Hemoglobin subunit beta

mammalian protein found in Rattus norvegicus
Protein protein Q28556477
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Hemoglobin subunit beta

Summary

Hemoglobin subunit beta is a protein[1].

Key Facts

  • Hemoglobin subunit beta's instance of is recorded as protein[2].
  • Hemoglobin subunit beta's subclass of is recorded as protein[3].
  • Hemoglobin subunit beta's UniProt protein ID is recorded as P02091[4].
  • Hemoglobin subunit beta's part of is recorded as globin-like superfamily[5].
  • Hemoglobin subunit beta's part of is recorded as Haemoglobin, beta-type[6].
  • Hemoglobin subunit beta's part of is recorded as globin/protoglobin[7].
  • Hemoglobin subunit beta's part of is recorded as globin[8].
  • Hemoglobin subunit beta's has part is recorded as Globin domain[9].
  • Hemoglobin subunit beta's RefSeq protein ID is recorded as NP_150237[10].
  • Hemoglobin subunit beta's molecular function is recorded as peroxidase activity[11].
  • Hemoglobin subunit beta's molecular function is recorded as oxygen carrier activity[12].
  • Hemoglobin subunit beta's molecular function is recorded as protein binding[13].
  • Hemoglobin subunit beta's molecular function is recorded as oxygen binding[14].
  • Hemoglobin subunit beta's molecular function is recorded as heme binding[15].
  • Hemoglobin subunit beta's molecular function is recorded as haptoglobin binding[16].
  • Hemoglobin subunit beta's molecular function is recorded as hemoglobin alpha binding[17].
  • Hemoglobin subunit beta's molecular function is recorded as hemoglobin beta binding[18].
  • Hemoglobin subunit beta's molecular function is recorded as organic acid binding[19].
  • Hemoglobin subunit beta's molecular function is recorded as metal ion binding[20].
  • Hemoglobin subunit beta's cell component is recorded as hemoglobin complex[21].
  • Hemoglobin subunit beta's cell component is recorded as haptoglobin-hemoglobin complex[22].
  • Hemoglobin subunit beta's biological process is recorded as glutathione metabolic process[23].
  • Hemoglobin subunit beta's biological process is recorded as oxygen transport[24].
  • Hemoglobin subunit beta's biological process is recorded as hydrogen peroxide catabolic process[25].
  • Hemoglobin subunit beta's biological process is recorded as protein heterooligomerization[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] . Q905695. Retrieved . wikidata.org.
  4. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  5. [6] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . wikidata.org.
  8. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . Q20641742. Retrieved . wikidata.org.
  10. [11] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Rat haemoglobin heterogeneity. Two structurally distinct alpha chains and functional behaviour of selected components. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Rat haemoglobin heterogeneity. Two structurally distinct alpha chains and functional behaviour of selected components. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. 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] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . Cellular redox potential and hemoglobin S-glutathionylation in human and rat erythrocytes: A comparative study. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Rat haemoglobin heterogeneity. Two structurally distinct alpha chains and functional behaviour of selected components. 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). Hemoglobin subunit beta. Retrieved May 3, 2026, from https://4ort.xyz/entity/hemoglobin-subunit-beta-q28556477
MLA “Hemoglobin subunit beta.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/hemoglobin-subunit-beta-q28556477.
BibTeX @misc{4ortxyz_hemoglobin-subunit-beta-q28556477_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Hemoglobin subunit beta}}, year = {2026}, url = {https://4ort.xyz/entity/hemoglobin-subunit-beta-q28556477}, note = {Accessed: 2026-05-03}}
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