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.
Knowledge-based Evidence
from curated databases
textmining
Assay-based Predictions
experimentally determined
co-expression
Genomic Predictions
gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
HSP31Glutathione-independent glyoxalase HSP31; Methylglyoxalase that converts methylglyoxal to D-lactate; involved in oxidative stress resistance, diauxic shift, and stationary phase survival; has similarity to E. coli Hsp31 and C. albicans Glx3p; member of the DJ-1/ThiJ/PfpI superfamily, which includes human DJ-1 involved in Parkinson's disease and cancer; exists as a dimer and contains a putative metal-binding site; protein abundance increases in response to DNA replication stress; Belongs to the peptidase C56 family. HSP31-like subfamily. (237 aa)    
Predicted Functional Partners:
SNO4
Probable glutathione-independent glyoxalase SNO4; Possible chaperone and cysteine protease; required for transcriptional reprogramming during the diauxic shift and for survival in stationary phase; similar to bacterial Hsp31 and yeast Hsp31p, Hsp32p, and Hsp33p; DJ-1/ThiJ/PfpI superfamily member; predicted involvement in pyridoxine metabolism; induced by mild heat stress and copper deprivation.
  
 
0.990
GLO1
Lactoylglutathione lyase; Monomeric glyoxalase I; catalyzes the detoxification of methylglyoxal (a by-product of glycolysis) via condensation with glutathione to produce S-D-lactoylglutathione; expression regulated by methylglyoxal levels and osmotic stress.
   
 0.977
GLO2
Hydroxyacylglutathione hydrolase, cytoplasmic isozyme; Cytoplasmic glyoxalase II; catalyzes the hydrolysis of S-D-lactoylglutathione into glutathione and D-lactate; GLO2 has a paralog, GLO4, that arose from the whole genome duplication.
   
 
 0.960
GRE2
3-methylbutanal reductase and NADPH-dependent methylglyoxal reductase; stress induced (osmotic, ionic, oxidative, heat shock and heavy metals); regulated by the HOG pathway; restores resistance to glycolaldehyde by coupling reduction of glycolaldehyde to ethylene glycol and oxidation of NADPH to NADP+; protein abundance increases in response to DNA replication stress; methylglyoxal reductase (NADPH-dependent) is also known as D-lactaldehyde dehydrogenase; Belongs to the NAD(P)-dependent epimerase/dehydratase family. Dihydroflavonol-4-reductase subfamily.
   
 0.950
GLO4
Hydroxyacylglutathione hydrolase, mitochondrial; Mitochondrial glyoxalase II; catalyzes the hydrolysis of S-D-lactoylglutathione into glutathione and D-lactate; GLO4 has a paralog, GLO2, that arose from the whole genome duplication.
   
 
 0.946
DLD2
D-2-hydroxyglutarate--pyruvate transhydrogenase DLD2; D-2-hydroxyglutarate dehydrogenase, and minor D-lactate dehydrogenase; mitochondrial matrix protein that oxidizes D-2-hydroxyglutarate (D-2HG), an oncometabolite, to alpha-ketoglutarate with a minor role in lactate catabolism; located in the mitochondrial matrix; Belongs to the FAD-binding oxidoreductase/transferase type 4 family.
   
 
  0.904
DLD3
D-2-hydroxyglutarate--pyruvate transhydrogenase DLD3; 2-hydroxyglutarate transhydrogenase, and minor D-lactate dehydrogenase; converts D-2-hydroxyglutarate (D-2HG), an oncometabolite, to alpha-ketoglutarate in the presence of FAD, with concomitant reduction of pyruvate to D-lactate; minor lactate dehydrogenase activity; component of the retrograde regulon that consists of genes whose expression are stimulated by damage to mitochondria and reduced in cells grown with glutamate as the sole nitrogen source; located in the cytoplasm.
   
 
  0.904
DLD1
Major mitochondrial D-lactate dehydrogenase; oxidizes D-lactate to pyruvate, transcription is heme-dependent, repressed by glucose, and derepressed in ethanol or lactate; located in the mitochondrial inner membrane.
   
 
  0.903
HSP104
Disaggregase; heat shock protein that cooperates with Ydj1p (Hsp40) and Ssa1p (Hsp70) to refold and reactivate previously denatured, aggregated proteins; responsive to stresses including: heat, ethanol, and sodium arsenite; involved in [PSI+] propagation; protein becomes more abundant and forms cytoplasmic foci in response to DNA replication stress; potentiated Hsp104p variants decrease TDP-43 proteotoxicity by eliminating its cytoplasmic aggregation; Belongs to the ClpA/ClpB family.
   
 
 0.835
DSD1
D-serine dehydratase (aka D-serine ammonia-lyase); converts D-serine to pyruvate and ammonia by a reaction dependent on pyridoxal 5'-phosphate and zinc; may play a role in D-serine detoxification; L-serine is not a substrate.
   
 
  0.811
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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