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.
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
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
prfCPeptide chain release factor RF-3; Increases the formation of ribosomal termination complexes and stimulates activities of RF-1 and RF-2. It binds guanine nucleotides and has strong preference for UGA stop codons. It may interact directly with the ribosome. The stimulation of RF-1 and RF-2 is significantly reduced by GTP and GDP, but not by GMP; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. PrfC subfamily. (529 aa)    
Predicted Functional Partners:
prfB
Peptide chain release factor RF-2; Peptide chain release factor 2 directs the termination of translation in response to the peptide chain termination codons UGA and UAA.
  
 
 0.977
prfA
Peptide chain release factor RF-1; Peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA.
   
 
 0.961
frr
Ribosome releasing factor; Responsible for the release of ribosomes from messenger RNA at the termination of protein biosynthesis. May increase the efficiency of translation by recycling ribosomes from one round of translation to another; Belongs to the RRF family.
   
 
 0.890
rpmA
Similar to E. coli 50S ribosomal subunit protein L27 (AAC76217.1); Blastp hit to AAC76217.1 (85 aa), 95% identity in aa 1 - 85; Belongs to the bacterial ribosomal protein bL27 family.
   
 
 0.864
prfH
Similar to E. coli probable peptide chain release factor (AAC73340.1); Blastp hit to AAC73340.1 (166 aa), 82% identity in aa 2 - 163.
  
 
 0.825
rplK
50 S ribosomal subunit protein L11; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors.
  
  0.807
ybjF
Putative tRNA (uracil-5-)-methyltransferase; Catalyzes the formation of 5-methyl-uridine at position 747 (m5U747) in 23S rRNA; Belongs to the class I-like SAM-binding methyltransferase superfamily. RNA M5U methyltransferase family. RlmC subfamily.
   
  
 0.796
yecE
Putative cytoplasmic protein; Similar to E. coli orf, hypothetical protein (AAC74938.1); Blastp hit to AAC74938.1 (272 aa), 82% identity in aa 1 - 272.
     
 0.787
rplT
50S ribosomal subunit protein L20; Binds directly to 23S ribosomal RNA and is necessary for the in vitro assembly process of the 50S ribosomal subunit. It is not involved in the protein synthesizing functions of that subunit (By similarity).
  
 
 0.778
rplL
50S ribosomal subunit protein L7/L12; Forms part of the ribosomal stalk which helps the ribosome interact with GTP-bound translation factors. Is thus essential for accurate translation.
   
 
 0.768
Your Current Organism:
Salmonella enterica Typhimurium
NCBI taxonomy Id: 99287
Other names: S. enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium LT2, Salmonella enterica subsp. enterica serovar Typhimurium str. LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2, Salmonella enterica subsp. enterica serovar Typhimurium strain LT2-LTL2, Salmonella typhimurium LT2
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.