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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
EDM43648.1Hypothetical protein; COG0526 Thiol-disulfide isomerase and thioredoxins. (200 aa)    
Predicted Functional Partners:
EDM43472.1
COG0652 Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family.
    
 0.849
EDM44691.1
COG0652 Peptidyl-prolyl cis-trans isomerase (rotamase) - cyclophilin family.
    
 0.849
EDM43937.1
Heat shock protein 90; COG0326 Molecular chaperone, HSP90 family.
   
  0.679
EDM43127.1
COG4232 Thiol:disulfide interchange protein.
  
 
 0.662
EDM44054.1
Peptidyl-prolyl cis-trans isomerase, cyclophilin-type; PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides; Belongs to the cyclophilin-type PPIase family.
    
  0.641
EDM44932.1
Heat shock protein Hsp70; COG0443 Molecular chaperone.
   
  0.633
EDM44934.1
COG0443 Molecular chaperone; Belongs to the heat shock protein 70 family.
   
  0.633
EDM44004.1
Heat shock protein Hsp70; COG0443 Molecular chaperone; Belongs to the heat shock protein 70 family.
   
  0.633
dnaK
Molecular chaperone DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
  0.633
dnaJ
Molecular chaperone, heat shock protein; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interaction [...]
    
  0.631
Your Current Organism:
unidentified eubacterium SCB49
NCBI taxonomy Id: 50743
Other names: u. eubacterium SCB49
Server load: low (20%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.