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

Stable Identifier
R-HSA-1234166
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
18184961 A gain-of-function mutation in the HIF2A gene in familial erythrocytosis

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

N Engl J Med 2008
19208626 Erythrocytosis-associated HIF-2alpha mutations demonstrate a critical role for residues C-terminal to the hydroxylacceptor proline

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

J Biol Chem 2009
12615973 Intracellular localisation of human HIF-1 alpha hydroxylases: implications for oxygen sensing

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

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

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

J Biol Chem 2003
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
peptidyl-proline 4-dioxygenase activity of PHD1,3 [nucleoplasm]
Physical Entity
Activity
Inferred From
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