cytochrome P450 family 2 subfamily D member 6

mammalian protein found in Homo sapiens
Protein protein Q3271142
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cytochrome P450 family 2 subfamily D member 6

Summary

cytochrome P450 family 2 subfamily D member 6 is a protein[1]. It ranks in the top 0.61% of protein entities by monthly Wikipedia readership (1,714 views/month, #6 of 987).[2]

Key Facts

  • cytochrome P450 family 2 subfamily D member 6's instance of is recorded as protein[3].
  • cytochrome P450 family 2 subfamily D member 6's physically interacts with is recorded as liver kidney microsomal type 1 antibody[4].
  • cytochrome P450 family 2 subfamily D member 6's physically interacts with is recorded as raubasine[5].
  • cytochrome P450 family 2 subfamily D member 6 is part of cytochrome P450 superfamily[6].
  • cytochrome P450 family 2 subfamily D member 6 is part of cytochrome P450, E-class, group I, CYP2D-like[7].
  • cytochrome P450 family 2 subfamily D member 6 is part of cytochrome P450, conserved site, protein family[8].
  • cytochrome P450 family 2 subfamily D member 6 comprises cytochrome P450, conserved site[9].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as iron ion binding[10].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as metal ion binding[11].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as heme binding[12].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen[13].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as oxidoreductase activity[14].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as aromatase activity[15].
  • cytochrome P450 family 2 subfamily D member 6'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[16].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as steroid hydroxylase activity[17].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as monooxygenase activity[18].
  • cytochrome P450 family 2 subfamily D member 6'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[19].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as heme binding[20].
  • cytochrome P450 family 2 subfamily D member 6's molecular function is recorded as monooxygenase activity[21].
  • cytochrome P450 family 2 subfamily D member 6'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[22].
  • cytochrome P450 family 2 subfamily D member 6's cell component is recorded as organelle membrane[23].
  • cytochrome P450 family 2 subfamily D member 6's cell component is recorded as endoplasmic reticulum membrane[24].
  • cytochrome P450 family 2 subfamily D member 6's cell component is recorded as membrane[25].
  • cytochrome P450 family 2 subfamily D member 6's cell component is recorded as intracellular membrane-bounded organelle[26].
  • cytochrome P450 family 2 subfamily D member 6's cell component is recorded as endoplasmic reticulum[27].

Why It Matters

cytochrome P450 family 2 subfamily D member 6 ranks in the top 0.61% of protein entities by monthly Wikipedia readership (1,714 views/month, #6 of 987).[2] It has Wikipedia articles in 13 language editions, a strong signal of global cultural recognition.[28] It is known by 20 alternative names across languages and contexts.[29]

References

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

Direct Wikidata claims

  1. [3] . Q905695. Retrieved . wikidata.org.
  2. [4] . wikidata.org.
  3. [5] . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  4. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [7] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [8] . wikidata.org.
  7. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [10] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] . GOA. 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] . Human liver mitochondrial cytochrome P450 2D6--individual variations and implications in drug metabolism. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] . Wikimedia Foundation. dumps.wikimedia.org.
  2. [28] . Wikidata sitelinks. wikidata.org.
  3. [29] . 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). cytochrome P450 family 2 subfamily D member 6. Retrieved May 3, 2026, from https://4ort.xyz/entity/cytochrome-p450-family-2-subfamily-d-member-6
MLA “cytochrome P450 family 2 subfamily D member 6.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/cytochrome-p450-family-2-subfamily-d-member-6.
BibTeX @misc{4ortxyz_cytochrome-p450-family-2-subfamily-d-member-6_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{cytochrome P450 family 2 subfamily D member 6}}, year = {2026}, url = {https://4ort.xyz/entity/cytochrome-p450-family-2-subfamily-d-member-6}, 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 2 subfamily D member 6 — https://4ort.xyz/entity/cytochrome-p450-family-2-subfamily-d-member-6 (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/cytochrome-p450-family-2-subfamily-d-member-6 · 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. 20d ago · Dirac · 2026-07-20 view diff on Wikidata ↗
    Molecular function iron ion binding, metal ion binding, heme binding +10
    Physically interacts with liver kidney microsomal type 1 antibody, raubasine
    Part of
    Cell component organelle membrane, endoplasmic reticulum membrane, membrane +5
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P18]]: CYP2D6 structure.png, [[:toollabs:quickstatements/#/batch/261337|batch #261337]]"
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