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
dnaK-2Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (637 aa)    
Predicted Functional Partners:
dnaJ
Chaperone protein DnaJ; 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 interactions between DnaJ, D [...]
 
 0.965
grpE-2
Molecular chaperone GrpE (heat shock protein); Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. 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. [...]
 
 
 0.915
AFY96518.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region.
 
 0.907
AFY93934.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
 
 0.906
AFY95788.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain; DnaJ C terminal region.
 
 0.903
AFY91840.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 0.898
AFY93827.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
 0.871
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.853
AFY92891.1
DNA/RNA helicase, superfamily II, SNF2 family; PFAM: Helicase conserved C-terminal domain; SNF2 family N-terminal domain.
  
 
 0.844
AFY91397.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
  
  0.828
Your Current Organism:
Chamaesiphon minutus
NCBI taxonomy Id: 1173020
Other names: C. minutus PCC 6605, Chamaesiphon minutus PCC 6605, Chamaesiphon sp. ACMM 446, Chamaesiphon sp. ATCC 27169, Chamaesiphon sp. PCC 6605
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