BAIT

CDC28

CDK1, HSL5, SRM5, cyclin-dependent serine/threonine-protein kinase CDC28, L000000267, YBR160W
Cyclin-dependent kinase (CDK) catalytic subunit; master regulator of mitotic and meiotic cell cycles; alternately associates with G1 (CLNs), S and G2/M (CLBs) phase cyclins, which provide substrate specificity; regulates cell cycle and basal transcription, chromosome duplication and segregation, lipid biosynthesis, membrane trafficking, polarized growth, and morphogenesis; abundance increases in DNA replication stress; transcript induction in osmostress involves antisense RNA
GO Process (24)
GO Function (5)
GO Component (8)
Saccharomyces cerevisiae (S288c)
PREY

LRS4

L000004395, YDR439W
Nucleolar protein that forms a complex with Csm1p; and then Mam1p at kinetochores during meiosis I to mediate accurate homolog segregation; required for condensin recruitment to the replication fork barrier site and rDNA repeat segregation
GO Process (4)
GO Function (0)
GO Component (3)
Saccharomyces cerevisiae (S288c)

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

Targets of the cyclin-dependent kinase Cdk1.

Ubersax JA, Woodbury EL, Quang PN, Paraz M, Blethrow JD, Shah K, Shokat KM, Morgan DO

The events of cell reproduction are governed by oscillations in the activities of cyclin-dependent kinases (Cdks). Cdks control the cell cycle by catalysing the transfer of phosphate from ATP to specific protein substrates. Despite their importance in cell-cycle control, few Cdk substrates have been identified. Here, we screened a budding yeast proteomic library for proteins that are directly phosphorylated by ... [more]

Nature Oct. 23, 2003; 425(6960);859-64 [Pubmed: 14574415]

Throughput

  • High Throughput

Additional Notes

  • A yeast proteomic library was screened for proteins that are directly phosphorylated by Cdk1 Clb2 complexes in whole-cell extracts.
  • Complex with cyclin Clb2

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CDC28 LRS4
Affinity Capture-MS
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.

High-BioGRID
1276938

Curated By

  • BioGRID