U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    CTL1 polynucleotide 5'-phosphatase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855218, updated on 9-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    CTL1
    Official Full Name
    polynucleotide 5'-phosphatase
    Primary source
    SGD:S000004792
    Locus tag
    YMR180C
    See related
    AllianceGenome:SGD:S000004792; FungiDB:YMR180C; VEuPathDB:YMR180C
    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
    CTH1
    Summary
    Enables polynucleotide 5'-phosphatase activity. Predicted to be involved in 7-methylguanosine mRNA capping. Located in cytoplasm and nucleus. [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 CTL1 in Genome Data Viewer
    Location:
    chromosome: XIII
    Exon count:
    1
    Sequence:
    Chromosome: XIII; NC_001145.3 (622251..623213, complement)

    Chromosome XIII - NC_001145.3Genomic Context describing neighboring genes Neighboring gene Fpy1p Neighboring gene Spt21p Neighboring gene uncharacterized protein Neighboring gene Rgm1p

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_001145.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. A Saccharomyces cerevisiae RNA 5'-triphosphatase related to mRNA capping enzyme. Rodriguez CR, et al. Nucleic Acids Res, 1999 May 15. PMID 10219091, Free PMC Article
    2. Mutational analyses of yeast RNA triphosphatases highlight a common mechanism of metal-dependent NTP hydrolysis and a means of targeting enzymes to pre-mRNAs in vivo by fusion to the guanylyltransferase component of the capping apparatus. Pei Y, et al. J Biol Chem, 1999 Oct 8. PMID 10506129
    3. Genome-wide screen identifies host genes affecting viral RNA recombination. Serviene E, et al. Proc Natl Acad Sci U S A, 2005 Jul 26. PMID 16027361, Free PMC Article
    4. Identification of novel Saccharomyces cerevisiae proteins with nuclear export activity: cell cycle-regulated transcription factor ace2p shows cell cycle-independent nucleocytoplasmic shuttling. Jensen TH, et al. Mol Cell Biol, 2000 Nov. PMID 11027275, Free PMC Article
    5. Cross-linking Mass Spectrometry Analysis of the Yeast Nucleus Reveals Extensive Protein-Protein Interactions Not Detected by Systematic Two-Hybrid or Affinity Purification-Mass Spectrometry. Bartolec TK, et al. Anal Chem, 2020 Jan 21. PMID 31851481

    See all (22) 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 hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables mRNA 5'-triphosphate monophosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables polynucleotide 5'-phosphatase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables polynucleotide 5'-phosphatase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables polynucleotide 5'-phosphatase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in 7-methylguanosine mRNA capping IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in biological_process ND
    No biological Data available
    more info
    		  
    involved_in mRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of mRNA capping enzyme complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

    Go to the top of the page Help
    Preferred Names
    polynucleotide 5'-phosphatase
    NP_013905.1
    • RNA 5'-triphosphatase, localizes to both the nucleus and cytoplasm; CTL1 has a paralog, CET1, that arose from the whole genome duplication

    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_001145.3 Reference assembly

      Range
      622251..623213 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182686.1 → NP_013905.1  TPA: polynucleotide 5'-phosphatase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_013905.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W003, Q03220
      UniProtKB/TrEMBL
      A6ZMP0, B3LM66, C8ZF43, N1P5R1
      Conserved Domains (1) summary
      pfam02940
      Location:61 → 278
      mRNA_triPase; mRNA capping enzyme, beta chain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q03220.1

    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