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
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.
Publication
Rad52 sumoylation and its involvement in the efficient induction of homologous recombination.
The protein Rad52 is a key player in various types of homologous recombination and is essential to maintenance of genomic integrity. Although evidence indicates that Rad52 is modified by SUMO, the physiological relevance of this sumoylation remains unclear. Here, we identify the conditions under which Rad52 sumoylation is induced, and clarify the role of this modification in homologous recombination. Oligomerization ... [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 | - | |
| 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 | - |
Curated By
- BioGRID