Reactome | Nuclear PHD1,3 hydroxylates proline residues on HIF3A

Nuclear PHD1,3 hydroxylates proline residues on HIF3A

Stable Identifier

R-HSA-1234165

Type

Reaction [transition]

Species

Homo sapiens

Compartment

nucleoplasm

ReviewStatus

5/5

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Nuclear PHD1,3 hydroxylates proline residues on HIF3A

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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
12538644	Multiple splice variants of the human HIF-3 alpha locus are targets of the von Hippel-Lindau E3 ubiquitin ligase complex Lee, EH, Chung, J, Maynard, MA, Qi, H, Ohh, M, Conaway, JW, Kondo, Y, Hara, S, Conaway, RC	J Biol Chem	2003
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