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
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Assay-based Predictions
experimentally determined
co-expression
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gene neighborhood
gene co-occurrence
gene fusions
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[Homology]
Score
Mnod_5188TIGRFAM: thioredoxin; PFAM: Thioredoxin domain; KEGG: met:M446_4464 thioredoxin. (302 aa)    
Predicted Functional Partners:
Mnod_4666
Glutathione-disulfide reductase; Maintains high levels of reduced glutathione.
  
 
 0.940
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 [...]
 
  
 0.878
hslV
20S proteasome A and B subunits; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.869
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.
  
 
 0.855
groL
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.838
groL-2
Chaperonin GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
  
 
 0.838
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 [...]
 
 
 0.823
Mnod_5189
PFAM: peptidase S16 lon domain protein; KEGG: met:M446_4463 peptidase S16 lon domain-containing protein.
 
  
 0.813
htpG
Heat shock protein Hsp90; Molecular chaperone. Has ATPase activity.
  
 
 0.794
Mnod_0012
PFAM: FAD dependent oxidoreductase; FAD-dependent pyridine nucleotide-disulphide oxidoreductase; KEGG: met:M446_0008 FAD-dependent pyridine nucleotide-disulphide oxidoreductase.
  
 
 0.784
Your Current Organism:
Methylobacterium nodulans
NCBI taxonomy Id: 460265
Other names: M. nodulans ORS 2060, Methylobacterium nodulans ORS 2060, Methylobacterium nodulans str. ORS 2060, Methylobacterium nodulans strain ORS 2060
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