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    T16G1.9 EIF3k [ Caenorhabditis elegans ]

    Gene ID: 179778, updated on 9-Dec-2024

    Summary

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    Official Symbol
    T16G1.9
    Official Full Name
    EIF3k
    Primary source
    WormBase:WBGene00011802
    Locus tag
    CELE_T16G1.9
    See related
    AllianceGenome:WB:WBGene00011802
    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 hydrolase activity. [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See T16G1.9 in Genome Data Viewer
    Location:
    chromosome: V
    Exon count:
    11
    Sequence:
    Chromosome: V; NC_003283.11 (12946798..12950862, complement)

    Chromosome V - NC_003283.11Genomic Context describing neighboring genes Neighboring gene CHK kinase-like domain-containing protein Neighboring gene CHK kinase-like domain-containing protein Neighboring gene ncRNA Neighboring gene Ground-like domain-containing protein Neighboring gene Uncharacterized protein Neighboring gene Uncharacterized protein Neighboring gene D-aminoacyl-tRNA deacylase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003283.11

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. KIN-4/MAST kinase promotes PTEN-mediated longevity of Caenorhabditis elegans via binding through a PDZ domain. An SWA, et al. Aging Cell, 2019 Jun. PMID 30773781, Free PMC Article
    2. CCAR-1 works together with the U2AF large subunit UAF-1 to regulate alternative splicing. Lugano DI, et al. RNA Biol, 2024 Jan. PMID 38126797, Free PMC Article
    3. A genome-wide study of PDZ-domain interactions in C. elegans reveals a high frequency of non-canonical binding. Lenfant N, et al. BMC Genomics, 2010 Nov 26. PMID 21110867, Free PMC Article
    4. SIN-3 acts in distinct complexes to regulate the germline transcriptional program in Caenorhabditis elegans. Robert VJ, et al. Development, 2023 Nov 1. PMID 37818613, 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 (8) 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 chloroplast targeting sequence binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in protein targeting to chloroplast IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    EIF3k
    NP_506239.1
    • 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_003283.11 Reference assembly

      Range
      12946798..12950862 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_073838.5 → NP_506239.1  EIF3k [Caenorhabditis elegans]

      See identical proteins and their annotated locations for NP_506239.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      Q9U367
      Conserved Domains (3) summary
      COG0666
      Location:87 → 248
      ANKYR; Ankyrin repeat [Signal transduction mechanisms]
      sd00045
      Location:49 → 77
      ANK; ANK repeat [structural motif]
      cl00281
      Location:460 → 595
      metallo-dependent_hydrolases; Superfamily of metallo-dependent hydrolases (also called amidohydrolase superfamily) is a large group of proteins that show conservation in their 3-dimensional fold (TIM barrel) and in details of their active site. The vast majority of the members have a ...
    Nucleotide Protein
    Heading Accession and Version

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