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EMC3 protein (Saccharomyces cerevisiae) - STRING interaction network
"EMC3" - 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
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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EMC3Member 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)    
Predicted Functional Partners:
EMC1
Member 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)
     
  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)
     
  0.995
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)
       
  0.988
SOP4
ER-membrane protein; suppressor of pma1-7, deletion of SOP4 slows down the export of wild-type Pma1p and Pma1-7 from the ER; Involved in the export of PMA1, possibly through the monitoring or assisting of PMA1 folding and acquisition of competence to enter vesicles (234 aa)
       
 
  0.948
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
EMC10
Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the endoplasmic reticulum; YDR056C is not an essential protein (205 aa)
       
 
  0.671
DER1
Endoplasmic reticulum membrane protein, required for ER-associated protein degradation of misfolded or unassembled proteins; N- and C- termini protrude into the cytoplasm, has similarity to Dfm1p; Component of the endoplasmic reticulum-associated degradation (ERAD) pathway. Specifically required for the ERAD-L pathway which mediates the degradation of proteins with misfolded lumenal domains within the endoplasmic reticulum (211 aa)
       
 
  0.627
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)
       
      0.602
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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