BAIT

TWF1

L000004372, YGR080W
Twinfilin; highly conserved actin monomer-sequestering protein involved in regulation of the cortical actin cytoskeleton; coordinates actin filament severing and monomer sequestering at sites of rapid actin turnover; composed of two cofilin-like regions, localizes actin monomers to sites of rapid filament assembly
Saccharomyces cerevisiae (S288c)
PREY

SRV2

CAP, L000002068, YNL138W
CAP (cyclase-associated protein); N-terminus binds adenylate cyclase and facilitates activation by RAS; N-terminus forms novel hexameric star-shaped shuriken structures that directly catalyze cofilin-mediated severing of actin filaments; C-terminus, in physically and genetically separate activity, binds and recycles cofilin bound, ADP-actin monomers, facilitating regulation of actin dynamics and cell morphogenesis
GO Process (3)
GO Function (2)
GO Component (2)
Saccharomyces cerevisiae (S288c)

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.

Publication

A global protein kinase and phosphatase interaction network in yeast.

Breitkreutz A, Choi H, Sharom JR, Boucher L, Neduva V, Larsen B, Lin ZY, Breitkreutz BJ, Stark C, Liu G, Ahn J, Dewar-Darch D, Reguly T, Tang X, Almeida R, Qin ZS, Pawson T, Gingras AC, Nesvizhskii AI, Tyers M

The interactions of protein kinases and phosphatases with their regulatory subunits and substrates underpin cellular regulation. We identified a kinase and phosphatase interaction (KPI) network of 1844 interactions in budding yeast by mass spectrometric analysis of protein complexes. The KPI network contained many dense local regions of interactions that suggested new functions. Notably, the cell cycle phosphatase Cdc14 associated with ... [more]

Science May. 21, 2010; 328(5981);1043-6 [Pubmed: 20489023]

Quantitative Score

  • 1.0 [Saint Score]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
SRV2 TWF1
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-0.2745BioGRID
2009443
TWF1 SRV2
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-0.1905BioGRID
2044829
TWF1 SRV2
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
-
SRV2 TWF1
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
SRV2 TWF1
Synthetic Lethality
Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Low-BioGRID
2386149

Curated By

  • BioGRID