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OGG1

Protein FULL name:

N-glycosylase/DNA lyase, Includes: 8-oxoguanine DNA glycosylase, Includes: DNA-(apurinic or apyrimidinic site) lyase


OGG1 (Homo sapiens) is product of expression of OGG1 gene.


OGG1 is involved in:

BER in Homo sapiens

Keywords:



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.

INTERACTION: P62306:SNRPF; NbExp=1; IntAct=EBI-721675, EBI-356900;

SUBCELLULAR LOCATION: Isoform 1A: Nucleus.

SUBCELLULAR LOCATION: Isoform 2A: Mitochondrion.

TISSUE SPECIFICITY: Ubiquitous.

DISEASE: Note=Defects in OGG1 are associated with tumor formation.

DISEASE: Defects in OGG1 are a cause of renal cell carcinoma type 1 (RCC1) [MIM:144700].

SIMILARITY: Belongs to the type-1 OGG1 family.

SEQUENCE CAUTION: Sequence=AAB84013.1; Type=Erroneous initiation;

WEB RESOURCE: Name=NIEHS-SNPs; [LINK]


NCBI GenPept GI number(s): 12643548
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot O15527 O15527
PFAM: PF00730
PF07934
PF00730
PF07934
InterPro: IPR011257
IPR003265
IPR004577
IPR012904
IPR012294
IPR011257
IPR003265
IPR004577
IPR012904
IPR012294
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MPARALLPRRMGHRTLASTPALWASIPCPRSELRLDLVLPSGQSFRWREQ
SPAHWSGVLADQVWTLTQTEEQLHCTVYRGDKSQASRPTPDELEAVRKYF
QLDVTLAQLYHHWGSVDSHFQEVAQKFQGVRLLRQDPIECLFSFICSSNN
NIARITGMVERLCQAFGPRLIQLDDVTYHGFPSLQALAGPEVEAHLRKLG
LGYRARYVSASARAILEEQGGLAWLQQLRESSYEEAHKALCILPGVGTKV
ADCICLMALDKPQAVPVDVHMWHIAQRDYSWHPTTSQAKGPSPQTNKELG
NFFRSLWGPYAGWAQAVLFSADLRQSRHAQEPPAKRRKGSKGPEG

OGG1 (Homo sapiens) is able to recognize following damages:
References:

Title Authors Journal
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 Cancer Res June 1, 1997
A mammalian DNA repair enzyme that excises oxidatively damaged guanines maps to a locus frequently lost in lung cancer. Lu R, Nash HM, Verdine GL Curr Biol June 1, 1997
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, Kim SR, Nohmi T, Taniwaki M, Ohwada S, Yokota J Oncogene June 12, 1997
Cloning and characterization of a mammalian 8-oxoguanine DNA glycosylase. Rosenquist TA, Zharkov DO, Grollman AP Proc Natl Acad Sci U S A July 8, 1997
Molecular cloning and functional expression of a human cDNA encoding the antimutator enzyme 8-hydroxyguanine-DNA glycosylase. Roldan-Arjona T, Wei YF, Carter KC, Klungland A, Anselmino C, Wang RP, Augustus M, Lindahl T Proc Natl Acad Sci U S A July 22, 1997
Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Radicella JP, Dherin C, Desmaze C, Fox MS, Boiteux S Proc Natl Acad Sci U S A July 22, 1997
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, Hoff E, Haug T, Rognes T, Seeberg E EMBO J Oct. 15, 1997
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 FC, Sklar J J Exp Med Nov. 3, 1997
Mutations in OGG1, a gene involved in the repair of oxidative DNA damage, are found in human lung and kidney tumours. Chevillard S, Radicella JP, Levalois C, Lebeau J, Poupon MF, Oudard S, Dutrillaux B, Boiteux S Oncogene June 11, 1998
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 Aug. 1, 1998
Structure and chromosome location of human OGG1. Ishida T, Hippo Y, Nakahori Y, Matsushita I, Kodama T, Nishimura S, Aburatani H Cytogenet Cell Genet Jan. 1, 1999
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 May 1, 1999
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 JP, Dizdaroglu M, Boiteux S Nucleic Acids Res Oct. 15, 1999
Structural basis for recognition and repair of the endogenous mutagen 8-oxoguanine in DNA. Bruner SD, Norman DP, Verdine GL Nature Jan. 24, 2000
The human OGG1 gene: structure, functions, and its implication in the process of carcinogenesis. Boiteux S, Radicella JP Arch Biochem Biophys May 1, 2000
Effect of single mutations in the OGG1 gene found in human tumors on the substrate specificity of the Ogg1 protein. Audebert M, Radicella JP, Dizdaroglu M Nucleic Acids Res July 15, 2000
Reciprocal "flipping" underlies substrate recognition and catalytic activation by the human 8-oxo-guanine DNA glycosylase. Bjoras M, Seeberg E, Luna L, Pearl LH, Barrett TE J Mol Biol March 22, 2002
Mitochondrial targeting of human 8-oxoguanine DNA glycosylase hOGG1 is impaired by a somatic mutation found in kidney cancer. Audebert M, Charbonnier JB, Boiteux S, Radicella JP DNA Repair (Amst) July 17, 2002
Structural and biochemical exploration of a critical amino acid in human 8-oxoguanine glycosylase. Norman DP, Chung SJ, Verdine GL Biochemistry Jan. 18, 2003
Product-assisted catalysis in base-excision DNA repair. Fromme JC, Bruner SD, Yang W, Karplus M, Verdine GL Nat Struct Biol March 1, 2003
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 TO, 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 Feb. 1, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J Genome Res Oct. 1, 2004
Structures of end products resulting from lesion processing by a DNA glycosylase/lyase. Chung SJ, Verdine GL Chem Biol Dec. 1, 2004
The DNA sequence, annotation and analysis of human chromosome 3. Muzny DM, Scherer SE, Kaul R, Wang J, Yu J, Sudbrak R, Buhay CJ, Chen R, Cree A, Ding Y, Dugan-Rocha S, Gill R, Gunaratne P, Harris RA, Hawes AC, Hernandez J, Hodgson AV, Hume J, Jackson A, Khan ZM, Kovar-Smith C, Lewis LR, Lozado RJ, Metzker ML, Milosavljevic A, Miner GR, Morgan MB, Nazareth LV, Scott G, Sodergren E, Song XZ, Steffen D, Wei S, Wheeler DA, Wright MW, Worley KC, Yuan Y, Zhang Z, Adams CQ, Ansari-Lari MA, Ayele M, Brown MJ, Chen G, Chen Z, Clendenning J, Clerc-Blankenburg KP, Chen R, Chen Z, Davis C, Delgado O, Dinh HH, Dong W, Draper H, Ernst S, Fu G, Gonzalez-Garay ML, Garcia DK, Gillett W, Gu J, Hao B, Haugen E, Havlak P, He X, Hennig S, Hu S, Huang W, Jackson LR, Jacob LS, Kelly SH, Kube M, Levy R, Li Z, Liu B, Liu J, Liu W, Lu J, Maheshwari M, Nguyen BV, Okwuonu GO, Palmeiri A, Pasternak S, Perez LM, Phelps KA, Plopper FJ, Qiang B, Raymond C, Rodriguez R, Saenphimmachak C, Santibanez J, Shen H, Shen Y, Subramanian S, Tabor PE, Verduzco D, Waldron L, Wang J, Wang J, Wang Q, Williams GA, Wong GK, Yao Z, Zhang J, Zhang X, Zhao G, Zhou J, Zhou Y, Nelson D, Lehrach H, Reinhardt R, Naylor SL, Yang H, Olson M, Weinstock G, Gibbs RA Nature April 27, 2006
Structural characterization of human 8-oxoguanine DNA glycosylase variants bearing active site mutations. Radom CT, Banerjee A, Verdine GL J Biol Chem March 23, 2007


Last modification of this entry: Oct. 14, 2010.

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