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O08760 (OGG1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 123. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
N-glycosylase/DNA lyase

Including the following 2 domains:

  1. 8-oxoguanine DNA glycosylase
    EC=3.2.2.-
  2. DNA-(apurinic or apyrimidinic site) lyase
    Short name=AP lyase
    EC=4.2.99.18
Gene names
Name:Ogg1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 activity

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.

Subcellular location

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.

Tissue specificity

Highest expression in testis.

Sequence similarities

Belongs to the type-1 OGG1 family.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentNucleus
   Molecular functionGlycosidase
Hydrolase
Lyase
   Technical termComplete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Inferred from direct assay Ref.4. Source: GOC

DNA repair

Inferred from mutant phenotype PubMed 11532868PubMed 12447686PubMed 12874039PubMed 17213818. Source: MGI

acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

base-excision repair

Inferred from direct assay Ref.4. Source: MGI

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

nucleotide-excision repair

Inferred from electronic annotation. Source: InterPro

regulation of protein import into nucleus, translocation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from sequence or structural similarity. Source: UniProtKB

response to drug

Inferred from electronic annotation. Source: Ensembl

response to estradiol

Inferred from electronic annotation. Source: Ensembl

response to ethanol

Inferred from electronic annotation. Source: Ensembl

response to folic acid

Inferred from electronic annotation. Source: Ensembl

response to oxidative stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to radiation

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from direct assay PubMed 14651853PubMed 18614015. Source: MGI

nuclear matrix

Inferred from sequence or structural similarity. Source: UniProtKB

nuclear speck

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from mutant phenotype PubMed 10557315. Source: MGI

   Molecular_function8-oxo-7,8-dihydroguanine DNA N-glycosylase activity

Inferred from mutant phenotype PubMed 12447686. Source: MGI

DNA N-glycosylase activity

Traceable author statement PubMed 12200441. Source: MGI

damaged DNA binding

Inferred from electronic annotation. Source: InterPro

microtubule binding

Inferred from direct assay PubMed 15725623. Source: MGI

oxidized base lesion DNA N-glycosylase activity

Traceable author statement PubMed 12200441. Source: MGI

oxidized purine nucleobase lesion DNA N-glycosylase activity

Inferred from direct assay Ref.4. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345N-glycosylase/DNA lyase
PRO_0000058592

Sites

Active site2491Schiff-base intermediate with DNA By similarity
Binding site1491DNA By similarity
Binding site1541DNA By similarity
Binding site2041DNA By similarity
Binding site26618-oxoguanine; via carbonyl oxygen By similarity
Binding site26818-oxoguanine By similarity
Binding site2701DNA By similarity
Binding site2871DNA By similarity
Binding site31518-oxoguanine By similarity
Binding site31918-oxoguanine By similarity

Experimental info

Sequence conflict101S → Q in AAB61289. Ref.1
Sequence conflict23 – 253WAS → SVA in AAB61289. Ref.1
Sequence conflict2391A → G in AAB61289. Ref.1
Sequence conflict2991L → S in CAA73883. Ref.6
Sequence conflict3291S → F in AAB81133. Ref.4
Sequence conflict3361R → H in CAA73883. Ref.6
Sequence conflict3361R → H in CAB65240. Ref.7

Sequences

Sequence LengthMass (Da)Tools
O08760 [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: 75BB0DDB084E4947

FASTA34538,883
        10         20         30         40         50         60 
MLFRSWLPSS MRHRTLSSSP ALWASIPCPR SELRLDLVLA SGQSFRWKEQ SPAHWSGVLA 

        70         80         90        100        110        120 
DQVWTLTQTE DQLYCTVYRG DDSQVSRPTL EELETLHKYF QLDVSLAQLY SHWASVDSHF 

       130        140        150        160        170        180 
QRVAQKFQGV RLLRQDPTEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG 

       190        200        210        220        230        240 
FPNLHALAGP EAETHLRKLG LGYRARYVRA SAKAILEEQG GPAWLQQLRV APYEEAHKAL 

       250        260        270        280        290        300 
CTLPGVGAKV ADCICLMALD KPQAVPVDVH VWQIAHRDYG WHPKTSQAKG PSPLANKELG 

       310        320        330        340 
NFFRNLWGPY AGWAQAVLFS ADLRQPSLSR EPPAKRKKGS KRPEG 

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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 expand/collapse EMBL AC list , AF012912, AF012913, AF012914, AF012915 Genomic DNA. Translation: AAB94512.1.
Y13479 mRNA. Translation: CAA73883.1.
AJ001307 Genomic DNA. Translation: CAB65240.1.
CCDSCCDS20414.1.
PIRT46962.
RefSeqNP_035087.3. NM_010957.4.
UniGeneMm.43612.

3D structure databases

ProteinModelPortalO08760.
SMRO08760. Positions 13-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid201906. 2 interactions.
IntActO08760. 2 interactions.
STRING10090.ENSMUSP00000032406.

PTM databases

PhosphoSiteO08760.

Proteomic databases

PRIDEO08760.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000032406; ENSMUSP00000032406; ENSMUSG00000030271.
GeneID18294.
KEGGmmu:18294.
UCSCuc009dfh.2. mouse.

Organism-specific databases

CTD4968.
MGIMGI:1097693. Ogg1.

Phylogenomic databases

eggNOGCOG0122.
HOVERGENHBG001047.
InParanoidO08760.
KOK03660.
OMASPQANKE.
OrthoDBEOG7XDBGB.
PhylomeDBO08760.
TreeFamTF323702.

Gene expression databases

ArrayExpressO08760.
BgeeO08760.
CleanExMM_OGG1.
GenevestigatorO08760.

Family and domain databases

Gene3D1.10.1670.10. 1 hit.
1.10.340.30. 1 hit.
InterProIPR011257. DNA_glycosylase.
IPR003265. HhH-GPD_domain.
IPR023170. HTH_base_excis_C.
IPR004577. Ogg.
IPR012904. OGG_N.
[Graphical view]
PfamPF00730. HhH-GPD. 1 hit.
PF07934. OGG_N. 1 hit.
[Graphical view]
SMARTSM00478. ENDO3c. 1 hit.
[Graphical view]
SUPFAMSSF48150. SSF48150. 1 hit.
TIGRFAMsTIGR00588. ogg. 1 hit.
ProtoNetSearch...

Other

NextBio293744.
PROO08760.
SOURCESearch...

Entry information

Entry nameOGG1_MOUSE
AccessionPrimary (citable) accession number: O08760
Secondary accession number(s): O08733 expand/collapse secondary AC list , O08910, O08991, O35617, O35915, Q9QXE8
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 123 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot