RAD18 E3 ubiquitin protein ligase

mammalian protein found in Homo sapiens
Protein protein Q21135006
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Summary

RAD18 E3 ubiquitin protein ligase is a protein[1]. It is known by 11 alternative names across languages and contexts.[2]

Key Facts

  • Molecular function: metal ion binding[3], polyubiquitin modification-dependent protein binding[4], Y-form DNA binding[5], ubiquitin protein ligase activity[6], damaged DNA binding[7], DNA binding[8], ubiquitin protein ligase binding[9], single-stranded DNA helicase activity[10], protein binding[11], identical protein binding[12], transferase activity[13], protein-containing complex binding[14], single-stranded DNA binding[15]
  • Cell component: cytoplasm[16], site of double-strand break[17], microtubule organizing center[18], nucleus[19], replication fork[20], centrosome[21], Rad6-Rad18 complex[22], nuclear inclusion body[23], cytoskeleton[24], nucleoplasm[25], nuclear body[26]
  • Biological process: protein monoubiquitination[27], response to UV[28], negative regulation of cell death[29], positive regulation of chromosome segregation[30], cellular response to DNA damage stimulus[31], postreplication repair[32], protein autoubiquitination[33], DNA repair[34], protein ubiquitination[35]
  • Encoded by: RAD18[36]
  • Found in taxon: Homo sapiens[37]

References

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

Direct Wikidata claims

  1. [3] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  2. [4] ↑ . Tandem protein interaction modules organize the ubiquitin-dependent response to DNA double-strand breaks. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  3. [5] ↑ . Recognition of forked and single-stranded DNA structures by human RAD18 complexed with RAD6B protein triggers its recruitment to stalled replication forks. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  4. [6] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  5. [7] ↑ . Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  6. [8] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  7. [9] ↑ . The human RAD18 gene product interacts with HHR6A and HHR6B. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  8. [10] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  9. [11] ↑ . A DNA Damage Response Screen Identifies RHINO, a 9-1-1 and TopBP1 Interacting Protein Required for ATR Signaling. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  10. [12] ↑ . DNA damage-specific deubiquitination regulates Rad18 functions to suppress mutagenesis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  11. [13] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  12. [14] ↑ . DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  13. [15] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  14. [16] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  15. [17] ↑ . DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  16. [18] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  17. [19] ↑ . Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  18. [20] ↑ . Recognition of forked and single-stranded DNA structures by human RAD18 complexed with RAD6B protein triggers its recruitment to stalled replication forks. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  19. [21] ↑ . BRCTx is a novel, highly conserved RAD18-interacting protein. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  20. [22] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  21. [23] ↑ . RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  22. [24] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  23. [25] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  24. [26] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  25. [27] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  26. [28] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  27. [29] ↑ . RAD18-BRCTx interaction is required for efficient repair of UV-induced DNA damage. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  28. [30] ↑ . DNA repair. Proteomics reveals dynamic assembly of repair complexes during bypass of DNA cross-links. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  29. [31] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  30. [32] ↑ . Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  31. [33] ↑ . DNA damage-specific deubiquitination regulates Rad18 functions to suppress mutagenesis. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  32. [34] ↑ . Dysfunction of human Rad18 results in defective postreplication repair and hypersensitivity to multiple mutagens. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  33. [35] ↑ . GOA. Retrieved . ebi.ac.uk. Provenance: wikidata.org.
  34. [36] ↑ . UniProt. Retrieved . wikidata.org.
  35. [37] ↑ . UniProt. Retrieved . wikidata.org.

Class ancestry

  1. [1] ↑ . Wikidata. wikidata.org.

Aggregate / graph-position facts

  1. [2] ↑ . Wikidata aliases. wikidata.org.

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APA 4ort.xyz Knowledge Graph. (2026). RAD18 E3 ubiquitin protein ligase. Retrieved May 3, 2026, from https://4ort.xyz/entity/rad18-e3-ubiquitin-protein-ligase
MLA “RAD18 E3 ubiquitin protein ligase.” 4ort.xyz Knowledge Graph, 4ort.xyz, 3 May. 2026, https://4ort.xyz/entity/rad18-e3-ubiquitin-protein-ligase.
BibTeX @misc{4ortxyz_rad18-e3-ubiquitin-protein-ligase_2026, author = {{4ort.xyz Knowledge Graph}}, title = {{RAD18 E3 ubiquitin protein ligase}}, year = {2026}, url = {https://4ort.xyz/entity/rad18-e3-ubiquitin-protein-ligase}, note = {Accessed: 2026-05-03}}
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Edit History

Rolling log of changes to this entity's Wikidata record. Values shown reflect the current state of each edited property — follow the history link to see the precise diff for any edit.

  1. 12w ago · Boghog · 2026-07-24 view diff on Wikidata ↗
    Imported from → —
    Encoded by → RAD18
    Wikidata description → mammalian protein found in Homo sapiens
    Molecular function → metal ion binding, polyubiquitin modification-dependent protein binding, Y-form DNA binding +11
    + 9 other properties edited (see Wikidata diff for full list)
    "/* wbcreateclaim-create:1| */ Ec enzyme number: 2.3.2.27, [[:toollabs:quickstatements/#/batch/261491|batch #261491]]"
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