Prolyl 4-hydroxylase subunit alpha 2

mammalian protein found in Homo sapiens
Protein protein Q21119666
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Summary

Prolyl 4-hydroxylase subunit alpha 2 is a protein[1]. It is known by 9 alternative names across languages and contexts.[2]

Key Facts

  • Prolyl 4-hydroxylase subunit alpha 2's instance of is recorded as protein[3].
  • Prolyl 4-hydroxylase subunit alpha 2 is part of Tetratricopeptide-like helical domain superfamily[4].
  • Prolyl 4-hydroxylase subunit alpha 2 is part of Prolyl 4-hydroxylase alpha-subunit, N-terminal domain, protein family[5].
  • Prolyl 4-hydroxylase subunit alpha 2 is part of Tetratricopeptide repeat-containing domain, protein family[6].
  • Prolyl 4-hydroxylase subunit alpha 2 is part of Prolyl 4-hydroxylase, alpha subunit, protein family[7].
  • Prolyl 4-hydroxylase subunit alpha 2 is part of Oxoglutarate/iron-dependent dioxygenase family[8].
  • Prolyl 4-hydroxylase subunit alpha 2 is part of Tetratricopeptide repeat family[9].
  • Prolyl 4-hydroxylase subunit alpha 2 comprises tetratricopeptide repeat[10].
  • Prolyl 4-hydroxylase subunit alpha 2 comprises Prolyl 4-hydroxylase alpha-subunit, N-terminal[11].
  • Prolyl 4-hydroxylase subunit alpha 2 comprises Prolyl 4-hydroxylase, alpha subunit[12].
  • Prolyl 4-hydroxylase subunit alpha 2 comprises Tetratricopeptide repeat-containing domain[13].
  • Prolyl 4-hydroxylase subunit alpha 2 comprises Oxoglutarate/iron-dependent dioxygenase[14].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as iron ion binding[15].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as electron transfer activity[16].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as L-ascorbic acid binding[17].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as oxidoreductase activity[18].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as protein binding[19].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen[20].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as dioxygenase activity[21].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as procollagen-proline 4-dioxygenase activity[22].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen[23].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as metal ion binding[24].
  • Prolyl 4-hydroxylase subunit alpha 2's molecular function is recorded as procollagen-proline 4-dioxygenase activity[25].
  • Prolyl 4-hydroxylase subunit alpha 2's cell component is recorded as endoplasmic reticulum[26].
  • Prolyl 4-hydroxylase subunit alpha 2's cell component is recorded as intracellular membrane-bounded organelle[27].

Why It Matters

Prolyl 4-hydroxylase subunit alpha 2 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] ↑ . wikidata.org.
  4. [6] ↑ . wikidata.org.
  5. [7] ↑ . wikidata.org.
  6. [8] ↑ . wikidata.org.
  7. [9] ↑ . wikidata.org.
  8. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . A proteome-scale map of the human interactome network. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . GOA. 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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Use these citations when quoting this entity in research, articles, AI prompts, or wherever provenance matters. We aggregate Wikidata + Wikipedia + authoritative open-data sources; the stitched, scored, cross-referenced view is what 4ort.xyz contributes.

APA 4ort.xyz Knowledge Graph. (2026). Prolyl 4-hydroxylase subunit alpha 2. Retrieved May 3, 2026, from https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-alpha-2-q21119666
MLA “Prolyl 4-hydroxylase subunit alpha 2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-alpha-2-q21119666.
BibTeX @misc{4ortxyz_prolyl-4-hydroxylase-subunit-alpha-2-q21119666_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Prolyl 4-hydroxylase subunit alpha 2}}, year = {2026}, url = {https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-alpha-2-q21119666}, 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 → P4HA2
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → iron ion binding, electron transfer activity, L-ascorbic acid binding +8
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 1.14.11.2, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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