Superoxide dismutase 2

mammalian protein found in Rattus norvegicus
Protein protein Q28559481
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Superoxide dismutase 2

Summary

Superoxide dismutase 2 is a protein[1].

Key Facts

  • Superoxide dismutase 2's instance of is recorded as protein[2].
  • Superoxide dismutase 2's subclass of is recorded as protein[3].
  • Superoxide dismutase 2's UniProt protein ID is recorded as P07895[4].
  • Superoxide dismutase 2's part of is recorded as Manganese/iron superoxide dismutase, C-terminal domain superfamily[5].
  • Superoxide dismutase 2's part of is recorded as Manganese/iron superoxide dismutase, N-terminal domain superfamily[6].
  • Superoxide dismutase 2's part of is recorded as Manganese/iron superoxide dismutase[7].
  • Superoxide dismutase 2's part of is recorded as Manganese/iron superoxide dismutase, C-terminal domain, protein family[8].
  • Superoxide dismutase 2's part of is recorded as Manganese/iron superoxide dismutase, N-terminal domain, protein family[9].
  • Superoxide dismutase 2's part of is recorded as Manganese/iron superoxide dismutase, binding site, protein family[10].
  • Superoxide dismutase 2's has part is recorded as Manganese/iron superoxide dismutase, C-terminal[11].
  • Superoxide dismutase 2's has part is recorded as Manganese/iron superoxide dismutase, binding site[12].
  • Superoxide dismutase 2's has part is recorded as Manganese/iron superoxide dismutase, N-terminal[13].
  • Superoxide dismutase 2's RefSeq protein ID is recorded as NP_058747[14].
  • Superoxide dismutase 2's molecular function is recorded as DNA binding[15].
  • Superoxide dismutase 2's molecular function is recorded as superoxide dismutase activity[16].
  • Superoxide dismutase 2's molecular function is recorded as oxidoreductase activity[17].
  • Superoxide dismutase 2's molecular function is recorded as oxygen binding[18].
  • Superoxide dismutase 2's molecular function is recorded as enzyme binding[19].
  • Superoxide dismutase 2's molecular function is recorded as manganese ion binding[20].
  • Superoxide dismutase 2's molecular function is recorded as identical protein binding[21].
  • Superoxide dismutase 2's molecular function is recorded as metal ion binding[22].
  • Superoxide dismutase 2's molecular function is recorded as manganese ion binding[23].
  • Superoxide dismutase 2's cell component is recorded as cytoplasm[24].
  • Superoxide dismutase 2's cell component is recorded as mitochondrion[25].
  • Superoxide dismutase 2's cell component is recorded as mitochondrial matrix[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] . wikidata.org.
  9. [10] . 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] . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Q20641742. Retrieved . wikidata.org.
  14. [15] . Association of mitochondrial antioxidant enzymes with mitochondrial DNA as integral nucleoid constituents. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . Age-associated increases in oxidative stress and antioxidant enzyme activities in cardiac interfibrillar mitochondria: implications for the mitochondrial theory of aging. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Age-related decrease in the mitochondrial sirtuin deacetylase Sirt3 expression associated with ROS accumulation in the auditory cortex of the mimetic aging rat model.. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . Rat mitochondrial manganese superoxide dismutase: amino acid positions involved in covalent modifications, activity, and heat stability. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . Superoxide dismutase in the prostate lobes of aging Brown Norway rats. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. 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). Superoxide dismutase 2. Retrieved May 3, 2026, from https://4ort.xyz/entity/superoxide-dismutase-2-q28559481
MLA “Superoxide dismutase 2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/superoxide-dismutase-2-q28559481.
BibTeX @misc{4ortxyz_superoxide-dismutase-2-q28559481_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Superoxide dismutase 2}}, year = {2026}, url = {https://4ort.xyz/entity/superoxide-dismutase-2-q28559481}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Superoxide dismutase 2 — https://4ort.xyz/entity/superoxide-dismutase-2-q28559481 (retrieved 2026-05-03)

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