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HYR1 protein (Saccharomyces cerevisiae) - STRING interaction network
"HYR1" - Thiol peroxidase that functions as a hydroperoxide receptor to sense intracellular hydroperoxide levels and transduce a redox signal to the Yap1p transcription factor in Saccharomyces cerevisiae
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Predicted Interactions
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textmining
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HYR1Thiol 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)    
Predicted Functional Partners:
GTT1
ER associated glutathione S-transferase capable of homodimerization; expression induced during the diauxic shift and throughout stationary phase; functional overlap with Gtt2p, Grx1p, and Grx2p (234 aa)
     
 
  0.994
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)
   
  0.973
GSH2
Glutathione synthetase, catalyzes the ATP-dependent synthesis of glutathione (GSH) from gamma-glutamylcysteine and glycine; induced by oxidative stress and heat shock (491 aa)
         
  0.972
URE2
Nitrogen catabolite repression transcriptional regulator that acts by inhibition of GLN3 transcription in good nitrogen source; has glutathione peroxidase activity and can mutate to acquire GST activity; altered form creates [URE3] prion; Plays an important role in nitrogen catabolite repression. Down-regulates the expression of many genes involved in nitrogen utilization by inhibiting the GATA transcriptional activators GLN3 and GAT1. Under good nitrogen conditions, binds to the phosphorylated forms of GLN3 and GAT1 and sequesters them in the cytoplasm, preventing transcription of gen [...] (354 aa)
     
 
  0.970
EUG1
Protein 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)
   
  0.960
GLR1
Cytosolic and mitochondrial glutathione oxidoreductase, converts oxidized glutathione to reduced glutathione; mitochondrial but not cytosolic form has a role in resistance to hyperoxia; Maintains high levels of reduced glutathione in the cytosol (483 aa)
   
 
  0.943
SOD2
Mitochondrial manganese superoxide dismutase; protects cells against oxygen toxicity; Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems (233 aa)
     
  0.936
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)
     
 
  0.932
TRX2
Cytoplasmic thioredoxin isoenzyme of the thioredoxin system which protects cells against oxidative and reductive stress, forms LMA1 complex with Pbi2p, acts as a cofactor for Tsa1p, required for ER-Golgi transport and vacuole inheritance; Participates as a hydrogen donor in redox reactions through the reversible oxidation of its active center dithiol to a disulfide, accompanied by the transfer of 2 electrons and 2 protons. It is involved in many cellular processes, including deoxyribonucleotide synthesis, repair of oxidatively damaged proteins, protein folding, sulfur metabolism, and r [...] (104 aa)
   
 
  0.931
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)
     
  0.931
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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