Nuclear PHD1,3 hydroxylates proline residues on HIF3A

Stable Identifier
R-HSA-1234165
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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Proline hydroxylases PHD1 (EGLN2) and PHD3 (EGLN3) located in the nucleus (Metzen et al. 2003) hydroxylate HIF3A at proline-492 (Hirsila et al. 2003, Maynard et al. 2003). Note that proline-492 of the reference isoform is proline-490 in isoform 2, the protein cited by Maynard et al. 2003. The amount of hydroxylation occurring in the nucleus is controversial. Most hydroxylation is believed to occur in the cytosol.

Literature References
PubMed ID Title Journal Year
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
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
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
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Catalyst Activity
Catalyst Activity
Title
peptidyl-proline 4-dioxygenase activity of PHD1,3 [nucleoplasm]
Physical Entity
Activity
Orthologous Events
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Reviewed
Created