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UniProtKB/Swiss-Prot entry O15527


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name OGG1_HUMAN
Primary accession number O15527
Secondary accession numbers A8K1E3 O00390 O00670 O00705 O14876 O95488 P78554 Q9BW42 Q9UIK0 Q9UIK1 Q9UIK2 Q9UL34 Q9Y2C0 Q9Y2C1 Q9Y6C3 Q9Y6C4
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on December 1, 2000 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 106)
Name and origin of the protein
Protein name N-glycosylase/DNA lyase
Synonyms None
Includes 8-oxoguanine DNA glycosylase
     (EC 3.2.2.-)
DNA-(apurinic or apyrimidinic site) lyase
     (AP lyase)
     (EC 4.2.99.18)
Gene name
Name: OGG1
Synonyms: MMH, MUTM, OGH1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 2).
TISSUE=Colon;
PubMed=9187114 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Cloning and characterization of mammalian 8-hydroxyguanine-specific DNA glycosylase/apurinic, apyrimidinic lyase, a functional mutM homologue.";
Cancer Res. 57:2151-2156(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
DOI=10.1073/pnas.94.14.7429; PubMed=9207108 [NCBI, ExPASy, EBI, Israel, Japan]
Rosenquist T.A., Zharkov D.O., Grollman A.P.;
"Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase.";
Proc. Natl. Acad. Sci. U.S.A. 94:7429-7434(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
DOI=10.1073/pnas.94.15.8016; PubMed=9223306 [NCBI, ExPASy, EBI, Israel, Japan]
Roldan-Arjona T., Wei Y.-F., Carter K.C., Klungland A., Anselmino C., Wang R.-P., Augustus M., Lindahl T.;
"Molecular cloning and functional expression of a human cDNA encoding the antimutator enzyme 8-hydroxyguanine-DNA glycosylase.";
Proc. Natl. Acad. Sci. U.S.A. 94:8016-8020(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
DOI=10.1073/pnas.94.15.8010; PubMed=9223305 [NCBI, ExPASy, EBI, Israel, Japan]
Radicella J.P., Dherin C., Desmaze C., Fox M.S., Boiteux S.;
"Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae.";
Proc. Natl. Acad. Sci. U.S.A. 94:8010-8015(1997).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A), ACTIVE SITE, AND MUTAGENESIS OF LYS-249.
DOI=10.1016/S0960-9822(06)00187-4; PubMed=9197244 [NCBI, ExPASy, EBI, Israel, Japan]
Lu R., Nash H.M., Verdine G.L.;
"A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer.";
Curr. Biol. 7:397-407(1997).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
DOI=10.1038/sj.onc.1201139; PubMed=9190902 [NCBI, ExPASy, EBI, Israel, Japan]
Arai K., Morishita K., Shinmura K., Kohno T., Taniwaki M., Ohwada S., Yokota J.;
"Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage.";
Oncogene 14:2857-2861(1997).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
DOI=10.1084/jem.186.9.1547; PubMed=9348312 [NCBI, ExPASy, EBI, Israel, Japan]
Kuo F.C., Sklar J.L.;
"Augmented expression of a human gene for 8-oxoguanine DNA glycosylase (MutM) in B lymphocytes of the dark zone in lymph node germinal centers.";
J. Exp. Med. 186:1547-1556(1997).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1A).
DOI=10.1093/emboj/16.20.6314; PubMed=9321410 [NCBI, ExPASy, EBI, Israel, Japan]
Bjoras M., Luna L., Johnsen B.E., Hoff E., Haug T., Rognes T., Seeberg E.;
"Opposite base-dependent reactions of a human base excision repair enzyme on DNA containing 7,8-dihydro-8-oxoguanine and abasic sites.";
EMBO J. 16:6314-6322(1997).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Dhenaut A., Boiteux S., Radicella J.;
"Genomic structure and promoter characterization of the human 8-OH-guanine glycosylase gene (OGG1) gene.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING.
PubMed=10449904 [NCBI, ExPASy, EBI, Israel, Japan]
Ishida T., Hippo Y., Nakahori Y., Matsushita I., Kodama T., Nishimura S., Aburatani H.;
"Structure and chromosome location of human OGG1.";
Cytogenet. Cell Genet. 85:232-236(1999).
[11]
NUCLEOTIDE SEQUENCE [MRNA], AND ALTERNATIVE SPLICING.
PubMed=10233168 [NCBI, ExPASy, EBI, Israel, Japan]
Nishioka K., Ohtsubo T., Oda H., Fujiwara T., Kang D., Sugimachi K., Nakabeppu Y.;
"Expression and differential intracellular localization of two major forms of human 8-Oxoguanine DNA glycosylase encoded by alternatively spliced OGG1 mRNAs.";
Mol. Biol. Cell 10:1637-1652(1999).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A), AND VARIANT CYS-326.
TISSUE=Brain;
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS GLN-229; VAL-288; ASN-322 AND CYS-326.
NIEHS SNPs program;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04728; PubMed=16641997 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence, annotation and analysis of human chromosome 3.";
Nature 440:1194-1198(2006).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT CYS-326.
TISSUE=Eye;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[16]
REVIEW.
DOI=10.1006/abbi.2000.1773; PubMed=10775435 [NCBI, ExPASy, EBI, Israel, Japan]
Boiteux S., Radicella J.P.;
"The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis.";
Arch. Biochem. Biophys. 377:1-8(2000).
[17]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-327 OF MUTANT GLN-247 IN COMPLEX WITH DNA, AND CHARACTERIZATION OF VARIANT HIS-154.
DOI=10.1038/35002510; PubMed=10706276 [NCBI, ExPASy, EBI, Israel, Japan]
Bruner S.D., Norman D.P.G., Verdine G.L.;
"Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA.";
Nature 403:859-866(2000).
[18]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH DNA AND 8-OXO-GUANINE.
DOI=10.1006/jmbi.2002.5400; PubMed=11902834 [NCBI, ExPASy, EBI, Israel, Japan]
Bjoras M., Seeberg E., Luna L., Pearl L.H., Barrett T.E.;
"Reciprocal 'flipping'; underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase.";
J. Mol. Biol. 317:171-177(2002).
[19]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 12-327 OF MUTANTS ASN-268; GLU-268 AND GLN-268 IN COMPLEX WITH DNA, AND MUTAGENESIS OF ASP-268.
DOI=10.1021/bi026823d; PubMed=12578369 [NCBI, ExPASy, EBI, Israel, Japan]
Norman D.P.G., Chung S.J., Verdine G.L.;
"Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase.";
Biochemistry 42:1564-1572(2003).
[20]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 12-327 IN COMPLEX WITH DNA AND 8-OXO-GUANINE.
DOI=10.1038/nsb902; PubMed=12592398 [NCBI, ExPASy, EBI, Israel, Japan]
Fromme J.C., Bruner S.D., Yang W., Karplus M., Verdine G.L.;
"Product-assisted catalysis in base-excision DNA repair.";
Nat. Struct. Biol. 10:204-211(2003).
[21]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-325 OF MUTANT GLU-268 IN COMPLEX WITH DNA.
DOI=10.1016/j.chembiol.2004.09.014; PubMed=15610848 [NCBI, ExPASy, EBI, Israel, Japan]
Chung S.J., Verdine G.L.;
"Structures of end products resulting from lesion processing by a DNA glycosylase/lyase.";
Chem. Biol. 11:1643-1649(2004).
[22]
X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 12-327 OF MUTANTS ALA-42/ALA-270/ALA-315/PHE-315 IN COMPLEXES WITH DNA.
DOI=10.1074/jbc.M608989200; PubMed=17114185 [NCBI, ExPASy, EBI, Israel, Japan]
Radom C.T., Banerjee A., Verdine G.L.;
"Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations.";
J. Biol. Chem. 282:9182-9194(2007).
[23]
VARIANT HIS-154.
PubMed=9765618 [NCBI, ExPASy, EBI, Israel, Japan]
Shinmura K., Kohno T., Kasai H., Koda K., Sugimura H., Yokota J.;
"Infrequent mutations of the hOGG1 gene, that is involved in the excision of 8-hydroxyguanine in damaged DNA, in human gastric cancer.";
Jpn. J. Cancer Res. 89:825-828(1998).
[24]
VARIANTS SER-85; GLN-131 AND THR-232, AND CHARACTERIZATION OF VARIANT GLN-131.
DOI=10.1038/sj.onc.1202096; PubMed=9662341 [NCBI, ExPASy, EBI, Israel, Japan]
Chevillard S., Radicella J.P., Levalois C., Lebeau J., Poupon M.-F., Oudard S., Dutrillaux B., Boiteux S.;
"Mutations in OGG1, a gene involved in the repair of oxidative DNA damage, are found in human lung and kidney tumours.";
Oncogene 16:3083-3086(1998).
[25]
CHARACTERIZATION OF VARIANT CYS-326.
DOI=10.1093/nar/27.20.4001; PubMed=10497264 [NCBI, ExPASy, EBI, Israel, Japan]
Dherin C., Radicella J.P., Dizdaroglu M., Boiteux S.;
"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.";
Nucleic Acids Res. 27:4001-4007(1999).
[26]
CHARACTERIZATION OF VARIANTS GLN-46 AND HIS-154.
DOI=10.1093/nar/28.14.2672; PubMed=10908322 [NCBI, ExPASy, EBI, Israel, Japan]
Audebert M., Radicella J.P., Dizdaroglu M.;
"Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the ogg1 protein.";
Nucleic Acids Res. 28:2672-2678(2000).
[27]
CHARACTERIZATION OF VARIANT GLU-12.
DOI=10.1016/S1568-7864(02)00034-4; PubMed=12509224 [NCBI, ExPASy, EBI, Israel, Japan]
Audebert M., Charbonnier J.-B., Boiteux S., Radicella J.P.;
"Mitochondrial targeting of human 8-oxoguanine DNA glycosylase hOGG1 is impaired by a somatic mutation found in kidney cancer.";
DNA Repair 1:497-505(2002).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U96710; AAB81132.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11838; CAA72536.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y11731; CAA72414.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB000410; BAA19103.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF003595; AAB61340.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U88527; AAB68614.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U88620; AAB68615.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
Y13277; CAA73726.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF026691; AAB84013.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AJ131341; CAA10351.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF088282; AAD41680.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF088282; AAD41681.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF088282; AAD41682.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB019528; BAA76635.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB019529; BAA76636.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB019530; BAA76637.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB019531; BAA76638.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB019532; BAA76639.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK289858; BAF82547.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF521807; AAM74236.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.[EMBL / GenBank / DDBJ]
BC000657; AAH00657.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00007312; -.
IPI00025730; -.
IPI00026574; -.
IPI00220178; -.
IPI00220179; -.
IPI00220180; -.
IPI00294126; -.
IPI00303869; -.
PIR T45069; T45069.
RefSeq NP_002533.1; -.
NP_058212.1; -.
NP_058213.1; -.
NP_058214.1; -.
NP_058434.1; -.
NP_058436.1; -.
NP_058437.1; -.
NP_058438.1; -.
UniGene Hs.380271
3D structure databases
PDB
1EBM; X-ray; 2.10 A; A=12-325.[ExPASy / RCSB / EBI]
1FN7; X-ray; 2.60 A; A=12-325.[ExPASy / RCSB / EBI]
1HU0; X-ray; 2.35 A; A=12-327.[ExPASy / RCSB / EBI]
1KO9; X-ray; 2.15 A; A=1-345.[ExPASy / RCSB / EBI]
1LWV; X-ray; 2.30 A; A=12-327.[ExPASy / RCSB / EBI]
1LWW; X-ray; 2.10 A; A=12-327.[ExPASy / RCSB / EBI]
1LWY; X-ray; 2.01 A; A=12-327.[ExPASy / RCSB / EBI]
1M3H; X-ray; 2.05 A; A=12-325.[ExPASy / RCSB / EBI]
1M3Q; X-ray; 1.90 A; A=12-325.[ExPASy / RCSB / EBI]
1N39; X-ray; 2.20 A; A=12-325.[ExPASy / RCSB / EBI]
1N3A; X-ray; 2.20 A; A=12-325.[ExPASy / RCSB / EBI]
1N3C; X-ray; 2.70 A; A=12-325.[ExPASy / RCSB / EBI]
1YQK; X-ray; 2.50 A; A=12-327.[ExPASy / RCSB / EBI]
1YQL; X-ray; 2.60 A; A=12-327.[ExPASy / RCSB / EBI]
1YQM; X-ray; 2.50 A; A=12-327.[ExPASy / RCSB / EBI]
1YQR; X-ray; 2.43 A; A=12-327.[ExPASy / RCSB / EBI]
2I5W; X-ray; 2.60 A; A=12-323.[ExPASy / RCSB / EBI]
2NOB; X-ray; 2.10 A; A=12-327.[ExPASy / RCSB / EBI]
2NOE; X-ray; 2.20 A; A=12-327.[ExPASy / RCSB / EBI]
2NOF; X-ray; 2.35 A; A=12-327.[ExPASy / RCSB / EBI]
2NOH; X-ray; 2.01 A; A=12-327.[ExPASy / RCSB / EBI]
2NOI; X-ray; 2.35 A; A=12-327.[ExPASy / RCSB / EBI]
2NOL; X-ray; 2.57 A; A=12-327.[ExPASy / RCSB / EBI]
2NOZ; X-ray; 2.43 A; A=12-327.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1EBM; -.
1FN7; -.
1HU0; -.
1KO9; -.
1LWV; -.
1LWW; -.
1LWY; -.
1M3H; -.
1M3Q; -.
1N39; -.
1N3A; -.
1N3C; -.
1YQK; -.
1YQL; -.
1YQM; -.
1YQR; -.
2I5W; -.
2NOB; -.
2NOE; -.
2NOF; -.
2NOH; -.
2NOI; -.
2NOL; -.
2NOZ; -.
ModBase O15527.
Protein-protein interaction databases
IntAct O15527; 3.
Enzyme and pathway databases
BRENDA 4.2.99.18; 247.
Reactome REACT_216; DNA Repair.
Organism-specific databases
GeneCards GC03P009772; -.
H-InvDB HIX0003031; -.
HGNC HGNC:8125; OGG1.
GenAtlas OGG1.
MIM 144700; phenotype. [NCBI / EBI]
601982; gene. [NCBI / EBI]
Orphanet 151; Renal cell carcinoma, familial.
PharmGKB PA31912; -.
Gene expression databases
ArrayExpress O15527; -.
Bgee O15527; -.
GermOnline ENSG00000114026; Homo sapiens.
Ontologies
GO
GO:0005739; Cellular component: mitochondrion (inferred from electronic annotation from UniProtKB-KW).
GO:0005654; Cellular component: nucleoplasm (inferred from experiment from Reactome).
GO:0003684; Molecular function: damaged DNA binding (traceable author statement from ProtInc).
GO:0008534; Molecular function: oxidized purine base lesion DNA N-glycosylase activity (inferred from experiment from Reactome).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0045007; Biological process: depurination (inferred from experiment from Reactome).
GO:0006289; Biological process: nucleotide-excision repair (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR003265; HhH-GPD_domain.
IPR004577; Ogg.
IPR012904; OGG_N.
Graphical view of domain structure.
Pfam PF00730; HhH-GPD; 1.
PF07934; OGG_N; 1.
Pfam graphical view of domain structure.
SMART SM00478; ENDO3c; 1.
SMART graphical view of domain structure.
TIGRFAMs TIGR00588; ogg; 1.
Proteomic databases
PRIDE O15527; -.
Genome annotation databases
Ensembl ENSG00000114026; Homo sapiens. [Contig view]
GeneID 4968; -.
KEGG hsa:4968; -.
Phylogenomic databases
HOVERGEN O15527; -.
OMA O15527; GLRLIRQ.
Other
NextBio 19116; -.
SOURCE OGG1; Homo sapiens.
ProtoNet O15527.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; DNA damage; DNA repair; Glycosidase; Hydrolase; Lyase; Mitochondrion; Multifunctional enzyme; Nucleus; Polymorphism.
Features
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KeyFrom   To Length Description FTId
CHAIN   1   345  345     N-glycosylase/DNA lyase. PRO_0000058591
ACT_SITE   249   249        Schiff-base intermediate with DNA. 
BINDING   149   149        DNA. 
BINDING   154   154        DNA. 
BINDING   204   204        DNA. 
BINDING   266   266        8-oxoguanine; via carbonyl oxygen. 
BINDING   268   268        8-oxoguanine. 
BINDING   270   270        DNA. 
BINDING   287   287        DNA. 
BINDING   315   315        8-oxoguanine. 
BINDING   319   319        8-oxoguanine. 
VAR_SEQ   191   195        EVEAH -> PWQCI (in isoform 2C). VSP_003750
VAR_SEQ   196   345        Missing (in isoform 2C). VSP_003751
VAR_SEQ   250   345        VADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAK GPSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHA QEPPAKRRKGSKGPEG -> GLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHVMQASLLAL (in isoform 2B). VSP_003749
VAR_SEQ   317   345        VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> VSVPRCPP (in isoform 1B). VSP_003746
VAR_SEQ   317   345        VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> TPPSYRCCSVPTCANPAMLRSHQQSAERVPKGRKARWGTL DKEIPQAPSPPFPTSLSPSPPSLMLGRGLPVTTSKARHPQ IKQSVCTTRWGGGY (in isoform 1C). VSP_003747
VAR_SEQ   317   345        VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> GLLGNAFDGHQLLRPLIFCQDHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWTKDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHVMQASLLAL (in isoform 2A). VSP_003748
VAR_SEQ   317   345        VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> LCQVITTFMTFLGPHRLDQMPPEELQTSSSRLGGPPWQCI (in isoform 2D). VSP_003752
VAR_SEQ   317   345        VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> AGSDAS (in isoform 2E). VSP_003753
VARIANT   12    12  1     G -> E (in kidney cancer; no effect on activity. Abolishes mitochondrial localization). VAR_024831 [3D]
VARIANT   46    46  1     R -> Q (in kidney cancer; diminished activity). VAR_009519 [3D]
VARIANT   85    85  1     A -> S (in lung cancer; dbSNP:rs17050550 [NCBI]). VAR_024832 [3D]
VARIANT   131   131  1     R -> Q (in lung cancer; loss of activity). VAR_024833 [3D]
VARIANT   154   154  1     R -> H (in gastric cancer; No effect on base-excision activity. Alters substrate specificity and strongly increases mutagenic mis-repair; dbSNP:rs56053615 [NCBI]). VAR_009520 [3D]
VARIANT   229   229  1     R -> Q (in dbSNP:rs1805373 [NCBI]). VAR_014487 [3D]
VARIANT   232   232  1     S -> T (in kidney cancer). VAR_024834 [3D]
VARIANT   288   288  1     A -> V (in dbSNP:rs3219012 [NCBI]). VAR_018890 [3D]
VARIANT   320   320  1     S -> T (in dbSNP:rs1801128 [NCBI]). VAR_014488 [3D]
VARIANT   322   322  1     D -> N (in dbSNP:rs3219014 [NCBI]). VAR_018891 [3D]
VARIANT   326   326  1     S -> C (common polymorphism in the Japanese population; dbSNP:rs1052133 [NCBI]). VAR_009521 
MUTAGEN   249   249        K->Q: Loss of activity. 
MUTAGEN   268   268        D->E,Q: No effect on activity. 
MUTAGEN   268   268        D->N: Decreases activity about 65-fold. 
CONFLICT   47    47        W -> WW (in Ref. 9; CAA10351). 
CONFLICT   308   308        G -> E (in Ref. 9; CAA10351). 
CONFLICT   316   316        A -> ATPPSLQ (in Ref. 2). 
TURN   16    18  3      
HELIX   20    22  3      
STRAND   24    27  4      
TURN   30    32  3      
HELIX   35    38  4      
TURN   39    42  4      
STRAND   48    51  4      
STRAND   54    58  5      
STRAND   60    68  9      
STRAND   70    78  9      
HELIX   90    99  10      
TURN   100   103  4      
HELIX   106   116  11      
HELIX   118   124  7      
HELIX   137   145  9      
TURN   146   149  4      
HELIX   152   166  15      
STRAND   169   173  5      
STRAND   176   179  4      
HELIX   184   187  4      
HELIX   192   198  7      
HELIX   204   217  14      
HELIX   221   227  7      
TURN   228   230  3      
HELIX   233   240  8      
HELIX   248   258  11      
HELIX   269   279  11      
STRAND   284   287  4      
HELIX   293   307  15      
HELIX   311   323  13      
Sequence information
Length: 345 AA [This is the length of the unprocessed precursor] Molecular weight: 38782 Da [This is the MW of the unprocessed precursor] CRC64: C284106ADEEC1FDD [This is a checksum on the sequence]
        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 

O15527 in FASTA format

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