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    CET1 polynucleotide 5'-phosphatase [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855873, updated on 29-Jun-2024

    Summary

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    Gene symbol
    CET1
    Gene description
    polynucleotide 5'-phosphatase
    Primary source
    FungiDB:YPL228W
    Locus tag
    YPL228W
    See related
    SGD:S000006149; AllianceGenome:SGD:S000006149; VEuPathDB:YPL228W
    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
    CES5
    Summary
    Enables polynucleotide 5'-phosphatase activity. Involved in several processes, including 7-methylguanosine mRNA capping; polynucleotide dephosphorylation; and positive regulation of transcription elongation from RNA polymerase II promoter. Part of mRNA cap methyltransferase complex. [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See CET1 in Genome Data Viewer
    Location:
    chromosome: XVI
    Exon count:
    1
    Sequence:
    Chromosome: XVI; NC_001148.4 (118382..120031)

    Chromosome XVI - NC_001148.4Genomic Context describing neighboring genes Neighboring gene Usv1p Neighboring gene uncharacterized protein Neighboring gene dolichyl-phosphate beta-glucosyltransferase Neighboring gene New1p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001148.4

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Kribellosides, novel RNA 5'-triphosphatase inhibitors from the rare actinomycete Kribbella sp. MI481-42F6. Igarashi M, et al. J Antibiot (Tokyo), 2017 May. PMID 28074052
    2. High-throughput assays for yeast RNA 5' triphosphatase (Cet1p). Xu Y, et al. Anal Biochem, 2008 Jan 1. PMID 17707331
    3. Investigating the role of metal ions in the catalytic mechanism of the yeast RNA triphosphatase. Bisaillon M, et al. J Biol Chem, 2003 Sep 5. PMID 12819229
    4. Functional groups required for the stability of yeast RNA triphosphatase in vitro and in vivo. Bisaillon M, et al. J Biol Chem, 2001 Aug 10. PMID 11395522
    5. Structure-function analysis of the active site tunnel of yeast RNA triphosphatase. Bisaillon M, et al. J Biol Chem, 2001 May 18. PMID 11279161

    See all (75) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The results indicate that the Cet1p-Ceg1p interaction is important not only for the activation of Ceg1p, but also for nuclear import of the complex.
      Title: The essential role for the RNA triphosphatase Cet1p in nuclear import of the mRNA capping enzyme Cet1p-Ceg1p complex of Saccharomyces cerevisiae.
    2. The results demonstrate a novel role of Cet1p in regulation of promoter proximal accumulation of RNA polymerase II independently of mRNA capping activity, and hence transcription in vivo.
      Title: A novel role for Cet1p mRNA 5'-triphosphatase in promoter proximal accumulation of RNA polymerase II in Saccharomyces cerevisiase.
    3. Data show that the early Pol II elongation factor Spt5 contributes to stable recruitment of the mRNA capping enzymes Cet1, Ceg1, and Abd1 in the initiation-elongation transition of RNA polymerase II.
      Title: Cap completion and C-terminal repeat domain kinase recruitment underlie the initiation-elongation transition of RNA polymerase II.
    4. A crystal structure of Cet1-Ceg1 revealed a 176 kDa heterotetrameric complex composed of one Cet1 homodimer that associates with two Ceg1 molecules via interactions between the Ceg1 oligonucleotide binding domain and an extended Cet1 amino acid motif.
      Title: Structure of the Saccharomyces cerevisiae Cet1-Ceg1 mRNA capping apparatus.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    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 7-methylguanosine mRNA capping IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in 7-methylguanosine mRNA capping IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    involved_in positive regulation of protein localization to nucleus IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in positive regulation of transcription elongation by RNA polymerase II IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    part_of mRNA capping enzyme complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of mRNA capping enzyme complex IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    part_of mRNA capping enzyme complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  

    General protein information

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    Preferred Names
    polynucleotide 5'-phosphatase
    NP_015096.1
    • RNA 5'-triphosphatase involved in mRNA 5' capping; subunit of mRNA capping enzyme, which is a heterotetramer composed of a Cet1p homodimer and two molecules of guanylyltransferase Ceg1p; Cet1p also has a role in regulation of RNAPII pausing at promoter-proximal sites; interaction between Cet1p and Ceg1p is required for Ceg1p nuclear import; mammalian enzyme is single bifunctional polypeptide; human homolog RNGTT can complement yeast cet1 null mutant

    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_001148.4 Reference assembly

      Range
      118382..120031
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001184042.1 → NP_015096.1  TPA: polynucleotide 5'-phosphatase [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_015096.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W3E2, O13297, Q12197
      UniProtKB/TrEMBL
      A0A8H4BUE4, A6ZW27, B3LKK3, B5VSV5, C7GU67, C8ZIF1, G2WNV7, N1NVM9
      Conserved Domains (1) summary
      pfam02940
      Location:278 → 497
      mRNA_triPase; mRNA capping enzyme, beta chain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    O13297.2

    Gene LinkOut

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