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Protein

N-glycosylase/DNA lyase

Gene

Ogg1

Organism
Rattus norvegicus (Rat)
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

  • 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Source: Ensembl
  • damaged DNA binding Source: RGD
  • DNA N-glycosylase activity Source: RGD
  • oxidized purine nucleobase lesion DNA N-glycosylase activity Source: RGD

GO - Biological processi

  • acute inflammatory response Source: RGD
  • aging Source: RGD
  • base-excision repair Source: RGD
  • cellular response to cadmium ion Source: RGD
  • negative regulation of apoptotic process Source: RGD
  • nucleotide-excision repair Source: InterPro
  • regulation of protein import into nucleus, translocation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • response to drug Source: RGD
  • response to estradiol Source: RGD
  • response to ethanol Source: RGD
  • response to folic acid Source: RGD
  • response to light stimulus Source: RGD
  • response to oxidative stress Source: UniProtKB
  • 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_302616. Displacement of DNA glycosylase by APEX1.
REACT_311799. Cleavage of the damaged pyrimidine.
REACT_327769. Cleavage of the damaged purine.
REACT_358884. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

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
Synonyms:Mmh, Ogh1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621168. Ogg1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: RGD
  • nuclear matrix Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: RGD
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345N-glycosylase/DNA lyasePRO_0000058593Add
BLAST

Proteomic databases

PRIDEiO70249.

PTM databases

PhosphoSiteiO70249.

Expressioni

Gene expression databases

ExpressionAtlasiO70249. baseline.
GenevisibleiO70249. RN.

Interactioni

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011352.

Structurei

3D structure databases

ProteinModelPortaliO70249.
SMRiO70249. Positions 13-323.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the type-1 OGG1 family.Curated

Phylogenomic databases

eggNOGiCOG0122.
HOGENOMiHOG000180756.
HOVERGENiHBG001047.
InParanoidiO70249.
KOiK03660.
PhylomeDBiO70249.

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.

O70249-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLFSSSLSSS MRHRTLTSSP ALWASIPCPR SELRLDLVLA SGQSFRWREQ
60 70 80 90 100
SPAHWSGVLA DQVWTLTQTE DQLYCTVYRG DKGQVGRPTL EELETLHKYF
110 120 130 140 150
QLDVSLTQLY SHWASVDSHF QSVAQKFQGV RLLRQDPTEC LFSFICSSNN
160 170 180 190 200
NIARITGMVE RLCQAFGPRL VQLDDVTYHG FPNLHALAGP EVETHLRKLG
210 220 230 240 250
LGYRARYVCA SAKAILEEQG GPAWLQQLRV ASYEEAHKAL CTLPGVGTKV
260 270 280 290 300
ADCICLMALD KPQAVPVDIH VWQIAHRDYG WQPKTSQTKG PSPLANKELG
310 320 330 340
NFFRNLWGPY AGWAQAVLFS ADLRQQNLSR EPPAKRKKGS KKTEG
Length:345
Mass (Da):38,711
Last modified:August 1, 1998 - v1
Checksum:iB7FDF8C782644C41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029690 mRNA. Translation: AAC77525.1.
RefSeqiNP_110497.1. NM_030870.1.
UniGeneiRn.22623.

Genome annotation databases

GeneIDi81528.
KEGGirno:81528.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029690 mRNA. Translation: AAC77525.1.
RefSeqiNP_110497.1. NM_030870.1.
UniGeneiRn.22623.

3D structure databases

ProteinModelPortaliO70249.
SMRiO70249. Positions 13-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000011352.

PTM databases

PhosphoSiteiO70249.

Proteomic databases

PRIDEiO70249.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi81528.
KEGGirno:81528.

Organism-specific databases

CTDi4968.
RGDi621168. Ogg1.

Phylogenomic databases

eggNOGiCOG0122.
HOGENOMiHOG000180756.
HOVERGENiHBG001047.
InParanoidiO70249.
KOiK03660.
PhylomeDBiO70249.

Enzyme and pathway databases

ReactomeiREACT_302616. Displacement of DNA glycosylase by APEX1.
REACT_311799. Cleavage of the damaged pyrimidine.
REACT_327769. Cleavage of the damaged purine.
REACT_358884. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

Miscellaneous databases

NextBioi615069.
PROiO70249.

Gene expression databases

ExpressionAtlasiO70249. baseline.
GenevisibleiO70249. RN.

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. "Rat 7,8-dihydro-8-oxoguanine DNA glycosylase: substrate specificity, kinetics and cleavagemechanism at an apurinic site."
    Prieto Alamo M.J., Jurado J., Francastel E., Laval F.
    Nucleic Acids Res. 26:5199-5202(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Hepatoma.

Entry informationi

Entry nameiOGG1_RAT
AccessioniPrimary (citable) accession number: O70249
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: June 24, 2015
This is version 108 of the entry and version 1 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. 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.