STRINGSTRING
STRING protein interaction network
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
Your Input:
Neighborhood
Gene Fusion
Co-occurrence
Co-expression
Experiments
Databases
Textmining
[Homology]
Score
ADP18050.1Glyoxalase/bleomycin resistance protein/dioxygenase superfamily protein 20. (160 aa)    
Predicted Functional Partners:
ADP18049.1
Bacterial regulatory protein, ArsR family protein 7.
 
   
 0.870
ADP18051.1
Protein tyrosine phosphatase; Belongs to the low molecular weight phosphotyrosine protein phosphatase family.
  
 0.839
ADP18052.1
Sodium bile acid symporter family protein 4.
  
  
 0.820
ADP18053.1
Major facilitator superfamily MFS_1 domain protein.
     
 0.768
arsC2
Arsenate reductase (glutaredoxin) 2.
 
     0.720
arsH2
Arsenical resistance protein ArsH 2.
  
  
 0.704
ADP14434.1
Bacterial regulatory protein, ArsR family protein 1.
 
   
 0.527
nuoI
NADH-quinone oxidoreductase subunit 9; NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient.
  
  
 0.480
Your Current Organism:
Achromobacter xylosoxidans
NCBI taxonomy Id: 762376
Other names: A. xylosoxidans A8, Achromobacter xylosoxidans A8, Achromobacter xylosoxidans str. A8, Achromobacter xylosoxidans strain A8
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