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
MST1Threonine--tRNA ligase, mitochondrial; Mitochondrial threonyl-tRNA synthetase; aminoacylates both the canonical threonine tRNA tT(UGU)Q1 and the unusual threonine tRNA tT(UAG)Q2 in vitro; lacks a typical editing domain, but has pre-transfer editing activity stimulated by the unusual tRNA-Thr. (462 aa)    
Predicted Functional Partners:
NAM2
Leucine--tRNA ligase, mitochondrial; Mitochondrial leucyl-tRNA synthetase; also has direct role in splicing of several mitochondrial group I introns; indirectly required for mitochondrial genome maintenance; human homolog LARS2 can complement yeast null mutant, and is implicated in Perrault syndrome; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
 
 0.970
CDC60
Leucine--tRNA ligase, cytoplasmic; Cytosolic leucyl tRNA synthetase; ligates leucine to the appropriate tRNA; human homolog LARS can complement yeast temperature-sensitive mutant at restrictive temperature.
  
 
 0.969
HTS1
Histidine--tRNA ligase, mitochondrial; Cytoplasmic and mitochondrial histidine tRNA synthetase; efficient mitochondrial localization requires both a presequence and an amino-terminal sequence; mutations in human ortholog HARS2 are associated with Perrault syndrome; Belongs to the class-II aminoacyl-tRNA synthetase family.
  
 
 0.957
VAS1
Valine--tRNA ligase, mitochondrial; Mitochondrial and cytoplasmic valyl-tRNA synthetase; human homolog VARS2 implicated in mitochondrial diseases, can partially complement yeast null mutant; Belongs to the class-I aminoacyl-tRNA synthetase family.
  
  
 0.956
KRS1
Lysine--tRNA ligase, cytoplasmic; Lysyl-tRNA synthetase.
  
 
 0.952
ILS1
Isoleucine--tRNA ligase, cytoplasmic; Cytoplasmic isoleucine-tRNA synthetase; target of the G1-specific inhibitor reveromycin A.
  
 
 0.950
AIM10
Probable proline--tRNA ligase, mitochondrial; Protein with similarity to tRNA synthetases; non-tagged protein is detected in purified mitochondria; null mutant is viable and displays elevated frequency of mitochondrial genome loss.
   
 
 0.948
MSK1
Lysine--tRNA ligase, mitochondrial; Mitochondrial lysine-tRNA synthetase; required for import of both aminoacylated and deacylated forms of tRNA(Lys) into mitochondria and for aminoacylation of mitochondrially encoded tRNA(Lys).
  
 
 0.948
ISM1
Isoleucine--tRNA ligase, mitochondrial; Mitochondrial isoleucyl-tRNA synthetase; null mutant is deficient in respiratory growth; human homolog IARS2 implicated in mitochondrial diseases, can partially complement yeast null mutant.
  
 
 0.947
DIA4
Serine--tRNA ligase, mitochondrial; Probable mitochondrial seryl-tRNA synthetase; mutant displays increased invasive and pseudohyphal growth; Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily.
   
 
 0.944
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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STRING is a Core Data Resource as designated by Global Biodata Coalition and ELIXIR.