Lysyl oxidase

mammalian protein found in Rattus norvegicus
Protein protein Q28561705
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Lysyl oxidase

Summary

Lysyl oxidase is a protein[1].

Key Facts

  • Lysyl oxidase's instance of is recorded as protein[2].
  • Lysyl oxidase's subclass of is recorded as protein[3].
  • Lysyl oxidase's UniProt protein ID is recorded as P16636[4].
  • Lysyl oxidase's part of is recorded as Lysyl oxidase[5].
  • Lysyl oxidase's part of is recorded as Lysyl oxidase, conserved site, protein family[6].
  • Lysyl oxidase's has part is recorded as Lysyl oxidase, conserved site[7].
  • Lysyl oxidase's RefSeq protein ID is recorded as NP_058757[8].
  • Lysyl oxidase's RefSeq protein ID is recorded as XP_006254775[9].
  • Lysyl oxidase's RefSeq protein ID is recorded as XP_006254777[10].
  • Lysyl oxidase's molecular function is recorded as protein-lysine 6-oxidase activity[11].
  • Lysyl oxidase's molecular function is recorded as copper ion binding[12].
  • Lysyl oxidase's molecular function is recorded as oxidoreductase activity[13].
  • Lysyl oxidase's molecular function is recorded as oxidoreductase activity, acting on the CH-NH2 group of donors, oxygen as acceptor[14].
  • Lysyl oxidase's molecular function is recorded as metal ion binding[15].
  • Lysyl oxidase's cell component is recorded as extracellular region[16].
  • Lysyl oxidase's cell component is recorded as collagen[17].
  • Lysyl oxidase's cell component is recorded as extracellular space[18].
  • Lysyl oxidase's cell component is recorded as nucleus[19].
  • Lysyl oxidase's cell component is recorded as extracellular matrix[20].
  • Lysyl oxidase's biological process is recorded as blood vessel development[21].
  • Lysyl oxidase's biological process is recorded as development of the heart[22].
  • Lysyl oxidase's biological process is recorded as response to hormone[23].
  • Lysyl oxidase's biological process is recorded as peptidyl-lysine oxidation[24].
  • Lysyl oxidase's biological process is recorded as collagen fibril organization[25].
  • Lysyl oxidase's biological process is recorded as lung development[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] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . wikidata.org.
  6. [7] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . Q20641742. Retrieved . wikidata.org.
  8. [9] . Q20641742. Retrieved . wikidata.org.
  9. [10] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Inhibition of the expression of lysyl oxidase and its substrates in cadmium-resistant rat fetal lung fibroblasts. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . Inhibition of the expression of lysyl oxidase and its substrates in cadmium-resistant rat fetal lung fibroblasts. 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Fully processed lysyl oxidase catalyst translocates from the extracellular space into nuclei of aortic smooth-muscle cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. 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] . Lysyl oxidase gene expression and enzyme activity in the rat ovary: regulation by follicle-stimulating hormone, androgen, and transforming growth factor-beta superfamily members in vitro. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Inhibition of the expression of lysyl oxidase and its substrates in cadmium-resistant rat fetal lung fibroblasts. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. 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). Lysyl oxidase. Retrieved May 3, 2026, from https://4ort.xyz/entity/lysyl-oxidase-q28561705
MLA “Lysyl oxidase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/lysyl-oxidase-q28561705.
BibTeX @misc{4ortxyz_lysyl-oxidase-q28561705_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Lysyl oxidase}}, year = {2026}, url = {https://4ort.xyz/entity/lysyl-oxidase-q28561705}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Lysyl oxidase — https://4ort.xyz/entity/lysyl-oxidase-q28561705 (retrieved 2026-05-03)

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