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:
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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. (637 aa)    
Predicted Functional Partners:
EHA63430.1
KEGG: pmf:P9303_15251 heat shock protein 90; PFAM: ATPase-like, ATP-binding domain; Heat shock protein Hsp90, C-terminal; SMART: ATPase-like, ATP-binding domain.
   
 0.985
grpE
Protein grpE; 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 [...]
 
 0.985
EHA60479.1
KEGG: pmf:P9303_03871 DnaJ3 protein; PFAM: Chaperone DnaJ, C-terminal; Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal.
 
 0.980
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 [...]
 
 0.969
EHA63419.1
KEGG: pmf:P9303_15171 DnaJ2 protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal.
  
 0.964
EHA60656.1
KEGG: pmt:PMT1977 putative heat shock protein DnaJ; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal.
  
 0.908
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.
   
 
 0.898
EHA63474.1
PFAM: Tetratricopeptide TPR-1; Tetratricopeptide TPR2; KEGG: pmf:P9303_28691 hypothetical protein.
 
 0.896
EHA60431.1
KEGG: pmf:P9303_04511 DnaJ-like protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal.
  
 0.896
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 
 0.893
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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