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
TOS4
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
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 TOS4 | 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 | 1114827 | |
| CDC28 TOS4 | 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 | 151941 |
Curated By
- BioGRID