Home › Entities › protein › Rad23p YEL037C

Rad23p YEL037C

fungal protein found in Saccharomyces cerevisiae S288c
Protein protein Q27549370
Press Enter · cited answer in seconds

Rad23p YEL037C

Summary

Rad23p YEL037C is a protein[1].

Key Facts

  • Rad23p YEL037C's instance of is recorded as protein[2].
  • Rad23p YEL037C's subclass of is recorded as protein[3].
  • Rad23p YEL037C's UniProt protein ID is recorded as P32628[4].
  • Rad23p YEL037C's part of is recorded as UBA-like superfamily[5].
  • Rad23p YEL037C's part of is recorded as Ubiquitin-like domain superfamily[6].
  • Rad23p YEL037C's part of is recorded as UV excision repair protein Rad23[7].
  • Rad23p YEL037C's part of is recorded as XPC-binding domain superfamily[8].
  • Rad23p YEL037C's part of is recorded as Ubiquitin-associated domain, protein family[9].
  • Rad23p YEL037C's part of is recorded as Heat shock chaperonin-binding domain, protein family[10].
  • Rad23p YEL037C's part of is recorded as Ubiquitin-like domain, protein family[11].
  • Rad23p YEL037C's part of is recorded as XPC-binding domain, protein family[12].
  • Rad23p YEL037C's has part is recorded as XPC-binding domain[13].
  • Rad23p YEL037C's has part is recorded as Ubiquitin domain[14].
  • Rad23p YEL037C's has part is recorded as Heat shock chaperonin-binding[15].
  • Rad23p YEL037C's has part is recorded as Ubiquitin-associated domain[16].
  • Rad23p YEL037C's RefSeq protein ID is recorded as NP_010877[17].
  • Rad23p YEL037C's molecular function is recorded as protein-macromolecule adaptor activity[18].
  • Rad23p YEL037C's molecular function is recorded as damaged DNA binding[19].
  • Rad23p YEL037C's molecular function is recorded as ubiquitin binding[20].
  • Rad23p YEL037C's molecular function is recorded as peptide-N4-(N-acetyl-beta-glucosaminyl)asparagine amidase activity[21].
  • Rad23p YEL037C's molecular function is recorded as proteasome binding[22].
  • Rad23p YEL037C's molecular function is recorded as protein binding[23].
  • Rad23p YEL037C's molecular function is recorded as polyubiquitin modification-dependent protein binding[24].
  • Rad23p YEL037C's molecular function is recorded as ubiquitin binding[25].
  • Rad23p YEL037C's molecular function is recorded as proteasome binding[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] ↑ . Q20641742. 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] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  8. [9] ↑ . wikidata.org.
  9. [10] ↑ . wikidata.org.
  10. [11] ↑ . wikidata.org.
  11. [12] ↑ . wikidata.org.
  12. [13] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  13. [14] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  14. [15] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  15. [16] ↑ . InterPro Release 71.0. ebi.ac.uk. Provenance: wikidata.org.
  16. [17] ↑ . Q20641742. Retrieved . wikidata.org.
  17. [18] ↑ . Multiple interactions of rad23 suggest a mechanism for ubiquitylated substrate delivery important in proteolysis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [19] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [20] ↑ . UBA domains of DNA damage-inducible proteins interact with ubiquitin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [21] ↑ . N-terminal deletion of peptide:N-glycanase results in enhanced deglycosylation activity. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [22] ↑ . Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [23] ↑ . Rad23 links DNA repair to the ubiquitin/proteasome pathway. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [24] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [25] ↑ . UBA domains of DNA damage-inducible proteins interact with ubiquitin. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [26] ↑ . Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain. Retrieved . ebi.ac.uk. Provenance: wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. 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). Rad23p YEL037C. Retrieved May 3, 2026, from https://4ort.xyz/entity/rad23p-yel037c
MLA “Rad23p YEL037C.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/rad23p-yel037c.
BibTeX @misc{4ortxyz_rad23p-yel037c_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Rad23p YEL037C}}, year = {2026}, url = {https://4ort.xyz/entity/rad23p-yel037c}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Rad23p YEL037C — https://4ort.xyz/entity/rad23p-yel037c (retrieved 2026-05-03)

Canonical URL: https://4ort.xyz/entity/rad23p-yel037c · Last refreshed: