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dopamine beta-hydroxylase

mammalian protein found in Homo sapiens
Protein protein Q415762
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dopamine beta-hydroxylase

Summary

dopamine beta-hydroxylase is a protein[1]. It has Wikipedia articles in 15 language editions, a strong signal of global cultural recognition.[2]

Key Facts

  • dopamine beta-hydroxylase's instance of is recorded as protein[3].
  • dopamine beta-hydroxylase's physically interacts with is recorded as nepicastat[4].
  • dopamine beta-hydroxylase is part of PHM/PNGase F domain superfamily[5].
  • dopamine beta-hydroxylase is part of Copper type II, ascorbate-dependent monooxygenase, N-terminal domain superfamily[6].
  • dopamine beta-hydroxylase is part of Tyramine beta-hydroxylase/Dopamine beta-hydroxylase[7].
  • dopamine beta-hydroxylase is part of Copper type II, ascorbate-dependent monooxygenase-like, C-terminal[8].
  • dopamine beta-hydroxylase is part of Copper type II, ascorbate-dependent monooxygenase, N-terminal domain, protein family[9].
  • dopamine beta-hydroxylase is part of DOMON domain, protein family[10].
  • dopamine beta-hydroxylase is part of Copper type II ascorbate-dependent monooxygenase, C-terminal domain, protein family[11].
  • dopamine beta-hydroxylase is part of Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site, protein family[12].
  • dopamine beta-hydroxylase is part of Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site, protein family[13].
  • dopamine beta-hydroxylase comprises Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site[14].
  • dopamine beta-hydroxylase comprises Copper type II ascorbate-dependent monooxygenase, C-terminal[15].
  • dopamine beta-hydroxylase comprises Copper type II, ascorbate-dependent monooxygenase, N-terminal[16].
  • dopamine beta-hydroxylase comprises DOMON domain[17].
  • dopamine beta-hydroxylase comprises Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site[18].
  • dopamine beta-hydroxylase's EC enzyme number is recorded as 1.14.17.1[19].
  • dopamine beta-hydroxylase's molecular function is recorded as metal ion binding[20].
  • dopamine beta-hydroxylase's molecular function is recorded as monooxygenase activity[21].
  • dopamine beta-hydroxylase's molecular function is recorded as oxidoreductase activity[22].
  • dopamine beta-hydroxylase's molecular function is recorded as oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced ascorbate as one donor, and incorporation of one atom of oxygen[23].
  • dopamine beta-hydroxylase's molecular function is recorded as L-ascorbic acid binding[24].
  • dopamine beta-hydroxylase's molecular function is recorded as catalytic activity[25].
  • dopamine beta-hydroxylase's molecular function is recorded as dopamine beta-monooxygenase activity[26].
  • dopamine beta-hydroxylase's molecular function is recorded as copper ion binding[27].

Why It Matters

dopamine beta-hydroxylase has Wikipedia articles in 15 language editions, a strong signal of global cultural recognition.[2] It is known by 15 alternative names across languages and contexts.[28]

References

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

Direct Wikidata claims

  1. [3] ↑ . Q905695. Retrieved . wikidata.org.
  2. [4] ↑ . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  3. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: 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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . wikidata.org.
  8. [10] ↑ . wikidata.org.
  9. [11] ↑ . wikidata.org.
  10. [12] ↑ . wikidata.org.
  11. [13] ↑ . wikidata.org.
  12. [14] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . 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] ↑ . The primary structure of human dopamine-beta-hydroxylase: insights into the relationship between the soluble and the membrane-bound forms of the enzyme. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata sitelinks. wikidata.org.
  2. [28] ↑ . Wikidata aliases. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). dopamine beta-hydroxylase. Retrieved May 3, 2026, from https://4ort.xyz/entity/dopamine-beta-hydroxylase
MLA “dopamine beta-hydroxylase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/dopamine-beta-hydroxylase.
BibTeX @misc{4ortxyz_dopamine-beta-hydroxylase_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{dopamine beta-hydroxylase}}, year = {2026}, url = {https://4ort.xyz/entity/dopamine-beta-hydroxylase}, note = {Accessed: 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. 9d ago · Dirac · 2026-07-20 view diff on Wikidata ↗
    Molecular function → metal ion binding, monooxygenase activity, oxidoreductase activity +9
    Physically interacts with → nepicastat
    Part of → —
    Cell component → cytoplasm, transport vesicle membrane, integral component of membrane +14
    + 10 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P18]]: 4zel.jpg, [[:toollabs:quickstatements/#/batch/261337|batch #261337]]"
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