STRINGSTRING
STRING protein interaction network
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
htpGHeat shock protein Hsp90; Molecular chaperone. Has ATPase activity. (653 aa)    
Predicted Functional Partners:
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 [...]
  
 0.985
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.979
AEB83089.1
KEGG: dia:Dtpsy_0618 heat shock protein DnaJ domain protein; PFAM: Heat shock protein DnaJ, N-terminal; Chaperone DnaJ, C-terminal; SMART: Heat shock protein DnaJ, N-terminal.
  
 0.966
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
 
 0.952
AEB82962.1
KEGG: ajs:Ajs_3698 DnaK-related protein.
  
 0.925
AEB82963.1
KEGG: dac:Daci_5720 putative heat-shock chaperone protein; Belongs to the heat shock protein 70 family.
  
 0.925
hscA
Fe-S protein assembly chaperone HscA; Chaperone involved in the maturation of iron-sulfur cluster- containing proteins. Has a low intrinsic ATPase activity which is markedly stimulated by HscB.
  
 0.925
AEB85116.1
PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein.
  
 0.913
AEB85624.1
PRTRC system protein D; TIGRFAM: ParB-related, ThiF-related cassette, protein D; KEGG: ajs:Ajs_1600 hypothetical protein.
  
 0.913
hslV
ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.904
Your Current Organism:
Alicycliphilus denitrificans
NCBI taxonomy Id: 596154
Other names: A. denitrificans K601, Alicycliphilus denitrificans DSM 14773, Alicycliphilus denitrificans K601, Alicycliphilus denitrificans str. K601, Alicycliphilus denitrificans strain K601, Pseudomonas sp. K601, beta proteobacterium K601
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