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
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
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[Homology]
Score
groLGroEL2 protein (Chaperonin cpn60 2); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (565 aa)    
Predicted Functional Partners:
groES
GroES protein (Chaperonin cpn10); Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.994
grpE
Heat shock 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- [...]
  
 0.945
htpG
Heat shock protein HtpG; Molecular chaperone. Has ATPase activity.
   
 
 0.928
groEL
GroEL protein (Chaperonin cpn60); Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
  
 
0.902
dnaK
Molecular chaperone DnaK, heat shock protein hsp70; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.871
dnaK-2
Molecular chaperone DnaK2, heat shock protein hsp70-2; Acts as a chaperone; Belongs to the heat shock protein 70 family.
  
 0.871
ABX09481.1
Putative DnaK-type molecular chaperone (HSP70 family); COG443 Molecular chaperone [Posttranslational modification, protein turnover, chaperones]; Belongs to the heat shock protein 70 family.
  
 0.869
ABX09372.1
Contains TPR repeats; COG5010 Flp pilus assembly protein TadD, contains TPR repeats [Intracellular trafficking and secretion].
   
 0.822
dnaJ
DnaJ 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 interactions between DnaJ, DnaK and Gr [...]
   
 0.733
ABX09525.1
DnaJ-like protein.
   
 0.685
Your Current Organism:
Prochlorococcus marinus MIT9211
NCBI taxonomy Id: 93059
Other names: P. marinus str. MIT 9211, Prochlorococcus marinus str. MIT 9211, Prochlorococcus sp. MIT 9211, Prochlorococcus sp. MIT9211
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