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
pheSPhenylalanyl-tRNA synthetase alpha chain; Belongs to the class-II aminoacyl-tRNA synthetase family. Phe-tRNA synthetase alpha subunit type 2 subfamily. (492 aa)    
Predicted Functional Partners:
pheT
Phenylalanyl-tRNA synthetase beta chain.
 
 0.999
rpl2
LSU ribosomal protein L8e (L2p); One of the primary rRNA binding proteins. Required for association of the 30S and 50S subunits to form the 70S ribosome, for tRNA binding and peptide bond formation. It has been suggested to have peptidyltransferase activity; this is somewhat controversial. Makes several contacts with the 16S rRNA in the 70S ribosome. Belongs to the universal ribosomal protein uL2 family.
 
  
 0.931
fusA
Translation elongation factor 2; Catalyzes the GTP-dependent ribosomal translocation step during translation elongation. During this step, the ribosome changes from the pre-translocational (PRE) to the post-translocational (POST) state as the newly formed A-site-bound peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E sites, respectively. Catalyzes the coordinated movement of the two tRNA molecules, the mRNA and conformational changes in the ribosome; Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-G/EF-2 s [...]
 
 
 0.862
AKB66002.1
O-phosphoseryl-tRNA:Cysteinyl-tRNA synthase; Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L- cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)); Belongs to the SepCysS family.
   
 0.843
rpl10e
LSU ribosomal protein L10e (L16p); Belongs to the universal ribosomal protein uL16 family.
 
 0.838
trpS
Tryptophanyl-tRNA synthetase; Catalyzes the attachment of tryptophan to tRNA(Trp).
  
  
 0.784
valS
Valyl-tRNA synthetase; Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA- dependent manner; Belongs to the class-I aminoacyl-tRNA synthetase family. ValS type 2 subfamily.
 
  
 0.768
rpl5
LSU ribosomal protein L11e (L5p); This is 1 of the proteins that binds and probably mediates the attachment of the 5S RNA into the large ribosomal subunit, where it forms part of the central protuberance. In the 70S ribosome it contacts protein S13 of the 30S subunit (bridge B1b), connecting the 2 subunits; this bridge is implicated in subunit movement. May contact the P site tRNA; the 5S rRNA and some of its associated proteins might help stabilize positioning of ribosome-bound tRNAs.
 
  
 0.765
rps19p
SSU ribosomal protein S15e (S19p); Protein S19 forms a complex with S13 that binds strongly to the 16S ribosomal RNA.
 
  
 0.752
rps5
SSU ribosomal protein S2e (S5p); With S4 and S12 plays an important role in translational accuracy.
 
 
 0.742
Your Current Organism:
Methanosarcina mazei
NCBI taxonomy Id: 213585
Other names: M. mazei S-6, Methanosarcina mazei S-6
Server load: low (18%) [HD]
STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.