Peroxiredoxin 2

mammalian protein found in Rattus norvegicus
Protein protein Q28558498
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Peroxiredoxin 2

Summary

Peroxiredoxin 2 is a protein[1].

Key Facts

  • Peroxiredoxin 2's instance of is recorded as protein[2].
  • Peroxiredoxin 2's subclass of is recorded as protein[3].
  • Peroxiredoxin 2's UniProt protein ID is recorded as P35704[4].
  • Peroxiredoxin 2's part of is recorded as Thioredoxin-like superfamily[5].
  • Peroxiredoxin 2's part of is recorded as Peroxiredoxin, AhpC-type[6].
  • Peroxiredoxin 2's part of is recorded as Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant, protein family[7].
  • Peroxiredoxin 2's part of is recorded as Thioredoxin domain, protein family[8].
  • Peroxiredoxin 2's part of is recorded as Peroxiredoxin, C-terminal domain, protein family[9].
  • Peroxiredoxin 2's has part is recorded as Thioredoxin domain[10].
  • Peroxiredoxin 2's has part is recorded as Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant[11].
  • Peroxiredoxin 2's has part is recorded as Peroxiredoxin, C-terminal[12].
  • Peroxiredoxin 2's RefSeq protein ID is recorded as NP_058865[13].
  • Peroxiredoxin 2's RefSeq protein ID is recorded as XP_006255306[14].
  • Peroxiredoxin 2's molecular function is recorded as molecular function[15].
  • Peroxiredoxin 2's molecular function is recorded as peroxidase activity[16].
  • Peroxiredoxin 2's molecular function is recorded as thioredoxin peroxidase activity[17].
  • Peroxiredoxin 2's molecular function is recorded as antioxidant activity[18].
  • Peroxiredoxin 2's molecular function is recorded as oxidoreductase activity[19].
  • Peroxiredoxin 2's molecular function is recorded as peroxiredoxin activity[20].
  • Peroxiredoxin 2's cell component is recorded as cytoplasm[21].
  • Peroxiredoxin 2's cell component is recorded as cytosol[22].
  • Peroxiredoxin 2's biological process is recorded as response to oxidative stress[23].
  • Peroxiredoxin 2's biological process is recorded as hydrogen peroxide catabolic process[24].
  • Peroxiredoxin 2's biological process is recorded as negative regulation of neuron apoptotic process[25].
  • Peroxiredoxin 2's biological process is recorded as cell redox homeostasis[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] ↑ . wikidata.org.
  7. [8] ↑ . wikidata.org.
  8. [9] ↑ . wikidata.org.
  9. [10] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [11] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  11. [12] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  12. [13] ↑ . Q20641742. Retrieved . wikidata.org.
  13. [14] ↑ . Q20641742. Retrieved . wikidata.org.
  14. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] ↑ . GOA. 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] ↑ . Rat lung peroxiredoxins I and II are differentially regulated during development and by hyperoxia. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Peroxiredoxin 2 overexpression protects cortical neuronal cultures from ischemic and oxidative injury but not glutamate excitotoxicity, whereas Cu/Zn superoxide dismutase 1 overexpression protects only against oxidative injury. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . Peroxiredoxin 2 overexpression protects cortical neuronal cultures from ischemic and oxidative injury but not glutamate excitotoxicity, whereas Cu/Zn superoxide dismutase 1 overexpression protects only against oxidative injury. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . GOA. 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). Peroxiredoxin 2. Retrieved May 3, 2026, from https://4ort.xyz/entity/peroxiredoxin-2-q28558498
MLA “Peroxiredoxin 2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/peroxiredoxin-2-q28558498.
BibTeX @misc{4ortxyz_peroxiredoxin-2-q28558498_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Peroxiredoxin 2}}, year = {2026}, url = {https://4ort.xyz/entity/peroxiredoxin-2-q28558498}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Peroxiredoxin 2 — https://4ort.xyz/entity/peroxiredoxin-2-q28558498 (retrieved 2026-05-03)

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