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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textmining
Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
Pro_0963Cyanobacteria-specific chaperone containing DNAJ domain. (354 aa)    
Predicted Functional Partners:
grpE
Molecular chaperone GrpE, heat 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. S [...]
  
 
 0.751
htpG
HSP90 family molecular chaperone; Molecular chaperone. Has ATPase activity.
   
 0.678
dnaK
Molecular chaperone, DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
  0.598
dnaK-2
Molecular chaperone DnaK; Belongs to the heat shock protein 70 family.
   
  0.598
dnaK-3
Molecular chaperone, DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
  0.598
groL
Chaperonin GroEL, HSP60 family; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.528
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.528
Pro_0962
Predicted protein.
       0.494
groS
Co-chaperonin GroES; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
   
 
 0.450
clpA
ATPases with chaperone activity, ATP-binding subunit; Belongs to the ClpA/ClpB family.
   
   0.429
Your Current Organism:
Prochlorococcus marinus CCMP1375
NCBI taxonomy Id: 167539
Other names: P. marinus subsp. marinus str. CCMP1375, Prochlorococcus marinus SS120, Prochlorococcus marinus subsp. marinus str. CCMP1375, Prochlorococcus marinus subsp. marinus str. SS120
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