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Protein

N-glycosylase/DNA lyase

Gene

OGG1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein 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)DescriptionActionsGraphical viewLength
Binding sitei149DNA5 Publications1
Binding sitei154DNA5 Publications1
Binding sitei204DNA5 Publications1
Active sitei249Schiff-base intermediate with DNA1 Publication1
Binding sitei2668-oxoguanine; via carbonyl oxygen1
Binding sitei2688-oxoguanine1
Binding sitei270DNA5 Publications1
Binding sitei287DNA5 Publications1
Binding sitei3158-oxoguanine1
Binding sitei3198-oxoguanine1

GO - Molecular functioni

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

GO - Biological processi

  • acute inflammatory response Source: Ensembl
  • aging Source: Ensembl
  • base-excision repair Source: ProtInc
  • cellular response to cadmium ion Source: Ensembl
  • cellular response to DNA damage stimulus Source: MGI
  • depurination Source: Reactome
  • depyrimidination Source: Reactome
  • negative regulation of apoptotic process Source: Ensembl
  • negative regulation of double-strand break repair via single-strand annealing Source: MGI
  • nucleotide-excision repair, DNA incision Source: MGI
  • regulation of protein import into nucleus, translocation Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • response to drug Source: Ensembl
  • response to estradiol Source: Ensembl
  • response to ethanol Source: Ensembl
  • response to folic acid Source: Ensembl
  • response to light stimulus Source: Ensembl
  • 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

BioCyciZFISH:HS03734-MONOMER.
BRENDAi3.2.2.23. 2681.
4.2.99.18. 2681.
ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110330. Recognition and association of DNA glycosylase with site containing an affected purine.
R-HSA-110331. Cleavage of the damaged purine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.
R-HSA-5649702. 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, MUTM, OGH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8125. OGG1.

Subcellular locationi

GO - Cellular componenti

  • mitochondrion Source: UniProtKB-SubCell
  • nuclear matrix Source: UniProtKB
  • nuclear speck Source: UniProtKB
  • nucleoplasm Source: UniProtKB
  • nucleus Source: MGI
  • protein complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion, Nucleus

Pathology & Biotechi

Involvement in diseasei

Renal cell carcinoma (RCC)
The disease may be caused by mutations affecting the gene represented in this entry.
Disease descriptionRenal cell carcinoma is a heterogeneous group of sporadic or hereditary carcinoma derived from cells of the proximal renal tubular epithelium. It is subclassified into clear cell renal carcinoma (non-papillary carcinoma), papillary renal cell carcinoma, chromophobe renal cell carcinoma, collecting duct carcinoma with medullary carcinoma of the kidney, and unclassified renal cell carcinoma. Clear cell renal cell carcinoma is the most common subtype.
See also OMIM:144700

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi249K → Q: Loss of activity. 1 Publication1
Mutagenesisi268D → E or Q: No effect on activity. 1 Publication1
Mutagenesisi268D → N: Decreases activity about 65-fold. 1 Publication1

Organism-specific databases

DisGeNETi4968.
MalaCardsiOGG1.
MIMi144700. phenotype.
OpenTargetsiENSG00000114026.
PharmGKBiPA31912.

Chemistry databases

ChEMBLiCHEMBL3396944.

Polymorphism and mutation databases

BioMutaiOGG1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000585911 – 345N-glycosylase/DNA lyaseAdd BLAST345

Proteomic databases

MaxQBiO15527.
PeptideAtlasiO15527.
PRIDEiO15527.

PTM databases

iPTMnetiO15527.
PhosphoSitePlusiO15527.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiENSG00000114026.
ExpressionAtlasiO15527. baseline and differential.
GenevisibleiO15527. HS.

Organism-specific databases

HPAiCAB047301.
HPA027514.

Interactioni

Protein-protein interaction databases

BioGridi111018. 8 interactors.
IntActiO15527. 4 interactors.
MINTiMINT-3292093.

Chemistry databases

BindingDBiO15527.

Structurei

Secondary structure

1345
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni16 – 18Combined sources3
Helixi20 – 22Combined sources3
Beta strandi24 – 27Combined sources4
Turni30 – 32Combined sources3
Helixi35 – 38Combined sources4
Turni39 – 42Combined sources4
Beta strandi48 – 51Combined sources4
Beta strandi54 – 59Combined sources6
Beta strandi62 – 68Combined sources7
Beta strandi70 – 78Combined sources9
Beta strandi81 – 83Combined sources3
Helixi90 – 99Combined sources10
Turni100 – 103Combined sources4
Helixi106 – 116Combined sources11
Helixi118 – 126Combined sources9
Helixi137 – 145Combined sources9
Turni146 – 149Combined sources4
Helixi152 – 166Combined sources15
Beta strandi169 – 173Combined sources5
Beta strandi176 – 179Combined sources4
Helixi184 – 187Combined sources4
Helixi192 – 198Combined sources7
Helixi204 – 217Combined sources14
Helixi222 – 226Combined sources5
Helixi227 – 229Combined sources3
Helixi233 – 240Combined sources8
Helixi248 – 258Combined sources11
Helixi269 – 279Combined sources11
Beta strandi284 – 287Combined sources4
Beta strandi289 – 292Combined sources4
Helixi293 – 307Combined sources15
Helixi311 – 323Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBMX-ray2.10A12-325[»]
1FN7X-ray2.60A12-325[»]
1HU0X-ray2.35A12-327[»]
1KO9X-ray2.15A1-345[»]
1LWVX-ray2.30A12-327[»]
1LWWX-ray2.10A12-327[»]
1LWYX-ray2.01A12-327[»]
1M3HX-ray2.05A12-325[»]
1M3QX-ray1.90A12-325[»]
1N39X-ray2.20A12-325[»]
1N3AX-ray2.20A12-325[»]
1N3CX-ray2.70A12-325[»]
1YQKX-ray2.50A12-327[»]
1YQLX-ray2.60A12-327[»]
1YQMX-ray2.50A12-327[»]
1YQRX-ray2.43A12-327[»]
2I5WX-ray2.60A12-323[»]
2NOBX-ray2.10A12-327[»]
2NOEX-ray2.20A12-327[»]
2NOFX-ray2.35A12-327[»]
2NOHX-ray2.01A12-327[»]
2NOIX-ray2.35A12-327[»]
2NOLX-ray2.57A12-327[»]
2NOZX-ray2.43A12-327[»]
2XHIX-ray1.55A1-345[»]
3IH7X-ray3.10A12-325[»]
3KTUX-ray2.30A12-325[»]
5AN4X-ray1.60A12-323[»]
ProteinModelPortaliO15527.
SMRiO15527.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15527.

Family & Domainsi

Sequence similaritiesi

Belongs to the type-1 OGG1 family.Curated

Phylogenomic databases

GeneTreeiENSGT00640000091554.
HOVERGENiHBG001047.
InParanoidiO15527.
KOiK03660.
OMAiFFRNLWG.
PhylomeDBiO15527.
TreeFamiTF323702.

Family and domain databases

CDDicd00056. ENDO3c. 1 hit.
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. Ogg1.
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.

Sequences (8)i

Sequence statusi: Complete.

This entry describes 8 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1A (identifier: O15527-1) [UniParc]FASTAAdd to basket
Also known as: Alpha

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPARALLPRR MGHRTLASTP ALWASIPCPR SELRLDLVLP SGQSFRWREQ
60 70 80 90 100
SPAHWSGVLA DQVWTLTQTE EQLHCTVYRG DKSQASRPTP DELEAVRKYF
110 120 130 140 150
QLDVTLAQLY HHWGSVDSHF QEVAQKFQGV RLLRQDPIEC LFSFICSSNN
160 170 180 190 200
NIARITGMVE RLCQAFGPRL IQLDDVTYHG FPSLQALAGP EVEAHLRKLG
210 220 230 240 250
LGYRARYVSA SARAILEEQG GLAWLQQLRE SSYEEAHKAL CILPGVGTKV
260 270 280 290 300
ADCICLMALD KPQAVPVDVH MWHIAQRDYS WHPTTSQAKG PSPQTNKELG
310 320 330 340
NFFRSLWGPY AGWAQAVLFS ADLRQSRHAQ EPPAKRRKGS KGPEG
Length:345
Mass (Da):38,782
Last modified:December 1, 2000 - v2
Checksum:iC284106ADEEC1FDD
GO
Isoform 1B (identifier: O15527-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → VSVPRCPP

Show »
Length:324
Mass (Da):36,433
Checksum:iFB6DAF62F162C353
GO
Isoform 1C (identifier: O15527-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → TPPSYRCCSV...VCTTRWGGGY

Show »
Length:410
Mass (Da):45,761
Checksum:iCA01660C056A09F0
GO
Isoform 2A (identifier: O15527-4) [UniParc]FASTAAdd to basket
Also known as: Beta

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → GLLGNAFDGH...HVMQASLLAL

Show »
Length:424
Mass (Da):47,237
Checksum:i0013B0F2D51FD316
GO
Isoform 2B (identifier: O15527-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     250-345: VADCICLMAL...RRKGSKGPEG → GLLGNAFDGH...HVMQASLLAL

Show »
Length:357
Mass (Da):39,729
Checksum:i0FAA63310FC13ADB
GO
Isoform 2C (identifier: O15527-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     191-195: EVEAH → PWQCI
     196-345: Missing.

Show »
Length:195
Mass (Da):22,210
Checksum:i16628F612964E282
GO
Isoform 2D (identifier: O15527-7) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → LCQVITTFMTFLGPHRLDQMPPEELQTSSSRLGGPPWQCI

Show »
Length:356
Mass (Da):40,095
Checksum:i40D1E4783F042C8F
GO
Isoform 2E (identifier: O15527-8) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → AGSDAS

Show »
Length:322
Mass (Da):36,085
Checksum:iE47B3CA5AE8CFABB
GO

Sequence cautioni

The sequence AAB84013 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti47W → WW in CAA10351 (Ref. 9) Curated1
Sequence conflicti308G → E in CAA10351 (Ref. 9) Curated1
Sequence conflicti316A → ATPPSLQ in AAB81132 (PubMed:9207108).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02483112G → E Found in a kidney cancer sample; no effect on activity; abolishes mitochondrial localization. 1 PublicationCorresponds to variant rs772520254dbSNPEnsembl.1
Natural variantiVAR_00951946R → Q Found in a clear cell renal cell carcinoma sample; somatic mutation; diminished activity. 1 PublicationCorresponds to variant rs104893751dbSNPEnsembl.1
Natural variantiVAR_02483285A → S Found in a lung cancer sample. 1 PublicationCorresponds to variant rs17050550dbSNPEnsembl.1
Natural variantiVAR_024833131R → Q Found in a lung cancer sample; loss of activity. 1 PublicationCorresponds to variant rs747638147dbSNPEnsembl.1
Natural variantiVAR_009520154R → H Found in a gastric cancer sample; no effect on base-excision activity; alters substrate specificity and strongly increases mutagenic mis-repair. 3 PublicationsCorresponds to variant rs56053615dbSNPEnsembl.1
Natural variantiVAR_014487229R → Q.1 PublicationCorresponds to variant rs1805373dbSNPEnsembl.1
Natural variantiVAR_024834232S → T Found in a kidney cancer sample. 1 Publication1
Natural variantiVAR_018890288A → V.1 PublicationCorresponds to variant rs3219012dbSNPEnsembl.1
Natural variantiVAR_014488320S → T.Corresponds to variant rs1801128dbSNPEnsembl.1
Natural variantiVAR_018891322D → N.1 PublicationCorresponds to variant rs3219014dbSNPEnsembl.1
Natural variantiVAR_009521326S → C Common polymorphism in the Japanese population. 4 PublicationsCorresponds to variant rs1052133dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_003750191 – 195EVEAH → PWQCI in isoform 2C. Curated5
Alternative sequenceiVSP_003751196 – 345Missing in isoform 2C. CuratedAdd BLAST150
Alternative sequenceiVSP_003749250 – 345VADCI…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2B. CuratedAdd BLAST96
Alternative sequenceiVSP_003746317 – 345VLFSA…KGPEG → VSVPRCPP in isoform 1B. 1 PublicationAdd BLAST29
Alternative sequenceiVSP_003747317 – 345VLFSA…KGPEG → TPPSYRCCSVPTCANPAMLR SHQQSAERVPKGRKARWGTL DKEIPQAPSPPFPTSLSPSP PSLMLGRGLPVTTSKARHPQ IKQSVCTTRWGGGY in isoform 1C. CuratedAdd BLAST29
Alternative sequenceiVSP_003748317 – 345VLFSA…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2A. 2 PublicationsAdd BLAST29
Alternative sequenceiVSP_003752317 – 345VLFSA…KGPEG → LCQVITTFMTFLGPHRLDQM PPEELQTSSSRLGGPPWQCI in isoform 2D. CuratedAdd BLAST29
Alternative sequenceiVSP_003753317 – 345VLFSA…KGPEG → AGSDAS in isoform 2E. CuratedAdd BLAST29

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88527 mRNA. Translation: AAB68614.1.
U88620 mRNA. Translation: AAB68615.1.
U96710 mRNA. Translation: AAB81132.1.
Y13277 mRNA. Translation: CAA73726.1.
Y11731 mRNA. Translation: CAA72414.1.
AF003595 mRNA. Translation: AAB61340.1.
AB000410 mRNA. Translation: BAA19103.1.
AF026691 mRNA. Translation: AAB84013.1. Different initiation.
Y11838 mRNA. Translation: CAA72536.1.
AJ131341 Genomic DNA. Translation: CAA10351.1.
AF088282 Genomic DNA. Translation: AAD41680.1.
AF088282 Genomic DNA. Translation: AAD41681.1.
AF088282 Genomic DNA. Translation: AAD41682.1.
AB019528 mRNA. Translation: BAA76635.1.
AB019529 mRNA. Translation: BAA76636.1.
AB019530 mRNA. Translation: BAA76637.1.
AB019531 mRNA. Translation: BAA76638.1.
AB019532 mRNA. Translation: BAA76639.1.
AK289858 mRNA. Translation: BAF82547.1.
AF521807 Genomic DNA. Translation: AAM74236.1.
AC022382 Genomic DNA. No translation available.
BC000657 mRNA. Translation: AAH00657.1.
CCDSiCCDS2576.1. [O15527-4]
CCDS2577.1. [O15527-5]
CCDS2578.1. [O15527-6]
CCDS2579.1. [O15527-7]
CCDS2580.1. [O15527-3]
CCDS2581.1. [O15527-1]
CCDS43046.1. [O15527-2]
CCDS46742.1. [O15527-8]
PIRiT45069.
RefSeqiNP_002533.1. NM_002542.5. [O15527-1]
NP_058212.1. NM_016819.3. [O15527-2]
NP_058213.1. NM_016820.3. [O15527-3]
NP_058214.1. NM_016821.2. [O15527-4]
NP_058434.1. NM_016826.2. [O15527-5]
NP_058436.1. NM_016827.2. [O15527-6]
NP_058437.1. NM_016828.2. [O15527-7]
NP_058438.1. NM_016829.2. [O15527-8]
UniGeneiHs.380271.

Genome annotation databases

EnsembliENST00000302003; ENSP00000305584; ENSG00000114026. [O15527-3]
ENST00000302008; ENSP00000305527; ENSG00000114026. [O15527-7]
ENST00000302036; ENSP00000306561; ENSG00000114026. [O15527-4]
ENST00000339511; ENSP00000345520; ENSG00000114026. [O15527-2]
ENST00000344629; ENSP00000342851; ENSG00000114026. [O15527-1]
ENST00000349503; ENSP00000303132; ENSG00000114026. [O15527-5]
ENST00000383826; ENSP00000373337; ENSG00000114026. [O15527-6]
ENST00000449570; ENSP00000403598; ENSG00000114026. [O15527-8]
GeneIDi4968.
KEGGihsa:4968.
UCSCiuc003bsh.4. human. [O15527-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U88527 mRNA. Translation: AAB68614.1.
U88620 mRNA. Translation: AAB68615.1.
U96710 mRNA. Translation: AAB81132.1.
Y13277 mRNA. Translation: CAA73726.1.
Y11731 mRNA. Translation: CAA72414.1.
AF003595 mRNA. Translation: AAB61340.1.
AB000410 mRNA. Translation: BAA19103.1.
AF026691 mRNA. Translation: AAB84013.1. Different initiation.
Y11838 mRNA. Translation: CAA72536.1.
AJ131341 Genomic DNA. Translation: CAA10351.1.
AF088282 Genomic DNA. Translation: AAD41680.1.
AF088282 Genomic DNA. Translation: AAD41681.1.
AF088282 Genomic DNA. Translation: AAD41682.1.
AB019528 mRNA. Translation: BAA76635.1.
AB019529 mRNA. Translation: BAA76636.1.
AB019530 mRNA. Translation: BAA76637.1.
AB019531 mRNA. Translation: BAA76638.1.
AB019532 mRNA. Translation: BAA76639.1.
AK289858 mRNA. Translation: BAF82547.1.
AF521807 Genomic DNA. Translation: AAM74236.1.
AC022382 Genomic DNA. No translation available.
BC000657 mRNA. Translation: AAH00657.1.
CCDSiCCDS2576.1. [O15527-4]
CCDS2577.1. [O15527-5]
CCDS2578.1. [O15527-6]
CCDS2579.1. [O15527-7]
CCDS2580.1. [O15527-3]
CCDS2581.1. [O15527-1]
CCDS43046.1. [O15527-2]
CCDS46742.1. [O15527-8]
PIRiT45069.
RefSeqiNP_002533.1. NM_002542.5. [O15527-1]
NP_058212.1. NM_016819.3. [O15527-2]
NP_058213.1. NM_016820.3. [O15527-3]
NP_058214.1. NM_016821.2. [O15527-4]
NP_058434.1. NM_016826.2. [O15527-5]
NP_058436.1. NM_016827.2. [O15527-6]
NP_058437.1. NM_016828.2. [O15527-7]
NP_058438.1. NM_016829.2. [O15527-8]
UniGeneiHs.380271.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EBMX-ray2.10A12-325[»]
1FN7X-ray2.60A12-325[»]
1HU0X-ray2.35A12-327[»]
1KO9X-ray2.15A1-345[»]
1LWVX-ray2.30A12-327[»]
1LWWX-ray2.10A12-327[»]
1LWYX-ray2.01A12-327[»]
1M3HX-ray2.05A12-325[»]
1M3QX-ray1.90A12-325[»]
1N39X-ray2.20A12-325[»]
1N3AX-ray2.20A12-325[»]
1N3CX-ray2.70A12-325[»]
1YQKX-ray2.50A12-327[»]
1YQLX-ray2.60A12-327[»]
1YQMX-ray2.50A12-327[»]
1YQRX-ray2.43A12-327[»]
2I5WX-ray2.60A12-323[»]
2NOBX-ray2.10A12-327[»]
2NOEX-ray2.20A12-327[»]
2NOFX-ray2.35A12-327[»]
2NOHX-ray2.01A12-327[»]
2NOIX-ray2.35A12-327[»]
2NOLX-ray2.57A12-327[»]
2NOZX-ray2.43A12-327[»]
2XHIX-ray1.55A1-345[»]
3IH7X-ray3.10A12-325[»]
3KTUX-ray2.30A12-325[»]
5AN4X-ray1.60A12-323[»]
ProteinModelPortaliO15527.
SMRiO15527.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111018. 8 interactors.
IntActiO15527. 4 interactors.
MINTiMINT-3292093.

Chemistry databases

BindingDBiO15527.
ChEMBLiCHEMBL3396944.

PTM databases

iPTMnetiO15527.
PhosphoSitePlusiO15527.

Polymorphism and mutation databases

BioMutaiOGG1.

Proteomic databases

MaxQBiO15527.
PeptideAtlasiO15527.
PRIDEiO15527.

Protocols and materials databases

DNASUi4968.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302003; ENSP00000305584; ENSG00000114026. [O15527-3]
ENST00000302008; ENSP00000305527; ENSG00000114026. [O15527-7]
ENST00000302036; ENSP00000306561; ENSG00000114026. [O15527-4]
ENST00000339511; ENSP00000345520; ENSG00000114026. [O15527-2]
ENST00000344629; ENSP00000342851; ENSG00000114026. [O15527-1]
ENST00000349503; ENSP00000303132; ENSG00000114026. [O15527-5]
ENST00000383826; ENSP00000373337; ENSG00000114026. [O15527-6]
ENST00000449570; ENSP00000403598; ENSG00000114026. [O15527-8]
GeneIDi4968.
KEGGihsa:4968.
UCSCiuc003bsh.4. human. [O15527-1]

Organism-specific databases

CTDi4968.
DisGeNETi4968.
GeneCardsiOGG1.
HGNCiHGNC:8125. OGG1.
HPAiCAB047301.
HPA027514.
MalaCardsiOGG1.
MIMi144700. phenotype.
601982. gene.
neXtProtiNX_O15527.
OpenTargetsiENSG00000114026.
PharmGKBiPA31912.
GenAtlasiSearch...

Phylogenomic databases

GeneTreeiENSGT00640000091554.
HOVERGENiHBG001047.
InParanoidiO15527.
KOiK03660.
OMAiFFRNLWG.
PhylomeDBiO15527.
TreeFamiTF323702.

Enzyme and pathway databases

BioCyciZFISH:HS03734-MONOMER.
BRENDAi3.2.2.23. 2681.
4.2.99.18. 2681.
ReactomeiR-HSA-110328. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
R-HSA-110329. Cleavage of the damaged pyrimidine.
R-HSA-110330. Recognition and association of DNA glycosylase with site containing an affected purine.
R-HSA-110331. Cleavage of the damaged purine.
R-HSA-110357. Displacement of DNA glycosylase by APEX1.
R-HSA-5649702. APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.

Miscellaneous databases

ChiTaRSiOGG1. human.
EvolutionaryTraceiO15527.
GeneWikiiOxoguanine_glycosylase.
GenomeRNAii4968.
PROiO15527.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000114026.
ExpressionAtlasiO15527. baseline and differential.
GenevisibleiO15527. HS.

Family and domain databases

CDDicd00056. ENDO3c. 1 hit.
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. Ogg1.
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...

Entry informationi

Entry nameiOGG1_HUMAN
AccessioniPrimary (citable) accession number: O15527
Secondary accession number(s): A8K1E3
, O00390, O00670, O00705, O14876, O95488, P78554, Q9BW42, Q9UIK0, Q9UIK1, Q9UIK2, Q9UL34, Q9Y2C0, Q9Y2C1, Q9Y6C3, Q9Y6C4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 2, 2016
This is version 183 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

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 one 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.