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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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei149 – 1491DNA5 Publications
Binding sitei154 – 1541DNA5 Publications
Binding sitei204 – 2041DNA5 Publications
Active sitei249 – 2491Schiff-base intermediate with DNA1 Publication
Binding sitei266 – 26618-oxoguanine; via carbonyl oxygen
Binding sitei268 – 26818-oxoguanine
Binding sitei270 – 2701DNA5 Publications
Binding sitei287 – 2871DNA5 Publications
Binding sitei315 – 31518-oxoguanine
Binding sitei319 – 31918-oxoguanine

GO - Molecular functioni

  1. 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity Source: Ensembl
  2. damaged DNA binding Source: ProtInc
  3. DNA N-glycosylase activity Source: GO_Central
  4. endonuclease activity Source: ProtInc
  5. oxidized purine nucleobase lesion DNA N-glycosylase activity Source: ProtInc

GO - Biological processi

  1. acute inflammatory response Source: Ensembl
  2. aging Source: Ensembl
  3. base-excision repair Source: GO_Central
  4. base-excision repair, AP site formation Source: Reactome
  5. cellular response to cadmium ion Source: Ensembl
  6. depurination Source: Reactome
  7. DNA repair Source: Reactome
  8. negative regulation of apoptotic process Source: Ensembl
  9. nucleic acid phosphodiester bond hydrolysis Source: GOC
  10. nucleotide-excision repair Source: InterPro
  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

BRENDAi3.2.2.23. 2681.
4.2.99.18. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_1729. Cleavage of the damaged purine.
REACT_2176. Recognition and association of DNA glycosylase with site containing an affected 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
Synonyms:MMH, MUTM, OGH1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:8125. OGG1.

Subcellular locationi

  1. Nucleusnucleoplasm 1 Publication
  2. Nucleus speckle 1 Publication
  3. Nucleus matrix 1 Publication

  4. Note: Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells.

GO - Cellular componenti

  1. mitochondrion Source: UniProtKB-SubCell
  2. nuclear matrix Source: UniProtKB
  3. nuclear speck Source: UniProtKB
  4. nucleoplasm Source: UniProtKB
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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi249 – 2491K → Q: Loss of activity. 1 Publication
Mutagenesisi268 – 2681D → E or Q: No effect on activity. 1 Publication
Mutagenesisi268 – 2681D → N: Decreases activity about 65-fold. 1 Publication

Organism-specific databases

MIMi144700. phenotype.
PharmGKBiPA31912.

Polymorphism and mutation databases

BioMutaiOGG1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 345345N-glycosylase/DNA lyasePRO_0000058591Add
BLAST

Proteomic databases

MaxQBiO15527.
PaxDbiO15527.
PRIDEiO15527.

PTM databases

PhosphoSiteiO15527.

Expressioni

Tissue specificityi

Ubiquitous.

Gene expression databases

BgeeiO15527.
ExpressionAtlasiO15527. baseline and differential.
GenevestigatoriO15527.

Organism-specific databases

HPAiCAB047301.
HPA027514.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
SNRPFP623061EBI-721675,EBI-356900

Protein-protein interaction databases

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

Structurei

Secondary structure

1
345
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni16 – 183Combined sources
Helixi20 – 223Combined sources
Beta strandi24 – 274Combined sources
Turni30 – 323Combined sources
Helixi35 – 384Combined sources
Turni39 – 424Combined sources
Beta strandi48 – 514Combined sources
Beta strandi54 – 596Combined sources
Beta strandi62 – 687Combined sources
Beta strandi70 – 789Combined sources
Beta strandi81 – 833Combined sources
Helixi90 – 9910Combined sources
Turni100 – 1034Combined sources
Helixi106 – 11611Combined sources
Helixi118 – 1269Combined sources
Helixi137 – 1459Combined sources
Turni146 – 1494Combined sources
Helixi152 – 16615Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi176 – 1794Combined sources
Helixi184 – 1874Combined sources
Helixi192 – 1987Combined sources
Helixi204 – 21714Combined sources
Helixi222 – 2265Combined sources
Helixi227 – 2293Combined sources
Helixi233 – 2408Combined sources
Helixi248 – 25811Combined sources
Helixi269 – 27911Combined sources
Beta strandi284 – 2874Combined sources
Beta strandi289 – 2924Combined sources
Helixi293 – 30715Combined sources
Helixi311 – 32313Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliO15527.
SMRiO15527. Positions 12-323.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO15527.

Family & Domainsi

Sequence similaritiesi

Belongs to the type-1 OGG1 family.Curated

Phylogenomic databases

eggNOGiCOG0122.
GeneTreeiENSGT00640000091554.
HOVERGENiHBG001047.
InParanoidiO15527.
KOiK03660.
OMAiHRFPTIE.
OrthoDBiEOG7XDBGB.
PhylomeDBiO15527.
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.

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 AAB84013.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti47 – 471W → WW in CAA10351 (Ref. 9) Curated
Sequence conflicti308 – 3081G → E in CAA10351 (Ref. 9) Curated
Sequence conflicti316 – 3161A → ATPPSLQ in AAB81132 (PubMed:9207108).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti12 – 121G → E Found in a kidney cancer sample; no effect on activity; abolishes mitochondrial localization. 1 Publication
VAR_024831
Natural varianti46 – 461R → Q Found in a clear cell renal cell carcinoma sample; somatic mutation; diminished activity. 1 Publication
Corresponds to variant rs104893751 [ dbSNP | Ensembl ].
VAR_009519
Natural varianti85 – 851A → S Found in a lung cancer sample. 1 Publication
Corresponds to variant rs17050550 [ dbSNP | Ensembl ].
VAR_024832
Natural varianti131 – 1311R → Q Found in a lung cancer sample; loss of activity. 1 Publication
VAR_024833
Natural varianti154 – 1541R → H Found in a gastric cancer sample; no effect on base-excision activity; alters substrate specificity and strongly increases mutagenic mis-repair. 3 Publications
Corresponds to variant rs56053615 [ dbSNP | Ensembl ].
VAR_009520
Natural varianti229 – 2291R → Q.1 Publication
Corresponds to variant rs1805373 [ dbSNP | Ensembl ].
VAR_014487
Natural varianti232 – 2321S → T Found in a kidney cancer sample. 1 Publication
VAR_024834
Natural varianti288 – 2881A → V.1 Publication
Corresponds to variant rs3219012 [ dbSNP | Ensembl ].
VAR_018890
Natural varianti320 – 3201S → T.
Corresponds to variant rs1801128 [ dbSNP | Ensembl ].
VAR_014488
Natural varianti322 – 3221D → N.1 Publication
Corresponds to variant rs3219014 [ dbSNP | Ensembl ].
VAR_018891
Natural varianti326 – 3261S → C Common polymorphism in the Japanese population. 4 Publications
Corresponds to variant rs1052133 [ dbSNP | Ensembl ].
VAR_009521

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei191 – 1955EVEAH → PWQCI in isoform 2C. CuratedVSP_003750
Alternative sequencei196 – 345150Missing in isoform 2C. CuratedVSP_003751Add
BLAST
Alternative sequencei250 – 34596VADCI…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2B. CuratedVSP_003749Add
BLAST
Alternative sequencei317 – 34529VLFSA…KGPEG → VSVPRCPP in isoform 1B. 1 PublicationVSP_003746Add
BLAST
Alternative sequencei317 – 34529VLFSA…KGPEG → TPPSYRCCSVPTCANPAMLR SHQQSAERVPKGRKARWGTL DKEIPQAPSPPFPTSLSPSP PSLMLGRGLPVTTSKARHPQ IKQSVCTTRWGGGY in isoform 1C. CuratedVSP_003747Add
BLAST
Alternative sequencei317 – 34529VLFSA…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2A. 2 PublicationsVSP_003748Add
BLAST
Alternative sequencei317 – 34529VLFSA…KGPEG → LCQVITTFMTFLGPHRLDQM PPEELQTSSSRLGGPPWQCI in isoform 2D. CuratedVSP_003752Add
BLAST
Alternative sequencei317 – 34529VLFSA…KGPEG → AGSDAS in isoform 2E. CuratedVSP_003753Add
BLAST

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.3. human. [O15527-2]
uc003bsi.3. human. [O15527-1]

Polymorphism and mutation databases

BioMutaiOGG1.

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
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[»]
ProteinModelPortaliO15527.
SMRiO15527. Positions 12-323.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

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

PTM databases

PhosphoSiteiO15527.

Polymorphism and mutation databases

BioMutaiOGG1.

Proteomic databases

MaxQBiO15527.
PaxDbiO15527.
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.3. human. [O15527-2]
uc003bsi.3. human. [O15527-1]

Organism-specific databases

CTDi4968.
GeneCardsiGC03P009791.
HGNCiHGNC:8125. OGG1.
HPAiCAB047301.
HPA027514.
MIMi144700. phenotype.
601982. gene.
neXtProtiNX_O15527.
PharmGKBiPA31912.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0122.
GeneTreeiENSGT00640000091554.
HOVERGENiHBG001047.
InParanoidiO15527.
KOiK03660.
OMAiHRFPTIE.
OrthoDBiEOG7XDBGB.
PhylomeDBiO15527.
TreeFamiTF323702.

Enzyme and pathway databases

BRENDAi3.2.2.23. 2681.
4.2.99.18. 2681.
ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_1729. Cleavage of the damaged purine.
REACT_2176. Recognition and association of DNA glycosylase with site containing an affected purine.

Miscellaneous databases

ChiTaRSiOGG1. human.
EvolutionaryTraceiO15527.
GeneWikiiOxoguanine_glycosylase.
GenomeRNAii4968.
NextBioi19116.
PROiO15527.
SOURCEiSearch...

Gene expression databases

BgeeiO15527.
ExpressionAtlasiO15527. baseline and differential.
GenevestigatoriO15527.

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

« Hide 'large scale' publications
  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] (ISOFORMS 1A; 1B AND 2A).
    Tissue: Colon.
  2. "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] (ISOFORM 1A).
  3. "Molecular cloning and functional expression of a human cDNA encoding the antimutator enzyme 8-hydroxyguanine-DNA glycosylase."
    Roldan-Arjona T., Wei Y.-F., Carter K.C., Klungland A., Anselmino C., Wang R.-P., Augustus M., Lindahl T.
    Proc. Natl. Acad. Sci. U.S.A. 94:8016-8020(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2A).
  4. "Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae."
    Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S.
    Proc. Natl. Acad. Sci. U.S.A. 94:8010-8015(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
  5. "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] (ISOFORM 1A), ACTIVE SITE, MUTAGENESIS OF LYS-249.
  6. "Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage."
    Arai K., Morishita K., Shinmura K., Kohno T., Taniwaki M., Ohwada S., Yokota J.
    Oncogene 14:2857-2861(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
  7. "Augmented expression of a human gene for 8-oxoguanine DNA glycosylase (MutM) in B lymphocytes of the dark zone in lymph node germinal centers."
    Kuo F.C., Sklar J.L.
    J. Exp. Med. 186:1547-1556(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
  8. "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] (ISOFORM 1A).
  9. "Genomic structure and promoter characterization of the human 8-OH-guanine glycosylase gene (OGG1) gene."
    Dhenaut A., Boiteux S., Radicella J.
    Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  10. "Structure and chromosome location of human OGG1."
    Ishida T., Hippo Y., Nakahori Y., Matsushita I., Kodama T., Nishimura S., Aburatani H.
    Cytogenet. Cell Genet. 85:232-236(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING.
  11. "Expression and differential intracellular localization of two major forms of human 8-Oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs."
    Nishioka K., Ohtsubo T., Oda H., Fujiwara T., Kang D., Sugimachi K., Nakabeppu Y.
    Mol. Biol. Cell 10:1637-1652(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
  12. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A), VARIANT CYS-326.
    Tissue: Brain.
  13. NIEHS SNPs program
    Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-229; VAL-288; ASN-322 AND CYS-326.
  14. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  15. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT CYS-326.
    Tissue: Eye.
  16. "The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis."
    Boiteux S., Radicella J.P.
    Arch. Biochem. Biophys. 377:1-8(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  17. "UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles."
    Campalans A., Amouroux R., Bravard A., Epe B., Radicella J.P.
    J. Cell Sci. 120:23-32(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  18. "Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA."
    Bruner S.D., Norman D.P.G., Verdine G.L.
    Nature 403:859-866(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-327 OF MUTANT GLN-247 IN COMPLEX WITH DNA, CHARACTERIZATION OF VARIANT HIS-154.
  19. "Reciprocal 'flipping'; underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase."
    Bjoras M., Seeberg E., Luna L., Pearl L.H., Barrett T.E.
    J. Mol. Biol. 317:171-177(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH DNA AND 8-OXO-GUANINE.
  20. "Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase."
    Norman D.P.G., Chung S.J., Verdine G.L.
    Biochemistry 42:1564-1572(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 12-327 OF MUTANTS ASN-268; GLU-268 AND GLN-268 IN COMPLEX WITH DNA, MUTAGENESIS OF ASP-268.
  21. "Product-assisted catalysis in base-excision DNA repair."
    Fromme J.C., Bruner S.D., Yang W., Karplus M., Verdine G.L.
    Nat. Struct. Biol. 10:204-211(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 12-327 IN COMPLEX WITH DNA AND 8-OXO-GUANINE.
  22. "Structures of end products resulting from lesion processing by a DNA glycosylase/lyase."
    Chung S.J., Verdine G.L.
    Chem. Biol. 11:1643-1649(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-325 OF MUTANT GLU-268 IN COMPLEX WITH DNA.
  23. "Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations."
    Radom C.T., Banerjee A., Verdine G.L.
    J. Biol. Chem. 282:9182-9194(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 12-327 OF MUTANTS ALA-42/ALA-270/ALA-315/PHE-315 IN COMPLEXES WITH DNA.
  24. "Infrequent mutations of the hOGG1 gene, that is involved in the excision of 8-hydroxyguanine in damaged DNA, in human gastric cancer."
    Shinmura K., Kohno T., Kasai H., Koda K., Sugimura H., Yokota J.
    Jpn. J. Cancer Res. 89:825-828(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT HIS-154.
  25. "Mutations in OGG1, a gene involved in the repair of oxidative DNA damage, are found in human lung and kidney tumours."
    Chevillard S., Radicella J.P., Levalois C., Lebeau J., Poupon M.-F., Oudard S., Dutrillaux B., Boiteux S.
    Oncogene 16:3083-3086(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS SER-85; GLN-131 AND THR-232, CHARACTERIZATION OF VARIANT GLN-131.
  26. "Excision of oxidatively damaged DNA bases by the human alpha-hOgg1 protein and the polymorphic alpha-hOgg1(Ser326Cys) protein which is frequently found in human populations."
    Dherin C., Radicella J.P., Dizdaroglu M., Boiteux S.
    Nucleic Acids Res. 27:4001-4007(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT CYS-326.
  27. "Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the ogg1 protein."
    Audebert M., Radicella J.P., Dizdaroglu M.
    Nucleic Acids Res. 28:2672-2678(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS GLN-46 AND HIS-154.
  28. "Mitochondrial targeting of human 8-oxoguanine DNA glycosylase hOGG1 is impaired by a somatic mutation found in kidney cancer."
    Audebert M., Charbonnier J.-B., Boiteux S., Radicella J.P.
    DNA Repair 1:497-505(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANT GLU-12.

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: April 29, 2015
This is version 166 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

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.