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    Yars2 tyrosyl-tRNA synthetase 2 [ Rattus norvegicus (Norway rat) ]

    Gene ID: 287924, updated on 17-Aug-2024

    Summary

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    Official Symbol
    Yars2provided by RGD
    Official Full Name
    tyrosyl-tRNA synthetase 2provided by RGD
    Primary source
    RGD:1311696
    See related
    AllianceGenome:RGD:1311696
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Rattus norvegicus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Rattus
    Also known as
    CGI-04; RGD1311696
    Summary
    Predicted to enable several functions, including protein homodimerization activity; tyrosine binding activity; and tyrosine-tRNA ligase activity. Predicted to be involved in mitochondrial tyrosyl-tRNA aminoacylation. Predicted to be located in nuclear body. Predicted to be active in cytosol and mitochondrion. Human ortholog(s) of this gene implicated in myopathy, lactic acidosis, and sideroblastic anemia 2. Orthologous to human YARS2 (tyrosyl-tRNA synthetase 2). [provided by Alliance of Genome Resources, Apr 2022]
    Expression
    Biased expression in Heart (RPKM 56.6), Adrenal (RPKM 56.1) and 9 other tissues See more
    Orthologs
    human mouse all
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    Genomic context

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    See Yars2 in Genome Data Viewer
    Location:
    11q23
    Exon count:
    5
    Annotation release Status Assembly Chr Location
    RS_2024_02 current GRCr8 (GCF_036323735.1) 11 NC_086029.1 (98136530..98142320, complement)
    RS_2023_06 previous assembly mRatBN7.2 (GCF_015227675.2) 11 NC_051346.1 (84632350..84638138, complement)
    106 previous assembly Rnor_6.0 (GCF_000001895.5) 11 NC_005110.4 (88882615..88888377, complement)

    Chromosome 11 - NC_086029.1Genomic Context describing neighboring genes Neighboring gene glyceraldehyde-3-phosphate dehydrogenase-like Neighboring gene dynamin 1-like Neighboring gene glyceraldehyde-3-phosphate dehydrogenase-like Neighboring gene U4 spliceosomal RNA Neighboring gene plakophilin 2

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Expression

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    • Project title: A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages A rat RNA-Seq transcriptomic BodyMap across 11 organs and 4 developmental stages
    • Description: 320 RNA samples isolated from 11 organs (adrenal gland, brain, heart, kidney, liver, lung, muscle, spleen, thymus, and testes or uterus) from both sexes of Fischer 344 rats across four developmental stages (2-, 6-, 21-, and 104-weeks-old)
    • BioProject: PRJNA238328
    • Publication: PMID 24510058
    • Analysis date: Mon Jun 6 17:44:12 2016

    Bibliography

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    Related articles in PubMed

    1. Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia--MLASA syndrome. Riley LG, et al. Am J Hum Genet, 2010 Jul 9. PMID 20598274, Free PMC Article
    2. Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features. Bonnefond L, et al. Structure, 2007 Nov. PMID 17997975
    3. Human mitochondrial TyrRS disobeys the tyrosine identity rules. Bonnefond L, et al. RNA, 2005 May. PMID 15840810, Free PMC Article
    4. Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Bonnefond L, et al. Biochemistry, 2005 Mar 29. PMID 15779907
    5. The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Baltz AG, et al. Mol Cell, 2012 Jun 8. PMID 22681889

    See all (9) citations in PubMed

    GeneRIFs: Gene References Into Functions

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by RGD

    Function Evidence Code Pubs
    enables ATP binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables L-tyrosine binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables L-tyrosine binding ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables protein homodimerization activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein homodimerization activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables tRNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tRNA binding ISO
    Inferred from Sequence Orthology
    more info
    		  
    enables tyrosine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables tyrosine-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables tyrosine-tRNA ligase activity ISO
    Inferred from Sequence Orthology
    more info
    		  
    Process Evidence Code Pubs
    involved_in mitochondrial tyrosyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in mitochondrial tyrosyl-tRNA aminoacylation ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tRNA aminoacylation ISO
    Inferred from Sequence Orthology
    more info
    		  
    Component Evidence Code Pubs
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrial matrix IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrial matrix ISO
    Inferred from Sequence Orthology
    more info
    		  
    is_active_in mitochondrion IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in mitochondrion ISO
    Inferred from Sequence Orthology
    more info
    		  
    located_in nuclear body IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nuclear body ISO
    Inferred from Sequence Orthology
    more info
    		  

    General protein information

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    Preferred Names
    tyrosine--tRNA ligase, mitochondrial
    Names
    tyrRS
    tyrosyl-tRNA synthetase 2 (mitochondrial)
    tyrosyl-tRNA synthetase, mitochondrial
    NP_001009627.1
    XP_038943984.1

    NCBI Reference Sequences (RefSeq)

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    RefSeqs maintained independently of Annotated Genomes

    These reference sequences exist independently of genome builds. Explain

    These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

    mRNA and Protein(s)

    1. NM_001009627.1 → NP_001009627.1  tyrosine--tRNA ligase, mitochondrial

      See identical proteins and their annotated locations for NP_001009627.1

      Status: PROVISIONAL

      Source sequence(s)
      BC088224
      UniProtKB/Swiss-Prot
      Q5I0L3
      UniProtKB/TrEMBL
      A6JSQ9
      Conserved Domains (2) summary
      cd00805
      Location:68 → 350
      TyrRS_core; catalytic core domain of tyrosinyl-tRNA synthetase
      PRK05912
      Location:37 → 468
      PRK05912; tyrosyl-tRNA synthetase; Validated

    RefSeqs of Annotated Genomes: GCF_036323735.1-RS_2024_02

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

    Reference GRCr8

    Genomic

    1. NC_086029.1 Reference GRCr8

      Range
      98136530..98142320 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_039088056.2 → XP_038943984.1  tyrosine--tRNA ligase, mitochondrial isoform X1

      Conserved Domains (1) summary
      PRK05912
      Location:44 → 317
      PRK05912; tyrosyl-tRNA synthetase; Validated
    Nucleotide Protein Strain
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q5I0L3.1 GenPept UniProtKB/Swiss-Prot:Q5I0L3

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Chemical Information
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