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N-glycosylase/DNA lyase [Includes: 8-oxoguanine DNA glycosylase (EC 3.2.2.-); DNA-(apurinic or apyrimidinic site) lyase (AP lyase) (EC 4.2.99.18)]

 OGG1_HUMAN              Reviewed;         345 AA.
O15527; A8K1E3; O00390; O00670; O00705; O14876; O95488; P78554;
Q9BW42; Q9UIK0; Q9UIK1; Q9UIK2; Q9UL34; Q9Y2C0; Q9Y2C1; Q9Y6C3;
Q9Y6C4;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
12-SEP-2018, entry version 200.
RecName: Full=N-glycosylase/DNA lyase;
Includes:
RecName: Full=8-oxoguanine DNA glycosylase;
EC=3.2.2.-;
Includes:
RecName: Full=DNA-(apurinic or apyrimidinic site) lyase;
Short=AP lyase;
EC=4.2.99.18;
Name=OGG1; Synonyms=MMH, MUTM, OGH1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 2A).
TISSUE=Colon;
PubMed=9187114;
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).
PubMed=9207108; DOI=10.1073/pnas.94.14.7429;
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 2A).
PubMed=9223306; DOI=10.1073/pnas.94.15.8016;
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).
PubMed=9223305; DOI=10.1073/pnas.94.15.8010;
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.
PubMed=9197244; DOI=10.1016/S0960-9822(06)00187-4;
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).
PubMed=9190902; DOI=10.1038/sj.onc.1201139;
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).
PubMed=9348312; DOI=10.1084/jem.186.9.1547;
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).
PubMed=9321410; DOI=10.1093/emboj/16.20.6314;
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;
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; DOI=10.1091/mbc.10.5.1637;
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;
PubMed=14702039; DOI=10.1038/ng1285;
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].
PubMed=16641997; DOI=10.1038/nature04728;
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;
PubMed=15489334; DOI=10.1101/gr.2596504;
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.
PubMed=10775435; DOI=10.1006/abbi.2000.1773;
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]
SUBCELLULAR LOCATION.
PubMed=17148573; DOI=10.1242/jcs.03312;
Campalans A., Amouroux R., Bravard A., Epe B., Radicella J.P.;
"UVA irradiation induces relocalisation of the DNA repair protein
hOGG1 to nuclear speckles.";
J. Cell Sci. 120:23-32(2007).
[18]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 12-327 OF MUTANT GLN-247 IN
COMPLEX WITH DNA, AND CHARACTERIZATION OF VARIANT HIS-154.
PubMed=10706276; DOI=10.1038/35002510;
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).
[19]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH DNA AND
8-OXO-GUANINE.
PubMed=11902834; DOI=10.1006/jmbi.2002.5400;
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).
[20]
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.
PubMed=12578369; DOI=10.1021/bi026823d;
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).
[21]
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 12-327 IN COMPLEX WITH DNA
AND 8-OXO-GUANINE.
PubMed=12592398; DOI=10.1038/nsb902;
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).
[22]
X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-325 OF MUTANT GLU-268 IN
COMPLEX WITH DNA.
PubMed=15610848; DOI=10.1016/j.chembiol.2004.09.014;
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).
[23]
X-RAY CRYSTALLOGRAPHY (2.57 ANGSTROMS) OF 12-327 OF MUTANTS
ALA-42/ALA-270/ALA-315/PHE-315 IN COMPLEXES WITH DNA.
PubMed=17114185; DOI=10.1074/jbc.M608989200;
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).
[24]
VARIANT HIS-154.
PubMed=9765618; DOI=10.1111/j.1349-7006.1998.tb00635.x;
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).
[25]
VARIANTS SER-85; GLN-131 AND THR-232, AND CHARACTERIZATION OF VARIANT
GLN-131.
PubMed=9662341; DOI=10.1038/sj.onc.1202096;
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).
[26]
CHARACTERIZATION OF VARIANT CYS-326.
PubMed=10497264; DOI=10.1093/nar/27.20.4001;
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).
[27]
CHARACTERIZATION OF VARIANTS GLN-46 AND HIS-154.
PubMed=10908322; DOI=10.1093/nar/28.14.2672;
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).
[28]
CHARACTERIZATION OF VARIANT GLU-12.
PubMed=12509224; DOI=10.1016/S1568-7864(02)00034-4;
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).
-!- 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: Nucleus, nucleoplasm
{ECO:0000269|PubMed:17148573}. Nucleus speckle
{ECO:0000269|PubMed:17148573}. Nucleus matrix
{ECO:0000269|PubMed:17148573}. Note=Together with APEX1 is
recruited to nuclear speckles in UVA-irradiated cells.
-!- SUBCELLULAR LOCATION: Isoform 1A: Nucleus.
-!- SUBCELLULAR LOCATION: Isoform 2A: Mitochondrion.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=1A; Synonyms=Alpha;
IsoId=O15527-1; Sequence=Displayed;
Name=1B;
IsoId=O15527-2; Sequence=VSP_003746;
Name=1C;
IsoId=O15527-3; Sequence=VSP_003747;
Name=2A; Synonyms=Beta;
IsoId=O15527-4; Sequence=VSP_003748;
Name=2B;
IsoId=O15527-5; Sequence=VSP_003749;
Name=2C;
IsoId=O15527-6; Sequence=VSP_003750, VSP_003751;
Name=2D;
IsoId=O15527-7; Sequence=VSP_003752;
Name=2E;
IsoId=O15527-8; Sequence=VSP_003753;
-!- TISSUE SPECIFICITY: Ubiquitous.
-!- 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.
-!- SIMILARITY: Belongs to the type-1 OGG1 family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB84013.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/ogg1/";
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EMBL; U88527; AAB68614.1; -; mRNA.
EMBL; U88620; AAB68615.1; -; mRNA.
EMBL; U96710; AAB81132.1; -; mRNA.
EMBL; Y13277; CAA73726.1; -; mRNA.
EMBL; Y11731; CAA72414.1; -; mRNA.
EMBL; AF003595; AAB61340.1; -; mRNA.
EMBL; AB000410; BAA19103.1; -; mRNA.
EMBL; AF026691; AAB84013.1; ALT_INIT; mRNA.
EMBL; Y11838; CAA72536.1; -; mRNA.
EMBL; AJ131341; CAA10351.1; -; Genomic_DNA.
EMBL; AF088282; AAD41680.1; -; Genomic_DNA.
EMBL; AF088282; AAD41681.1; -; Genomic_DNA.
EMBL; AF088282; AAD41682.1; -; Genomic_DNA.
EMBL; AB019528; BAA76635.1; -; mRNA.
EMBL; AB019529; BAA76636.1; -; mRNA.
EMBL; AB019530; BAA76637.1; -; mRNA.
EMBL; AB019531; BAA76638.1; -; mRNA.
EMBL; AB019532; BAA76639.1; -; mRNA.
EMBL; AK289858; BAF82547.1; -; mRNA.
EMBL; AF521807; AAM74236.1; -; Genomic_DNA.
EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000657; AAH00657.1; -; mRNA.
CCDS; CCDS2576.1; -. [O15527-4]
CCDS; CCDS2577.1; -. [O15527-5]
CCDS; CCDS2578.1; -. [O15527-6]
CCDS; CCDS2579.1; -. [O15527-7]
CCDS; CCDS2580.1; -. [O15527-3]
CCDS; CCDS2581.1; -. [O15527-1]
CCDS; CCDS43046.1; -. [O15527-2]
CCDS; CCDS46742.1; -. [O15527-8]
PIR; T45069; T45069.
RefSeq; NP_002533.1; NM_002542.5. [O15527-1]
RefSeq; NP_058212.1; NM_016819.3. [O15527-2]
RefSeq; NP_058213.1; NM_016820.3. [O15527-3]
RefSeq; NP_058214.1; NM_016821.2. [O15527-4]
RefSeq; NP_058434.1; NM_016826.2. [O15527-5]
RefSeq; NP_058436.1; NM_016827.2. [O15527-6]
RefSeq; NP_058437.1; NM_016828.2. [O15527-7]
RefSeq; NP_058438.1; NM_016829.2. [O15527-8]
UniGene; Hs.380271; -.
PDB; 1EBM; X-ray; 2.10 A; A=12-325.
PDB; 1FN7; X-ray; 2.60 A; A=12-325.
PDB; 1HU0; X-ray; 2.35 A; A=12-327.
PDB; 1KO9; X-ray; 2.15 A; A=1-345.
PDB; 1LWV; X-ray; 2.30 A; A=12-327.
PDB; 1LWW; X-ray; 2.10 A; A=12-327.
PDB; 1LWY; X-ray; 2.01 A; A=12-327.
PDB; 1M3H; X-ray; 2.05 A; A=12-325.
PDB; 1M3Q; X-ray; 1.90 A; A=12-325.
PDB; 1N39; X-ray; 2.20 A; A=12-325.
PDB; 1N3A; X-ray; 2.20 A; A=12-325.
PDB; 1N3C; X-ray; 2.70 A; A=12-325.
PDB; 1YQK; X-ray; 2.50 A; A=12-327.
PDB; 1YQL; X-ray; 2.60 A; A=12-327.
PDB; 1YQM; X-ray; 2.50 A; A=12-327.
PDB; 1YQR; X-ray; 2.43 A; A=12-327.
PDB; 2I5W; X-ray; 2.60 A; A=12-323.
PDB; 2NOB; X-ray; 2.10 A; A=12-327.
PDB; 2NOE; X-ray; 2.20 A; A=12-327.
PDB; 2NOF; X-ray; 2.35 A; A=12-327.
PDB; 2NOH; X-ray; 2.01 A; A=12-327.
PDB; 2NOI; X-ray; 2.35 A; A=12-327.
PDB; 2NOL; X-ray; 2.57 A; A=12-327.
PDB; 2NOZ; X-ray; 2.43 A; A=12-327.
PDB; 2XHI; X-ray; 1.55 A; A=1-345.
PDB; 3IH7; X-ray; 3.10 A; A=12-325.
PDB; 3KTU; X-ray; 2.30 A; A=12-325.
PDB; 5AN4; X-ray; 1.60 A; A=12-323.
PDBsum; 1EBM; -.
PDBsum; 1FN7; -.
PDBsum; 1HU0; -.
PDBsum; 1KO9; -.
PDBsum; 1LWV; -.
PDBsum; 1LWW; -.
PDBsum; 1LWY; -.
PDBsum; 1M3H; -.
PDBsum; 1M3Q; -.
PDBsum; 1N39; -.
PDBsum; 1N3A; -.
PDBsum; 1N3C; -.
PDBsum; 1YQK; -.
PDBsum; 1YQL; -.
PDBsum; 1YQM; -.
PDBsum; 1YQR; -.
PDBsum; 2I5W; -.
PDBsum; 2NOB; -.
PDBsum; 2NOE; -.
PDBsum; 2NOF; -.
PDBsum; 2NOH; -.
PDBsum; 2NOI; -.
PDBsum; 2NOL; -.
PDBsum; 2NOZ; -.
PDBsum; 2XHI; -.
PDBsum; 3IH7; -.
PDBsum; 3KTU; -.
PDBsum; 5AN4; -.
ProteinModelPortal; O15527; -.
SMR; O15527; -.
BioGrid; 111018; 9.
IntAct; O15527; 4.
MINT; O15527; -.
BindingDB; O15527; -.
ChEMBL; CHEMBL3396944; -.
iPTMnet; O15527; -.
PhosphoSitePlus; O15527; -.
BioMuta; OGG1; -.
EPD; O15527; -.
MaxQB; O15527; -.
PeptideAtlas; O15527; -.
PRIDE; O15527; -.
ProteomicsDB; 48726; -.
ProteomicsDB; 48727; -. [O15527-2]
ProteomicsDB; 48728; -. [O15527-3]
ProteomicsDB; 48729; -. [O15527-4]
ProteomicsDB; 48730; -. [O15527-5]
ProteomicsDB; 48731; -. [O15527-6]
ProteomicsDB; 48732; -. [O15527-7]
ProteomicsDB; 48733; -. [O15527-8]
DNASU; 4968; -.
Ensembl; ENST00000302003; ENSP00000305584; ENSG00000114026. [O15527-3]
Ensembl; ENST00000302008; ENSP00000305527; ENSG00000114026. [O15527-7]
Ensembl; ENST00000302036; ENSP00000306561; ENSG00000114026. [O15527-4]
Ensembl; ENST00000339511; ENSP00000345520; ENSG00000114026. [O15527-2]
Ensembl; ENST00000344629; ENSP00000342851; ENSG00000114026. [O15527-1]
Ensembl; ENST00000349503; ENSP00000303132; ENSG00000114026. [O15527-5]
Ensembl; ENST00000383826; ENSP00000373337; ENSG00000114026. [O15527-6]
Ensembl; ENST00000449570; ENSP00000403598; ENSG00000114026. [O15527-8]
GeneID; 4968; -.
KEGG; hsa:4968; -.
UCSC; uc003bsh.4; human. [O15527-1]
CTD; 4968; -.
DisGeNET; 4968; -.
EuPathDB; HostDB:ENSG00000114026.21; -.
GeneCards; OGG1; -.
HGNC; HGNC:8125; OGG1.
HPA; CAB047301; -.
HPA; HPA027514; -.
MalaCards; OGG1; -.
MIM; 144700; phenotype.
MIM; 601982; gene.
neXtProt; NX_O15527; -.
OpenTargets; ENSG00000114026; -.
PharmGKB; PA31912; -.
GeneTree; ENSGT00640000091554; -.
HOVERGEN; HBG001047; -.
InParanoid; O15527; -.
KO; K03660; -.
OMA; EYAGYAQ; -.
PhylomeDB; O15527; -.
TreeFam; TF323702; -.
BRENDA; 3.2.2.23; 2681.
BRENDA; 4.2.99.18; 2681.
Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
Reactome; R-HSA-110330; Recognition and association of DNA glycosylase with site containing an affected purine.
Reactome; R-HSA-110331; Cleavage of the damaged purine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
Reactome; R-HSA-5649702; APEX1-Independent Resolution of AP Sites via the Single Nucleotide Replacement Pathway.
SIGNOR; O15527; -.
ChiTaRS; OGG1; human.
EvolutionaryTrace; O15527; -.
GeneWiki; Oxoguanine_glycosylase; -.
GenomeRNAi; 4968; -.
PRO; PR:O15527; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000114026; Expressed in 222 organ(s), highest expression level in adult mammalian kidney.
ExpressionAtlas; O15527; baseline and differential.
Genevisible; O15527; HS.
GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
GO; GO:0016363; C:nuclear matrix; IDA:UniProtKB.
GO; GO:0016607; C:nuclear speck; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0032991; C:protein-containing complex; IDA:MGI.
GO; GO:0034039; F:8-oxo-7,8-dihydroguanine DNA N-glycosylase activity; IEA:Ensembl.
GO; GO:0140078; F:class I DNA-(apurinic or apyrimidinic site) endonuclease activity; IEA:UniProtKB-EC.
GO; GO:0003684; F:damaged DNA binding; IDA:UniProtKB.
GO; GO:0019104; F:DNA N-glycosylase activity; IBA:GO_Central.
GO; GO:0004519; F:endonuclease activity; TAS:ProtInc.
GO; GO:0008017; F:microtubule binding; IEA:Ensembl.
GO; GO:0032357; F:oxidized purine DNA binding; IDA:UniProtKB.
GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; TAS:Reactome.
GO; GO:0002526; P:acute inflammatory response; IEA:Ensembl.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006284; P:base-excision repair; TAS:ProtInc.
GO; GO:0071276; P:cellular response to cadmium ion; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IGI:MGI.
GO; GO:0045007; P:depurination; TAS:Reactome.
GO; GO:0045008; P:depyrimidination; TAS:Reactome.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:1901291; P:negative regulation of double-strand break repair via single-strand annealing; IDA:MGI.
GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IDA:MGI.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:UniProtKB.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0051593; P:response to folic acid; IEA:Ensembl.
GO; GO:0009416; P:response to light stimulus; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IDA:UniProtKB.
GO; GO:0009314; P:response to radiation; IDA:UniProtKB.
CDD; cd00056; ENDO3c; 1.
Gene3D; 1.10.1670.10; -; 2.
InterPro; IPR011257; DNA_glycosylase.
InterPro; IPR003265; HhH-GPD_domain.
InterPro; IPR023170; HTH_base_excis_C.
InterPro; IPR004577; Ogg1.
InterPro; IPR012904; OGG_N.
Pfam; PF00730; HhH-GPD; 1.
Pfam; PF07934; OGG_N; 1.
SMART; SM00478; ENDO3c; 1.
SUPFAM; SSF48150; SSF48150; 1.
TIGRFAMs; TIGR00588; ogg; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome; DNA damage;
DNA repair; Glycosidase; Hydrolase; Lyase; Mitochondrion;
Multifunctional enzyme; Nucleus; Polymorphism; Reference proteome.
CHAIN 1 345 N-glycosylase/DNA lyase.
/FTId=PRO_0000058591.
ACT_SITE 249 249 Schiff-base intermediate with DNA.
{ECO:0000269|PubMed:9197244}.
BINDING 149 149 DNA. {ECO:0000269|PubMed:10706276,
ECO:0000269|PubMed:11902834,
ECO:0000269|PubMed:12578369,
ECO:0000269|PubMed:12592398,
ECO:0000269|PubMed:15610848}.
BINDING 154 154 DNA. {ECO:0000269|PubMed:10706276,
ECO:0000269|PubMed:11902834,
ECO:0000269|PubMed:12578369,
ECO:0000269|PubMed:12592398,
ECO:0000269|PubMed:15610848}.
BINDING 204 204 DNA. {ECO:0000269|PubMed:10706276,
ECO:0000269|PubMed:11902834,
ECO:0000269|PubMed:12578369,
ECO:0000269|PubMed:12592398,
ECO:0000269|PubMed:15610848}.
BINDING 266 266 8-oxoguanine; via carbonyl oxygen.
BINDING 268 268 8-oxoguanine.
BINDING 270 270 DNA. {ECO:0000269|PubMed:10706276,
ECO:0000269|PubMed:11902834,
ECO:0000269|PubMed:12578369,
ECO:0000269|PubMed:12592398,
ECO:0000269|PubMed:15610848}.
BINDING 287 287 DNA. {ECO:0000269|PubMed:10706276,
ECO:0000269|PubMed:11902834,
ECO:0000269|PubMed:12578369,
ECO:0000269|PubMed:12592398,
ECO:0000269|PubMed:15610848}.
BINDING 315 315 8-oxoguanine.
BINDING 319 319 8-oxoguanine.
VAR_SEQ 191 195 EVEAH -> PWQCI (in isoform 2C).
{ECO:0000305}.
/FTId=VSP_003750.
VAR_SEQ 196 345 Missing (in isoform 2C). {ECO:0000305}.
/FTId=VSP_003751.
VAR_SEQ 250 345 VADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKG
PSPQTNKELGNFFRSLWGPYAGWAQAVLFSADLRQSRHAQE
PPAKRRKGSKGPEG -> GLLGNAFDGHQLLRPLIFCQDHL
REGPPIGRGDSQGEELEPQLPSSLSSIPYGFCDHCWTKDVD
DPPLVTHPSPGSRDGHMTQAWPVKVVSPLATVIGHVMQASL
LAL (in isoform 2B). {ECO:0000305}.
/FTId=VSP_003749.
VAR_SEQ 317 345 VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> VSVPRCPP
(in isoform 1B).
{ECO:0000303|PubMed:9187114}.
/FTId=VSP_003746.
VAR_SEQ 317 345 VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> TPPSYRCC
SVPTCANPAMLRSHQQSAERVPKGRKARWGTLDKEIPQAPS
PPFPTSLSPSPPSLMLGRGLPVTTSKARHPQIKQSVCTTRW
GGGY (in isoform 1C). {ECO:0000305}.
/FTId=VSP_003747.
VAR_SEQ 317 345 VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> GLLGNAFD
GHQLLRPLIFCQDHLREGPPIGRGDSQGEELEPQLPSSLSS
IPYGFCDHCWTKDVDDPPLVTHPSPGSRDGHMTQAWPVKVV
SPLATVIGHVMQASLLAL (in isoform 2A).
{ECO:0000303|PubMed:9187114,
ECO:0000303|PubMed:9223306}.
/FTId=VSP_003748.
VAR_SEQ 317 345 VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> LCQVITTF
MTFLGPHRLDQMPPEELQTSSSRLGGPPWQCI (in
isoform 2D). {ECO:0000305}.
/FTId=VSP_003752.
VAR_SEQ 317 345 VLFSADLRQSRHAQEPPAKRRKGSKGPEG -> AGSDAS
(in isoform 2E). {ECO:0000305}.
/FTId=VSP_003753.
VARIANT 12 12 G -> E (found in a kidney cancer sample;
no effect on activity; abolishes
mitochondrial localization;
dbSNP:rs772520254).
{ECO:0000269|PubMed:12509224}.
/FTId=VAR_024831.
VARIANT 46 46 R -> Q (found in a clear cell renal cell
carcinoma sample; somatic mutation;
diminished activity; dbSNP:rs104893751).
{ECO:0000269|PubMed:10908322}.
/FTId=VAR_009519.
VARIANT 85 85 A -> S (found in a lung cancer sample;
dbSNP:rs17050550).
{ECO:0000269|PubMed:9662341}.
/FTId=VAR_024832.
VARIANT 131 131 R -> Q (found in a lung cancer sample;
loss of activity; dbSNP:rs747638147).
{ECO:0000269|PubMed:9662341}.
/FTId=VAR_024833.
VARIANT 154 154 R -> H (found in a gastric cancer sample;
no effect on base-excision activity;
alters substrate specificity and strongly
increases mutagenic mis-repair;
dbSNP:rs56053615).
{ECO:0000269|PubMed:10706276,
ECO:0000269|PubMed:10908322,
ECO:0000269|PubMed:9765618}.
/FTId=VAR_009520.
VARIANT 229 229 R -> Q (in dbSNP:rs1805373).
{ECO:0000269|Ref.13}.
/FTId=VAR_014487.
VARIANT 232 232 S -> T (found in a kidney cancer sample).
{ECO:0000269|PubMed:9662341}.
/FTId=VAR_024834.
VARIANT 288 288 A -> V (in dbSNP:rs3219012).
{ECO:0000269|Ref.13}.
/FTId=VAR_018890.
VARIANT 320 320 S -> T (in dbSNP:rs1801128).
/FTId=VAR_014488.
VARIANT 322 322 D -> N (in dbSNP:rs3219014).
{ECO:0000269|Ref.13}.
/FTId=VAR_018891.
VARIANT 326 326 S -> C (common polymorphism in the
Japanese population; dbSNP:rs1052133).
{ECO:0000269|PubMed:10497264,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.13}.
/FTId=VAR_009521.
MUTAGEN 249 249 K->Q: Loss of activity.
{ECO:0000269|PubMed:9197244}.
MUTAGEN 268 268 D->E,Q: No effect on activity.
{ECO:0000269|PubMed:12578369}.
MUTAGEN 268 268 D->N: Decreases activity about 65-fold.
{ECO:0000269|PubMed:12578369}.
CONFLICT 47 47 W -> WW (in Ref. 9; CAA10351).
{ECO:0000305}.
CONFLICT 308 308 G -> E (in Ref. 9; CAA10351).
{ECO:0000305}.
CONFLICT 316 316 A -> ATPPSLQ (in Ref. 2; AAB81132).
{ECO:0000305}.
STRAND 11 13 {ECO:0000244|PDB:1EBM}.
TURN 16 18 {ECO:0000244|PDB:2XHI}.
HELIX 20 22 {ECO:0000244|PDB:2XHI}.
STRAND 24 27 {ECO:0000244|PDB:2XHI}.
TURN 30 32 {ECO:0000244|PDB:2XHI}.
HELIX 35 38 {ECO:0000244|PDB:2XHI}.
TURN 39 42 {ECO:0000244|PDB:2XHI}.
STRAND 48 51 {ECO:0000244|PDB:2XHI}.
STRAND 54 59 {ECO:0000244|PDB:2XHI}.
STRAND 62 68 {ECO:0000244|PDB:2XHI}.
STRAND 70 78 {ECO:0000244|PDB:2XHI}.
STRAND 81 83 {ECO:0000244|PDB:2XHI}.
HELIX 90 99 {ECO:0000244|PDB:2XHI}.
TURN 100 103 {ECO:0000244|PDB:2XHI}.
HELIX 106 116 {ECO:0000244|PDB:2XHI}.
HELIX 118 126 {ECO:0000244|PDB:2XHI}.
HELIX 137 145 {ECO:0000244|PDB:2XHI}.
TURN 146 149 {ECO:0000244|PDB:2XHI}.
HELIX 152 166 {ECO:0000244|PDB:2XHI}.
STRAND 169 173 {ECO:0000244|PDB:2XHI}.
STRAND 176 179 {ECO:0000244|PDB:2XHI}.
HELIX 184 187 {ECO:0000244|PDB:2XHI}.
HELIX 192 198 {ECO:0000244|PDB:2XHI}.
HELIX 204 217 {ECO:0000244|PDB:2XHI}.
HELIX 222 226 {ECO:0000244|PDB:2XHI}.
HELIX 227 229 {ECO:0000244|PDB:2XHI}.
HELIX 233 240 {ECO:0000244|PDB:2XHI}.
HELIX 248 258 {ECO:0000244|PDB:2XHI}.
HELIX 269 279 {ECO:0000244|PDB:2XHI}.
STRAND 284 287 {ECO:0000244|PDB:5AN4}.
STRAND 289 292 {ECO:0000244|PDB:1M3Q}.
HELIX 293 307 {ECO:0000244|PDB:2XHI}.
HELIX 311 323 {ECO:0000244|PDB:2XHI}.
SEQUENCE 345 AA; 38782 MW; C284106ADEEC1FDD CRC64;
MPARALLPRR MGHRTLASTP ALWASIPCPR SELRLDLVLP SGQSFRWREQ SPAHWSGVLA
DQVWTLTQTE EQLHCTVYRG DKSQASRPTP DELEAVRKYF QLDVTLAQLY HHWGSVDSHF
QEVAQKFQGV RLLRQDPIEC LFSFICSSNN NIARITGMVE RLCQAFGPRL IQLDDVTYHG
FPSLQALAGP EVEAHLRKLG LGYRARYVSA SARAILEEQG GLAWLQQLRE SSYEEAHKAL
CILPGVGTKV ADCICLMALD KPQAVPVDVH MWHIAQRDYS WHPTTSQAKG PSPQTNKELG
NFFRSLWGPY AGWAQAVLFS ADLRQSRHAQ EPPAKRRKGS KGPEG


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