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-3Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (672 aa)    
Predicted Functional Partners:
grpE
GrpE 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. Several rounds of ATP-dependent i [...]
 
 0.992
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 [...]
 0.974
AFZ47450.1
ATP-binding region ATPase domain protein; Molecular chaperone. Has ATPase activity.
   
 0.945
clpB
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.936
clpB-2
ATP-dependent chaperone ClpB; Part of a stress-induced multi-chaperone system, it is involved in the recovery of the cell from heat-induced damage, in cooperation with DnaK, DnaJ and GrpE; Belongs to the ClpA/ClpB family.
  
 
 0.936
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.934
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.933
AFZ46503.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ domain; DnaJ C terminal region; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623:IPR002939:IPR003095:IPR018253; KEGG: npu:Npun_R6085 chaperone DnaJ domain-containing protein; PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Chaperone DnaJ domain protein.
 
 0.925
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.918
AFZ48504.1
Heat shock protein DnaJ domain protein; PFAM: DnaJ C terminal region; DnaJ domain; COGs: COG0484 DnaJ-class molecular chaperone with C-terminal Zn finger domain; InterPro IPR001623:IPR002939:IPR018253:IPR003095; KEGG: cyt:cce_1355 heat shock protein HSP40; PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; SMART: heat shock protein DnaJ domain protein; SPTR: Heat shock protein Hsp40; manually curated.
 
 0.914
Your Current Organism:
Cyanobacterium stanieri
NCBI taxonomy Id: 292563
Other names: C. stanieri PCC 7202, Cyanobacterium stanieri PCC 7202, Synechococcus cedrorum CCAP 14792a (no longer available), Synechococcus cedrorum CCAP 14792b (no longer available), Synechococcus cedrorum M137/1a, Synechococcus cedrorum SAG 88.79, Synechococcus sp. ATCC 29140, Synechococcus sp. PCC 7202
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