Ribosomal oxygenase 2

mammalian protein found in Mus musculus
Protein protein Q21982609
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Summary

Ribosomal oxygenase 2 is a protein[1].

Key Facts

  • Ribosomal oxygenase 2's instance of is recorded as protein[2].
  • Ribosomal oxygenase 2's subclass of is recorded as protein[3].
  • Ribosomal oxygenase 2's UniProt protein ID is recorded as Q8CD15[4].
  • Ribosomal oxygenase 2's RefSeq protein ID is recorded as NP_080186[5].
  • Ribosomal oxygenase 2's RefSeq protein ID is recorded as XP_006522542[6].
  • Ribosomal oxygenase 2's molecular function is recorded as dioxygenase activity[7].
  • Ribosomal oxygenase 2's molecular function is recorded as metal ion binding[8].
  • Ribosomal oxygenase 2's molecular function is recorded as oxidoreductase activity[9].
  • Ribosomal oxygenase 2's molecular function is recorded as histone H3-methyl-lysine-4 demethylase activity[10].
  • Ribosomal oxygenase 2's molecular function is recorded as identical protein binding[11].
  • Ribosomal oxygenase 2's molecular function is recorded as histone H3-methyl-lysine-36 demethylase activity[12].
  • Ribosomal oxygenase 2's molecular function is recorded as transcription corepressor activity[13].
  • Ribosomal oxygenase 2's cell component is recorded as transcription regulator complex[14].
  • Ribosomal oxygenase 2's cell component is recorded as nucleolus[15].
  • Ribosomal oxygenase 2's cell component is recorded as nucleus[16].
  • Ribosomal oxygenase 2's cell component is recorded as cytosol[17].
  • Ribosomal oxygenase 2's biological process is recorded as regulation of transcription, DNA-templated[18].
  • Ribosomal oxygenase 2's biological process is recorded as transcription, DNA-templated[19].
  • Ribosomal oxygenase 2's biological process is recorded as regulation of cell population proliferation[20].
  • Ribosomal oxygenase 2's biological process is recorded as negative regulation of transcription by RNA polymerase II[21].
  • Ribosomal oxygenase 2's biological process is recorded as chromatin remodeling[22].
  • Ribosomal oxygenase 2's biological process is recorded as peptidyl-arginine hydroxylation[23].
  • Ribosomal oxygenase 2's biological process is recorded as histone H3-K4 demethylation[24].
  • Ribosomal oxygenase 2's biological process is recorded as ribosome biogenesis[25].
  • Ribosomal oxygenase 2's biological process is recorded as histone H3-K36 demethylation[26].

References

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

Direct Wikidata claims

  1. [2] ↑ . UniProt. Retrieved . wikidata.org.
  2. [3] ↑ . UniProt. Retrieved . wikidata.org.
  3. [4] ↑ . UniProt. Retrieved . wikidata.org.
  4. [5] ↑ . Q20641742. Retrieved . wikidata.org.
  5. [6] ↑ . Q20641742. Retrieved . wikidata.org.
  6. [7] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [8] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . GOA. 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] ↑ . Mina, an Il4 repressor, controls T helper type 2 bias. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . Mina, an Il4 repressor, controls T helper type 2 bias. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . A novel myc target gene, mina53, that is involved in cell proliferation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . A novel myc target gene, mina53, that is involved in cell proliferation. 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] ↑ . A novel myc target gene, mina53, that is involved in cell proliferation. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . GOA. 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] ↑ . GOA. 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). Ribosomal oxygenase 2. Retrieved May 3, 2026, from https://4ort.xyz/entity/ribosomal-oxygenase-2-q21982609
MLA “Ribosomal oxygenase 2.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/ribosomal-oxygenase-2-q21982609.
BibTeX @misc{4ortxyz_ribosomal-oxygenase-2-q21982609_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Ribosomal oxygenase 2}}, year = {2026}, url = {https://4ort.xyz/entity/ribosomal-oxygenase-2-q21982609}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Ribosomal oxygenase 2 — https://4ort.xyz/entity/ribosomal-oxygenase-2-q21982609 (retrieved 2026-05-03)

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