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:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
GPM3Homolog of Gpm1p phosphoglycerate mutase; converts 3-phosphoglycerate to 2-phosphoglycerate in glycolysis; may be non-functional; GPM3 has a paralog, GPM2, that arose from the whole genome duplication; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily (303 aa)    
Predicted Functional Partners:
GPM2
Homolog of Gpm1p phosphoglycerate mutase; converts 3-phosphoglycerate to 2-phosphoglycerate in glycolysis; may be non-functional; GPM2 has a paralog, GPM3, that arose from the whole genome duplication
  
 
0.999
GPM1
Tetrameric phosphoglycerate mutase; mediates the conversion of 3-phosphoglycerate to 2-phosphoglycerate during glycolysis and the reverse reaction during gluconeogenesis; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily
  
 
0.985
ENO2
Enolase II, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression induced in response to glucose; ENO2 has a paralog, ENO1, that arose from the whole genome duplication
  
 0.976
PGK1
3-phosphoglycerate kinase; catalyzes transfer of high-energy phosphoryl groups from the acyl phosphate of 1,3-bisphosphoglycerate to ADP to produce ATP; key enzyme in glycolysis and gluconeogenesis
   
 0.973
ENO1
Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication
  
 0.948
ERR1
Phosphopyruvate hydratase err1; Protein of unknown function, has similarity to enolases; Putative phosphopyruvate hydratase
  
 0.948
ERR2
Enolase-related protein 1; Enolase, a phosphopyruvate hydratase; catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate; complements the growth defect of an ENO1 ENO2 double mutant
  
 0.946
ERR3
Enolase-related protein 3; Enolase, a phosphopyruvate hydratase; catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate; complements the growth defect of an ENO1 ENO2 double mutant in glucose
  
 0.945
YOR283W
Broad-specificity phosphatase YOR283W; Phosphatase with a broad substrate specificity; has some similarity to GPM1/YKL152C, a phosphoglycerate mutase; YOR283W is not an essential gene; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily
  
   
 0.935
PGI1
Glycolytic enzyme phosphoglucose isomerase; catalyzes the interconversion of glucose-6-phosphate and fructose-6-phosphate; required for cell cycle progression and completion of the gluconeogenic events of sporulation
   
 
 0.932
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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