dopamine beta-hydroxylase

mammalian protein found in Homo sapiens
Protein protein Q415762

Facts

10 properties
Instance of
protein
Part of
PHM/PNGase F domain superfamily, Copper type II, ascorbate-dependent monooxygenase, N-terminal domain superfamily, Tyramine beta-hydroxylase/Dopamine beta-hydroxylase, Copper type II, ascorbate-dependent monooxygenase-like, C-terminal, Copper type II, ascorbate-dependent monooxygenase, N-terminal domain, protein family, DOMON domain, protein family, Copper type II ascorbate-dependent monooxygenase, C-terminal domain, protein family, Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site, protein family, Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site, protein family[2][3][4][5][6][7][8][9][10]
Biological process
response to amphetamine, chemical synaptic transmission, homoiothermy, leukocyte mediated immunity, visual learning, fear response, behavioral response to ethanol, locomotory behavior, regulation of extrinsic apoptotic signaling pathway, regulation of cell population proliferation, positive regulation of vasoconstriction, glucose homeostasis, maternal behavior, memory, leukocyte migration, response to pain, blood vessel remodeling, cytokine production, associative learning, catecholamine biosynthetic process, dopamine catabolic process, norepinephrine biosynthetic process, octopamine biosynthetic process, dopamine catabolic process, norepinephrine biosynthetic process, positive regulation of cold-induced thermogenesis[39][40][41][42][43][44][45][46][47][48][49][50][51][52]
Cell component
cytoplasm, transport vesicle membrane, integral component of membrane, chromaffin granule lumen, chromaffin granule membrane, cytoplasmic vesicle, membrane, extracellular region, extracellular space, secretory granule membrane, secretory granule lumen, intracellular membrane-bounded organelle, endoplasmic reticulum, microtubule organizing center, extracellular space, cytoplasm, secretory granule membrane[25][26][27][28][29][30][31][32][33][34][35][36][37][38]
EC enzyme number
1.14.17.1[16]
Encoded by
DBH[53]
Found in taxon
Homo sapiens
Has part(s)
Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-2 conserved site, Copper type II ascorbate-dependent monooxygenase, C-terminal, Copper type II, ascorbate-dependent monooxygenase, N-terminal, DOMON domain, Copper type II, ascorbate-dependent monooxygenase, histidine-cluster-1 conserved site[11][12][13][14][15]
Molecular function
metal ion binding, monooxygenase activity, oxidoreductase activity, 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, L-ascorbic acid binding, catalytic activity, dopamine beta-monooxygenase activity, copper ion binding, dopamine beta-monooxygenase activity, copper ion binding, 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, dopamine beta-monooxygenase activity[17][18][19][20][21][22][23][24]
Physically interacts with
nepicastat[1]
🏷️ Also known as
en Dopamine beta-hydroxylase en Dopamine beta-monooxygenase en dopamine beta-hydroxylase (dopamine beta-monooxygenase) en DBH en dopamine beta-hydroxylase ar بيتا-هيدروكسيلاز الدوبامين de Dopamin-β-Hydroxylase de Dopaminhydroxylase es Dopamina beta-hidroxilasa es Dopamina β-hidroxilasa fi Dopamiini-beeta-hydroksylaasi fr Dopamine bêta-hydroxylase id Dopamin beta-hidroksilase it Dopamina beta-monoossigenasi ja ドーパミン-β-モノオキシゲナーゼ ko 도파민 베타-하이드록실화효소 pt Dopamina beta-hidroxilase sv Dopamin-beta-hydroxylas sv Dopamin-β-hydroxylas tr DBH
🔖 Identifiers · 12
OpenAlex ID
C203531881
Image (Wikimedia Commons)
4zel.jpg ↗
Ensembl protein ID
ENSP00000376776, ENSP00000263611
Exact match
purl.uniprot.org
Freebase ID
/m/026zbk3
MeSH descriptor ID
D004299
Microsoft Academic ID (discontinued)
203531881
PDB structure ID
4ZEL
RefSeq protein ID
NP_000778
UMLS CUI
C0013032
UniProt protein ID
P09172

Report an error or request removal Lineage (PROV-JSON)

🔗 Connections
Cell component 6
Biological process 2
← Physically interacts with 2
Found in taxon 1
Instance of 1
Molecular function 1
Physically interacts with 1
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References

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

Direct Wikidata claims

  1. [1] ↑ . IUPHAR/BPS Guide to PHARMACOLOGY. Retrieved . wikidata.org.
  2. [2] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [3] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [4] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [5] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [6] ↑ . wikidata.org.
  7. [7] ↑ . wikidata.org.
  8. [8] ↑ . wikidata.org.
  9. [9] ↑ . wikidata.org.
  10. [10] ↑ . wikidata.org.
  11. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [12] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [13] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  14. [14] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  15. [15] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [16] ↑ . wikidata.org.
  17. [17] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [20] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [21] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [22] ↑ . 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.
  23. [23] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [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.
  26. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  27. [27] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  28. [28] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  29. [29] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  30. [30] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  31. [31] ↑ . 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.
  32. [32] ↑ . The human plasma proteome: a nonredundant list developed by combination of four separate sources. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  33. [33] ↑ . Functional and high level expression of human dopamine beta-hydroxylase in transgenic mice. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  34. [34] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  35. [35] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  36. [36] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  37. [37] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  38. [38] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  39. [39] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  40. [40] ↑ . Congenital dopamine-beta-hydroxylase deficiency. A novel orthostatic syndrome. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  41. [41] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  42. [42] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  43. [43] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  44. [44] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  45. [45] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  46. [46] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  47. [47] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  48. [48] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  49. [49] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  50. [50] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  51. [51] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  52. [52] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  53. [53] ↑ . UniProt. Retrieved . wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). dopamine beta-hydroxylase. Retrieved November 5, 2026, from https://4ort.xyz/entity/dopamine-beta-hydroxylase
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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: 2026-11-05}}
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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. 15w 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| */ Image: 4zel.jpg, [[:toollabs:quickstatements/#/batch/261337|batch #261337]]"
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