, Percy et al. 2008, Furlow et al. 2009). The amount of hydroxylation occurring in the nucleus is controversial. Most hydroxylation is believed to be cytosolic.
Literature References
PubMed ID Title Journal Year
19208626 Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline

McMullin, MF, Furlow, PW, Percy, MJ, Lappin, TR, Bierl, C, Master, SR, Sutherland, S

J Biol Chem 2009
18184961 A gain-of-function mutation in the HIF2A gene in familial erythrocytosis

McMullin, MF, Furlow, PW, Li, X, Lucas, GS, Percy, MJ, Lappin, TR

N Engl J Med 2008
12615973 Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing

Stengel, P, Klinger, M, Acker, H, Hellwig-Bürgel, T, Fandrey, J, Wotzlaw, C, Metzen, E, Berchner-Pfannschmidt, U, Huang, WQ, Marxsen, JH, Stolze, I, Jelkmann, W

J Cell Sci 2003
12788921 Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor

Hirsilä, M, Günzler, V, Koivunen, P, Myllyharju, J, Kivirikko, KI

J Biol Chem 2003
Catalyst Activity

peptidyl-proline 4-dioxygenase activity of PHD1,3 [nucleoplasm]

Inferred From
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