EC Number   |
Natural Substrates |
|---|
   1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
- |
| 1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
activity of the hypoxia-inducible factor (HIF) complex is controlled by oxygen-dependent hydroxylation of prolyl and asparaginyl residues. Hydroxylation of specific prolyl residues by 2-oxoglutarate-dependent oxygenases mediates ubiquitinylation and proteasomal destruction of HIF-alpha. Hydroxylation of an asparagine residue (ASn803) in the C-terminal transactivation domain of HIF-alpha abrogates interaction with p300, preventing transcriptional activation |
| 1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
the activity of hypoxia-inducible transcription factor HIF, an alphabeta heterodimer that has an essential role in adaptation to low oxygen availability, is regulated by two oxygen-dependent hydroxylation events. Hydroxylation of specific proline residues by HIF prolyl 4-hydroxylases targets the HIF-alpha subunit for proteasomal destruction, whereas hydroxylation of an asparagine in the C-terminal transactivation domain prevents its interaction with the transcriptional coactivator p300 |
| 1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
FIH hydroxylates Asn803 of HIF-1alpha |
| 1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
FIH hydroxylates at the asparaginyl residue in the FIH transcriptional activation domain C-TAD |
| 1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
HIF-1alpha |
| 1.14.11.30 | hypoxia-inducible factor-L-asparagine + 2-oxoglutarate + O2 |
hydroxylation at Asn803 |
| 1.14.11.30 | TRPV3 channel ankyrin repeat domain + 2-oxoglutarate + O2 |
- |
