Ribonucleotide reductase M1

mammalian protein found in Mus musculus
Protein protein Q21986411
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Ribonucleotide reductase M1

Summary

Ribonucleotide reductase M1 is a protein[1].

Key Facts

  • Ribonucleotide reductase M1's instance of is recorded as protein[2].
  • Ribonucleotide reductase M1's subclass of is recorded as protein[3].
  • Ribonucleotide reductase M1's UniProt protein ID is recorded as P07742[4].
  • Ribonucleotide reductase M1's RefSeq protein ID is recorded as NP_033129[5].
  • Ribonucleotide reductase M1's molecular function is recorded as nucleotide binding[6].
  • Ribonucleotide reductase M1's molecular function is recorded as catalytic activity[7].
  • Ribonucleotide reductase M1's molecular function is recorded as protein binding[8].
  • Ribonucleotide reductase M1's molecular function is recorded as purine nucleotide binding[9].
  • Ribonucleotide reductase M1's molecular function is recorded as oxidoreductase activity[10].
  • Ribonucleotide reductase M1's molecular function is recorded as ATP binding[11].
  • Ribonucleotide reductase M1's molecular function is recorded as ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor[12].
  • Ribonucleotide reductase M1's molecular function is recorded as disordered domain specific binding[13].
  • Ribonucleotide reductase M1's molecular function is recorded as identical protein binding[14].
  • Ribonucleotide reductase M1's molecular function is recorded as ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor[15].
  • Ribonucleotide reductase M1's cell component is recorded as ribonucleoside-diphosphate reductase complex[16].
  • Ribonucleotide reductase M1's cell component is recorded as cytosol[17].
  • Ribonucleotide reductase M1's cell component is recorded as nuclear envelope[18].
  • Ribonucleotide reductase M1's cell component is recorded as cytoplasm[19].
  • Ribonucleotide reductase M1's cell component is recorded as cell projection[20].
  • Ribonucleotide reductase M1's cell component is recorded as soma[21].
  • Ribonucleotide reductase M1's cell component is recorded as ribonucleoside-diphosphate reductase complex[22].
  • Ribonucleotide reductase M1's biological process is recorded as response to ionizing radiation[23].
  • Ribonucleotide reductase M1's biological process is recorded as male gonad development[24].
  • Ribonucleotide reductase M1's biological process is recorded as pyrimidine nucleobase metabolic process[25].
  • Ribonucleotide reductase M1's biological process is recorded as deoxyribonucleotide biosynthetic process[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] . Q20641742. Retrieved . wikidata.org.
  5. [6] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  6. [7] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] . The involvement of Arg265 of mouse ribonucleotide reductase R2 protein in proton transfer and catalysis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] . Enzymatically active mammalian ribonucleotide reductase exists primarily as an alpha6beta2 octamer. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [10] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [11] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . 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.
  13. [14] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . 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.
  16. [17] . GOA. 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] . 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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] . Molecular mechanisms of thioredoxin and glutaredoxin as hydrogen donors for Mammalian s phase ribonucleotide reductase. 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 M1. Retrieved May 3, 2026, from https://4ort.xyz/entity/ribonucleotide-reductase-m1
MLA “Ribonucleotide reductase M1.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ribonucleotide-reductase-m1.
BibTeX @misc{4ortxyz_ribonucleotide-reductase-m1_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ribonucleotide reductase M1}}, year = {2026}, url = {https://4ort.xyz/entity/ribonucleotide-reductase-m1}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Ribonucleotide reductase M1 — https://4ort.xyz/entity/ribonucleotide-reductase-m1 (retrieved 2026-05-03)

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