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
Reconstituted Complex
An interaction is detected between purified proteins in vitro.
Publication
Rad52 Oligomeric N-Terminal Domain Stabilizes Rad51 Nucleoprotein Filaments and Contributes to Their Protection against Srs2.
Homologous recombination (HR) depends on the formation of a nucleoprotein filament of the recombinase Rad51 to scan the genome and invade the homologous sequence used as a template for DNA repair synthesis. Therefore, HR is highly accurate and crucial for genome stability. Rad51 filament formation is controlled by positive and negative factors. In Saccharomyces cerevisiae, the mediator protein Rad52 catalyzes ... [more]
Throughput
- Low Throughput
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 | Phenotypic Suppression 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. | Low | - | BioGRID | 1240480 | |
| 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