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.
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]
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grpEHeat 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. Several rounds of ATP-depen [...] (240 aa)    
Predicted Functional Partners:
dnaK-5
Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.971
dnaK
Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.968
dnaK-2
Heat shock protein 70; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 
 0.967
dnaJ-5
Heat shock protein 40; 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, Dn [...]
 
 
 0.965
groEL1
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.960
groEL2
60 kDa molecular chaperonin 2; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.954
groES
10 kDa chaperonin; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 
 0.937
dnaK-3
Heat shock protein 70.
  
 
 0.907
dnaJ-2
Heat shock protein 40; Molecular chaperone.
 
 
 0.902
dnaJ-3
Heat shock protein 40; Molecular chaperone.
 
 
 0.901
Your Current Organism:
Microcystis aeruginosa
NCBI taxonomy Id: 449447
Other names: M. aeruginosa NIES-843, Microcystis aeruginosa NIES-843
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