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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from curated databases
textmining
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experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
Bind_2792TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: xau:Xaut_1982 thioredoxin. (307 aa)    
Predicted Functional Partners:
Bind_0881
Glutathione-disulfide reductase; Maintains high levels of reduced glutathione.
  
 
 0.942
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 [...]
 
  
 0.884
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.873
hslU
Heat shock protein HslVU, ATPase subunit HslU; 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.
  
 
 0.858
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.803
Bind_3393
Chaperonin Cpn60/TCP-1; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. Belongs to the chaperonin (HSP60) family.
   
 
 0.778
Bind_3110
PFAM: FxsA cytoplasmic membrane protein; KEGG: pfo:Pfl_4503 FxsA.
   
    0.737
Bind_0056
TIGRFAM: thioredoxin reductase; PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: mex:Mext_1092 thioredoxin reductase.
  
 
 0.724
Bind_2345
PFAM: FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: bbt:BBta_5550 putative thioredoxin reductase, FAD/NAD(P)-binding.
  
 
 0.724
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 
 0.707
Your Current Organism:
Beijerinckia indica
NCBI taxonomy Id: 395963
Other names: B. indica subsp. indica ATCC 9039, Beijerinckia indica subsp. indica ATCC 9039, Beijerinckia indica subsp. indica str. ATCC 9039, Beijerinckia indica subsp. indica strain ATCC 9039
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