BAIT

CDC14

OAF3, phosphoprotein phosphatase CDC14, L000000254, YFR028C
Protein phosphatase required for mitotic exit; required for rDNA segregation, cytokinesis, meiosis I spindle disassembly, and environmental stress response; maintained in nucleolus by Cdc55p in early meiosis until liberated by the FEAR and Mitotic Exit Network in anaphase, enabling it to effect a decrease in CDK/B-cyclin activity and mitotic exit; sequestered in metaphase II, then released again upon entry into anaphase II
Saccharomyces cerevisiae (S288c)
PREY

INN1

YNL152W
Essential protein that associates with contractile actomyosin ring; required for ingression of the plasma membrane into the bud neck during cytokinesis; C2 domain, a membrane targeting module, is required for function; activates chitin synthase activity of Chs2p during cytokinesis
GO Process (3)
GO Function (2)
GO Component (3)
Saccharomyces cerevisiae (S288c)

Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Publication

Cdc14-dependent dephosphorylation of Inn1 contributes to Inn1-Cyk3 complex formation.

Palani S, Meitinger F, Boehm ME, Lehmann WD, Pereira G

In Saccharomyces cerevisiae, the Cdc14 phosphatase plays a well-established role in reverting phosphorylation events on substrates of the mitotic cyclin-dependent kinase (M-Cdk1), thereby promoting mitotic exit and down-regulation of M-Cdk1 activity. Cdc14 localizes at the site of cell cleavage after M-Cdk1 inactivation, suggesting that Cdc14 may perform a critical, yet ill-defined, role during cytokinesis. Here, we identified Inn1, as a ... [more]

Unknown Mar. 27, 2012; 0(0); [Pubmed: 22454527]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
CDC14 INN1
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
644386
INN1 CDC14
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.1517BioGRID
1949088
INN1 CDC14
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.

Low-BioGRID
666171
CDC14 INN1
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
-
INN1 CDC14
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