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TYS1 tyrosine--tRNA ligase TYS1 [ Saccharomyces cerevisiae S288C ]

Gene ID: 853097, updated on 17-May-2024

Summary

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Gene symbol
TYS1
Gene description
tyrosine--tRNA ligase TYS1
Primary source
FungiDB:YGR185C
Locus tag
YGR185C
See related
SGD:S000003417; AllianceGenome:SGD:S000003417
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Saccharomyces cerevisiae S288C (strain: S288C)
Lineage
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
Also known as
TTS1
Summary
Enables tyrosine-tRNA ligase activity. Involved in tyrosyl-tRNA aminoacylation. Located in cytoplasm and nucleus. Used to study cancer. Human ortholog(s) of this gene implicated in Charcot-Marie-Tooth disease dominant intermediate C. Orthologous to human YARS1 (tyrosyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Apr 2022]
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Genomic context

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Location:
chromosome: VII
Exon count:
1
Sequence:
Chromosome: VII; NC_001139.9 (866336..867520, complement)

Chromosome VII - NC_001139.9Genomic Context describing neighboring genes Neighboring gene ubiquinol--cytochrome-c reductase subunit 9 Neighboring gene E3 ubiquitin-protein ligase UBR1 Neighboring gene transcription factor IIF subunit TFG1 Neighboring gene Hgh1p

Genomic regions, transcripts, and products

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Genomic Sequence:
NC_001139.9

Go to nucleotide: Graphics FASTA GenBank

Bibliography

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Related articles in PubMed

  1. Structural basis for recognition of cognate tRNA by tyrosyl-tRNA synthetase from three kingdoms. Tsunoda M, et al. Nucleic Acids Res, 2007. PMID 17576676, Free PMC Article
  2. Three-dimensional structure of the ternary complex of yeast tyrosyl-tRNA synthetase. Tsunoda M, et al. Nucleic Acids Symp Ser (Oxf), 2004. PMID 17150525
  3. Crystallization and preliminary X-ray crystallographic analysis of yeast tyrosyl-tRNA synthetase complexed with its cognate tRNA. Kusakabe Y, et al. Protein Pept Lett, 2006. PMID 16712521
  4. Twenty-first aminoacyl-tRNA synthetase-suppressor tRNA pairs for possible use in site-specific incorporation of amino acid analogues into proteins in eukaryotes and in eubacteria. Kowal AK, et al. Proc Natl Acad Sci U S A, 2001 Feb 27. PMID 11226228, Free PMC Article
  5. Identity of tRNA for yeast tyrosyl-tRNA synthetase: tyrosylation is more sensitive to identity nucleotides than to structural features. Fechter P, et al. Biochemistry, 2000 Feb 22. PMID 10677221

See all (62) citations in PubMed

GeneRIFs: Gene References Into Functions

Pathways from PubChem

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Interactions

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Products Interactant Other Gene Complex Source Pubs Description

General gene information

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Homology

Gene Ontology Provided by SGD

Function Evidence Code Pubs
enables ATP binding IEA
Inferred from Electronic Annotation
more info
  
enables aminoacyl-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
enables mRNA binding HDA PubMed 
enables sequence-specific mRNA binding IDA
Inferred from Direct Assay
more info
 PubMed 
enables tyrosine-tRNA ligase activity IBA
Inferred from Biological aspect of Ancestor
more info
  
enables tyrosine-tRNA ligase activity IDA
Inferred from Direct Assay
more info
 PubMed 
enables tyrosine-tRNA ligase activity IEA
Inferred from Electronic Annotation
more info
  
Process Evidence Code Pubs
involved_in translation IEA
Inferred from Electronic Annotation
more info
  
involved_in tyrosyl-tRNA aminoacylation IBA
Inferred from Biological aspect of Ancestor
more info
  
involved_in tyrosyl-tRNA aminoacylation IDA
Inferred from Direct Assay
more info
 PubMed 
involved_in tyrosyl-tRNA aminoacylation IEA
Inferred from Electronic Annotation
more info
  
Component Evidence Code Pubs
is_active_in cytoplasm IBA
Inferred from Biological aspect of Ancestor
more info
  
located_in cytoplasm IDA
Inferred from Direct Assay
more info
 PubMed 
located_in cytoplasm IEA
Inferred from Electronic Annotation
more info
  
located_in cytoplasmic stress granule HDA PubMed 
located_in nucleus IDA
Inferred from Direct Assay
more info
 PubMed 
located_in nucleus IEA
Inferred from Electronic Annotation
more info
  
located_in nucleus IMP
Inferred from Mutant Phenotype
more info
 PubMed 

General protein information

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Preferred Names
tyrosine--tRNA ligase TYS1
NP_011701.3
  • 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

NCBI Reference Sequences (RefSeq)

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Genome Annotation

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference assembly

Genomic

  1. NC_001139.9 Reference assembly

    Range
    866336..867520 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_001181314.3 → NP_011701.3  TPA: tyrosine--tRNA ligase TYS1 [Saccharomyces cerevisiae S288C]

    See identical proteins and their annotated locations for NP_011701.3

    Status: REVIEWED

    UniProtKB/Swiss-Prot
    D6VUW8, P36421
    UniProtKB/TrEMBL
    A0A6A5PW80, A6ZUJ6, B3LI49, C7GVV6, C8Z978, G2WER4, N1P478
    Conserved Domains (1) summary
    TIGR00234
    Location:9 → 344
    tyrS; tyrosyl-tRNA synthetase
Nucleotide Protein
Heading Accession and Version
Protein Accession Links
GenPept Link UniProtKB Link
P36421.3

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