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TRX2 protein (Saccharomyces cerevisiae) - STRING interaction network
"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 in Saccharomyces cerevisiae
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Known Interactions
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Predicted Interactions
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gene co-occurrence
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textmining
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protein homology
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TRX2Cytoplasmic 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)    
Predicted Functional Partners:
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)
   
  0.999
AHP1
Thiol-specific peroxiredoxin, reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p; Thiol-specific antioxidant protein with alkyl hydroperoxidase activity. Involved in osmotic stress resistance and detoxification of the cell. Preferentially eliminates organic peroxides rather than H(2)O(2). Involved in cellular Mn(2+) homeostasis (176 aa)
     
  0.999
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)
   
  0.999
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)
   
  0.998
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)
   
 
  0.997
SOD1
Cytosolic copper-zinc superoxide dismutase; some mutations are analogous to those that cause ALS (amyotrophic lateral sclerosis) in humans; Destroys radicals which are normally produced within the cells and which are toxic to biological systems (154 aa)
     
  0.994
MXR1
Methionine-S-sulfoxide reductase, involved in the response to oxidative stress; protects iron-sulfur clusters from oxidative inactivation along with MXR2; involved in the regulation of lifespan; Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reversible oxidation-reduction of methionine sulfoxide in proteins to methionine. Also able to reduce dimethyl sulfoxide (DMSO) as well, with DMS as the product (184 aa)
   
  0.994
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)
   
 
  0.981
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)
   
 
  0.980
BCK1
Mitogen-activated protein (MAP) kinase kinase kinase acting in the protein kinase C signaling pathway, which controls cell integrity; upon activation by Pkc1p phosphorylates downstream kinases Mkk1p and Mkk2p; Serine/threonine protein kinase involved in a signal transduction pathway that plays a role in yeast cell morphogenesis and cell growth. This pathway seems to start by SMP3; then involve the kinase PKC1 that may act on this kinase. BCK1 probably phosphorylates MKK1 and MKK2 which themselves phosphorylate the MPK1 kinase (1478 aa)
       
  0.967
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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