STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
some 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
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Gene Fusion
Cooccurence
Coexpression
Experiments
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[Homology]
Score
DOT5Peroxiredoxin DOT5; Nuclear thiol peroxidase; functions as an alkyl-hydroperoxide reductase during post-diauxic growth; Belongs to the peroxiredoxin family. BCP/PrxQ subfamily (215 aa)    
Predicted Functional Partners:
AHP1
Thiol-specific peroxiredoxin; reduces hydroperoxides to protect against oxidative damage; function in vivo requires covalent conjugation to Urm1p
   
  
 0.982
TSA2
Peroxiredoxin 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; protein abundance increases in response to DNA replication stress; TSA2 has a paralog, TSA1, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily
  
 
 0.974
TSA1
Peroxiredoxin TSA1; Thioredoxin peroxidase; acts as both ribosome-associated and free cytoplasmic antioxidant; self-associates to form high-molecular weight chaperone complex under oxidative stress; chaperone activity essential for growth in zinc deficiency; required for telomere length maintenance; binds and modulates Cdc19p activity; protein abundance increases, forms cytoplasmic foci during DNA replication stress; TSA1 has a paralog, TSA2, that arose from the whole genome duplication; Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily
  
 
 0.974
PRX1
Mitochondrial peroxiredoxin with thioredoxin peroxidase activity; has a role in reduction of hydroperoxides; reactivation requires Trr2p and glutathione; induced during respiratory growth and oxidative stress; phosphorylated; protein abundance increases in response to DNA replication stress
  
 
 0.923
MRPL7
Mitochondrial 54s ribosomal protein yml7/yml5; Mitochondrial ribosomal protein of the large subunit; MRPL7 produces both YmL5 and YmL7, which are two different modified forms of the same protein
   
    0.896
YNL122C
54S ribosomal protein bL35m; Mitochondrial ribosomal protein of the large subunit; homologous to bacterial L35 and human MRPL35 ribosomal proteins
  
    0.892
SRX1
Sulfiredoxin; contributes to oxidative stress resistance by reducing cysteine-sulfinic acid groups in the peroxiredoxin Tsa1p, which is formed upon exposure to oxidants; conserved in higher eukaryotes; protein abundance increases in response to DNA replication stress
      
 0.875
GLR1
Cytosolic and mitochondrial glutathione oxidoreductase; converts oxidized glutathione to reduced glutathione; cytosolic Glr1p is the main determinant of the glutathione redox state of the mitochondrial intermembrane space; mitochondrial Glr1p has a role in resistance to hyperoxia; protein abundance increases in response to DNA replication stress
  
  
 0.832
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; protein abundance increases in response to DNA replication stress; TRR1 has a paralog, TRR2, that arose from the whole genome duplication; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family
  
  
 0.828
GPX1
Glutathione peroxidase-like peroxiredoxin 1; Phospholipid hydroperoxide glutathione peroxidase; induced by glucose starvation that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress; GPX1 has a paralog, HYR1, that arose from the whole genome duplication
  
  
 0.822
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.