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ENT3 protein (Saccharomyces cerevisiae) - STRING interaction network
"ENT3" - Protein containing an N-terminal epsin-like domain involved in clathrin recruitment and traffic between the Golgi and endosomes in Saccharomyces cerevisiae
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Predicted Interactions
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protein homology
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ENT3Protein containing an N-terminal epsin-like domain involved in clathrin recruitment and traffic between the Golgi and endosomes; associates with the clathrin adaptor Gga2p; Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol- 3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB) (408 aa)    
Predicted Functional Partners:
CHC1
Clathrin heavy chain, subunit of the major coat protein involved in intracellular protein transport and endocytosis; two heavy chains form the clathrin triskelion structural component; the light chain (CLC1) is thought to regulate function; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi (1653 aa)
     
  0.992
CLC1
Clathrin light chain, subunit of the major coat protein involved in intracellular protein transport and endocytosis; thought to regulate clathrin function; two Clathrin heavy chains (CHC1) form the clathrin triskelion structural component; Clathrin is the major protein of the polyhedral coat of coated pits and vesicles. In yeast, it is involved in the retention of proteins in an intracellular membrane compartment, presumably the trans-Golgi. The yeast light chain is important for cell growth. The light chain may help to properly orient the assembly/ disassembly of the clathrin coats (233 aa)
       
  0.988
VTI1
Protein involved in cis-Golgi membrane traffic; v-SNARE that interacts with two t-SNARES, Sed5p and Pep12p; required for multiple vacuolar sorting pathways; t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse (217 aa)
     
 
  0.987
ENT5
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, clathrin adaptor complex AP-1, and clathrin; Involved in the recruitment of clathrin to the Golgi network and endosomes to form clathrin coated vesicles. Plays a role in the trafficking of clathrin between the Golgi network and endosomes. Binds to membranes enriched in phosphatidylinositol- 3,5-bisphosphate (PtdIns(3,5)P2) and, in association with VPS27, is involved in protein sorting at the multivesicular body (MVB) (411 aa)
       
0.979
APL3
Alpha-adaptin, large subunit of the clathrin associated protein complex (AP-2); involved in vesicle mediated transport; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Alpha adaptin is a subunit of the plasma membrane adaptor. Facilitates interaction between APL1 and APS2 (1025 aa)
     
  0.975
APL4
Gamma-adaptin, large subunit of the clathrin-associated protein (AP-1) complex; binds clathrin; involved in vesicle mediated transport; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin (832 aa)
     
  0.964
DSK2
Nuclear-enriched ubiquitin-like polyubiquitin-binding protein, required for spindle pole body (SPB) duplication and for transit through the G2/M phase of the cell cycle, involved in proteolysis, interacts with the proteasome; Involved, with RAD23 in spindle pole body duplication. Involved in the ubiquitin-proteasome proteolytic pathway (373 aa)
       
    0.953
SEC13
Component of the Nup84 nuclear pore sub-complex, the Sec13p-Sec31p complex of the COPII vesicle coat, and the SEA (Seh1-associated) complex; required for vesicle formation in ER to Golgi transport and nuclear pore complex organization; the Nup84 sub /.../x has a role in transcription elongation; Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double- membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral [...] (297 aa)
       
  0.928
APL1
Beta-adaptin, large subunit of the clathrin associated protein complex (AP-2); involved in vesicle mediated transport; similar to mammalian beta-chain of the clathrin associated protein complex; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Beta adaptin is a subunit of the plasma membrane adaptor (700 aa)
     
  0.918
SEC31
Component of the Sec13p-Sec31p complex of the COPII vesicle coat, required for vesicle formation in ER to Golgi transport; mutant has increased aneuploidy tolerance; Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules (1273 aa)
     
 
  0.918
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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