Ribonucleotide reductase M2

mammalian protein found in Mus musculus
Protein protein Q21987493
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Ribonucleotide reductase M2

Summary

Ribonucleotide reductase M2 is a protein[1].

Key Facts

  • Ribonucleotide reductase M2's instance of is recorded as protein[2].
  • Ribonucleotide reductase M2's subclass of is recorded as protein[3].
  • Ribonucleotide reductase M2's UniProt protein ID is recorded as P11157[4].
  • Ribonucleotide reductase M2's part of is recorded as Ferritin-like superfamily[5].
  • Ribonucleotide reductase M2's part of is recorded as Ribonucleotide reductase small subunit[6].
  • Ribonucleotide reductase M2's part of is recorded as Ribonucleotide reductase-like[7].
  • Ribonucleotide reductase M2's part of is recorded as Ribonucleotide reductase small subunit, acitve site, protein family[8].
  • Ribonucleotide reductase M2's has part is recorded as Ribonucleotide reductase small subunit, acitve site[9].
  • Ribonucleotide reductase M2's RefSeq protein ID is recorded as NP_033130[10].
  • Ribonucleotide reductase M2's PDB structure ID is recorded as 1AFT[11].
  • Ribonucleotide reductase M2's PDB structure ID is recorded as 1H0N[12].
  • Ribonucleotide reductase M2's PDB structure ID is recorded as 1H0O[13].
  • Ribonucleotide reductase M2's PDB structure ID is recorded as 1W68[14].
  • Ribonucleotide reductase M2's PDB structure ID is recorded as 1W69[15].
  • Ribonucleotide reductase M2's PDB structure ID is recorded as 1XSM[16].
  • Ribonucleotide reductase M2's molecular function is recorded as protein binding[17].
  • Ribonucleotide reductase M2's molecular function is recorded as metal ion binding[18].
  • Ribonucleotide reductase M2's molecular function is recorded as ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor[19].
  • Ribonucleotide reductase M2's molecular function is recorded as oxidoreductase activity[20].
  • Ribonucleotide reductase M2's molecular function is recorded as ferric iron binding[21].
  • Ribonucleotide reductase M2's molecular function is recorded as protein homodimerization activity[22].
  • Ribonucleotide reductase M2's molecular function is recorded as ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor[23].
  • Ribonucleotide reductase M2's cell component is recorded as cytoplasm[24].
  • Ribonucleotide reductase M2's cell component is recorded as ribonucleoside-diphosphate reductase complex[25].
  • Ribonucleotide reductase M2's cell component is recorded as cytosol[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] . Q905695. Retrieved . wikidata.org.
  11. [12] . Q905695. Retrieved . wikidata.org.
  12. [13] . Q905695. Retrieved . wikidata.org.
  13. [14] . Q905695. Retrieved . wikidata.org.
  14. [15] . Q905695. Retrieved . wikidata.org.
  15. [16] . Q905695. Retrieved . wikidata.org.
  16. [17] . The involvement of Arg265 of mouse ribonucleotide reductase R2 protein in proton transfer and catalysis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [18] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] . Molecular cloning and expression of the functional gene encoding the M2 subunit of mouse ribonucleotide reductase: a new dominant marker gene. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] . The three-dimensional structure of mammalian ribonucleotide reductase protein R2 reveals a more-accessible iron-radical site than Escherichia coli R2. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] . 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] . Molecular cloning and expression of the functional gene encoding the M2 subunit of mouse ribonucleotide reductase: a new dominant marker gene. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . 1H NMR studies of mouse ribonucleotide reductase: the R2 protein carboxyl-terminal tail, essential for subunit interaction, is highly flexible but becomes rigid in the presence of protein R1. 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). Ribonucleotide reductase M2. Retrieved May 3, 2026, from https://4ort.xyz/entity/ribonucleotide-reductase-m2
MLA “Ribonucleotide reductase M2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ribonucleotide-reductase-m2.
BibTeX @misc{4ortxyz_ribonucleotide-reductase-m2_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ribonucleotide reductase M2}}, year = {2026}, url = {https://4ort.xyz/entity/ribonucleotide-reductase-m2}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Ribonucleotide reductase M2 — https://4ort.xyz/entity/ribonucleotide-reductase-m2 (retrieved 2026-05-03)

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