cytochrome P450 family 3 subfamily A member 5

mammalian protein found in Homo sapiens
Protein protein Q21117300
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cytochrome P450 family 3 subfamily A member 5

Summary

cytochrome P450 family 3 subfamily A member 5 is a protein[1].

Key Facts

  • cytochrome P450 family 3 subfamily A member 5's instance of is recorded as protein[2].
  • cytochrome P450 family 3 subfamily A member 5's physically interacts with is recorded as ritonavir[3].
  • cytochrome P450 family 3 subfamily A member 5 is part of cytochrome P450 superfamily[4].
  • cytochrome P450 family 3 subfamily A member 5 is part of cytochrome P450, E-class, CYP3A[5].
  • cytochrome P450 family 3 subfamily A member 5 is part of cytochrome P450, conserved site, protein family[6].
  • cytochrome P450 family 3 subfamily A member 5 comprises cytochrome P450, conserved site[7].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as iron ion binding[8].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as oxidoreductase activity[9].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as oxygen binding[10].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as aromatase activity[11].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen[12].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as heme binding[13].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen[14].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as metal ion binding[15].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as monooxygenase activity[16].
  • cytochrome P450 family 3 subfamily A member 5's molecular function is recorded as estrogen 16-alpha-hydroxylase activity[17].
  • cytochrome P450 family 3 subfamily A member 5's cell component is recorded as organelle membrane[18].
  • cytochrome P450 family 3 subfamily A member 5's cell component is recorded as endoplasmic reticulum membrane[19].
  • cytochrome P450 family 3 subfamily A member 5's cell component is recorded as intracellular membrane-bounded organelle[20].
  • cytochrome P450 family 3 subfamily A member 5's cell component is recorded as endoplasmic reticulum[21].
  • cytochrome P450 family 3 subfamily A member 5's cell component is recorded as membrane[22].
  • cytochrome P450 family 3 subfamily A member 5's biological process is recorded as xenobiotic metabolic process[23].
  • cytochrome P450 family 3 subfamily A member 5's biological process is recorded as alkaloid catabolic process[24].
  • cytochrome P450 family 3 subfamily A member 5's biological process is recorded as oxidative demethylation[25].
  • cytochrome P450 family 3 subfamily A member 5's biological process is recorded as lipid hydroxylation[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] . IUPHAR/BPS Guide to PHARMACOLOGY. 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of [...]. 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] . Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of [...]. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Human cytochrome P450 3A7 has a distinct high catalytic activity for the 16alpha-hydroxylation of estrone but not 17beta-estradiol. 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] . Cytochrome P-450 hPCN3, a novel cytochrome P-450 IIIA gene product that is differentially expressed in adult human liver. cDNA and deduced amino acid sequence and distinct specificities of cDNA-expressed hPCN1 and hPCN3 for the metabolism of [...]. 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] . Quantitative contribution of CYP2D6 and CYP3A to oxycodone metabolism in human liver and intestinal microsomes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Quantitative contribution of CYP2D6 and CYP3A to oxycodone metabolism in human liver and intestinal microsomes. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Human cytochrome P450 3A7 has a distinct high catalytic activity for the 16alpha-hydroxylation of estrone but not 17beta-estradiol. 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). cytochrome P450 family 3 subfamily A member 5. Retrieved May 3, 2026, from https://4ort.xyz/entity/cytochrome-p450-family-3-subfamily-a-member-5
MLA “cytochrome P450 family 3 subfamily A member 5.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/cytochrome-p450-family-3-subfamily-a-member-5.
BibTeX @misc{4ortxyz_cytochrome-p450-family-3-subfamily-a-member-5_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{cytochrome P450 family 3 subfamily A member 5}}, year = {2026}, url = {https://4ort.xyz/entity/cytochrome-p450-family-3-subfamily-a-member-5}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): cytochrome P450 family 3 subfamily A member 5 — https://4ort.xyz/entity/cytochrome-p450-family-3-subfamily-a-member-5 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/cytochrome-p450-family-3-subfamily-a-member-5 · 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. 18d ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from
    Encoded by CYP3A5
    Wikidata description mammalian protein found in Homo sapiens
    Molecular function iron ion binding, oxidoreductase activity, oxygen binding +7
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 1.14.14.1, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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