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    POP1 ribonuclease P/MRP protein subunit POP1 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855500, updated on 18-Sep-2024

    Summary

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    Official Symbol
    POP1
    Official Full Name
    ribonuclease P/MRP protein subunit POP1
    Primary source
    SGD:S000005165
    Locus tag
    YNL221C
    See related
    AllianceGenome:SGD:S000005165; FungiDB:YNL221C; VEuPathDB:YNL221C
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables RNA binding activity. Contributes to ribonuclease MRP activity and ribonuclease P activity. Involved in RNA metabolic process. Part of nucleolar ribonuclease P complex; ribonuclease MRP complex; and telomerase holoenzyme complex. Human ortholog(s) of this gene implicated in anauxetic dysplasia 2. Orthologous to human POP1 (POP1 homolog, ribonuclease P/MRP subunit). [provided by Alliance of Genome Resources, Apr 2022]
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    Genomic context

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    See POP1 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (231068..233695, complement)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene RNA polymerase II subunit A C-terminal domain phosphatase Neighboring gene ncRNA Neighboring gene adenylosuccinate synthase Neighboring gene dolichyl-P-Man:Man(6)GlcNAc(2)-PP-dolichol alpha-1,2-mannosyltransferase

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001146.8

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP. Xiao S, et al. RNA, 2006 Jun. PMID 16618965, Free PMC Article
    2. The POP1 gene encodes a protein component common to the RNase MRP and RNase P ribonucleoproteins. Lygerou Z, et al. Genes Dev, 1994 Jun 15. PMID 7926742
    3. Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components. Fagerlund RD, et al. RNA, 2015 Sep. PMID 26135751, Free PMC Article
    4. A new role for proteins subunits of RNase P: stabilization of the telomerase holoenzyme. Garcia PD, et al. Microb Cell, 2020 Jun 17. PMID 32904320, Free PMC Article
    5. Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate. Esakova O, et al. Nucleic Acids Res, 2013 Aug. PMID 23700311, Free PMC Article

    See all (58) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. In pop mutants, TLC1 is more abundant, telomeres are short, and TLC1 accumulates in the cytoplasm. Although Est1/2 binding to TLC1 occurs at normal levels, Est1 (and hence Est3) binding is highly unstable.
      Title: Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP.
    2. Study reports that the Pop1, Pop6, and Pop7 proteins, known components of RNase P and RNase MRP, bind to yeast telomerase RNA and are essential constituents of the telomerase holoenzyme.
      Title: Active Yeast Telomerase Shares Subunits with Ribonucleoproteins RNase P and RNase MRP.
    3. Results suggest that Pop1 plays the role of a scaffold for the stabilization of the global architecture of eukaryotic RNase P RNA, substituting for the network of RNA-RNA tertiary interactions that maintain the global RNA structure in bacterial RNase P.
      Title: Footprinting analysis of interactions between the largest eukaryotic RNase P/MRP protein Pop1 and RNase P/MRP RNA components.
    4. This study shows that the Pop1p subunit plays multiple roles in the assembly and function of of RNases P and MRP, and that the functions can be differentiated through the mutations in conserved residues.
      Title: Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP.
    Submit: New GeneRIF Correction

    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 RNA binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables hydrolase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to ribonuclease MRP activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    enables ribonuclease P activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    contributes_to ribonuclease P activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in intronic box C/D snoRNA processing IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in nuclear-transcribed mRNA catabolic process, RNase MRP-dependent IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in rRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in rRNA processing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in tRNA 5'-leader removal IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA processing IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in tRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in tRNA processing IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of nucleolar ribonuclease P complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of nucleolar ribonuclease P complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of nucleolar ribonuclease P complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of ribonuclease MRP complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of ribonuclease MRP complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of ribonuclease MRP complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of ribonuclease MRP complex IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    part_of telomerase holoenzyme complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    ribonuclease P/MRP protein subunit POP1
    NP_014178.1
    • Subunit of RNase MRP, nuclear RNase P and telomerase complexes; RNase MRP cleaves pre-rRNA, nuclear RNase P cleaves tRNA precursors to generate mature 5' ends and facilitates turnover of nuclear RNAs, while telomerase replenishes telomeric DNA; binds to the RPR1 RNA subunit in RNase P

    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_001146.8 Reference assembly

      Range
      231068..233695 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183059.1 → NP_014178.1  TPA: ribonuclease P/MRP protein subunit POP1 [Saccharomyces cerevisiae S288C]

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W0W9, P41812
      UniProtKB/TrEMBL
      B3LP65, C7GPD6, N1NXP8
      Conserved Domains (2) summary
      pfam06978
      Location:62 → 299
      POP1; Ribonucleases P/MRP protein subunit POP1
      pfam08170
      Location:555 → 661
      POPLD; POPLD (NUC188) domain
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P41812.1

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