RAD52
Gene Ontology Biological Process
- DNA amplification [IMP]
- DNA recombinase assembly [IDA]
- DNA strand renaturation [IDA]
- double-strand break repair via break-induced replication [IMP]
- double-strand break repair via homologous recombination [IMP]
- double-strand break repair via single-strand annealing [IGI]
- meiotic joint molecule formation [IGI, IMP]
- postreplication repair [IMP]
- telomere maintenance via recombination [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
RAD52
Gene Ontology Biological Process
- DNA amplification [IMP]
- DNA recombinase assembly [IDA]
- DNA strand renaturation [IDA]
- double-strand break repair via break-induced replication [IMP]
- double-strand break repair via homologous recombination [IMP]
- double-strand break repair via single-strand annealing [IGI]
- meiotic joint molecule formation [IGI, IMP]
- postreplication repair [IMP]
- telomere maintenance via recombination [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Phenotypic Suppression
A genetic interaction is inferred when mutation or over expression of one gene results in suppression of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.
Publication
Rad52/Rad59-dependent recombination as a means to rectify faulty Okazaki fragment processing.
The correct removal of 5'-flap structures by Rad27 and Dna2 during Okazaki fragment maturation is crucial for the stable maintenance of genetic materials and cell viability. In this study, we identified RAD52, a key recombination protein, as a multicopy suppressor of dna2-K1080E, a lethal helicase-negative mutant allele of DNA2 in yeasts. In contrast, the overexpression of Rad51, which works conjointly ... [more]
Throughput
- Low Throughput
Ontology Terms
- phenotype: vegetative growth (APO:0000106)
Additional Notes
- Figure 8
- Suppression of dna2 by Elg1 overexpression is dependent on RAD52
- genetic complex
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| RAD52 RAD52 | Co-crystal Structure Co-crystal Structure Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex. | Low | - | BioGRID | 3588460 | |
| RAD52 RAD52 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | - | |
| RAD52 RAD52 | Reconstituted Complex Reconstituted Complex An interaction is detected between purified proteins in vitro. | Low | - | BioGRID | 256118 | |
| RAD52 RAD52 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| RAD52 RAD52 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| RAD52 RAD52 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - | |
| RAD52 RAD52 | Two-hybrid Two-hybrid Bait protein expressed as a DNA binding domain (DBD) fusion and prey expressed as a transcriptional activation domain (TAD) fusion and interaction measured by reporter gene activation. | Low | - | BioGRID | - |
Curated By
- BioGRID