MCM7
Gene Ontology Biological Process
- DNA replication initiation [IGI, IMP]
- DNA strand elongation involved in DNA replication [IGI, IMP]
- DNA unwinding involved in DNA replication [IDA]
- chromatin silencing at silent mating-type cassette [IMP]
- chromatin silencing at telomere [IMP]
- double-strand break repair via break-induced replication [IMP]
- nuclear DNA replication [IMP]
- pre-replicative complex assembly involved in nuclear cell cycle DNA replication [IDA, IPI]
Gene Ontology Molecular Function- ATP binding [IDA]
- ATP-dependent 3'-5' DNA helicase activity [IDA]
- ATP-dependent DNA helicase activity [IDA]
- ATP-dependent four-way junction helicase activity [IDA]
- DNA helicase activity [IDA]
- DNA replication origin binding [IDA]
- chromatin binding [IDA]
- single-stranded DNA binding [IMP]
- single-stranded DNA-dependent ATP-dependent DNA helicase activity [IDA]
- single-stranded DNA-dependent ATPase activity [IDA]
- ATP binding [IDA]
- ATP-dependent 3'-5' DNA helicase activity [IDA]
- ATP-dependent DNA helicase activity [IDA]
- ATP-dependent four-way junction helicase activity [IDA]
- DNA helicase activity [IDA]
- DNA replication origin binding [IDA]
- chromatin binding [IDA]
- single-stranded DNA binding [IMP]
- single-stranded DNA-dependent ATP-dependent DNA helicase activity [IDA]
- single-stranded DNA-dependent ATPase activity [IDA]
Gene Ontology Cellular Component
POL1
Gene Ontology Biological Process
- DNA replication [IMP]
- DNA replication checkpoint [IBA]
- DNA replication initiation [IC]
- DNA replication, synthesis of RNA primer [IBA]
- DNA strand elongation involved in DNA replication [IBA]
- DNA synthesis involved in DNA repair [IMP]
- RNA-dependent DNA replication [IDA]
- double-strand break repair [IMP]
- gene conversion at mating-type locus, DNA repair synthesis [IBA]
- lagging strand elongation [IC]
- premeiotic DNA replication [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
The social and structural architecture of the yeast protein interactome.
Cellular functions are mediated by protein-protein interactions, and mapping the interactome provides fundamental insights into biological systems. Affinity purification coupled to mass spectrometry is an ideal tool for such mapping, but it has been difficult to identify low copy number complexes, membrane complexes and complexes that are disrupted by protein tagging. As a result, our current knowledge of the interactome ... [more]
Quantitative Score
- 2.0 [Score_FDR+correlation]
Throughput
- High Throughput
Additional Notes
- Protein interactions were identified using statistically significant enrichment of the proteins in the forward and reverse pull-downs, as well as making use of the profile similarities of interacting proteins in a correlation analysis. High confidence interactions have a total score >=2. This score is a sum of the FDR score of the forward pull-down + FDR score of the reverse pull-down + correlation score.
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| POL1 MCM7 | 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 | -0.2801 | BioGRID | 1948587 | |
| POL1 MCM7 | 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