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O15527 (OGG1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·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
Synonyms:MMH, MUTM, OGH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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. Nucleus speckle. Nucleus matrix. Note: Together with APEX1 is recruited to nuclear speckles in UVA-irradiated cells. Ref.17

Isoform 1A: Nucleus Ref.17.

Isoform 2A: Mitochondrion Ref.17.

Tissue specificity

Ubiquitous.

Involvement in disease

Renal cell carcinoma (RCC) [MIM:144700]: Renal 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.
Note: The disease may be caused by mutations affecting the gene represented in this entry.

Sequence similarities

Belongs to the type-1 OGG1 family.

Sequence caution

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

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentMitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   Molecular functionGlycosidase
Hydrolase
Lyase
   Technical term3D-structure
Complete proteome
Multifunctional enzyme
Reference proteome
Gene Ontology (GO)
   Biological_processDNA catabolic process, endonucleolytic

Traceable author statement Ref.6. Source: GOC

DNA repair

Traceable author statement. Source: Reactome

acute inflammatory response

Inferred from electronic annotation. Source: Ensembl

base-excision repair

Traceable author statement. Source: Reactome

base-excision repair, AP site formation

Traceable author statement. Source: Reactome

cellular response to cadmium ion

Inferred from electronic annotation. Source: Ensembl

depurination

Traceable author statement. Source: Reactome

nucleic acid phosphodiester bond hydrolysis

Traceable author statement Ref.4. Source: GOC

nucleotide-excision repair

Inferred from electronic annotation. Source: InterPro

regulation of protein import into nucleus, translocation

Inferred from direct assay Ref.17. Source: UniProtKB

regulation of transcription, DNA-templated

Inferred from mutant phenotype PubMed 8621488. 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 direct assay Ref.17. Source: UniProtKB

response to radiation

Inferred from direct assay Ref.17. Source: UniProtKB

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nuclear matrix

Inferred from direct assay Ref.17. Source: UniProtKB

nuclear speck

Inferred from direct assay Ref.17. Source: UniProtKB

nucleoplasm

Inferred from direct assay Ref.17. Source: UniProtKB

nucleus

Inferred from direct assay. Source: HPA

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

Inferred from electronic annotation. Source: Ensembl

damaged DNA binding

Traceable author statement Ref.4. Source: ProtInc

endonuclease activity

Traceable author statement Ref.4. Source: ProtInc

oxidized purine nucleobase lesion DNA N-glycosylase activity

Traceable author statement Ref.6. Source: ProtInc

protein binding

Inferred from physical interaction PubMed 15518571. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SNRPFP623061EBI-721675,EBI-356900

Alternative products

This entry describes 8 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1A (identifier: O15527-1)

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.
Isoform 1B (identifier: O15527-2)

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → VSVPRCPP
Isoform 1C (identifier: O15527-3)

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → TPPSYRCCSV...VCTTRWGGGY
Isoform 2A (identifier: O15527-4)

Also known as: Beta;

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → GLLGNAFDGH...HVMQASLLAL
Isoform 2B (identifier: O15527-5)

The sequence of this isoform differs from the canonical sequence as follows:
     250-345: VADCICLMAL...RRKGSKGPEG → GLLGNAFDGH...HVMQASLLAL
Isoform 2C (identifier: O15527-6)

The sequence of this isoform differs from the canonical sequence as follows:
     191-195: EVEAH → PWQCI
     196-345: Missing.
Isoform 2D (identifier: O15527-7)

The sequence of this isoform differs from the canonical sequence as follows:
     317-345: VLFSADLRQSRHAQEPPAKRRKGSKGPEG → LCQVITTFMTFLGPHRLDQMPPEELQTSSSRLGGPPWQCI
Isoform 2E (identifier: O15527-8)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345N-glycosylase/DNA lyase
PRO_0000058591

Sites

Active site2491Schiff-base intermediate with DNA Ref.5
Binding site1491DNA
Binding site1541DNA
Binding site2041DNA
Binding site26618-oxoguanine; via carbonyl oxygen
Binding site26818-oxoguanine
Binding site2701DNA
Binding site2871DNA
Binding site31518-oxoguanine
Binding site31918-oxoguanine

Natural variations

Alternative sequence191 – 1955EVEAH → PWQCI in isoform 2C.
VSP_003750
Alternative sequence196 – 345150Missing in isoform 2C.
VSP_003751
Alternative sequence250 – 34596VADCI…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2B.
VSP_003749
Alternative sequence317 – 34529VLFSA…KGPEG → VSVPRCPP in isoform 1B.
VSP_003746
Alternative sequence317 – 34529VLFSA…KGPEG → TPPSYRCCSVPTCANPAMLR SHQQSAERVPKGRKARWGTL DKEIPQAPSPPFPTSLSPSP PSLMLGRGLPVTTSKARHPQ IKQSVCTTRWGGGY in isoform 1C.
VSP_003747
Alternative sequence317 – 34529VLFSA…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2A.
VSP_003748
Alternative sequence317 – 34529VLFSA…KGPEG → LCQVITTFMTFLGPHRLDQM PPEELQTSSSRLGGPPWQCI in isoform 2D.
VSP_003752
Alternative sequence317 – 34529VLFSA…KGPEG → AGSDAS in isoform 2E.
VSP_003753
Natural variant121G → E Found in a kidney cancer sample; no effect on activity; abolishes mitochondrial localization. Ref.28
VAR_024831
Natural variant461R → Q Found in a clear cell renal cell carcinoma sample; somatic mutation; diminished activity. Ref.27
Corresponds to variant rs104893751 [ dbSNP | Ensembl ].
VAR_009519
Natural variant851A → S Found in a lung cancer sample. Ref.25
Corresponds to variant rs17050550 [ dbSNP | Ensembl ].
VAR_024832
Natural variant1311R → Q Found in a lung cancer sample; loss of activity. Ref.25
VAR_024833
Natural variant1541R → H Found in a gastric cancer sample; no effect on base-excision activity; alters substrate specificity and strongly increases mutagenic mis-repair. Ref.18 Ref.24 Ref.27
Corresponds to variant rs56053615 [ dbSNP | Ensembl ].
VAR_009520
Natural variant2291R → Q. Ref.13
Corresponds to variant rs1805373 [ dbSNP | Ensembl ].
VAR_014487
Natural variant2321S → T Found in a kidney cancer sample. Ref.25
VAR_024834
Natural variant2881A → V. Ref.13
Corresponds to variant rs3219012 [ dbSNP | Ensembl ].
VAR_018890
Natural variant3201S → T.
Corresponds to variant rs1801128 [ dbSNP | Ensembl ].
VAR_014488
Natural variant3221D → N. Ref.13
Corresponds to variant rs3219014 [ dbSNP | Ensembl ].
VAR_018891
Natural variant3261S → C Common polymorphism in the Japanese population. Ref.12 Ref.13 Ref.15 Ref.26
Corresponds to variant rs1052133 [ dbSNP | Ensembl ].
VAR_009521

Experimental info

Mutagenesis2491K → Q: Loss of activity. Ref.5
Mutagenesis2681D → E or Q: No effect on activity. Ref.20
Mutagenesis2681D → N: Decreases activity about 65-fold. Ref.20
Sequence conflict471W → WW in CAA10351. Ref.9
Sequence conflict3081G → E in CAA10351. Ref.9
Sequence conflict3161A → ATPPSLQ in AAB81132. Ref.2

Secondary structure

............................................................ 345
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1A (Alpha) [UniParc].

Last modified December 1, 2000. Version 2.
Checksum: C284106ADEEC1FDD

FASTA34538,782
        10         20         30         40         50         60 
MPARALLPRR MGHRTLASTP ALWASIPCPR SELRLDLVLP SGQSFRWREQ SPAHWSGVLA 

        70         80         90        100        110        120 
DQVWTLTQTE EQLHCTVYRG DKSQASRPTP DELEAVRKYF QLDVTLAQLY HHWGSVDSHF 

       130        140        150        160        170        180 
QEVAQKFQGV RLLRQDPIEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG 

       190        200        210        220        230        240 
FPSLQALAGP EVEAHLRKLG LGYRARYVSA SARAILEEQG GLAWLQQLRE SSYEEAHKAL 

       250        260        270        280        290        300 
CILPGVGTKV ADCICLMALD KPQAVPVDVH MWHIAQRDYS WHPTTSQAKG PSPQTNKELG 

       310        320        330        340 
NFFRSLWGPY AGWAQAVLFS ADLRQSRHAQ EPPAKRRKGS KGPEG 

« Hide

Isoform 1B [UniParc].

Checksum: FB6DAF62F162C353
Show »

FASTA32436,433
Isoform 1C [UniParc].

Checksum: CA01660C056A09F0
Show »

FASTA41045,761
Isoform 2A (Beta) [UniParc].

Checksum: 0013B0F2D51FD316
Show »

FASTA42447,237
Isoform 2B [UniParc].

Checksum: 0FAA63310FC13ADB
Show »

FASTA35739,729
Isoform 2C [UniParc].

Checksum: 16628F612964E282
Show »

FASTA19522,210
Isoform 2D [UniParc].

Checksum: 40D1E4783F042C8F
Show »

FASTA35640,095
Isoform 2E [UniParc].

Checksum: E47B3CA5AE8CFABB
Show »

FASTA32236,085

References

« Hide 'large scale' 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] (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. expand/collapse author list , 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. expand/collapse author list , 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.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS2576.1. [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]
PIRT45069.
RefSeqNP_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]
UniGeneHs.380271.

3D structure databases

PDBe
RCSB-PDB
PDBj
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[»]
ProteinModelPortalO15527.
SMRO15527. Positions 12-323.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111018. 8 interactions.
IntActO15527. 4 interactions.
MINTMINT-3292093.

PTM databases

PhosphoSiteO15527.

Proteomic databases

MaxQBO15527.
PaxDbO15527.
PRIDEO15527.

Protocols and materials databases

DNASU4968.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000302003; 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]
GeneID4968.
KEGGhsa:4968.
UCSCuc003bsh.3. human. [O15527-2]
uc003bsi.3. human. [O15527-1]

Organism-specific databases

CTD4968.
GeneCardsGC03P009791.
HGNCHGNC:8125. OGG1.
HPACAB047301.
HPA027514.
MIM144700. phenotype.
601982. gene.
neXtProtNX_O15527.
PharmGKBPA31912.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0122.
HOVERGENHBG001047.
KOK03660.
OMASPQANKE.
OrthoDBEOG7XDBGB.
PhylomeDBO15527.
TreeFamTF323702.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.

Gene expression databases

ArrayExpressO15527.
BgeeO15527.
GenevestigatorO15527.

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

ChiTaRSOGG1. human.
EvolutionaryTraceO15527.
GeneWikiOxoguanine_glycosylase.
GenomeRNAi4968.
NextBio19116.
PROO15527.
SOURCESearch...

Entry information

Entry nameOGG1_HUMAN
AccessionPrimary (citable) accession number: O15527
Secondary accession number(s): A8K1E3 expand/collapse secondary AC list , O00390, O00670, O00705, O14876, O95488, P78554, Q9BW42, Q9UIK0, Q9UIK1, Q9UIK2, Q9UL34, Q9Y2C0, Q9Y2C1, Q9Y6C3, Q9Y6C4
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: July 9, 2014
This is version 159 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM