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
Kinome Project (Sc)
Saccharomyces cerevisiae (S288c)
PREY

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
Kinome Project (Sc)
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

A systematic survey identifies prions and illuminates sequence features of prionogenic proteins.

Alberti S, Halfmann R, King O, Kapila A, Lindquist S

Prions are proteins that convert between structurally and functionally distinct states, one or more of which is transmissible. In yeast, this ability allows them to act as non-Mendelian elements of phenotypic inheritance. To further our understanding of prion biology, we conducted a bioinformatic proteome-wide survey for prionogenic proteins in S. cerevisiae, followed by experimental investigations of 100 prion candidates. We ... [more]

Cell Apr. 03, 2009; 137(1);146-58 [Pubmed: 19345193]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CBK1 CBK1
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.

High-BioGRID
485928
CBK1 CBK1
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.

Low-BioGRID
-

Curated By

  • BioGRID