Prolyl 4-hydroxylase subunit beta

mammalian protein found in Homo sapiens
Protein protein Q22676720
Press Enter · cited answer in seconds

Prolyl 4-hydroxylase subunit beta

Summary

Prolyl 4-hydroxylase subunit beta is a protein[1]. It is known by 15 alternative names across languages and contexts.[2]

Key Facts

  • Prolyl 4-hydroxylase subunit beta's instance of is recorded as protein[3].
  • Prolyl 4-hydroxylase subunit beta is part of Thioredoxin-like superfamily[4].
  • Prolyl 4-hydroxylase subunit beta is part of Protein disulphide isomerase[5].
  • Prolyl 4-hydroxylase subunit beta is part of membrane protein[6].
  • Prolyl 4-hydroxylase subunit beta is part of Disulphide isomerase subgroup domain, protein family[7].
  • Prolyl 4-hydroxylase subunit beta is part of Thioredoxin domain, protein family[8].
  • Prolyl 4-hydroxylase subunit beta is part of Thioredoxin, conserved site, protein family[9].
  • Prolyl 4-hydroxylase subunit beta comprises Thioredoxin domain[10].
  • Prolyl 4-hydroxylase subunit beta comprises Disulphide isomerase subgroup domain[11].
  • Prolyl 4-hydroxylase subunit beta comprises Thioredoxin, conserved site[12].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as isomerase activity[13].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as integrin binding[14].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as protein binding[15].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as procollagen-proline 4-dioxygenase activity[16].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as protein heterodimerization activity[17].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as enzyme binding[18].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as RNA binding[19].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as protein disulfide isomerase activity[20].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as RNA binding[21].
  • Prolyl 4-hydroxylase subunit beta's molecular function is recorded as protein disulfide isomerase activity[22].
  • Prolyl 4-hydroxylase subunit beta's cell component is recorded as procollagen-proline 4-dioxygenase complex[23].
  • Prolyl 4-hydroxylase subunit beta's cell component is recorded as endoplasmic reticulum lumen[24].
  • Prolyl 4-hydroxylase subunit beta's cell component is recorded as membrane[25].
  • Prolyl 4-hydroxylase subunit beta's cell component is recorded as focal adhesion[26].
  • Prolyl 4-hydroxylase subunit beta's cell component is recorded as melanosome[27].

Why It Matters

Prolyl 4-hydroxylase subunit beta is known by 15 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] . Q905695. 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] . 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] . Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] . Loss of both phospholipid and triglyceride transfer activities of microsomal triglyceride transfer protein in abetalipoproteinemia. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] . Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. 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] . The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] . Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] . The mRNA-Bound Proteome and Its Global Occupancy Profile on Protein-Coding Transcripts. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] . Characterization of the human gene for a polypeptide that acts both as the beta subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] . Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] . Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. 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.

📑 Cite this page

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 beta. Retrieved May 3, 2026, from https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-beta
MLA “Prolyl 4-hydroxylase subunit beta.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-beta.
BibTeX @misc{4ortxyz_prolyl-4-hydroxylase-subunit-beta_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Prolyl 4-hydroxylase subunit beta}}, year = {2026}, url = {https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-beta}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Prolyl 4-hydroxylase subunit beta — https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-beta (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/prolyl-4-hydroxylase-subunit-beta · Last refreshed:

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. 8w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from
    Encoded by P4HB
    Wikidata description mammalian protein found in Homo sapiens
    Molecular function isomerase activity, integrin binding, protein binding +7
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 5.3.4.1, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
Live feed via Wikidata EventStreams. New edits appear within minutes of being made on Wikidata.