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    NTG2 bifunctional N-glycosylase/AP lyase NTG2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 854114, updated on 9-Dec-2024

    Summary

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    Official Symbol
    NTG2
    Official Full Name
    bifunctional N-glycosylase/AP lyase NTG2
    Primary source
    SGD:S000005403
    Locus tag
    YOL043C
    See related
    AllianceGenome:SGD:S000005403; FungiDB:YOL043C; VEuPathDB:YOL043C
    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
    SCR2
    Summary
    Enables DNA-(apurinic or apyrimidinic site) endonuclease activity and oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity. Involved in base-excision repair, AP site formation. Located in nucleus. Human ortholog(s) of this gene implicated in familial adenomatous polyposis 3. Orthologous to human NTHL1 (nth like DNA glycosylase 1). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See NTG2 in Genome Data Viewer
    Location:
    chromosome: XV
    Exon count:
    1
    Sequence:
    Chromosome: XV; NC_001147.6 (248392..249534, complement)

    Chromosome XV - NC_001147.6Genomic Context describing neighboring genes Neighboring gene serine/threonine protein kinase PSK2 Neighboring gene Pex15p Neighboring gene RNA exonuclease Neighboring gene Nop12p

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001147.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. Yeast redoxyendonuclease, a DNA repair enzyme similar to Escherichia coli endonuclease III. Gossett J, et al. Biochemistry, 1988 Apr 5. PMID 2454659
    2. Purification, characterization, gene cloning, and expression of Saccharomyces cerevisiae redoxyendonuclease, a homolog of Escherichia coli endonuclease III. Augeri L, et al. Biochemistry, 1997 Jan 28. PMID 9020769
    3. Saccharomyces cerevisiae possesses two functional homologues of Escherichia coli endonuclease III. You HJ, et al. Biochemistry, 1998 Apr 28. PMID 9558341
    4. Substrate specificities of the ntg1 and ntg2 proteins of Saccharomyces cerevisiae for oxidized DNA bases are not identical. Sentürker S, et al. Nucleic Acids Res, 1998 Dec 1. PMID 9826748, Free PMC Article
    5. The Saccharomyces cerevisiae homologues of endonuclease III from Escherichia coli, Ntg1 and Ntg2, are both required for efficient repair of spontaneous and induced oxidative DNA damage in yeast. Alseth I, et al. Mol Cell Biol, 1999 May. PMID 10207101, Free PMC Article

    See all (70) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. The intracellular localization of the Saccharomyces cerevisiae N-glycosylase/AP lyases, Ntg1 and Ntg2, in response to nuclear and mitochondrial oxidative stress, was determined.
      Title: Dynamic compartmentalization of base excision repair proteins in response to nuclear and mitochondrial oxidative stress.
    2. The roles of OGG1 and NTG2 genes in the repair of lethal and mutagenic oxidative lesions induced by H2O2 and their relationships with iron and copper ions are discussed.
      Title: Role of OGG1 and NTG2 in the repair of oxidative DNA damage and mutagenesis induced by hydrogen peroxide in Saccharomyces cerevisiae: relationships with transition metals iron and copper.
    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 4 iron, 4 sulfur cluster binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA N-glycosylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables DNA-(apurinic or apyrimidinic site) endonuclease activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables DNA-(apurinic or apyrimidinic site) endonuclease activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables DNA-(apurinic or apyrimidinic site) endonuclease activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables class I DNA-(apurinic or apyrimidinic site) endonuclease activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables hydrolase activity, acting on glycosyl bonds IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidized base lesion DNA N-glycosylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables oxidized pyrimidine nucleobase lesion DNA N-glycosylase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    Process Evidence Code Pubs
    involved_in DNA repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in base-excision repair IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in base-excision repair IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in base-excision repair, AP site formation IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in base-excision repair, AP site formation IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in base-excision repair, AP site formation IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in nucleotide-excision repair IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    Component Evidence Code Pubs
    located_in intracellular membrane-bounded organelle IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in mitochondrion IEA
    Inferred from Electronic Annotation
    more info
    		  
    is_active_in nucleus 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

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    Preferred Names
    bifunctional N-glycosylase/AP lyase NTG2
    NP_014599.1
    • DNA N-glycosylase and apurinic/apyrimidinic (AP) lyase; involved in base excision repair, localizes to the nucleus; sumoylated; NTG2 has a paralog, NTG1, that arose from the whole genome duplication

    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_001147.6 Reference assembly

      Range
      248392..249534 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001183297.1 → NP_014599.1  TPA: bifunctional N-glycosylase/AP lyase NTG2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_014599.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D6W223, Q08214
      UniProtKB/TrEMBL
      A6ZNG6, B3LJ15, B5VRL0, C7GK12, C8ZHS1, G2WMJ0, N1P2S0
      Conserved Domains (1) summary
      COG0177
      Location:96 → 343
      Nth; Endonuclease III [Replication, recombination and repair]
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    Q08214.1

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