CDC28
Gene Ontology Biological Process
- 7-methylguanosine mRNA capping [IMP]
- chromatin remodeling [IMP]
- meiotic DNA double-strand break processing [IGI]
- negative regulation of double-strand break repair via nonhomologous end joining [IMP]
- negative regulation of meiotic cell cycle [IMP]
- negative regulation of mitotic cell cycle [IDA]
- negative regulation of sister chromatid cohesion [IMP]
- negative regulation of transcription, DNA-templated [IDA, IMP]
- peptidyl-serine phosphorylation [IDA]
- phosphorylation of RNA polymerase II C-terminal domain [IDA]
- positive regulation of meiotic cell cycle [IDA, IMP]
- positive regulation of mitotic cell cycle [IMP]
- positive regulation of nuclear cell cycle DNA replication [IDA, IMP]
- positive regulation of spindle pole body separation [IGI, IMP]
- positive regulation of transcription from RNA polymerase II promoter [IMP]
- positive regulation of transcription, DNA-templated [IDA, IGI]
- positive regulation of triglyceride catabolic process [IGI, IMP]
- protein phosphorylation [IDA]
- regulation of budding cell apical bud growth [IGI, IMP]
- regulation of double-strand break repair via homologous recombination [IMP]
- regulation of filamentous growth [IMP]
- regulation of protein localization [IMP]
- synaptonemal complex assembly [IMP]
- vesicle-mediated transport [IMP]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
SWI5
Gene Ontology Biological Process
Gene Ontology Molecular Function
Biochemical Activity (Phosphorylation)
An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation.
Publication
Dynamics of Cdk1 Substrate Specificity during the Cell Cycle.
Cdk specificity is determined by the intrinsic selectivity of the active site and by substrate docking sites on the cyclin subunit. There is a long-standing debate about the relative importance of these factors in the timing of Cdk1 substrate phosphorylation. We analyzed major budding yeast cyclins (the G1/S-cyclin Cln2, S-cyclin Clb5, G2/M-cyclin Clb3, and M-cyclin Clb2) and found that the activity ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CDC28 SWI5 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | Low | - | BioGRID | 907961 | |
| CDC28 SWI5 | Biochemical Activity Biochemical Activity An interaction is inferred from the biochemical effect of one protein upon another, for example, GTP-GDP exchange activity or phosphorylation of a substrate by a kinase. The bait protein executes the activity on the substrate hit protein. A Modification value is recorded for interactions of this type with the possible values Phosphorylation, Ubiquitination, Sumoylation, Dephosphorylation, Methylation, Prenylation, Acetylation, Deubiquitination, Proteolytic Processing, Glucosylation, Nedd(Rub1)ylation, Deacetylation, No Modification, Demethylation. | High | - | BioGRID | 151950 | |
| CDC28 SWI5 | Dosage Lethality Dosage Lethality A genetic interaction is inferred when over expression or increased dosage of one gene causes lethality in a strain that is mutated or deleted for another gene. | High | - | BioGRID | 2202703 | |
| CDC28 SWI5 | PCA PCA A Protein-Fragment Complementation Assay (PCA) is a protein-protein interaction assay in which a bait protein is expressed as fusion to one of the either N- or C- terminal peptide fragments of a reporter protein and prey protein is expressed as fusion to the complementary N- or C- terminal fragment of the same reporter protein. Interaction of bait and prey proteins bring together complementary fragments, which can then fold into an active reporter, e.g. the split-ubiquitin assay. | Low | - | BioGRID | - | |
| CDC28 SWI5 | 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. | High | - | BioGRID | - |
Curated By
- BioGRID