Excision repair cross-complementing rodent repair deficiency, complementation group 4

mammalian protein found in Mus musculus
Protein protein Q21992306
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Excision repair cross-complementing rodent repair deficiency, complementation group 4

Summary

Excision repair cross-complementing rodent repair deficiency, complementation group 4 is a protein[1].

Key Facts

  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's instance of is recorded as protein[2].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's subclass of is recorded as protein[3].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's UniProt protein ID is recorded as Q9QZD4[4].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's part of is recorded as RuvA domain 2-like[5].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's part of is recorded as Restriction endonuclease type II-like[6].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's part of is recorded as DNA repair endonuclease XPF[7].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's part of is recorded as ERCC4 domain, protein family[8].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's has part is recorded as ERCC4 domain[9].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's RefSeq protein ID is recorded as NP_056584[10].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as protein N-terminus binding[11].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as single-stranded DNA binding[12].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as damaged DNA binding[13].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as single-stranded DNA endodeoxyribonuclease activity[14].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as protein C-terminus binding[15].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as protein binding[16].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as TFIID-class transcription factor complex binding[17].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as nuclease activity[18].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as endonuclease activity[19].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as endodeoxyribonuclease activity[20].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as hydrolase activity[21].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as DNA binding[22].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as 3' overhang single-stranded DNA endodeoxyribonuclease activity[23].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's molecular function is recorded as identical protein binding[24].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's cell component is recorded as ERCC4-ERCC1 complex[25].
  • Excision repair cross-complementing rodent repair deficiency, complementation group 4's cell component is recorded as transcription factor TFIID complex[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] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [12] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [13] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [14] . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [15] . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [16] . Cathepsin cleavage of sirtuin 1 in endothelial progenitor cells mediates stress-induced premature senescence. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [17] . Defective transcription initiation causes postnatal growth failure in a mouse model of nucleotide excision repair (NER) progeria. 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] . 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] . Defective transcription initiation causes postnatal growth failure in a mouse model of nucleotide excision repair (NER) progeria. 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). Excision repair cross-complementing rodent repair deficiency, complementation group 4. Retrieved May 3, 2026, from https://4ort.xyz/entity/excision-repair-cross-complementing-rodent-repair-deficiency-complementation-group-4
MLA “Excision repair cross-complementing rodent repair deficiency, complementation group 4.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/excision-repair-cross-complementing-rodent-repair-deficiency-complementation-group-4.
BibTeX @misc{4ortxyz_excision-repair-cross-complementing-rodent-repair-deficiency-complementation-group-4_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{Excision repair cross-complementing rodent repair deficiency, complementation group 4}}, year = {2026}, url = {https://4ort.xyz/entity/excision-repair-cross-complementing-rodent-repair-deficiency-complementation-group-4}, note = {Accessed: 2026-05-03}}
LLM prompt According to 4ort.xyz Knowledge Graph (aggregator of Wikidata, Wikipedia, and authoritative open-data sources): Excision repair cross-complementing rodent repair deficiency, complementation group 4 — https://4ort.xyz/entity/excision-repair-cross-complementing-rodent-repair-deficiency-complementation-group-4 (retrieved 2026-05-03)

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