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GRX7 protein (Saccharomyces cerevisiae) - STRING interaction network
"GRX7" - Cis-golgi localized monothiol glutaredoxin in Saccharomyces cerevisiae
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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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GRX7Cis-golgi localized monothiol glutaredoxin; more similar in activity to dithiol than other monothiol glutaredoxins; involved in the oxidative stress response; does not bind metal ions; functional overlap with GRX6 (203 aa)    
Predicted Functional Partners:
TRR1
Cytoplasmic thioredoxin reductase, key regulatory enzyme that determines the redox state of the thioredoxin system, which acts as a disulfide reductase system and protects cells against both oxidative and reductive stress; Acts on thioredoxins 1 and 2 (319 aa)
   
 
  0.845
TRR2
Mitochondrial thioredoxin reductase involved in protection against oxidative stress, required with Glr1p to maintain the redox state of Trx3p; contains active-site motif (CAVC) present in prokaryotic orthologs; binds NADPH and FAD; Acts on mitochondrial thioredoxin 3. Implicated in the defense against oxidative stress (342 aa)
   
 
  0.832
GRX3
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; monothiol glutaredoxin subfamily member along with Grx4p and Grx5p; protects cells from oxidative damage; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable) (285 aa)
   
 
  0.825
GRX1
Hydroperoxide and superoxide-radical responsive heat-stable glutathione-dependent disulfide oxidoreductase with active site cysteine pair; protects cells from oxidative damage; Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it is also involved in reducing cytosolic protein- and non-pro [...] (110 aa)
       
 
  0.820
GRX5
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; mitochondrial matrix protein involved in the synthesis/assembly of iron-sulfur centers; monothiol glutaredoxin subfamily member along with Grx3p and Grx4p; Monothiol glutaredoxin involved in iron-sulfur biogenesis. Required for normal iron homeostasis. Protects cells against oxidative damage due to reactive oxygen species (150 aa)
   
 
  0.733
GRX4
Hydroperoxide and superoxide-radical responsive glutathione-dependent oxidoreductase; monothiol glutaredoxin subfamily member along with Grx3p and Grx5p; protects cells from oxidative damage; mutant has increased aneuploidy tolerance; Monothiol glutaredoxin involved in the biogenesis of iron-sulfur clusters (By similarity). Binds one iron-sulfur cluster per dimer. The iron-sulfur cluster is bound between subunits, and is complexed by a bound glutathione and a cysteine residue from each subunit (Probable) (244 aa)
   
 
  0.718
GRX2
Cytoplasmic glutaredoxin, thioltransferase, glutathione-dependent disulfide oxidoreductase involved in maintaining redox state of target proteins, also exhibits glutathione peroxidase activity, expression induced in response to stress; Component of the glutathione system which performs several activities such as glutathione-dependent oxidoreductase, glutathione peroxidase and glutathione S-transferase (GST) activity. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase. In addition, it [...] (143 aa)
       
 
0.688
TRX3
Mitochondrial thioredoxin, highly conserved oxidoreductase required to maintain the redox homeostasis of the cell, forms the mitochondrial thioredoxin system with Trr2p, redox state is maintained by both Trr2p and Glr1p (127 aa)
   
   
  0.650
GRX8
Glutaredoxin that employs a dithiol mechanism of catalysis; monomeric; activity is low and null mutation does not affect sensitivity to oxidative stress; GFP-fusion protein localizes to the cytoplasm; expression strongly induced by arsenic; Glutathione-dependent oxidoreductase with lower activity compared to the other members of the glutaredoxin family. The disulfide bond functions as an electron carrier in the glutathione-dependent synthesis of deoxyribonucleotides by the enzyme ribonucleotide reductase (109 aa)
           
  0.642
HAM1
Conserved protein with deoxyribonucleoside triphosphate pyrophosphohydrolase activity, mediates exclusion of noncanonical purines from deoxyribonucleoside triphosphate pools; mutant is sensitive to the base analog 6-N-hydroxylaminopurine; Pyrophosphatase that hydrolyzes the non-canonical purine nucleotides inosine triphosphate (ITP), deoxyinosine triphosphate (dITP) as well as 2’-deoxy-N-6-hydroxylaminopurine triposphate (dHAPTP) and 5-bromodeoxyuridine 5’-triphosphate (BrdUTP) to their respective monophosphate derivatives. Xanthosine 5’-triphosphate (XTP) is also a potential substrate [...] (197 aa)
     
 
    0.624
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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