# Hypoxia inducible factor 1 subunit alpha inhibitor

> mammalian protein found in Homo sapiens

**Wikidata**: [Q21111638](https://www.wikidata.org/wiki/Q21111638)  
**Source**: https://4ort.xyz/entity/hypoxia-inducible-factor-1-subunit-alpha-inhibitor


## References

1. UniProt
2. [InterPro Release 71.0](http://www.ebi.ac.uk/interpro/protein/Q9NWT6)
3. Q20641742
4. [Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) Reveals Mechanism of Oxidative Modification of HIF-1α](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
5. [MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
6. [Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
7. [Substrate Requirements of the Oxygen-sensing Asparaginyl Hydroxylase Factor-inhibiting Hypoxia-inducible Factor](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
8. [Factor‐inhibiting hypoxia‐inducible factor (FIH) catalyses the post‐translational hydroxylation of histidinyl residues within ankyrin repeat domains](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
9. [Asparagine and Aspartate Hydroxylation of the Cytoskeletal Ankyrin Family Is Catalyzed by Factor-inhibiting Hypoxia-inducible Factor](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
10. [Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
11. [ASB4 Is a Hydroxylation Substrate of FIH and Promotes Vascular Differentiation via an Oxygen-Dependent Mechanism](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
12. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
13. [Posttranslational hydroxylation of ankyrin repeats in IκB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH)](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
14. [Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
15. [Asparaginyl Hydroxylation of the Notch Ankyrin Repeat Domain by Factor Inhibiting Hypoxia-inducible Factor](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
16. [Mint3 Enhances the Activity of Hypoxia-inducible Factor-1 (HIF-1) in Macrophages by Suppressing the Activity of Factor Inhibiting HIF-1](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
17. [FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
18. [NECAB3 Promotes Activation of Hypoxia-inducible factor-1 during Normoxia and Enhances Tumourigenicity of Cancer Cells](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
19. [FIH Regulates Cellular Metabolism through Hydroxylation of the Deubiquitinase OTUB1](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
20. [The LINK-A lncRNA activates normoxic HIF1α signalling in triple-negative breast cancer](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
21. [Substrate-Trapped Interactors of PHD3 and FIH Cluster in Distinct Signaling Pathways](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
22. [Factor‐inhibiting hypoxia‐inducible factor (FIH) catalyses the post‐translational hydroxylation of histidinyl residues within ankyrin repeat domains](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
23. [Towards a proteome-scale map of the human protein–protein interaction network](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
24. [Network Analysis of UBE3A/E6AP-Associated Proteins Provides Connections to Several Distinct Cellular Processes](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
25. [Proteomic analyses reveal distinct chromatin‐associated and soluble transcription factor complexes](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
26. [An empirical framework for binary interactome mapping](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
27. [Transcriptional activation of hypoxia‐inducible factor‐1α by HDAC4 and HDAC5 involves differential recruitment of p300 and FIH‐1](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
28. [Structural and Mechanistic Studies on the Inhibition of the Hypoxia-inducible Transcription Factor Hydroxylases by Tricarboxylic Acid Cycle Intermediates](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
29. [FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
30. [Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
31. [Catalytic Properties of the Asparaginyl Hydroxylase (FIH) in the Oxygen Sensing Pathway Are Distinct from Those of Its Prolyl 4-Hydroxylases](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
32. [Hypoxia-inducible Factor (HIF) Asparagine Hydroxylase Is Identical to Factor Inhibiting HIF (FIH) and Is Related to the Cupin Structural Family](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
33. [FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
34. [Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
35. [MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH)](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
36. [Hypoxia-inducible factor asparaginyl hydroxylase (FIH-1) catalyses hydroxylation at the β-carbon of asparagine-803](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
37. [Substrate Requirements of the Oxygen-sensing Asparaginyl Hydroxylase Factor-inhibiting Hypoxia-inducible Factor](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
38. [ASB4 Is a Hydroxylation Substrate of FIH and Promotes Vascular Differentiation via an Oxygen-Dependent Mechanism](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
39. [Asparagine and Aspartate Hydroxylation of the Cytoskeletal Ankyrin Family Is Catalyzed by Factor-inhibiting Hypoxia-inducible Factor](http://www.ebi.ac.uk/QuickGO/annotations?geneProductId=UniProtKB:Q9NWT6)
40. [GOA](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
41. [Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
42. [FIH-1: a novel protein that interacts with HIF-1α and VHL to mediate repression of HIF-1 transcriptional activity](http://www.ebi.ac.uk/QuickGO/annotations?protein=Q9NWT6&geneProductId=UniProtKB:Q9NWT6)
43. Ensembl Release 99