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VID22 protein (Saccharomyces cerevisiae) - STRING interaction network
"VID22" - Glycosylated integral membrane protein localized to the plasma membrane in Saccharomyces cerevisiae
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second shell of interactors
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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VID22Glycosylated integral membrane protein localized to the plasma membrane; plays a role in fructose-1,6-bisphosphatase (FBPase) degradation; involved in FBPase transport from the cytosol to Vid (vacuole import and degradation) vesicles; Has a role in the negative regulation of gluconeogenesis. Imports fructose-1,6-bisphosphatase (FBPase) into the intermediate vacuole import and degradation (Vid) vesicles. This is an indirect role and requires cyclophilin A (901 aa)    
Predicted Functional Partners:
TBF1
Telobox-containing general regulatory factor; binds TTAGGG repeats within subtelomeric anti-silencing regions (STARs), blocking silent chromatin propagation; binds majority of snoRNA gene promoters, required for full snoRNA expression; caps DSB flan /.../ long T2AG3 repeats and blocks checkpoint activation; Binds the telomeric double-stranded TTAGGG repeat and negatively regulates telomere length. Involved in the regulation of gene expression. 52 binding sites have been identified, distributed over 15 chromosomes. A member of the general regulatory factors (GRFs) which act as genome pa [...] (562 aa)
       
 
  0.923
ENV11
Protein proposed to be involved in vacuolar functions; mutant shows defect in CPY processing and fragmented vacuoles; deletion mutant has increased glycogen accumulation and displays elongated buds; green fluorescent protein (GFP)-fusion protein loc /.../ to the nucleus; Involved in vacuolar processing and morphology (860 aa)
       
 
0.758
VID24
Peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase; Has a role in the negative regulation of gluconeogenesis. Required for both proteasome-dependent and vacuolar catabolite degradation of fructose-1,6-bisphosphatase (FBPase). Probably regulates FBPase targeting from the FBPase- containing vesicles to the vacuole (362 aa)
           
  0.738
BRE5
Ubiquitin protease cofactor, forms deubiquitination complex with Ubp3p that coregulates anterograde and retrograde transport between the endoplasmic reticulum and Golgi compartments; null is sensitive to brefeldin A; Has a role in de-ubiquitination. In conjunction with UBP3, cleaves ubiquitin, leading to the subsequent mono- ubiquitination of sec23 (515 aa)
       
 
  0.693
YLR374C
Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data; partially overlaps the uncharacterized ORF STP3/YLR375W (129 aa)
           
  0.640
FBP1
Fructose-1,6-bisphosphatase, key regulatory enzyme in the gluconeogenesis pathway, required for glucose metabolism; undergoes either proteasome-mediated or autophagy-mediated degradation depending on growth conditions; interacts with Vid30p (348 aa)
           
  0.637
UBC1
Ubiquitin-conjugating enzyme that mediates selective degradation of short-lived and abnormal proteins; plays a role in vesicle biogenesis and ER-associated protein degradation (ERAD); component of the cellular stress response; Catalyzes the covalent attachment of ubiquitin to other proteins. Functions in degradation of misfolded or regulated proteins localized in the endoplasmic reticulum (ER) lumen or membrane via the ubiquitin-proteasome system. Cognate E2 conjugating enzyme for the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rap [...] (215 aa)
       
 
  0.593
SEC28
Epsilon-COP subunit of the coatomer; regulates retrograde Golgi-to-ER protein traffic; stabilizes Cop1p, the alpha-COP and the coatomer complex; non-essential for cell growth; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (296 aa)
       
 
  0.578
SSA2
ATP binding protein involved in protein folding and vacuolar import of proteins; member of heat shock protein 70 (HSP70) family; associated with the chaperonin-containing T-complex; present in the cytoplasm, vacuolar membrane and cell wall; 98% iden /.../with Ssa1p, but subtle differences between the two proteins provide functional specificity with respect to propagation of yeast [URE3] prions and vacuolar-mediated degradations of gluconeogenesis enzymes; May play a role in the transport of polypeptides both across the mitochondrial membranes and into the endoplasmic reticulum. A funct [...] (639 aa)
       
 
  0.547
PSD1
Phosphatidylserine decarboxylase of the mitochondrial inner membrane, converts phosphatidylserine to phosphatidylethanolamine; Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine (PubMed-8227017, PubMed-8407984, PubMed-17976194, PubMed-23124206, PubMed-25829489). Phosphatidylethanolamine formed in the mitochondria is exported to other membranes to fullfill their requirements for PtdEtn (PubMed-8530379, PubMed-11294902). Required for norm [...] (500 aa)
       
 
  0.465
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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