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EUG1 protein (Saccharomyces cerevisiae) - STRING interaction network
"EUG1" - Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p in Saccharomyces cerevisiae
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Predicted Interactions
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EUG1Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER; Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low (517 aa)    
Predicted Functional Partners:
CNE1
Calnexin; integral membrane ER chaperone involved in folding and quality control of glycoproteins; chaperone activity is inhibited by Mpd1p, with which Cne1p interacts; 24% identical to mammalian calnexin; Ca+ binding not yet shown in yeast; Interacts with newly synthesized glycoproteins in the endoplasmic reticulum. It may act in assisting protein assembly and/or in the retention within the ER of unassembled protein subunits. It seems to play a major role in the quality control apparatus of the ER by the retention of incorrectly folded proteins (502 aa)
     
  0.989
ERO1
Thiol oxidase required for oxidative protein folding in the endoplasmic reticulum; Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves elect [...] (563 aa)
     
  0.983
GPX1
Phospholipid hydroperoxide glutathione peroxidase induced by glucose starvation that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress; May constitute a glutathione peroxidase-like protective system against oxidative stresses (167 aa)
   
  0.960
HYR1
Thiol peroxidase that functions as a hydroperoxide receptor to sense intracellular hydroperoxide levels and transduce a redox signal to the Yap1p transcription factor; Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cere [...] (163 aa)
   
  0.960
GLT1
NAD(+)-dependent glutamate synthase (GOGAT), synthesizes glutamate from glutamine and alpha-ketoglutarate; with Gln1p, forms the secondary pathway for glutamate biosynthesis from ammonia; expression regulated by nitrogen source; Forms L-glutamate from L-glutamine and 2-oxoglutarate. Represents an alternative pathway to L-glutamate dehydrogenase for the biosynthesis of L-glutamate. Participates with glutamine synthetase in ammonia assimilation processes. The enzyme is specific for NADH, L-glutamine and 2-oxoglutarate (2145 aa)
   
 
  0.957
GTB1
Glucosidase II beta subunit, forms a complex with alpha subunit Rot2p, involved in removal of two glucose residues from N-linked glycans during glycoprotein biogenesis in the ER; Subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins. Specifically required for the cleavage of the final glucose (702 aa)
     
  0.954
PDI1
Protein disulfide isomerase; multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds; forms a complex with Mnl /.../t has exomannosidase activity, processing unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2 which promotes degradation in the unfolded protein response; Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bon [...] (522 aa)
       
0.953
ROT2
Glucosidase II catalytic subunit required for normal cell wall synthesis; mutations in rot2 suppress tor2 mutations, and are synthetically lethal with rot1 mutations; Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (954 aa)
     
  0.951
LHS1
Molecular chaperone of the endoplasmic reticulum lumen, involved in polypeptide translocation and folding; nucleotide exchange factor for the ER lumenal Hsp70 chaperone Kar2p; regulated by the unfolded protein response pathway; Chaperone required for protein translocation and folding in the endoplasmic reticulum (881 aa)
   
 
  0.944
MPD2
Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p; Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1 (277 aa)
     
 
  0.930
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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