Peroxiredoxin 4

mammalian protein found in Homo sapiens
Protein protein Q21116097
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Peroxiredoxin 4

Summary

Peroxiredoxin 4 is a protein[1]. It is known by 11 alternative names across languages and contexts.[2]

Key Facts

  • Peroxiredoxin 4's instance of is recorded as protein[3].
  • Peroxiredoxin 4 is part of Thioredoxin-like superfamily[4].
  • Peroxiredoxin 4 is part of Peroxiredoxin, AhpC-type[5].
  • Peroxiredoxin 4 is part of Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant, protein family[6].
  • Peroxiredoxin 4 is part of Thioredoxin domain, protein family[7].
  • Peroxiredoxin 4 is part of Peroxiredoxin, C-terminal domain, protein family[8].
  • Peroxiredoxin 4 comprises Thioredoxin domain[9].
  • Peroxiredoxin 4 comprises Peroxiredoxin, C-terminal[10].
  • Peroxiredoxin 4 comprises Alkyl hydroperoxide reductase subunit C/ Thiol specific antioxidant[11].
  • Peroxiredoxin 4's molecular function is recorded as protein homodimerization activity[12].
  • Peroxiredoxin 4's molecular function is recorded as peroxidase activity[13].
  • Peroxiredoxin 4's molecular function is recorded as thioredoxin peroxidase activity[14].
  • Peroxiredoxin 4's molecular function is recorded as antioxidant activity[15].
  • Peroxiredoxin 4's molecular function is recorded as protein binding[16].
  • Peroxiredoxin 4's molecular function is recorded as peroxiredoxin activity[17].
  • Peroxiredoxin 4's molecular function is recorded as oxidoreductase activity[18].
  • Peroxiredoxin 4's molecular function is recorded as thioredoxin peroxidase activity[19].
  • Peroxiredoxin 4's cell component is recorded as cytoplasm[20].
  • Peroxiredoxin 4's cell component is recorded as cytosol[21].
  • Peroxiredoxin 4's cell component is recorded as smooth endoplasmic reticulum[22].
  • Peroxiredoxin 4's cell component is recorded as endoplasmic reticulum[23].
  • Peroxiredoxin 4's cell component is recorded as mitochondrion[24].
  • Peroxiredoxin 4's cell component is recorded as extracellular exosome[25].
  • Peroxiredoxin 4's cell component is recorded as nucleus[26].
  • Peroxiredoxin 4's cell component is recorded as extracellular space[27].

Why It Matters

Peroxiredoxin 4 is known by 11 alternative names across languages and contexts.[2]

References

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

Direct Wikidata claims

  1. [3] . Q905695. Retrieved . wikidata.org.
  2. [4] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  3. [5] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  4. [6] . wikidata.org.
  5. [7] . wikidata.org.
  6. [8] . wikidata.org.
  7. [9] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [10] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  9. [11] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  10. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] . Regulatory Role for a Novel Human Thioredoxin Peroxidase in NF-κB Activation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] . Recycling of peroxiredoxin IV provides a novel pathway for disulphide formation in the endoplasmic reticulum. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] . Regulatory Role for a Novel Human Thioredoxin Peroxidase in NF-κB Activation. Retrieved . ebi.ac.uk. Provenance: 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] . Proteomic analysis of human parotid gland exosomes by multidimensional protein identification technology (MudPIT). Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] . Proteomic characterization of the human sperm nucleus. 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 aliases. wikidata.org.

📑 Cite this page

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 4. Retrieved May 3, 2026, from https://4ort.xyz/entity/peroxiredoxin-4
MLA “Peroxiredoxin 4.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/peroxiredoxin-4.
BibTeX @misc{4ortxyz_peroxiredoxin-4_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Peroxiredoxin 4}}, year = {2026}, url = {https://4ort.xyz/entity/peroxiredoxin-4}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Peroxiredoxin 4 — https://4ort.xyz/entity/peroxiredoxin-4 (retrieved 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. 7w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from
    Encoded by PRDX4
    Wikidata description mammalian protein found in Homo sapiens
    Molecular function protein homodimerization activity, peroxidase activity, thioredoxin peroxidase activity +5
    + 11 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ [[Property:P591]]: 1.11.1.24, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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