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O08760

- OGG1_MOUSE

UniProt

O08760 - OGG1_MOUSE

Protein

N-glycosylase/DNA lyase

Gene

Ogg1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 2 (01 Dec 2000)
      Previous versions | rss
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    Functioni

    DNA repair enzyme that incises DNA at 8-oxoG residues. Excises 7,8-dihydro-8-oxoguanine and 2,6-diamino-4-hydroxy-5-N-methylformamidopyrimidine (FAPY) from damaged DNA. Has a beta-lyase activity that nicks DNA 3' to the lesion.

    Catalytic activityi

    The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei149 – 1491DNABy similarity
    Binding sitei154 – 1541DNABy similarity
    Binding sitei204 – 2041DNABy similarity
    Active sitei249 – 2491Schiff-base intermediate with DNABy similarity
    Binding sitei266 – 26618-oxoguanine; via carbonyl oxygenBy similarity
    Binding sitei268 – 26818-oxoguanineBy similarity
    Binding sitei270 – 2701DNABy similarity
    Binding sitei287 – 2871DNABy similarity
    Binding sitei315 – 31518-oxoguanineBy similarity
    Binding sitei319 – 31918-oxoguanineBy similarity

    GO - Molecular functioni

    1. 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Source: MGI
    2. damaged DNA binding Source: InterPro
    3. DNA N-glycosylase activity Source: MGI
    4. microtubule binding Source: MGI
    5. oxidized base lesion DNA N-glycosylase activity Source: MGI
    6. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: MGI

    GO - Biological processi

    1. acute inflammatory response Source: Ensembl
    2. base-excision repair Source: MGI
    3. cellular response to cadmium ion Source: Ensembl
    4. DNA catabolic process, endonucleolytic Source: GOC
    5. DNA repair Source: MGI
    6. nucleotide-excision repair Source: InterPro
    7. regulation of protein import into nucleus, translocation Source: UniProtKB
    8. regulation of transcription, DNA-templated Source: UniProtKB
    9. response to drug Source: Ensembl
    10. response to estradiol Source: Ensembl
    11. response to ethanol Source: Ensembl
    12. response to folic acid Source: Ensembl
    13. response to oxidative stress Source: UniProtKB
    14. response to radiation Source: UniProtKB

    Keywords - Molecular functioni

    Glycosidase, Hydrolase, Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Enzyme and pathway databases

    ReactomeiREACT_205202. Recognition and association of DNA glycosylase with site containing an affected purine.
    REACT_205258. Cleavage of the damaged purine.
    REACT_220827. Displacement of DNA glycosylase by APE1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    N-glycosylase/DNA lyase
    Including the following 2 domains:
    8-oxoguanine DNA glycosylase (EC:3.2.2.-)
    DNA-(apurinic or apyrimidinic site) lyase (EC:4.2.99.18)
    Short name:
    AP lyase
    Gene namesi
    Name:Ogg1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:1097693. Ogg1.

    Subcellular locationi

    Nucleusnucleoplasm By similarity. Nucleus speckle By similarity. Nucleus matrix By similarity
    Note: Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells.By similarity

    GO - Cellular componenti

    1. mitochondrion Source: MGI
    2. nuclear matrix Source: UniProtKB
    3. nuclear speck Source: UniProtKB
    4. nucleoplasm Source: UniProtKB
    5. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 345345N-glycosylase/DNA lyasePRO_0000058592Add
    BLAST

    Proteomic databases

    PRIDEiO08760.

    PTM databases

    PhosphoSiteiO08760.

    Expressioni

    Tissue specificityi

    Highest expression in testis.

    Gene expression databases

    ArrayExpressiO08760.
    BgeeiO08760.
    CleanExiMM_OGG1.
    GenevestigatoriO08760.

    Interactioni

    Protein-protein interaction databases

    BioGridi201906. 2 interactions.
    IntActiO08760. 2 interactions.
    STRINGi10090.ENSMUSP00000032406.

    Structurei

    3D structure databases

    ProteinModelPortaliO08760.
    SMRiO08760. Positions 13-323.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the type-1 OGG1 family.Curated

    Phylogenomic databases

    eggNOGiCOG0122.
    HOVERGENiHBG001047.
    InParanoidiO08760.
    KOiK03660.
    OMAiSPQANKE.
    OrthoDBiEOG7XDBGB.
    PhylomeDBiO08760.
    TreeFamiTF323702.

    Family and domain databases

    Gene3Di1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    InterProiIPR011257. DNA_glycosylase.
    IPR003265. HhH-GPD_domain.
    IPR023170. HTH_base_excis_C.
    IPR004577. Ogg.
    IPR012904. OGG_N.
    [Graphical view]
    PfamiPF00730. HhH-GPD. 1 hit.
    PF07934. OGG_N. 1 hit.
    [Graphical view]
    SMARTiSM00478. ENDO3c. 1 hit.
    [Graphical view]
    SUPFAMiSSF48150. SSF48150. 1 hit.
    TIGRFAMsiTIGR00588. ogg. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O08760-1 [UniParc]FASTAAdd to Basket

    « Hide

    MLFRSWLPSS MRHRTLSSSP ALWASIPCPR SELRLDLVLA SGQSFRWKEQ    50
    SPAHWSGVLA DQVWTLTQTE DQLYCTVYRG DDSQVSRPTL EELETLHKYF 100
    QLDVSLAQLY SHWASVDSHF QRVAQKFQGV RLLRQDPTEC LFSFICSSNN 150
    NIARITGMVE RLCQAFGPRL IQLDDVTYHG FPNLHALAGP EAETHLRKLG 200
    LGYRARYVRA SAKAILEEQG GPAWLQQLRV APYEEAHKAL CTLPGVGAKV 250
    ADCICLMALD KPQAVPVDVH VWQIAHRDYG WHPKTSQAKG PSPLANKELG 300
    NFFRNLWGPY AGWAQAVLFS ADLRQPSLSR EPPAKRKKGS KRPEG 345
    Length:345
    Mass (Da):38,883
    Last modified:December 1, 2000 - v2
    Checksum:i75BB0DDB084E4947
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti10 – 101S → Q in AAB61289. (PubMed:9187114)Curated
    Sequence conflicti23 – 253WAS → SVA in AAB61289. (PubMed:9187114)Curated
    Sequence conflicti239 – 2391A → G in AAB61289. (PubMed:9187114)Curated
    Sequence conflicti299 – 2991L → S in CAA73883. 1 PublicationCurated
    Sequence conflicti329 – 3291S → F in AAB81133. (PubMed:9207108)Curated
    Sequence conflicti336 – 3361R → H in CAA73883. 1 PublicationCurated
    Sequence conflicti336 – 3361R → H in CAB65240. 1 PublicationCurated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003596 mRNA. Translation: AAB61289.1.
    Y11247 mRNA. Translation: CAA72117.1.
    U88621 mRNA. Translation: AAB68616.1.
    U96711 mRNA. Translation: AAB81133.1.
    AF000669 mRNA. Translation: AAB63151.1.
    AF012916
    , AF012912, AF012913, AF012914, AF012915 Genomic DNA. Translation: AAB94512.1.
    Y13479 mRNA. Translation: CAA73883.1.
    AJ001307 Genomic DNA. Translation: CAB65240.1.
    CCDSiCCDS20414.1.
    PIRiT46962.
    RefSeqiNP_035087.3. NM_010957.4.
    UniGeneiMm.43612.

    Genome annotation databases

    EnsembliENSMUST00000032406; ENSMUSP00000032406; ENSMUSG00000030271.
    GeneIDi18294.
    KEGGimmu:18294.
    UCSCiuc009dfh.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF003596 mRNA. Translation: AAB61289.1 .
    Y11247 mRNA. Translation: CAA72117.1 .
    U88621 mRNA. Translation: AAB68616.1 .
    U96711 mRNA. Translation: AAB81133.1 .
    AF000669 mRNA. Translation: AAB63151.1 .
    AF012916
    , AF012912 , AF012913 , AF012914 , AF012915 Genomic DNA. Translation: AAB94512.1 .
    Y13479 mRNA. Translation: CAA73883.1 .
    AJ001307 Genomic DNA. Translation: CAB65240.1 .
    CCDSi CCDS20414.1.
    PIRi T46962.
    RefSeqi NP_035087.3. NM_010957.4.
    UniGenei Mm.43612.

    3D structure databases

    ProteinModelPortali O08760.
    SMRi O08760. Positions 13-323.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201906. 2 interactions.
    IntActi O08760. 2 interactions.
    STRINGi 10090.ENSMUSP00000032406.

    PTM databases

    PhosphoSitei O08760.

    Proteomic databases

    PRIDEi O08760.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000032406 ; ENSMUSP00000032406 ; ENSMUSG00000030271 .
    GeneIDi 18294.
    KEGGi mmu:18294.
    UCSCi uc009dfh.2. mouse.

    Organism-specific databases

    CTDi 4968.
    MGIi MGI:1097693. Ogg1.

    Phylogenomic databases

    eggNOGi COG0122.
    HOVERGENi HBG001047.
    InParanoidi O08760.
    KOi K03660.
    OMAi SPQANKE.
    OrthoDBi EOG7XDBGB.
    PhylomeDBi O08760.
    TreeFami TF323702.

    Enzyme and pathway databases

    Reactomei REACT_205202. Recognition and association of DNA glycosylase with site containing an affected purine.
    REACT_205258. Cleavage of the damaged purine.
    REACT_220827. Displacement of DNA glycosylase by APE1.

    Miscellaneous databases

    NextBioi 293744.
    PROi O08760.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O08760.
    Bgeei O08760.
    CleanExi MM_OGG1.
    Genevestigatori O08760.

    Family and domain databases

    Gene3Di 1.10.1670.10. 1 hit.
    1.10.340.30. 1 hit.
    InterProi IPR011257. DNA_glycosylase.
    IPR003265. HhH-GPD_domain.
    IPR023170. HTH_base_excis_C.
    IPR004577. Ogg.
    IPR012904. OGG_N.
    [Graphical view ]
    Pfami PF00730. HhH-GPD. 1 hit.
    PF07934. OGG_N. 1 hit.
    [Graphical view ]
    SMARTi SM00478. ENDO3c. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48150. SSF48150. 1 hit.
    TIGRFAMsi TIGR00588. ogg. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue."
      Aburatani H., Hippo Y., Ishida T., Takashima R., Matsuba C., Kodama T., Takao M., Yasui A., Yamamoto K., Asano M., Fukasawa K., Yoshinari T., Inoue H., Otsuka E., Nishimura S.
      Cancer Res. 57:2151-2156(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer."
      Lu R., Nash H.M., Verdine G.L.
      Curr. Biol. 7:397-407(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    3. "Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites."
      Bjoras M., Luna L., Johnsen B.E., Hoff E., Haug T., Rognes T., Seeberg E.
      EMBO J. 16:6314-6322(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Lung.
    4. "Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase."
      Rosenquist T.A., Zharkov D.O., Grollman A.P.
      Proc. Natl. Acad. Sci. U.S.A. 94:7429-7434(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    5. "Genomic structure and chromosomal localization of the mouse Ogg1 gene that is involved in the repair of 8-hydroxyguanine in DNA damage."
      Tani M., Shinmura K., Kohno T., Takenoshita S., Nagamachi Y., Yokota J.
      Mamm. Genome 9:32-37(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: C3H/HeN.
      Tissue: Melanoma.
    6. Radicella J.P., Reille F., Dherin C., Boiteux S.
      Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
    7. "Complete genomic DNA sequence of the Mus musculus 8-oxoguanine DNA glycosylase 1 gene (OGH1)."
      Johnsen B., Luna L., Rognes T., Seeberg E.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: 129/Sv.
      Tissue: Embryonic stem cell.

    Entry informationi

    Entry nameiOGG1_MOUSE
    AccessioniPrimary (citable) accession number: O08760
    Secondary accession number(s): O08733
    , O08910, O08991, O35617, O35915, Q9QXE8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: December 1, 2000
    Last modified: October 1, 2014
    This is version 125 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Multifunctional enzyme, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3