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.
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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
groLChaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. (548 aa)    
Predicted Functional Partners:
groS
Chaperonin Cpn10; Binds to Cpn60 in the presence of Mg-ATP and suppresses the ATPase activity of the latter.
 
 0.999
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 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 [...]
 
 0.993
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
   
 0.992
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 [...]
 
 0.975
DvMF_0569
PFAM: heat shock protein DnaJ domain protein; chaperone DnaJ domain protein; KEGG: dde:Dde_1659 heat shock protein DnaJ-like.
 
 0.954
DvMF_3042
PFAM: heat shock protein DnaJ domain protein; KEGG: dde:Dde_1302 heat shock protein DnaJ-like.
 
 0.944
DvMF_0402
TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: dde:Dde_2067 thioredoxin; Belongs to the thioredoxin family.
 
 
 0.925
DvMF_2598
PFAM: cytochrome c class III; KEGG: dde:Dde_0653 high-molecular-weight cytochrome c.
  
 0.920
DvMF_0503
TIGRFAM: translation elongation factor G; small GTP-binding protein; PFAM: elongation factor G domain protein; protein synthesis factor GTP-binding; elongation factor Tu domain 2 protein; elongation factor G domain IV; KEGG: dde:Dde_2063 elongation factor G.
  
 0.888
Your Current Organism:
Desulfovibrio vulgaris Miyazaki
NCBI taxonomy Id: 883
Other names: D. vulgaris str. 'Miyazaki F', Desulfovibrio vulgaris (strain Miyazaki), Desulfovibrio vulgaris str. 'Miyazaki F'
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