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Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2

mammalian protein found in Homo sapiens
Protein protein Q21123268
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Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2

Summary

Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 is a protein[1].

Key Facts

  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's instance of is recorded as protein[2].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 is part of nucleotide-diphospho-sugar transferases[3].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 is part of Prolyl 4-hydroxylase, alpha subunit, protein family[4].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 is part of Oxoglutarate/iron-dependent dioxygenase family[5].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 is part of Procollagen-lysine 5-dioxygenase, conserved site, protein family[6].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 comprises Oxoglutarate/iron-dependent dioxygenase[7].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 comprises Prolyl 4-hydroxylase, alpha subunit[8].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 comprises Procollagen-lysine 5-dioxygenase, conserved site[9].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as iron ion binding[10].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as L-ascorbic acid binding[11].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as oxidoreductase activity[12].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as dioxygenase activity[13].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen[14].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as metal ion binding[15].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as procollagen-lysine 5-dioxygenase activity[16].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as procollagen glucosyltransferase activity[17].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's molecular function is recorded as procollagen-lysine 5-dioxygenase activity[18].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's cell component is recorded as rough endoplasmic reticulum membrane[19].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's cell component is recorded as extracellular exosome[20].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's cell component is recorded as endoplasmic reticulum membrane[21].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's cell component is recorded as endoplasmic reticulum[22].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's cell component is recorded as membrane[23].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's cell component is recorded as extracellular exosome[24].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's biological process is recorded as response to hypoxia[25].
  • Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2's biological process is recorded as protein O-linked glycosylation[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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [4] ↑ . wikidata.org.
  4. [5] ↑ . wikidata.org.
  5. [6] ↑ . wikidata.org.
  6. [7] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: 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] ↑ . Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Cloning and characterization of a novel human lysyl hydroxylase isoform highly expressed in pancreas and muscle. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Modulation of gene expression by hypoxia in human umbilical cord vein endothelial cells: A transcriptomic and proteomic study. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Lysyl hydroxylase 3 is a multifunctional protein possessing collagen glucosyltransferase activity.. 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). Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2. Retrieved May 3, 2026, from https://4ort.xyz/entity/procollagen-lysine-2-oxoglutarate-5-dioxygenase-2-q21123268
MLA “Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/procollagen-lysine-2-oxoglutarate-5-dioxygenase-2-q21123268.
BibTeX @misc{4ortxyz_procollagen-lysine-2-oxoglutarate-5-dioxygenase-2-q21123268_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2}}, year = {2026}, url = {https://4ort.xyz/entity/procollagen-lysine-2-oxoglutarate-5-dioxygenase-2-q21123268}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Procollagen-lysine,2-oxoglutarate 5-dioxygenase 2 — https://4ort.xyz/entity/procollagen-lysine-2-oxoglutarate-5-dioxygenase-2-q21123268 (retrieved 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. 8d ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → PLOD2
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → iron ion binding, L-ascorbic acid binding, oxidoreductase activity +6
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 1.14.11.4, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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