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GPM3 protein (Saccharomyces cerevisiae) - STRING interaction network
"GPM3" - Homolog of Gpm1p phosphoglycerate mutase, which converts 3-phosphoglycerate to 2-phosphoglycerate in glycolysis in Saccharomyces cerevisiae
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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[Homology]
Score
GPM3Homolog of Gpm1p phosphoglycerate mutase, which converts 3-phosphoglycerate to 2-phosphoglycerate in glycolysis; may be non-functional derivative of a gene duplication event; Could be non-functional (303 aa)    
Predicted Functional Partners:
ENO2
Enolase II, a phosphopyruvate hydratase that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression is induced in response to glucose (437 aa)
   
  0.996
ENO1
Enolase I, a phosphopyruvate hydratase that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression is repressed in response to glucose (437 aa)
   
  0.995
ERR1
Putative phosphopyruvate hydratase (437 aa)
   
  0.995
ERR3
Protein of unknown function, has similarity to enolases (437 aa)
   
  0.995
ERR2
Protein of unknown function, has similarity to enolases (437 aa)
   
  0.995
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 (416 aa)
     
  0.991
YOR283W
Phosphatase with a broad substrate specificity and some similarity to GPM1/YKL152C, a phosphoglycerate mutase; YOR283W is not an essential gene; Metal-independent phosphatase active against a broad range of phosphorylated substrates including nucleoside tri- and diphosphates, phosphorylated organic acids, and amino acids. Shows no activity against phytic acid, phosphorylated carbohydrates, and nucleoside monophosphates (230 aa)
   
 
  0.977
GPM1
Tetrameric phosphoglycerate mutase, mediates the conversion of 3-phosphoglycerate to 2-phosphoglycerate during glycolysis and the reverse reaction during gluconeogenesis; Interconversion of 3- and 2-phosphoglycerate with 2,3- bisphosphoglycerate as the primer of the reaction. Can also Catalyze the reaction of EC 5.4.2.4 (synthase) and EC 3.1.3.13 (phosphatase), but with a reduced activity (247 aa)
   
 
0.976
GPM2
Homolog of Gpm1p phosphoglycerate mutase, which converts 3-phosphoglycerate to 2-phosphoglycerate in glycolysis; may be non-functional derivative of a gene duplication event; Could be non-functional (311 aa)
   
 
0.973
TDA10
ATP-binding protein of unknown function; crystal structure resembles that of E.coli pantothenate kinase and other small kinases; null mutant is sensitive to expression of the top1-T722A allele; ATP-dependent kinase whose specificity is not yet known (290 aa)
         
    0.958
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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