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:
a 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:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
GCG1Glutathione-specific gamma-glutamylcyclotransferase; Gamma-glutamyl cyclotransferase; cleaves the gamma-glutamyl bond of glutathione to yield 5-oxoproline and a Cys-Gly dipeptide; similar to mammalian pro-apoptotic protein ChaC1; expression of mouse ChaC1 in yeast increases apoptosis; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and nucleus; periodically expressed during the metabolic cycle. (232 aa)    
Predicted Functional Partners:
ECM38
Glutathione hydrolase heavy chain; Gamma-glutamyltranspeptidase; major glutathione-degrading enzyme; involved in detoxification of electrophilic xenobiotics; expression induced mainly by nitrogen starvation.
   
 
 0.938
OXP1
5-oxoprolinase; enzyme is ATP-dependent and functions as a dimer; similar to mouse Oplah gene; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; protein abundance increases in response to DNA replication stress.
     
 0.920
GSH2
Glutathione synthetase; catalyzes the ATP-dependent synthesis of glutathione (GSH) from gamma-glutamylcysteine and glycine; induced by oxidative stress and heat shock.
     
 0.918
DUG1
Cys-Gly metallodipeptidase DUG1; Cys-Gly metallo-di-peptidase; forms a complex with Dug2p and Dug3p to degrade glutathione (GSH) and other peptides containing a gamma-glu-X bond in an alternative pathway to GSH degradation by gamma-glutamyl transpeptidase (Ecm38p); human homolog CNDP2 can complement yeast dug1 mutant.
     
 0.909
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.
   
 
 0.906
GTT1
ER associated glutathione S-transferase; capable of homodimerization; glutathione transferase for Yvc1p vacuolar cation channel; expression induced during the diauxic shift and throughout stationary phase; functional overlap with Gtt2p, Grx1p, and Grx2p.
   
 
  0.901
URE2
Nitrogen catabolite repression transcriptional regulator; inhibits GLN3 transcription in good nitrogen source; role in sequestering Gln3p and Gat1p to the cytoplasm; has glutathione peroxidase activity and can mutate to acquire GST activity; self-assembly under limited nitrogen conditions creates [URE3] prion and releases catabolite repression.
   
 
  0.900
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.
     
  0.900
JJJ1
J protein JJJ1; Co-chaperone that stimulates the ATPase activity of Ssa1p; required for a late step of ribosome biogenesis; associated with the cytosolic large ribosomal subunit; contains a J-domain; mutation causes defects in fluid-phase endocytosis.
 
      0.859
YER010C
Bifunctional HMG aldolase/oxaloacetate decarboxylase; requires divalent metal ions for activity; competitively inhibited by oxalate; forms a ring-shaped homotrimer; similar to members of the prokaryotic RraA family of class II (divalent metal ion dependent) pyruvate aldolases from the meta cleavage pathways of protocatechuate and gallate.
   
  
 0.807
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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