U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

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

    Gene ID: 851899, updated on 9-Dec-2024

    Summary

    Go to the top of the page Help
    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, Dec 2024]
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    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

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001136.10

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae. Brevet A, et al. J Bacteriol, 1991 Sep. PMID 1653209, Free PMC Article
    2. Control of 5',5'-dinucleoside triphosphate catabolism by APH1, a Saccharomyces cerevisiae analog of human FHIT. Chen J, et al. J Bacteriol, 1998 May. PMID 9573184, Free PMC Article
    3. Control of dinucleoside polyphosphates by the FHIT-homologous HNT2 gene, adenine biosynthesis and heat shock in Saccharomyces cerevisiae. Rubio-Texeira M, et al. BMC Mol Biol, 2002 May 20. PMID 12028594, Free PMC Article
    4. Elimination of cap structures generated by mRNA decay involves the new scavenger mRNA decapping enzyme Aph1/FHIT together with DcpS. Taverniti V, et al. Nucleic Acids Res, 2015 Jan. PMID 25432955, Free PMC Article
    5. The neurodegenerative disease protein aprataxin resolves abortive DNA ligation intermediates. Ahel I, et al. Nature, 2006 Oct 12. PMID 16964241

    See all (24) citations in PubMed

    GeneRIFs: Gene References Into Functions

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    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

    Go to the top of the page Help
    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)

    Go to the top of the page Help

    NEW Try the new Transcript table

    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_001180613.1 → NP_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:16 → 135
      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 ...
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.

    Other Literature Sources
    Molecular Biology Databases
    Research Materials
    Tools