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Protein

N-glycosylase/DNA lyase

Gene

Ogg1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

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 binding Source: MGI
  4. DNA N-glycosylase activity Source: MGI
  5. microtubule binding Source: MGI
  6. oxidized base lesion DNA N-glycosylase activity Source: MGI
  7. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: MGI

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. aging Source: Ensembl
  3. base-excision repair Source: MGI
  4. cellular response to cadmium ion Source: Ensembl
  5. cellular response to DNA damage stimulus Source: MGI
  6. DNA catabolic process, endonucleolytic Source: GOC
  7. DNA repair Source: MGI
  8. negative regulation of apoptotic process Source: Ensembl
  9. negative regulation of double-strand break repair via single-strand annealing Source: MGI
  10. nucleotide-excision repair, DNA incision Source: MGI
  11. regulation of protein import into nucleus, translocation Source: UniProtKB
  12. regulation of transcription, DNA-templated Source: UniProtKB
  13. response to drug Source: Ensembl
  14. response to estradiol Source: Ensembl
  15. response to ethanol Source: Ensembl
  16. response to folic acid Source: Ensembl
  17. response to oxidative stress Source: UniProtKB
  18. response to radiation Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Glycosidase, Hydrolase, Lyase

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_325412. Recognition and association of DNA glycosylase with site containing an affected purine.
REACT_338868. Displacement of DNA glycosylase by APE1.
REACT_347291. Cleavage of the damaged purine.

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 Componenti: 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
  6. protein complex Source: MGI
Complete GO annotation...

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

BgeeiO08760.
CleanExiMM_OGG1.
ExpressionAtlasiO08760. baseline and differential.
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.
OMAiFFRNLWG.
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

        10         20         30         40         50
MLFRSWLPSS MRHRTLSSSP ALWASIPCPR SELRLDLVLA SGQSFRWKEQ
60 70 80 90 100
SPAHWSGVLA DQVWTLTQTE DQLYCTVYRG DDSQVSRPTL EELETLHKYF
110 120 130 140 150
QLDVSLAQLY SHWASVDSHF QRVAQKFQGV RLLRQDPTEC LFSFICSSNN
160 170 180 190 200
NIARITGMVE RLCQAFGPRL IQLDDVTYHG FPNLHALAGP EAETHLRKLG
210 220 230 240 250
LGYRARYVRA SAKAILEEQG GPAWLQQLRV APYEEAHKAL CTLPGVGAKV
260 270 280 290 300
ADCICLMALD KPQAVPVDVH VWQIAHRDYG WHPKTSQAKG PSPLANKELG
310 320 330 340
NFFRNLWGPY AGWAQAVLFS ADLRQPSLSR EPPAKRKKGS KRPEG
Length:345
Mass (Da):38,883
Last modified:November 30, 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 (Ref. 6) Curated
Sequence conflicti329 – 3291S → F in AAB81133 (PubMed:9207108).Curated
Sequence conflicti336 – 3361R → H in CAA73883 (Ref. 6) Curated
Sequence conflicti336 – 3361R → H in CAB65240 (Ref. 7) Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiO08760.

Proteomic databases

PRIDEiO08760.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi4968.
MGIiMGI:1097693. Ogg1.

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiREACT_325412. Recognition and association of DNA glycosylase with site containing an affected purine.
REACT_338868. Displacement of DNA glycosylase by APE1.
REACT_347291. Cleavage of the damaged purine.

Miscellaneous databases

NextBioi293744.
PROiO08760.
SOURCEiSearch...

Gene expression databases

BgeeiO08760.
CleanExiMM_OGG1.
ExpressionAtlasiO08760. baseline and differential.
GenevestigatoriO08760.

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.
ProtoNetiSearch...

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(1996) [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(1996) [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(1996) [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(1996) [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(1997) [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 (MAY-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 (JUL-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: November 30, 2000
Last sequence update: November 30, 2000
Last modified: March 31, 2015
This is version 128 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.