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    M18.3 Asparagine synthetase domain-containing protein [ Caenorhabditis elegans ]

    Gene ID: 178154, updated on 7-Sep-2023

    Summary

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    Gene symbol
    M18.3
    Gene description
    Asparagine synthetase domain-containing protein
    Primary source
    WormBase:WBGene00010889
    Locus tag
    CELE_M18.3
    See related
    AllianceGenome:WB:WBGene00010889
    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 asparagine synthase (glutamine-hydrolyzing) activity. Predicted to be involved in asparagine biosynthetic process. Located in cytoplasm. Orthologous to human ASNSD1 (asparagine synthetase domain containing 1). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    Location:
    chromosome: IV
    Exon count:
    5
    Sequence:
    Chromosome: IV; NC_003282.8 (12105858..12108396)

    Chromosome IV - NC_003282.8Genomic Context describing neighboring genes Neighboring gene Protein ST7 homolog Neighboring gene Monensin-resistant homolog 2 Neighboring gene Collagen triple helix repeat protein;Nematode cuticle collagen N-terminal domain-containing protein Neighboring gene putative dynein light chain 2, cytoplasmic

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003282.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Determining the sub-cellular localization of proteins within Caenorhabditis elegans body wall muscle. Meissner B, et al. PLoS One, 2011. PMID 21611156, Free PMC Article
    2. EPIC: software toolkit for elution profile-based inference of protein complexes. Hu LZ, et al. Nat Methods, 2019 Aug. PMID 31308550, Free PMC Article
    3. Genome sequence of the nematode C. elegans: a platform for investigating biology. C. elegans Sequencing Consortium. Science, 1998 Dec 11. PMID 9851916

    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 asparagine synthase (glutamine-hydrolyzing) activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in asparagine biosynthetic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 

    General protein information

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    Preferred Names
    Asparagine synthetase domain-containing protein
    NP_502296.1
    • 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_003282.8 Reference assembly

      Range
      12105858..12108396
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_069895.8 → NP_502296.1  Asparagine synthetase domain-containing protein [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_502296.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q21555
      Conserved Domains (2) summary
      cd01991
      Location:201 → 446
      Asn_Synthase_B_C; The C-terminal domain of Asparagine Synthase B. This domain is always found associated n-terminal amidotransferase domain. Family members that contain this domain catalyse the conversion of aspartate to asparagine. Asparagine synthetase B catalyzes the ...
      cl00319
      Location:50 → 98
      Gn_AT_II; Glutamine amidotransferases class-II (GATase). The glutaminase domain catalyzes an amide nitrogen transfer from glutamine to the appropriate substrate. In this process, glutamine is hydrolyzed to glutamic acid and ammonia. This domain is related to ...
    Nucleotide Protein
    Heading Accession and Version

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