BAIT

CBK1

serine/threonine protein kinase CBK1, L000004609, YNL161W
Serine/threonine protein kinase of the the RAM signaling network; Ndr/LATS family member; binds regulatory subunit Mob2p; involved in regulation of cellular morphogenesis, polarized growth, and septum destruction; phosphorylation by Cbk1p regulates localization and activity of Ace2p transcription factor and Ssd1p translational repressor; Cbk1p activity is regulated by both phosphorylation and specific localization; relocalizes to cytoplasm upon DNA replication stress
Saccharomyces cerevisiae (S288c)
PREY

WWM1

YFL010C
WW domain containing protein of unknown function; binds to Mca1p, a caspase-related protease that regulates H2O2-induced apoptosis; overexpression causes G1 phase growth arrest and clonal death that is suppressed by overexpression of MCA1
GO Process (0)
GO Function (0)
GO Component (3)

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

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.

Publication

Diverse protein kinase interactions identified by protein microarrays reveal novel connections between cellular processes.

Fasolo J, Sboner A, Sun MG, Yu H, Chen R, Sharon D, Kim PM, Gerstein M, Snyder M

Protein kinases are key regulators of cellular processes. In spite of considerable effort, a full understanding of the pathways they participate in remains elusive. We globally investigated the proteins that interact with the majority of yeast protein kinases using protein microarrays. Eighty-five kinases were purified and used to probe yeast proteome microarrays. One-thousand-twenty-three interactions were identified, and the vast majority ... [more]

Genes Dev. Apr. 01, 2011; 25(7);767-78 [Pubmed: 21460040]

Throughput

  • High Throughput

Additional Notes

  • High Throughput: Proteome microarrays were used to identify proteins that interact with protein kinases.

Curated By

  • BioGRID