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Hypoxia inducible factor 1 subunit alpha inhibitor

mammalian protein found in Homo sapiens
Protein protein Q21111638
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Summary

Hypoxia inducible factor 1 subunit alpha inhibitor is a protein[1]. It is known by 9 alternative names across languages and contexts.[2]

Key Facts

  • Hypoxia inducible factor 1 subunit alpha inhibitor's instance of is recorded as protein[3].
  • Hypoxia inducible factor 1 subunit alpha inhibitor is part of Hypoxia-inducible factor 1-alpha inhibitor[4].
  • Hypoxia inducible factor 1 subunit alpha inhibitor is part of Hypoxia-inducible factor 1-alpha inhibitor, domain II[5].
  • Hypoxia inducible factor 1 subunit alpha inhibitor is part of JmjC domain, protein family[6].
  • Hypoxia inducible factor 1 subunit alpha inhibitor comprises JmjC domain[7].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as iron ion binding[8].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as peptidyl-asparagine 3-dioxygenase activity[9].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as protein homodimerization activity[10].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as ankyrin repeat binding[11].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as zinc ion binding[12].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as dioxygenase activity[13].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as metal ion binding[14].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as NF-kappaB binding[15].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as Notch binding[16].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as protein binding[17].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as carboxylic acid binding[18].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as oxidoreductase activity[19].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as peptidyl-histidine dioxygenase activity[20].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as oxygen gasoreceptor activity[21].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as 2-oxoglutarate-dependent dioxygenase activity[22].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as hypoxia-inducible factor-asparagine oxygenase activity[23].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as 2-oxoglutarate-dependent dioxygenase activity[24].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as peptidyl-histidine dioxygenase activity[25].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as peptidyl-asparagine 3-dioxygenase activity[26].
  • Hypoxia inducible factor 1 subunit alpha inhibitor's molecular function is recorded as ankyrin repeat binding[27].

Why It Matters

Hypoxia inducible factor 1 subunit alpha inhibitor is known by 9 alternative names across languages and contexts.[2]

References

Programmatic citations — every numbered marker resolves to a verifiable graph row below.

Direct Wikidata claims

  1. [3] ↑ . UniProt. Retrieved . wikidata.org.
  2. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . wikidata.org.
  5. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [8] ↑ . Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . Structure of factor-inhibiting hypoxia-inducible factor (HIF) reveals mechanism of oxidative modification of HIF-1 alpha. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . Posttranslational hydroxylation of ankyrin repeats in IkappaB proteins by the hypoxia-inducible factor (HIF) asparaginyl hydroxylase, factor inhibiting HIF (FIH). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . Interaction with factor inhibiting HIF-1 defines an additional mode of cross-coupling between the Notch and hypoxia signaling pathways. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . Mint3 enhances the activity of hypoxia-inducible factor-1 (HIF-1) in macrophages by suppressing the activity of factor inhibiting HIF-1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . MYPT1, the targeting subunit of smooth-muscle myosin phosphatase, is a substrate for the asparaginyl hydroxylase factor inhibiting hypoxia-inducible factor (FIH). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . ASB4 is a hydroxylation substrate of FIH and promotes vascular differentiation via an oxygen-dependent mechanism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). Hypoxia inducible factor 1 subunit alpha inhibitor. Retrieved May 3, 2026, from https://4ort.xyz/entity/hypoxia-inducible-factor-1-subunit-alpha-inhibitor
MLA “Hypoxia inducible factor 1 subunit alpha inhibitor.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/hypoxia-inducible-factor-1-subunit-alpha-inhibitor.
BibTeX @misc{4ortxyz_hypoxia-inducible-factor-1-subunit-alpha-inhibitor_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Hypoxia inducible factor 1 subunit alpha inhibitor}}, year = {2026}, url = {https://4ort.xyz/entity/hypoxia-inducible-factor-1-subunit-alpha-inhibitor}, note = {Accessed: 2026-05-03}}
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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 12w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → HIF1AN
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → iron ion binding, peptidyl-asparagine 3-dioxygenase activity, protein homodimerization activity +17
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 1.14.11.30, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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