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
TrkB2Transketolase, C-terminal subunit. (310 aa)    
Predicted Functional Partners:
TrkA1
Putative transketolase N-terminal section.
 0.999
TrkA2
Transketolase, N-terminal subunit.
 0.999
rpe
Ribulose-phosphate 3-epimerase Rpe; Belongs to the ribulose-phosphate 3-epimerase family.
 
 
 0.971
RpiB
Sugar-phosphate isomerase, RpiB/LacA/LacB family.
  
 
 0.948
pgiB
Glucose-6-phosphate isomerase PgiB; Belongs to the GPI family.
     
 0.943
TrkB1
Putative transketolase C-terminal section.
  
  
 
0.908
fba
Fructose-bisphosphate aldolase Fba.
    
  0.905
prs
Ribose-phosphate pyrophosphokinase Prs.
    
  0.904
prsA
Ribose-phosphate pyrophosphokinase PrsA; Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib- 5-P); Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily.
    
  0.904
pfp
Pyrophosphate--fructose 6-phosphate 1-phosphotransferase Pfp; Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP- PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions.
    
  0.902
Your Current Organism:
Thermoclostridium stercorarium
NCBI taxonomy Id: 1121335
Other names: Clostridium stercorarium subsp. stercorarium DSM 8532, T. stercorarium subsp. stercorarium DSM 8532, Thermoclostridium stercorarium subsp. stercorarium DSM 8532
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