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    rrp40 exosome subunit Rrp40 [ Schizosaccharomyces pombe (fission yeast) ]

    Gene ID: 2541837, updated on 18-Sep-2024

    Summary

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    Official Symbol
    rrp40
    Official Full Name
    exosome subunit Rrp40
    Primary source
    PomBase:SPAC22A12.12c
    Locus tag
    SPOM_SPAC22A12.12C
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Schizosaccharomyces pombe (strain: 972h-)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina; Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae; Schizosaccharomyces
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    Genomic context

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    See rrp40 in Genome Data Viewer
    Location:
    chromosome: I
    Exon count:
    1
    Sequence:
    Chromosome: I; NC_003424.3 (1178856..1179940, complement)

    Chromosome I - NC_003424.3Genomic Context describing neighboring genes Neighboring gene U2 snRNP-associated protein Sap114 Neighboring gene ncRNA Neighboring gene CDP-alcohol phosphatidyltransferase class-I family protein Neighboring gene ncRNA Neighboring gene dihydroxyacetone kinase Dak1 Neighboring gene BSD domain-containing protein Neighboring gene ncRNA Neighboring gene pig-P phosphatidylinositol N-acetylglucosaminyltransferase subunit Neighboring gene ncRNA Neighboring gene ER heat shock protein BiP

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_003424.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The RNA exosome promotes transcription termination of backtracked RNA polymerase II. Lemay JF, et al. Nat Struct Mol Biol, 2014 Oct. PMID 25240800
    2. Helicase-Dependent RNA Decay Illuminated by a Cryo-EM Structure of a Human Nuclear RNA Exosome-MTR4 Complex. Weick EM, et al. Cell, 2018 Jun 14. PMID 29906447, Free PMC Article
    3. The Sm complex is required for the processing of non-coding RNAs by the exosome. Coy S, et al. PLoS One, 2013. PMID 23755256, Free PMC Article
    4. The exoribonuclease Dis3L2 defines a novel eukaryotic RNA degradation pathway. Malecki M, et al. EMBO J, 2013 Jul 3. PMID 23503588, Free PMC Article
    5. Proteomic profiling and functional characterization of post-translational modifications of the fission yeast RNA exosome. Telekawa C, et al. Nucleic Acids Res, 2018 Nov 30. PMID 30321377, Free PMC Article

    See all (9) citations in PubMed

    GeneRIFs: Gene References Into Functions

    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 PomBase

    Function Evidence Code Pubs
    enables RNA binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Process Evidence Code Pubs
    involved_in CUT catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in TRAMP-dependent tRNA surveillance pathway IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in U4 snRNA 3'-end processing IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in exonucleolytic trimming to generate mature 3'-end of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in nonfunctional rRNA decay ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in nuclear mRNA surveillance TAS
    Traceable Author Statement
    more info
    		 PubMed 
    involved_in nuclear polyadenylation-dependent mRNA catabolic process ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in nuclear polyadenylation-dependent rRNA catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in nuclear-transcribed mRNA catabolic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in nuclear-transcribed mRNA catabolic process, 3'-5' exonucleolytic nonsense-mediated decay ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in nuclear-transcribed mRNA catabolic process, non-stop decay ISO
    Inferred from Sequence Orthology
    more info
    		  
    involved_in poly(A)-dependent snoRNA 3'-end processing IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    part_of cytoplasmic exosome (RNase complex) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of exosome (RNase complex) IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of nuclear exosome (RNase complex) EXP
    Inferred from Experiment
    more info
    		 PubMed 
    part_of nuclear exosome (RNase complex) IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  

    General protein information

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    Preferred Names
    exosome subunit Rrp40

    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_003424.3 Reference assembly

      Range
      1178856..1179940 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001018639.3 → NP_593242.1  exosome subunit Rrp40 [Schizosaccharomyces pombe]

      See identical proteins and their annotated locations for NP_593242.1

      Status: PROVISIONAL

      UniProtKB/Swiss-Prot
      O13903
      Conserved Domains (3) summary
      COG1097
      Location:8 → 240
      Rrp4; Exosome complex RNA-binding protein Rrp4, contains S1 and KH domains [Translation, ribosomal structure and biogenesis]
      cd05790
      Location:71 → 157
      S1_Rrp40; S1_Rrp40: Rrp40 S1-like RNA-binding domain. S1-like RNA-binding domains are found in a wide variety of RNA-associated proteins. Rrp4 protein is a subunit of the exosome complex. The exosome plays a central role in 3' to 5' RNA processing and degradation ...
      pfam15985
      Location:160 → 207
      KH_6; KH domain
    Nucleotide Protein
    Heading Accession and Version

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