SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O08760

- OGG1_MOUSE

UniProt

O08760 - OGG1_MOUSE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

N-glycosylase/DNA lyase

Gene
Ogg1
Organism
Mus musculus (Mouse)
Status
Reviewed - 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 – 1491DNA By similarity
Binding sitei154 – 1541DNA By similarity
Binding sitei204 – 2041DNA By similarity
Active sitei249 – 2491Schiff-base intermediate with DNA By similarity
Binding sitei266 – 26618-oxoguanine; via carbonyl oxygen By similarity
Binding sitei268 – 26818-oxoguanine By similarity
Binding sitei270 – 2701DNA By similarity
Binding sitei287 – 2871DNA By similarity
Binding sitei315 – 31518-oxoguanine By similarity
Binding sitei319 – 31918-oxoguanine By 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
Complete GO annotation...

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
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

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.

Family & Domainsi

Sequence similaritiesi

Belongs to the type-1 OGG1 family.

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

Sequence conflict

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

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: September 3, 2014
This is version 124 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