BAIT

VTI1

L000003598, YMR197C
Protein involved in cis-Golgi membrane traffic; v-SNARE that interacts with two t-SNARES, Sed5p and Pep12p; required for multiple vacuolar sorting pathways
GO Process (4)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

ENT3

YJR125C
Protein containing an N-terminal epsin-like domain; involved in clathrin recruitment and traffic between the Golgi and endosomes; associates with the clathrin adaptor Gga2p
Saccharomyces cerevisiae (S288c)

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.

Publication

Dissecting Ent3p: The ENTH domain binds different SNAREs via distinct amino acid residues while the C-terminus is sufficient for retrograde transport from endosomes.

Zimmermann J, Chidambaram S, Fischer von Mollard G

The epsin N-terminal homology (ENTH) domain protein Ent3p and the AP-180 N-terminal homology (ANTH) domain protein Ent5p serve as partially redundant adaptors in vesicle budding from the TGN in Saccharomyces cerevisiae. They interact with phosphoinositides, clathrin, adaptor proteins and cargo such as chitin synthase Chs3p and SNAREs. Here we show that ent3ent5 cells displayed defects in cell separation and bud-site ... [more]

Unknown Jul. 26, 2010; 0(0); [Pubmed: 20658963]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
VTI1 ENT3
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
-
ENT3 VTI1
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-0.5578BioGRID
2052671
VTI1 ENT3
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-0.663BioGRID
2006522
ENT3 VTI1
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-0.5209BioGRID
2438499
VTI1 ENT3
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
VTI1 ENT3
Reconstituted Complex
Reconstituted Complex

An interaction is detected between purified proteins in vitro.

Low-BioGRID
-
VTI1 ENT3
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
159069
VTI1 ENT3
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
-
VTI1 ENT3
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