STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
SES1Serine--tRNA ligase, cytoplasmic; Cytosolic seryl-tRNA synthetase; class II aminoacyl-tRNA synthetase that aminoacylates tRNA(Ser), displays tRNA-dependent amino acid recognition which enhances discrimination of the serine substrate, interacts with peroxin Pex21p (462 aa)    
Predicted Functional Partners:
Glycine--tRNA ligase 1, mitochondrial; Cytoplasmic and mitochondrial glycyl-tRNA synthase; ligates glycine to the cognate anticodon-bearing tRNA; transcription termination factor that may interact with the 3'-end of pre-mRNA to promote 3'-end formation; GRS1 has a paralog, GRS2, that arose from the whole genome duplication; human homolog GARS implicated in Charcot-Marie-Tooth disease, can complement yeast null mutant
Cysteine--tRNA ligase; Cysteinyl-tRNA synthetase; may interact with ribosomes, based on co-purification experiments; human gene CARS allows growth of the yeast haploid null mutant after sporulation of a heterozygous diploid
Tyrosine--tRNA ligase, cytoplasmic; Cytoplasmic tyrosyl-tRNA synthetase; required for cytoplasmic protein synthesis; interacts with positions 34 and 35 of the tRNATyr anticodon; mutations in human ortholog YARS are associated with Charcot-Marie-Tooth (CMT) neuropathies; human ortholog YARS functionally complements the heat sensitivity of a ts allele; protein abundance increases in response to DNA replication stress; Belongs to the class-I aminoacyl-tRNA synthetase family
Arginine--tRNA ligase, cytoplasmic; Arginyl-tRNA synthetase; the authentic, non-tagged protein is detected in highly purified mitochondria in high-throughput studies; YDR341C has a paralog, MSR1, that arose from the whole genome duplication
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
Threonine--tRNA ligase, cytoplasmic; Threonyl-tRNA synthetase; essential cytoplasmic protein; human homolog TARS can complement yeast null mutant
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
Methionine--tRNA ligase, cytoplasmic; Methionyl-tRNA synthetase; forms a complex with glutamyl-tRNA synthetase (Gus1p) and Arc1p, which increases the catalytic efficiency of both tRNA synthetases; also has a role in nuclear export of tRNAs; mutations in human ortholog MARS are associated with pediatric pulmonary alveolar proteinosis
Alanine--tRNA ligase, mitochondrial; Cytoplasmic and mitochondrial alanyl-tRNA synthetase; required for protein synthesis; point mutation (cdc64-1 allele) causes cell cycle arrest at G1; lethality of null mutation is functionally complemented by human homolog AARS; mutations in human homolog AARS are associated with autoimmune disease polymyositis/dermatomyositis
Glutamate--tRNA ligase, cytoplasmic; Glutamyl-tRNA synthetase (GluRS); forms a complex with methionyl-tRNA synthetase (Mes1p) and Arc1p; complex formation increases the catalytic efficiency of both tRNA synthetases and ensures their correct localization to the cytoplasm; protein abundance increases in response to DNA replication stress; Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 2 subfamily
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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