nucleotide-excision repair factor 1 complex
One of several protein complexes involved in nucleotide-excision repair; possesses DNA damage recognition and endodeoxynuclease activities. In S. cerevisiae, it is composed of Rad1p, Rad10p, and Rad14p; in human the subunits are ERCC4/XPF, ERCC1 and XPA, respectively. [GO:0000110]
Synonyms: NEF1 complex; XPA-ERCC1-ERCC4 complex
Components
| Component | Type | Part of / acts on | Grounding | Genes | Stoichiometry | Essential | Role |
|---|---|---|---|---|---|---|---|
| Rad1 NEF1 subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | RAD1 | UNKNOWN | Protein constituent of the budding-yeast nucleotide-excision repair factor 1 / NEF1 complex.
| |
| Rad10 NEF1 subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | RAD10 | UNKNOWN | Protein constituent of the budding-yeast nucleotide-excision repair factor 1 / NEF1 complex.
| |
| Rad14 NEF1 subunit | Protein | part of | Reviewed label only (reviewed name; no accession asserted) | RAD14 | UNKNOWN | Protein constituent of the budding-yeast nucleotide-excision repair factor 1 / NEF1 complex.
|
Taxonomic distribution
NCBITaxon:4932Saccharomyces cerevisiae — COMMON: Budding yeast is the organism in which GO:0000110 defines NEF1 as a nucleotide-excision repair factor complex with Rad1p, Rad10p and Rad14p constituents. [GO:0000110]
Canonical examples
NCBITaxon:4932Saccharomyces cerevisiae — Prakash and Prakash 2000 described budding-yeast Rad14 and Rad1-Rad10 as one nucleotide-excision repair subassembly called NEF1. [DOI:10.1016/s0027-5107(00)00037-3]
Functions
- nucleotide-excision repair
GO:0006289— The NEF1 complex participates in nucleotide-excision repair as a DNA-damage-recognition and endodeoxynuclease-containing protein complex.GO:0000110GO:0000110 defines NEF1 as a nucleotide-excision repair factor with DNA damage recognition and endodeoxynuclease activities.GO:0006289GO:0006289 is the Gene Ontology biological-process term for nucleotide-excision repair.DOI:10.1016/s0027-5107(00)00037-3Prakash and Prakash 2000 described Rad14 and the Rad1-Rad10 complex as the budding-yeast NEF1 multiprotein subassembly.
Mechanism graphs
NEF1 is a yeast nucleotide-excision repair factor (FUNCTION)
In Saccharomyces cerevisiae, Rad1p, Rad10p and Rad14p form the NEF1 subassembly of the nucleotide-excision repair protein system.
| Subject | Predicate | Object | Evidence |
|---|---|---|---|
| Rad1 NEF1 subunit | contributes to | NEF1 complex |
|
| Rad10 NEF1 subunit | contributes to | NEF1 complex |
|
| Rad14 NEF1 subunit | contributes to | NEF1 complex |
|
| NEF1 complex | supports | nucleotide-excision repair |
|
Discussions
- CURATION_TODO (OPEN): Resolve exact source-neutral family groundings for the Rad1, Rad10 and Rad14 constituents of the NEF1 complex. GO:0000110 defines budding-yeast Rad1p, Rad10p and Rad14p constituents and also maps the corresponding human subunits as ERCC4/XPF, ERCC1 and XPA. Exact cross-eukaryotic InterPro, Pfam, NCBIfam or UniProt family boundaries for these NER factor classes need narrower curation before these component labels can be grounded.
Evidence
GO:0000110Gene Ontology cellular-component term for the NEF1 complex and its exact NEF1 and XPA-ERCC1-ERCC4 synonyms.GO:0000109Gene Ontology cellular-component parent term for nucleotide-excision repair complexes.GO:0006289Gene Ontology biological-process term for nucleotide-excision repair.PMID:10915862PubMed identifier for Prakash and Prakash 2000, the Mutation Research yeast nucleotide-excision repair review cited by GO:0000110.DOI:10.1016/s0027-5107(00)00037-3DOI for Prakash and Prakash 2000, 'Nucleotide excision repair in yeast', verified through NCBI E-utilities.
Curation history
2026-09-26T01:51:21Zcodex · CREATED_RECORD — Scaffolded by scripts/new_record.py2026-09-26T01:52:24Zcodex · EXPANDED_RECORD — Added NEF1 and XPA-ERCC1-ERCC4 exact synonymy, nucleotide-excision repair complex parentage, three reviewed-label-only Rad constituent rows, budding-yeast scope, a nucleotide-excision-repair function, GO/PubMed/DOI evidence, a nonmechanistic function graph, and a NEF1 subunit-grounding TODO.
Source: data/structures/other/nucleotide_excision_repair_factor_1_complex.yaml