RFC4
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
POL30
Gene Ontology Biological Process
- chromatin silencing at silent mating-type cassette [IGI, IMP]
- chromatin silencing at telomere [IMP]
- error-free translesion synthesis [IGI]
- establishment of mitotic sister chromatid cohesion [IGI]
- lagging strand elongation [IDA, IPI]
- leading strand elongation [IDA]
- maintenance of DNA trinucleotide repeats [IGI, IMP]
- meiotic mismatch repair [IGI, IMP]
- mismatch repair [IGI, IMP, IPI]
- mitotic cell cycle [IGI]
- mitotic sister chromatid cohesion [IGI, IPI]
- nucleotide-excision repair [IMP]
- positive regulation of exodeoxyribonuclease activity [IDA]
- positive regulation of phosphodiesterase activity, acting on 3'-phosphoglycolate-terminated DNA strands [IDA]
- postreplication repair [IGI, IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Dosage Rescue
A genetic interaction is inferred when over expression or increased dosage of one gene rescues the lethality or growth defect of a strain that is mutated or deleted for another gene.
Publication
ATP utilization by yeast replication factor C. IV. RFC ATP-binding mutants show defects in DNA replication, DNA repair, and checkpoint regulation.
Replication factor C is required to load proliferating cell nuclear antigen onto primer-template junctions, using the energy of ATP hydrolysis. Four of the five RFC genes have consensus ATP-binding motifs. To determine the relative importance of these sites for proper DNA metabolism in the cell, the conserved lysine in the Walker A motif of RFC1, RFC2, RFC3, or RFC4 was ... [more]
Throughput
- Low Throughput
Ontology Terms
- cold sensitivity (APO:0000148)
Related interactions
Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
---|---|---|---|---|---|---|
POL30 RFC4 | 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 | - | |
POL30 RFC4 | FRET FRET An interaction is inferred when close proximity of interaction partners is detected by fluorescence resonance energy transfer between pairs of fluorophore-labeled molecules, such as occurs between CFP (donor) and YFP (acceptor) fusion proteins. | Low | - | BioGRID | - | |
POL30 RFC4 | Negative Genetic Negative Genetic Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores. | High | -0.17 | BioGRID | 1920625 | |
POL30 RFC4 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - | |
RFC4 POL30 | Reconstituted Complex Reconstituted Complex An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator. | Low | - | BioGRID | - |
Curated By
- BioGRID