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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Co-expression
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[Homology]
Score
htpGMolecular chaperone of HSP90 family; Molecular chaperone. Has ATPase activity. (642 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 [...]
  
 0.994
groL
Chaperonin GroL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
   
 0.992
EIC29258.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ C terminal region; DnaJ domain.
  
 0.969
EIC29777.1
Molecular chaperone; PFAM: DNA-K related protein; Hsp70 protein.
   
 0.967
dnaK
Chaperone protein DnaK; Acts as a chaperone; Belongs to the heat shock protein 70 family.
   
 0.967
EIC31062.1
Molecular chaperone; PFAM: Hsp70 protein; Belongs to the heat shock protein 70 family.
   
 0.967
hslV
ATP-dependent protease HslVU, peptidase subunit; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
   
  
 0.962
hslU
ATP-dependent protease HslVU, ATPase subunit; ATPase subunit of a proteasome-like degradation complex; this subunit has chaperone activity. The binding of ATP and its subsequent hydrolysis by HslU are essential for unfolding of protein substrates subsequently hydrolyzed by HslV. HslU recognizes the N-terminal part of its protein substrates and unfolds these before they are guided to HslV for hydrolysis.
   
  
 0.957
EIC30823.1
DnaJ-class molecular chaperone with C-terminal Zn finger domain; PFAM: DnaJ domain.
 
 0.957
EIC31190.1
Hypothetical protein.
   
 0.954
Your Current Organism:
Methylomicrobium album
NCBI taxonomy Id: 686340
Other names: M. album BG8, Methylomicrobium album BG8, Methylomicrobium album str. BG8, Methylomicrobium album strain BG8
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