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.
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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[Homology]
Score
AMS39831.1Thioredoxin; Pfam:pfam00085 Thioredoxin. (322 aa)    
Predicted Functional Partners:
AMS42070.1
Glutathione reductase; Maintains high levels of reduced glutathione.
  
 
 0.944
grpE
Heat shock protein GrpE; 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- [...]
 
  
 0.874
hslV
Peptidase; Protease subunit of a proteasome-like degradation complex believed to be a general protein degrading machinery.
  
  
 0.863
hslU
ATP-dependent protease; 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
AMS39731.1
Exclusion suppressor FxsA; Pfam:pfam04186 FxsA cytoplasmic membrane protein.
   
    0.759
groL-3
Molecular chaperone GroEL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.743
groL-4
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.743
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.741
groL-2
Cpn60 chaperonin GroEL, large subunit of GroESL; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions.
 
 
 0.740
AMS39830.1
Pfam:pfam02190 ATP-dependent protease La (LON) domain.
 
  
 0.734
Your Current Organism:
Aminobacter aminovorans
NCBI taxonomy Id: 83263
Other names: A. aminovorans, ATCC 23314, ATCC 29600, Aminobacter heintzii, CCUG 2081, CIP 106737, Chelatobacter heintzii, DSM 10368, DSM 7048, JCM 7852, KCTC 2477, LMG 2122, LMG:2122, NCCB 26039, NCIB 9039, NCIB:9039, NCIMB 9039, NCTC 10684, Pseudomonas aminovorans, VKM B-2058
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