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

KIN1

serine/threonine protein kinase KIN1, L000000901, YDR122W
Serine/threonine protein kinase involved in regulation of exocytosis; localizes to the cytoplasmic face of the plasma membrane; KIN1 has a paralog, KIN2, that arose from the whole genome duplication
Kinome Project (Sc)
GO Process (3)
GO Function (2)
GO Component (2)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)

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.

Publication

A constraint network of interactions: protein-protein interaction analysis of the yeast type II phosphatase Ptc1p and its adaptor protein Nbp2p.

Hruby A, Zapatka M, Heucke S, Rieger L, Wu Y, Nussbaumer U, Timmermann S, Duenkler A, Johnsson N

We used a generally applicable strategy to collect and structure the protein interactions of the yeast type II protein phosphatase Ptc1p and its binding partner Nbp2p. The procedure transformed primary unstructured protein interaction data into an ensemble of alternative interaction states. Certain combinations of proteins are allowed in different network configurations. Nbp2p serves as the network hub and brings seven ... [more]

J. Cell. Sci. Jan. 01, 2011; 124(0);35-46 [Pubmed: 21118957]

Throughput

  • High Throughput

Additional Notes

  • split-ubiquitin assay

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
KIN1 CBK1
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.

High1BioGRID
-
KIN1 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
485963

Curated By

  • BioGRID