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.
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colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
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empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
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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.
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experimentally determined
co-expression
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gene co-occurrence
gene fusions
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dnaK-3Chaperone protein dnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family. (637 aa)    
Predicted Functional Partners:
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 [...]
 
 0.991
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.
 
 0.975
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 [...]
 
 0.971
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.
   
 0.968
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.
  
 0.956
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.940
groL-2
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.940
EHA63474.1
PFAM: Tetratricopeptide TPR-1; Tetratricopeptide TPR2; KEGG: pmf:P9303_28691 hypothetical protein.
 
 0.913
groS
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.906
EHA60431.1
KEGG: pmf:P9303_04511 DnaJ-like protein; PFAM: Heat shock protein DnaJ, N-terminal; SMART: Heat shock protein DnaJ, N-terminal.
  
 0.903
Your Current Organism:
Synechococcus sp. WH 8016
NCBI taxonomy Id: 166318
Other names: S. sp. WH 8016, Synechococcus sp. WH8016
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