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
CDC23
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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
Phosphate-binding pocket on cyclin B governs CDK substrate phosphorylation and mitotic timing.
Cell cycle progression is governed by complexes of the cyclin-dependent kinases (CDKs) and their regulatory subunits cyclin and Cks1. CDKs phosphorylate hundreds of substrates, often at multiple sites. Multisite phosphorylation depends on Cks1, which binds initial priming phosphorylation sites to promote secondary phosphorylation at other sites. Here, we describe a similar role for a recently discovered phosphate-binding pocket (PP) on ... [more]
Throughput
- Low Throughput
Related interactions
| Interaction | Experimental Evidence Code | Dataset | Throughput | Score | Curated By | Notes |
|---|---|---|---|---|---|---|
| CDC28 CDC23 | 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 | 1035917 | |
| CDC28 CDC23 | 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 | 151302 | |
| CDC28 CDC23 | 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 | 3751318 | |
| CDC28 CDC23 | 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 | -0.2015 | BioGRID | 1921380 | |
| CDC23 CDC28 | 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 | -0.3587 | BioGRID | 1936820 | |
| CDC23 CDC28 | Synthetic Lethality Synthetic Lethality A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition. | Low | - | BioGRID | 157763 | |
| CDC28 CDC23 | Synthetic Lethality Synthetic Lethality A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition. | Low | - | BioGRID | 157782 |
Curated By
- BioGRID