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    ears-1 glutamate--tRNA ligase [ Caenorhabditis elegans ]

    Gene ID: 172904, updated on 9-Dec-2024

    Summary

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    Official Symbol
    ears-1
    Official Full Name
    glutamate--tRNA ligase
    Primary source
    WormBase:WBGene00001337
    Locus tag
    CELE_ZC434.5
    See related
    AllianceGenome:WB:WBGene00001337
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Caenorhabditis elegans (strain: Bristol N2)
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida; Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae; Caenorhabditis
    Summary
    Predicted to enable glutamate-tRNA ligase activity. Predicted to be involved in glutamyl-tRNA aminoacylation. Predicted to be located in cytoplasm. Predicted to be part of methionyl glutamyl tRNA synthetase complex. Predicted to be active in cytosol. Human ortholog(s) of this gene implicated in hypomyelinating leukodystrophy 15. Orthologous to human EPRS1 (glutamyl-prolyl-tRNA synthetase 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See ears-1 in Genome Data Viewer
    Location:
    chromosome: I
    Exon count:
    7
    Sequence:
    Chromosome: I; NC_003279.8 (10336395..10341178)

    Chromosome I - NC_003279.8Genomic Context describing neighboring genes Neighboring gene DUF3421 domain-containing protein Neighboring gene DUF3421 domain-containing protein Neighboring gene Nicastrin Neighboring gene Cytochrome c oxidase assembly factor 6 homolog;PRORP domain-containing protein Neighboring gene putative arginine kinase ZC434.8 Neighboring gene ShKT domain-containing protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003279.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Caenorhabditis elegans evolves a new architecture for the multi-aminoacyl-tRNA synthetase complex. Havrylenko S, et al. J Biol Chem, 2011 Aug 12. PMID 21685384, Free PMC Article
    2. AdipoR2 recruits protein interactors to promote fatty acid elongation and membrane fluidity. Ruiz M, et al. J Biol Chem, 2023 Jun. PMID 37164154, Free PMC Article
    3. Functional identification of microRNA-centered complexes in C. elegans. Hebbar S, et al. Sci Rep, 2022 May 3. PMID 35504914, Free PMC Article
    4. Caenorhabditis elegans ALG-1 antimorphic mutations uncover functions for Argonaute in microRNA guide strand selection and passenger strand disposal. Zinovyeva AY, et al. Proc Natl Acad Sci U S A, 2015 Sep 22. PMID 26351692, Free PMC Article
    5. Depletion of endogenously biotinylated carboxylases enhances the sensitivity of TurboID-mediated proximity labeling in Caenorhabditis elegans. Artan M, et al. J Biol Chem, 2022 Sep. PMID 35933017, Free PMC Article

    See all (11) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Markers

    Homology

    Gene Ontology Provided by WormBase

    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 catalytic activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables glutamate-tRNA ligase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables glutamate-tRNA ligase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in glutamyl-tRNA aminoacylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glutamyl-tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA aminoacylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA aminoacylation for protein translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in translation IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    part_of aminoacyl-tRNA synthetase multienzyme complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in cytosol IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of methionyl glutamyl tRNA synthetase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    glutamate--tRNA ligase
    NP_001366832.1
    • Confirmed by transcript evidence

    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_003279.8 Reference assembly

      Range
      10336395..10341178
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001381193.2 → NP_001366832.1  glutamate--tRNA ligase [Caenorhabditis elegans]

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q23315
      Conserved Domains (3) summary
      PLN02907
      Location:6 → 708
      PLN02907; glutamate-tRNA ligase
      cd00936
      Location:878 → 927
      WEPRS_RNA; WEPRS_RNA binding domain. This short RNA-binding domain is found in several higher eukaryote aminoacyl-tRNA synthetases (aaRSs). It is found in multiple copies in eukaryotic bifunctional glutamyl-prolyl-tRNA synthetases (EPRS) in a region that separates ...
      cl00349
      Location:733 → 782
      S15_NS1_EPRS_RNA-bind; S15/NS1/EPRS_RNA-binding domain. This short domain consists of a helix-turn-helix structure, which can bind to several types of RNA. It is found in the ribosomal protein S15, the influenza A viral nonstructural protein (NSA) and in several eukaryotic ...
    Nucleotide Protein
    Heading Accession and Version

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