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    NOP2 rRNA (cytosine-C5-)-methyltransferase NOP2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 855664, updated on 9-Dec-2024

    Summary

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    Official Symbol
    NOP2
    Official Full Name
    rRNA (cytosine-C5-)-methyltransferase NOP2
    Primary source
    SGD:S000005005
    Locus tag
    YNL061W
    See related
    AllianceGenome:SGD:S000005005; FungiDB:YNL061W; VEuPathDB:YNL061W
    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
    YNA1
    Summary
    Enables rRNA (cytosine-C5-)-methyltransferase activity. Involved in assembly of large subunit precursor of preribosome; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); and rRNA base methylation. Located in nucleolus. Part of preribosome, large subunit precursor. Used to study cancer. Orthologous to human NOP2 (NOP2 nucleolar protein). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See NOP2 in Genome Data Viewer
    Location:
    chromosome: XIV
    Exon count:
    1
    Sequence:
    Chromosome: XIV; NC_001146.8 (510540..512396)

    Chromosome XIV - NC_001146.8Genomic Context describing neighboring genes Neighboring gene S-adenosylmethionine-dependent methyltransferase Neighboring gene tRNA 1-methyladenosine methyltransferase subunit GCD10 Neighboring gene Arp5p Neighboring gene uncharacterized protein

    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. Yeast NOP2 encodes an essential nucleolar protein with homology to a human proliferation marker. de Beus E, et al. J Cell Biol, 1994 Dec. PMID 7806561, Free PMC Article
    2. Nop2p is required for pre-rRNA processing and 60S ribosome subunit synthesis in yeast. Hong B, et al. Mol Cell Biol, 1997 Jan. PMID 8972218, Free PMC Article
    3. A conserved motif in the yeast nucleolar protein Nop2p contains an essential cysteine residue. King M, et al. Biochem J, 1999 Jan 1. PMID 9854021, Free PMC Article
    4. Temperature sensitive nop2 alleles defective in synthesis of 25S rRNA and large ribosomal subunits in Saccharomyces cerevisiae. Hong B, et al. Nucleic Acids Res, 2001 Jul 15. PMID 11452018, Free PMC Article
    5. RNA methyltransferases utilize two cysteine residues in the formation of 5-methylcytosine. King MY, et al. Biochemistry, 2002 Sep 17. PMID 12220187

    See all (133) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Nop2 belongs to the large family of pre-ribosomal proteins and possesses two related functions in pre-rRNA processing: as an essential factor for cleavages and 5-methylcytosine : RNA : modification.
      Title: Eukaryotic rRNA Modification by Yeast 5-Methylcytosine-Methyltransferases and Human Proliferation-Associated Antigen p120.
    2. Nop2 catalyzes the methylation of m5C2870 in 25S rRNA.
      Title: Yeast Nop2 and Rcm1 methylate C2870 and C2278 of the 25S rRNA, respectively.
    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 IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables S-adenosylmethionine-dependent methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables methyltransferase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables rRNA (cytosine-C5-)-methyltransferase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables rRNA (cytosine-C5-)-methyltransferase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables rRNA (cytosine-C5-)-methyltransferase activity IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    enables rRNA (cytosine-C5-)-methyltransferase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in RNA methylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in RNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in assembly of large subunit precursor of preribosome IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in maturation of LSU-rRNA IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in methylation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in rRNA base methylation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in rRNA base methylation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in rRNA base methylation IGI
    Inferred from Genetic Interaction
    more info
    		 PubMed 
    involved_in rRNA base methylation IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in rRNA processing IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in ribosomal large subunit biogenesis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in ribosome biogenesis IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in nucleolus HDA PubMed 
    is_active_in nucleolus IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    located_in nucleolus IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in nucleolus IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in nucleus HDA PubMed 
    located_in nucleus IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of preribosome, large subunit precursor HDA PubMed 
    part_of preribosome, large subunit precursor IDA
    Inferred from Direct Assay
    more info
    		 PubMed 

    General protein information

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    Preferred Names
    rRNA (cytosine-C5-)-methyltransferase NOP2
    NP_014338.3
    • rRNA m5C methyltransferase; methylates cytosine at position 2870 of 25S rRNA; has an essential function independent of rRNA methylation; contains seven beta-strand methyltransferase motif; essential for processing and maturation of 27S pre-rRNA and large ribosomal subunit biogenesis; localized to the nucleolus; constituent of 66S pre-ribosomal particles; rRNA methylation defect and lethality are functionally complemented by human NOP2, a gene upregulated in cancer

    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
      510540..512396
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001182899.3 → NP_014338.3  TPA: rRNA (cytosine-C5-)-methyltransferase NOP2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014338.3

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W1B9, E9P914, P40991
      UniProtKB/TrEMBL
      A6ZS19, B3LNS0, B5VQY3, C7GLU2, G2WM44, N1NZI4
      Conserved Domains (1) summary
      TIGR00446
      Location:273 → 548
      nop2p; NOL1/NOP2/sun family putative RNA methylase
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P40991.1

    Gene LinkOut

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