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SNO4 protein (Saccharomyces cerevisiae) - STRING interaction network
"SNO4" - Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p in Saccharomyces cerevisiae
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Predicted Interactions
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SNO4Possible chaperone and cysteine protease, similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation; Catalyzes the conversion of methylglyoxal (MG) to D- lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient l [...] (237 aa)    
Predicted Functional Partners:
HSP32
Possible chaperone and cysteine protease with similarity to E. coli Hsp31 and S. cerevisiae Hsp31p, Hsp33p, and Sno4p; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson’s disease; Catalyzes the conversion of methylglyoxal (MG) to D- lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed-24706893) (237 aa)
   
 
0.939
HSP33
Possible chaperone and cysteine protease with similarity to E. coli Hsp31 and S. cerevisiae Hsp31p, Hsp32p, and Sno4p; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson’s disease; Catalyzes the conversion of methylglyoxal (MG) to D- lactate in a single glutathione (GSH)-independent step. May play a role in detoxifying endogenously produced glyoxals. Involved in protection against reactive oxygen species (ROS) (By similarity). Important for viability in stationary phase. May negatively regulate TORC1 in response to nutrient limitation (PubMed-24706893) (237 aa)
   
 
0.938
IMD2
Inosine monophosphate dehydrogenase, catalyzes the rate-limiting step in GTP biosynthesis, expression is induced by mycophenolic acid resulting in resistance to the drug, expression is repressed by nutrient limitatio; Catalyzes the conversion of inosine 5’-phosphate (IMP) to xanthosine 5’-phosphate (XMP), the first committed and rate- limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. In contrast to the other IMPDH alleles IMD3 and IMD4, the enzymatic activity of IMD2 seems to be intrinsically drug resistant (523 aa)
     
  0.909
IMD1
Nonfunctional protein with homology to IMP dehydrogenase; probable pseudogene, located close to the telomere; is not expressed at detectable levels; YAR073W and YAR075W comprise a continuous reading frame in some strains of S. cerevisiae (403 aa)
     
  0.909
URA2
Bifunctional carbamoylphosphate synthetase/aspartate transcarbamylase; catalyzes the first two enzymatic steps in the de novo biosynthesis of pyrimidines; both activities are subject to feedback inhibition by UTP; This protein is a "fusion" protein encoding three enzymatic activities of the pyrimidine pathway (GATase, CPSase, and ATCase) (2214 aa)
   
 
  0.861
PRX1
Mitochondrial peroxiredoxin (1-Cys Prx) with thioredoxin peroxidase activity, has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; Has a thioredoxin peroxidase activity with a role in reduction of hydroperoxides (261 aa)
   
 
  0.799
TSA1
Thioredoxin peroxidase, acts as both a ribosome-associated and free cytoplasmic antioxidant; self-associates to form a high-molecular weight chaperone complex under oxidative stress; deletion results in mutator phenotype; Physiologically important antioxidant which constitutes an enzymatic defense against sulfur-containing radicals. Can provide protection against a thiol-containing oxidation system but not against an oxidation system without thiol (196 aa)
   
 
  0.793
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)
     
 
  0.790
ARO1
Pentafunctional arom protein, catalyzes steps 2 through 6 in the biosynthesis of chorismate, which is a precursor to aromatic amino acids; The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis (1588 aa)
     
      0.788
TSA2
Stress inducible cytoplasmic thioredoxin peroxidase; cooperates with Tsa1p in the removal of reactive oxygen, nitrogen and sulfur species using thioredoxin as hydrogen donor; deletion enhances the mutator phenotype of tsa1 mutants; Reduces peroxides. May play an important role in eliminating peroxides generated during metabolism (By similarity) (196 aa)
   
 
  0.787
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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