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EMC1 protein (Saccharomyces cerevisiae) - STRING interaction network
"EMC1" - Member of a transmembrane complex required for efficient folding of proteins in the ER in Saccharomyces cerevisiae
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second shell of interactors
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Known Interactions
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experimentally determined
Predicted Interactions
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gene co-occurrence
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textmining
co-expression
protein homology
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EMC1Member of a transmembrane complex required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; interacts with Gal80p; The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER) (760 aa)    
Predicted Functional Partners:
EMC3
Member of a transmembrane complex required for efficient folding of proteins in the ER; required for respiratory growth; null mutant displays induction of the unfolded protein response; The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER) (253 aa)
     
  0.999
EMC2
Member of a transmembrane complex required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER) (292 aa)
     
  0.999
EMC4
Member of a transmembrane complex required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; human ortholog TMEM85 may function in apoptosis; The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER) (190 aa)
       
  0.999
EMC6
Member of a transmembrane complex required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response; The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER) (108 aa)
       
  0.994
EMC5
Member of a transmembrane complex required for efficient folding of proteins in the ER; null mutant displays induction of the unfolded protein response, and also shows K1 killer toxin resistance; The EMC seems to be required for efficient folding of proteins in the endoplasmic reticulum (ER) (141 aa)
       
  0.981
UBC7
Ubiquitin conjugating enzyme, involved in the ER-associated protein degradation pathway; requires Cue1p for recruitment to the ER membrane; proposed to be involved in chromatin assembly; 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 DOA10 ubiquitin ligase complex, which is part of the ERAD-C pathway responsible for the rapid degradation of membrane proteins with misfolded [...] (165 aa)
       
 
  0.900
PTK2
Putative serine/threonine protein kinase involved in regulation of ion transport across plasma membrane; enhances spermine uptake; Essential determinant for high-affinity spermidine transport. Required for the activation of the plasma membrane proton pump PMA1 via phosphorylation of ’Ser-899’ (818 aa)
       
      0.795
CUZ1
Putative protein of unknown function; contains a DHHC domain and an AN1-type zinc finger; predicted to have thiol-disulfide oxidoreductase active site; transcriptionally regulated by Rpn4p along with proteasome subunit genes; putative ortholog of hu /.../RAP, which stimulates proteasome activity in response to arsenic; May have a role in the ubiquitin-proteasome system (UPS) protecting cells from metalloid-induced proteotoxicity (274 aa)
       
      0.749
YHR180W
Dubious open reading frame unlikely to encode a protein, based on available experimental and comparative sequence data (163 aa)
           
  0.678
ELO1
Elongase I, medium-chain acyl elongase, catalyzes carboxy-terminal elongation of unsaturated C12-C16 fatty acyl-CoAs to C16-C18 fatty acids; Component of a microsomal membrane bound medium-chain fatty acid elongation system, which extends medium-chain-length fatty acids to long-chain fatty acids. Component of elongase I, which extends 12-16-carbon fatty acyl-CoAs such as lauroyl-CoA to 14-18-carbon fatty acids by incorporation of malonyl-CoA (310 aa)
       
      0.673
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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