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    Aars alanyl-tRNA synthetase [ Mus musculus (house mouse) ]

    Gene ID: 234734, updated on 31-Jan-2019

    Summary

    Official Symbol
    Aarsprovided by MGI
    Official Full Name
    alanyl-tRNA synthetaseprovided by MGI
    Primary source
    MGI:MGI:2384560
    See related
    Ensembl:ENSMUSG00000031960
    Gene type
    protein coding
    RefSeq status
    VALIDATED
    Organism
    Mus musculus
    Lineage
    Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
    Also known as
    sti; C76919; AI316495
    Expression
    Ubiquitous expression in cerebellum adult (RPKM 31.7), liver adult (RPKM 27.0) and 28 other tissues See more
    Orthologs

    Genomic context

    See Aars in Genome Data Viewer
    Location:
    8; 8 E1
    Exon count:
    25
    Annotation release Status Assembly Chr Location
    106 current GRCm38.p4 (GCF_000001635.24) 8 NC_000074.6 (111027827..111055569)
    Build 37.2 previous assembly MGSCv37 (GCF_000001635.18) 8 NC_000074.5 (113557867..113580770)

    Chromosome 8 - NC_000074.6Genomic Context describing neighboring genes Neighboring gene DEAD (Asp-Glu-Ala-Asp) box polypeptide 19a Neighboring gene DEAD (Asp-Glu-Ala-Asp) box polypeptide 19b Neighboring gene microRNA 3473d Neighboring gene exosome component 6 Neighboring gene predicted gene, 38523 Neighboring gene nuclear encoded tRNA glycine 2 (anticodon GCC)

    Genomic regions, transcripts, and products

    Expression

    • Project title: Mouse ENCODE transcriptome data
    • Description: RNA profiling data sets generated by the Mouse ENCODE project.
    • BioProject: PRJNA66167
    • Publication: PMID 25409824
    • Analysis date: n/a

    Bibliography

    Variation

    Alleles

    Alleles of this type are documented at Mouse Genome Informatics  (MGI)

    Pathways from BioSystems

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Markers

    Homology

    Clone Names

    • MGC37368

    Gene Ontology Provided by MGI

    Function Evidence Code Pubs
    ATP binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    ATP binding ISO
    Inferred from Sequence Orthology
    more info
     
    RNA binding IEA
    Inferred from Electronic Annotation
    more info
     
    Ser-tRNA(Ala) hydrolase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    Ser-tRNA(Ala) hydrolase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Ser-tRNA(Ala) hydrolase activity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    alanine-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    alanine-tRNA ligase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    alanine-tRNA ligase activity ISO
    Inferred from Sequence Orthology
    more info
     
    amino acid binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    amino acid binding ISO
    Inferred from Sequence Orthology
    more info
     
    aminoacyl-tRNA editing activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    aminoacyl-tRNA editing activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    aminoacyl-tRNA editing activity ISO
    Inferred from Sequence Orthology
    more info
     
    aminoacyl-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
     
    ligase activity IEA
    Inferred from Electronic Annotation
    more info
     
    metal ion binding IEA
    Inferred from Electronic Annotation
    more info
     
    nucleic acid binding IEA
    Inferred from Electronic Annotation
    more info
     
    nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
     
    protein binding IPI
    Inferred from Physical Interaction
    more info
    PubMed 
    tRNA binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    tRNA binding ISO
    Inferred from Sequence Orthology
    more info
     
    translation regulator activity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    Process Evidence Code Pubs
    alanyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    alanyl-tRNA aminoacylation IDA
    Inferred from Direct Assay
    more info
    PubMed 
    alanyl-tRNA aminoacylation IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    alanyl-tRNA aminoacylation ISO
    Inferred from Sequence Orthology
    more info
     
    cerebellar Purkinje cell layer development IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    cerebellar Purkinje cell layer development IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    negative regulation of neuron apoptotic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    negative regulation of neuron apoptotic process IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    neuromuscular process IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    neuromuscular process controlling balance IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    neuromuscular process controlling balance IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    regulation of cytoplasmic translational fidelity IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    regulation of cytoplasmic translational fidelity IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
     
    tRNA modification IBA
    Inferred from Biological aspect of Ancestor
    more info
    PubMed 
    tRNA modification IDA
    Inferred from Direct Assay
    more info
    PubMed 
    tRNA modification IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    translation IEA
    Inferred from Electronic Annotation
    more info
     
    Component Evidence Code Pubs
    cytoplasm ISO
    Inferred from Sequence Orthology
    more info
     
    cytosol ISO
    Inferred from Sequence Orthology
    more info
     

    General protein information

    Preferred Names
    alanine--tRNA ligase, cytoplasmic
    Names
    alaRS
    alanyl-tRNA synthetase, cytoplasmic
    protein sticky
    NP_666329.2
    XP_006530984.1
    XP_006530985.1
    XP_006530987.1
    XP_017168237.1

    NCBI Reference Sequences (RefSeq)

    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_146217.4NP_666329.2  alanine--tRNA ligase, cytoplasmic

      See identical proteins and their annotated locations for NP_666329.2

      Status: VALIDATED

      Source sequence(s)
      AA416313, AK085725, AK150227, BM943271
      Consensus CDS
      CCDS40478.1
      UniProtKB/Swiss-Prot
      Q8BGQ7
      UniProtKB/TrEMBL
      Q3UD67
      Related
      ENSMUSP00000034441.7, ENSMUST00000034441.7
      Conserved Domains (5) summary
      PLN02900
      Location:6961
      PLN02900; alanyl-tRNA synthetase
      cd00673
      Location:7254
      AlaRS_core; Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      pfam02272
      Location:886955
      DHHA1; DHHA1 domain
      pfam07973
      Location:694752
      tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
      cl02787
      Location:495531
      Translation_Factor_II_like; Domain II of Elongation factor Tu (EF-Tu)-like proteins

    RefSeqs of Annotated Genomes: Mus musculus Annotation Release 106

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

    Reference GRCm38.p4 C57BL/6J

    Genomic

    1. NC_000074.6 Reference GRCm38.p4 C57BL/6J

      Range
      111027827..111055569
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. XM_006530921.2XP_006530984.1  alanine--tRNA ligase, cytoplasmic isoform X1

      See identical proteins and their annotated locations for XP_006530984.1

      UniProtKB/Swiss-Prot
      Q8BGQ7
      Conserved Domains (5) summary
      PLN02900
      Location:6961
      PLN02900; alanyl-tRNA synthetase
      cd00673
      Location:7254
      AlaRS_core; Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      pfam02272
      Location:886955
      DHHA1; DHHA1 domain
      pfam07973
      Location:694752
      tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
      cl02787
      Location:495531
      Translation_Factor_II_like; Domain II of Elongation factor Tu (EF-Tu)-like proteins
    2. XM_006530922.1XP_006530985.1  alanine--tRNA ligase, cytoplasmic isoform X1

      See identical proteins and their annotated locations for XP_006530985.1

      UniProtKB/Swiss-Prot
      Q8BGQ7
      Conserved Domains (5) summary
      PLN02900
      Location:6961
      PLN02900; alanyl-tRNA synthetase
      cd00673
      Location:7254
      AlaRS_core; Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      pfam02272
      Location:886955
      DHHA1; DHHA1 domain
      pfam07973
      Location:694752
      tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
      cl02787
      Location:495531
      Translation_Factor_II_like; Domain II of Elongation factor Tu (EF-Tu)-like proteins
    3. XM_017312748.1XP_017168237.1  alanine--tRNA ligase, cytoplasmic isoform X1

      UniProtKB/Swiss-Prot
      Q8BGQ7
      Conserved Domains (5) summary
      PLN02900
      Location:6961
      PLN02900; alanyl-tRNA synthetase
      cd00673
      Location:7254
      AlaRS_core; Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      pfam02272
      Location:886955
      DHHA1; DHHA1 domain
      pfam07973
      Location:694752
      tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
      cl02787
      Location:495531
      Translation_Factor_II_like; Domain II of Elongation factor Tu (EF-Tu)-like proteins
    4. XM_006530924.1XP_006530987.1  alanine--tRNA ligase, cytoplasmic isoform X1

      See identical proteins and their annotated locations for XP_006530987.1

      UniProtKB/Swiss-Prot
      Q8BGQ7
      Conserved Domains (5) summary
      PLN02900
      Location:6961
      PLN02900; alanyl-tRNA synthetase
      cd00673
      Location:7254
      AlaRS_core; Alanyl-tRNA synthetase (AlaRS) class II core catalytic domain. AlaRS is a homodimer. It is responsible for the attachment of alanine to the 3' OH group of ribose of the appropriate tRNA. This domain is primarily responsible for ATP-dependent formation of ...
      pfam02272
      Location:886955
      DHHA1; DHHA1 domain
      pfam07973
      Location:694752
      tRNA_SAD; Threonyl and Alanyl tRNA synthetase second additional domain
      cl02787
      Location:495531
      Translation_Factor_II_like; Domain II of Elongation factor Tu (EF-Tu)-like proteins
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