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    HNT2 bis(5'-adenosyl)-triphosphatase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 851899, updated on 2-Nov-2024

    Summary

    Official Symbol
    HNT2
    Official Full Name
    bis(5'-adenosyl)-triphosphatase
    Primary source
    SGD:S000002713
    Locus tag
    YDR305C
    See related
    AllianceGenome:SGD:S000002713; FungiDB:YDR305C; VEuPathDB:YDR305C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Also known as
    APH1
    Summary
    Enables ribonucleoside triphosphate phosphatase activity. Involved in nucleoside catabolic process. Located in mitochondrion and nucleus. Human ortholog(s) of this gene implicated in carcinoma (multiple); invasive ductal carcinoma; reproductive organ cancer (multiple); and urinary bladder cancer. Orthologous to human FHIT (fragile histidine triad diadenosine triphosphatase). [provided by Alliance of Genome Resources, Nov 2024]
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    Genomic context

    See HNT2 in Genome Data Viewer
    Location:
    chromosome: IV
    Exon count:
    2
    Sequence:
    Chromosome: IV; NC_001136.10 (1072746..1073488, complement)

    Chromosome IV - NC_001136.10Genomic Context describing neighboring genes Neighboring gene Rsc3p Neighboring gene peptidylprolyl isomerase family protein CPR5 Neighboring gene Pfu1p Neighboring gene tRNA-Val

    Interactions

    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables bis(5'-adenosyl)-triphosphatase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity IBA
    Inferred from Biological aspect of Ancestor
    more info
     
    enables catalytic activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables hydrolase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
     
    enables nucleotide binding IEA
    Inferred from Electronic Annotation
    more info
     
    enables ribonucleoside triphosphate phosphatase activity IDA
    Inferred from Direct Assay
    more info
    PubMed 
    Process Evidence Code Pubs
    involved_in nucleoside catabolic process IMP
    Inferred from Mutant Phenotype
    more info
    PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
     
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
     
    located_in nucleus HDA PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
     

    General protein information

    Preferred Names
    bis(5'-adenosyl)-triphosphatase
    NP_010591.1
    • Dinucleoside triphosphate hydrolase; has similarity to the tumor suppressor FHIT and belongs to the histidine triad (HIT) superfamily of nucleotide-binding proteins

    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_001136.10 Reference assembly

      Range
      1072746..1073488 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001180613.1NP_010591.1  TPA: bis(5'-adenosyl)-triphosphatase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_010591.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      G2WB43
      Conserved Domains (1) summary
      cd01275
      Location:16135
      FHIT; FHIT (fragile histidine family): FHIT proteins, related to the HIT family carry a motif HxHxH/Qxx (x, is a hydrophobic amino acid), On the basis of sequence, substrate specificity, structure, evolution and mechanism, HIT proteins are classified into ...