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trxC protein (Yersinia pseudotuberculosis) - STRING interaction network
"trxC" - Thioredoxin: thioredoxin in Yersinia pseudotuberculosis
Nodes:
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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:
some 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 each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
trxCThioredoxin- thioredoxin (145 aa)    
Predicted Functional Partners:
gltB
annotation not available (1485 aa)
       
      0.849
fipA
Thioredoxin- thioredoxin; Belongs to the thioredoxin family (108 aa)
 
     
0.794
trxB
TRX_reduct- thioredoxin-disulfide reductase; Belongs to the class-II pyridine nucleotide-disulfide oxidoreductase family (320 aa)
 
 
  0.751
ahpC
Putative alkyl hydroperoxide reductase subunit c; C-terminal domain of 1-Cys peroxiredoxin family protein (200 aa)
     
 
  0.682
katG
Catalase-peroxidase; Bifunctional enzyme with both catalase and broad- spectrum peroxidase activity (737 aa)
       
 
  0.668
galE
UDP-galactose-4-epimerase; galE- UDP-glucose 4-epimerase GalE (338 aa)
   
     
  0.646
gor
Gluta_reduc_1- glutathione-disulfide reductase; Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family (450 aa)
     
 
  0.636
dnaK
Chaperone protein DnaK; Acts as a chaperone (636 aa)
 
 
  0.616
cadC
Transcriptional regulatory , C terminal family protein (219 aa)
           
  0.596
groL
60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (548 aa)
 
 
  0.592
Your Current Organism:
Yersinia pseudotuberculosis
NCBI taxonomy Id: 633
Other names: ATCC 29833, Bacillus pseudotuberkulosis, Bacterium pseudotuberculosis, CCUG 5855, CIP 55.85, DSM 8992, NCTC 10275, Pasteurella pseudotuberculosis, Shigella pseudotuberculosis, Y. pseudotuberculosis, Yersinia pseudotuberculosis
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