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
Your Input:
Neighborhood
Gene fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
dnaKdnaK protein; Acts as a chaperone; Belongs to the heat shock protein 70 family. (641 aa)    
Predicted Functional Partners:
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 [...]
 0.997
grpE
GrpE 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-dependent i [...]
 
 
 0.996
htpG
Heat shock protein HtpG; Molecular chaperone. Has ATPase activity.
   
 0.968
cbpA
Curved DNA-binding protein; Identified by similarity to SP:P36659; match to protein family HMM PF00226; match to protein family HMM PF01556.
 0.920
clpB
ATP-dependent Clp protease, ATP-binding subunit 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.
  
 
 0.906
groEL-1
Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.893
groEL-3
Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.893
groEL-2
Chaperonin, 60 kDa subunit; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 0.876
groES-1
Chaperonin, 10 kDa subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.865
groES-2
Chaperonin, 10 kDa subunit; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
  
 
 0.865
Your Current Organism:
Methylococcus capsulatus
NCBI taxonomy Id: 243233
Other names: M. capsulatus str. Bath, Methylococcus capsulatus ATCC 33009, Methylococcus capsulatus Bath, Methylococcus capsulatus MC, Methylococcus capsulatus NCIB 11132, Methylococcus capsulatus str. Bath
Server load: low (14%) [HD]