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pheT protein (Escherichia coli K12 MG1655) - STRING interaction network
"pheT" - Phenylalanine tRNA synthetase, beta-subunit in Escherichia coli K12 MG1655
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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Score
pheTPhenylalanine tRNA synthetase, beta-subunit; Protein involved in tRNA aminoacylation for protein translation (795 aa)    
Predicted Functional Partners:
pheS
Phenylalanine tRNA synthetase, alpha-subunit; Protein involved in tRNA aminoacylation for protein translation (327 aa)
  0.999
alaS
Alanine--tRNA ligase; Catalyzes the attachment of L-alanine to tRNA(Ala) in a two-step reaction- L-alanine is first activated by ATP to form Ala-AMP and then transferred to the acceptor end of tRNA(Ala). AlaRS also incorrectly activates the sterically smaller amino acid glycine as well as the sterically larger amino acid L-serine; generates 2-fold more mischarged Gly than Ser. These mischarged amino acids occur because the of inherent physicochemical limitations on discrimination between closely related amino acids (Ala, Gly and Ser) in the charging step (876 aa)
 
 
  0.972
ileS
Isoleucine--tRNA ligase; Catalyzes the attachment of isoleucine to tRNA(Ile). As IleRS can inadvertently accommodate and process structurally similar amino acids such as valine, to avoid such errors it has two additional distinct tRNA(Ile)-dependent editing activities. One activity is designated as ’pretransfer’ editing and involves the hydrolysis of activated Val-AMP. The other activity is designated ’posttransfer’ editing and involves deacylation of mischarged Val-tRNA(Ile) (938 aa)
   
 
  0.966
thrS
Threonine--tRNA ligase; Catalyzes the attachment of threonine to tRNA(Thr) in a two-step reaction- L-threonine is first activated by ATP to form Thr-AMP and then transferred to the acceptor end of tRNA(Thr). The rate- limiting step is amino acid activation in the presence of tRNA. The 2’-OH of the acceptor base (adenine 76, A76) of tRNA(Thr) and His-309 collaborate to transfer L-Thr to the tRNA; substitution of 2’-OH of A76 with hydrogen or fluorine decreases transfer efficiency 760 and 100-fold respectively. The zinc ion in the active site discriminates against charging of the isoster [...] (642 aa)
   
 
  0.958
tyrS
Tyrosine--tRNA ligase; Catalyzes the attachment of L-tyrosine to tRNA(Tyr) in a two-step reaction- tyrosine is first activated by ATP to form Tyr- AMP and then transferred to the acceptor end of tRNA(Tyr). Also mischarges tRNA(Tyr) with D-tyrosine, although Vmax is much lower (424 aa)
   
 
  0.948
guaA
GMP synthase [glutamine-hydrolyzing]; Catalyzes the synthesis of GMP from XMP (525 aa)
 
 
  0.937
argS
Arginine--tRNA ligase; Arginine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation (577 aa)
   
 
  0.935
ihfA
Integration host factor subunit alpha; One of the 2 subunits of integration host factor (IHF), a specific DNA-binding protein that functions in genetic recombination as well as in transcriptional and translational control. Binds to hundreds of transcriptionally inactive, AT-rich DNA sites, approximately half its binding sites are in non-coding DNA, which only accounts for about 10% of the genome (99 aa)
   
 
  0.920
leuS
Leucine--tRNA ligase; Leucine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation; Belongs to the class-I aminoacyl-tRNA synthetase family (860 aa)
   
   
  0.904
hisS
Histidine--tRNA ligase; Histidine tRNA synthetase; Protein involved in tRNA aminoacylation for protein translation (424 aa)
 
   
  0.900
Your Current Organism:
Escherichia coli K12 MG1655
NCBI taxonomy Id: 511145
Other names: E. coli str. K-12 substr. MG1655, Escherichia coli K12 MG1655, Escherichia coli K12 substr. MG1655, Escherichia coli MG1655, Escherichia coli str. K-12 substr. MG1655, Escherichia coli str. K12 substr. MG1655, Escherichia coli str. MG1655, Escherichia coli strain MG1655
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