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
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[Homology]
Score
ENO2Gamma-enolase; Has neurotrophic and neuroprotective properties on a broad spectrum of central nervous system (CNS) neurons. Binds, in a calcium-dependent manner, to cultured neocortical neurons and promotes cell survival (By similarity); Enolases (434 aa)    
Predicted Functional Partners:
PGAM1
2,3-bisphosphoglycerate-dependent phosphoglycerate mutase; Phosphoglycerate mutase 1; 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), but with a reduced activity
  
 0.985
PKM
Pyruvate kinase m1/2; Pyruvate kinase PKM; Glycolytic enzyme that catalyzes the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. Stimulates POU5F1-mediated transcriptional activation. Plays a general role in caspase independent cell death of tumor cells. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumo [...]
  
 0.982
PKLR
Pyruvate kinase PKLR; Plays a key role in glycolysis; Belongs to the pyruvate kinase family
  
 0.980
GPI
Glucose-6-phosphate isomerase; Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons
  
 0.978
PGAM2
Phosphoglycerate mutase 2; 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), but with a reduced activity; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily
  
 0.969
BPGM
Bisphosphoglycerate mutase; Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3- bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) activity; Belongs to the phosphoglycerate mutase family. BPG- dependent PGAM subfamily
  
 0.966
TPI1
Triosephosphate isomerase (tim); Triosephosphate isomerase 1; Belongs to the triosephosphate isomerase family
 
 
 0.962
ENO3
Beta-enolase; Appears to have a function in striated muscle development and regeneration; Belongs to the enolase family
  
 
0.947
PGK1
Phosphoglycerate kinase 1; In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). May play a role in sperm motility
 
 
 0.942
PCK2
Phosphoenolpyruvate carboxykinase [GTP], mitochondrial; Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle; Belongs to the phosphoenolpyruvate carboxykinase [GTP] family
     
 0.935
Your Current Organism:
Homo sapiens
NCBI taxonomy Id: 9606
Other names: H. sapiens, human, man
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