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Dual oxidase 1

mammalian protein found in Homo sapiens
Protein protein Q5310226
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Dual oxidase 1

Summary

Dual oxidase 1 is a protein[1].

Key Facts

  • Dual oxidase 1's instance of is recorded as protein[2].
  • Dual oxidase 1's UniProt protein ID is recorded as Q9NRD9[3].
  • Dual oxidase 1's part of is recorded as transmembrane 1-electron transfer carrier[4].
  • Dual oxidase 1's RefSeq protein ID is recorded as NP_059130[5].
  • Dual oxidase 1's RefSeq protein ID is recorded as NP_787954[6].
  • Dual oxidase 1's RefSeq protein ID is recorded as XP_011519983[7].
  • Dual oxidase 1's RefSeq protein ID is recorded as XP_011519984[8].
  • Dual oxidase 1's molecular function is recorded as calcium ion binding[9].
  • Dual oxidase 1's molecular function is recorded as peroxidase activity[10].
  • Dual oxidase 1's molecular function is recorded as metal ion binding[11].
  • Dual oxidase 1's molecular function is recorded as heme binding[12].
  • Dual oxidase 1's molecular function is recorded as NADP binding[13].
  • Dual oxidase 1's molecular function is recorded as oxidoreductase activity[14].
  • Dual oxidase 1's molecular function is recorded as NAD(P)H oxidase H2O2-forming activity[15].
  • Dual oxidase 1's molecular function is recorded as protein binding[16].
  • Dual oxidase 1's molecular function is recorded as NAD(P)H oxidase H2O2-forming activity[17].
  • Dual oxidase 1's molecular function is recorded as superoxide-generating NAD(P)H oxidase activity[18].
  • Dual oxidase 1's cell component is recorded as integral component of membrane[19].
  • Dual oxidase 1's cell component is recorded as membrane[20].
  • Dual oxidase 1's cell component is recorded as plasma membrane[21].
  • Dual oxidase 1's cell component is recorded as apical plasma membrane[22].
  • Dual oxidase 1's cell component is recorded as endoplasmic reticulum[23].
  • Dual oxidase 1's cell component is recorded as plasma membrane[24].
  • Dual oxidase 1's cell component is recorded as cell surface[25].
  • Dual oxidase 1's cell component is recorded as cell leading edge[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] ↑ . Retrieved . wikidata.org.
  4. [5] ↑ . Q20641742. Retrieved . wikidata.org.
  5. [6] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . Q20641742. Retrieved . wikidata.org.
  7. [8] ↑ . Q20641742. Retrieved . wikidata.org.
  8. [9] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] ↑ . GOA. 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] ↑ . Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. 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] ↑ . Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. 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] ↑ . Cloning of two human thyroid cDNAs encoding new members of the NADPH oxidase family. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . The type of DUOX-dependent ROS production is dictated by defined sequences in DUOXA.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Heterodimerization controls localization of Duox-DuoxA NADPH oxidases in airway cells. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

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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). Dual oxidase 1. Retrieved May 3, 2026, from https://4ort.xyz/entity/dual-oxidase-1
MLA “Dual oxidase 1.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/dual-oxidase-1.
BibTeX @misc{4ortxyz_dual-oxidase-1_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Dual oxidase 1}}, year = {2026}, url = {https://4ort.xyz/entity/dual-oxidase-1}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Dual oxidase 1 — https://4ort.xyz/entity/dual-oxidase-1 (retrieved 2026-05-03)

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