Cytosolic PHD2,3 hydroxylates proline residues on HIF3A

Stable Identifier
R-HSA-1234173
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

Proline hydroxylases PHD2 (EGLN1) and PHD3 (EGLN3) located in the cytosol (Metzen et al. 2003) hydroxylate HIF3A at proline-492 (Hirsila et al. 2003, Maynard et al. 2003). A portion of PHD3 (EGLN3) is also located in the nucleus (Rantanen et al. 2008).

Literature References
PubMed ID Title Journal Year
18337469 Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation

Rantanen, K, Pursiheimo, J, Högel, H, Himanen, V, Metzen, E, Jaakkola, PM

Mol. Biol. Cell 2008
12538644 Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex

Maynard, MA, Qi, H, Chung, J, Lee, EH, Kondo, Y, Hara, S, Conaway, RC, Conaway, JW, Ohh, M

J Biol Chem 2003
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 PHD2,3:LIMD1,AJUBA,WTIP:VHL:EloB:EloC:CUL2:RBX1 [cytosol]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created