Prolyl 4-hydroxylase, beta polypeptide

mammalian protein found in Mus musculus
Protein protein Q21990867
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Prolyl 4-hydroxylase, beta polypeptide

Summary

Prolyl 4-hydroxylase, beta polypeptide is a protein[1].

Key Facts

  • Prolyl 4-hydroxylase, beta polypeptide's instance of is recorded as protein[2].
  • Prolyl 4-hydroxylase, beta polypeptide's UniProt protein ID is recorded as P09103[3].
  • Prolyl 4-hydroxylase, beta polypeptide's part of is recorded as Thioredoxin-like superfamily[4].
  • Prolyl 4-hydroxylase, beta polypeptide's part of is recorded as Protein disulphide isomerase[5].
  • Prolyl 4-hydroxylase, beta polypeptide's part of is recorded as membrane protein[6].
  • Prolyl 4-hydroxylase, beta polypeptide's part of is recorded as Disulphide isomerase subgroup domain, protein family[7].
  • Prolyl 4-hydroxylase, beta polypeptide's part of is recorded as Thioredoxin domain, protein family[8].
  • Prolyl 4-hydroxylase, beta polypeptide's part of is recorded as Thioredoxin, conserved site, protein family[9].
  • Prolyl 4-hydroxylase, beta polypeptide's has part is recorded as Disulphide isomerase subgroup domain[10].
  • Prolyl 4-hydroxylase, beta polypeptide's has part is recorded as Thioredoxin domain[11].
  • Prolyl 4-hydroxylase, beta polypeptide's has part is recorded as Thioredoxin, conserved site[12].
  • Prolyl 4-hydroxylase, beta polypeptide's RefSeq protein ID is recorded as NP_035162[13].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as isomerase activity[14].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as protein disulfide isomerase activity[15].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as integrin binding[16].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as protein binding[17].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as procollagen-proline 4-dioxygenase activity[18].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as protein heterodimerization activity[19].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as peptidyl-proline 4-dioxygenase activity[20].
  • Prolyl 4-hydroxylase, beta polypeptide's molecular function is recorded as enzyme binding[21].
  • Prolyl 4-hydroxylase, beta polypeptide's cell component is recorded as procollagen-proline 4-dioxygenase complex[22].
  • Prolyl 4-hydroxylase, beta polypeptide's cell component is recorded as endoplasmic reticulum lumen[23].
  • Prolyl 4-hydroxylase, beta polypeptide's cell component is recorded as membrane[24].
  • Prolyl 4-hydroxylase, beta polypeptide's cell component is recorded as melanosome[25].
  • Prolyl 4-hydroxylase, beta polypeptide's cell component is recorded as plasma membrane[26].

References

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

Direct Wikidata claims

  1. [2] ↑ . Q905695. Retrieved . wikidata.org.
  2. [3] ↑ . Q905695. Retrieved . wikidata.org.
  3. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Q20641742. Retrieved . wikidata.org.
  13. [14] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . 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.
  17. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. 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, beta polypeptide. Retrieved May 3, 2026, from https://4ort.xyz/entity/prolyl-4-hydroxylase-beta-polypeptide
MLA “Prolyl 4-hydroxylase, beta polypeptide.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/prolyl-4-hydroxylase-beta-polypeptide.
BibTeX @misc{4ortxyz_prolyl-4-hydroxylase-beta-polypeptide_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Prolyl 4-hydroxylase, beta polypeptide}}, year = {2026}, url = {https://4ort.xyz/entity/prolyl-4-hydroxylase-beta-polypeptide}, 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, beta polypeptide — https://4ort.xyz/entity/prolyl-4-hydroxylase-beta-polypeptide (retrieved 2026-05-03)

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