Reviewed, UniProtKB/Swiss-Prot O15527 (OGG1_HUMAN)

Names and origin

Protein names

Recommended name:
    N-glycosylase/DNA lyase
Including the following 2 domains:
    1- Recommended name:
            8-oxoguanine DNA glycosylase
              EC=3.2.2.-
    2- Recommended name:
            DNA-(apurinic or apyrimidinic site) lyase
                Short name=AP lyase
              EC=4.2.99.18

Gene names

Name:	OGG1
Synonyms:	MMH, MUTM, OGH1

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	345 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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	Isoform 1A: Nucleus. Isoform 2A: Mitochondrion.
Tissue specificity	Ubiquitous.
Involvement in disease	Defects in OGG1 are associated with tumor formation. Defects in OGG1 are a cause of renal cell carcinoma (RCC1) [MIM:144700].
Sequence similarities	Belongs to the type-1 OGG1 family.

Ontologies

Keywords
Biological process	DNA damage DNA repair
Cellular component	Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Molecular function	Glycosidase Hydrolase Lyase
Technical term	3D-structure Multifunctional enzyme
Gene Ontology (GO)
Biological process	depurination Inferred from Experiment. Source: Reactome nucleotide-excision repair Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrion Inferred from electronic annotation. Source: UniProtKB-KW nucleoplasm Ref.4 Inferred from Experiment. Source: Reactome
Molecular function	damaged DNA binding Ref.4 Traceable author statement. Source: ProtInc oxidized purine base lesion DNA N-glycosylase activity Ref.6 Inferred from Experiment. Source: Reactome protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
SNRPF	P62306	1	EBI-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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 345

345

N-glycosylase/DNA lyase

PRO_0000058591

Sites

Active site

249

1

Schiff-base intermediate with DNA Ref.5

Binding site

149

1

DNA

Binding site

154

1

DNA

Binding site

204

1

DNA

Binding site

266

1

8-oxoguanine; via carbonyl oxygen

Binding site

268

1

8-oxoguanine

Binding site

270

1

DNA

Binding site

287

1

DNA

Binding site

315

1

8-oxoguanine

Binding site

319

1

8-oxoguanine

Natural variations

Alternative sequence

191 – 195

5

EVEAH → PWQCI in isoform 2C.

VSP_003750

Alternative sequence

196 – 345

150

Missing in isoform 2C.

VSP_003751

Alternative sequence

250 – 345

96

VADCI…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2B.

VSP_003749

Alternative sequence

317 – 345

29

VLFSA…KGPEG → VSVPRCPP in isoform 1B.

VSP_003746

Alternative sequence

317 – 345

29

VLFSA…KGPEG → TPPSYRCCSVPTCANPAMLR SHQQSAERVPKGRKARWGTL DKEIPQAPSPPFPTSLSPSP PSLMLGRGLPVTTSKARHPQ IKQSVCTTRWGGGY in isoform 1C.

VSP_003747

Alternative sequence

317 – 345

29

VLFSA…KGPEG → GLLGNAFDGHQLLRPLIFCQ DHLREGPPIGRGDSQGEELE PQLPSSLSSIPYGFCDHCWT KDVDDPPLVTHPSPGSRDGH MTQAWPVKVVSPLATVIGHV MQASLLAL in isoform 2A.

VSP_003748

Alternative sequence

317 – 345

29

VLFSA…KGPEG → LCQVITTFMTFLGPHRLDQM PPEELQTSSSRLGGPPWQCI in isoform 2D.

VSP_003752

Alternative sequence

317 – 345

29

VLFSA…KGPEG → AGSDAS in isoform 2E.

VSP_003753

Natural variant

12

1

G → E in kidney cancer; no effect on activity. Abolishes mitochondrial localization. Ref.27

VAR_024831

Natural variant

46

1

R → Q in kidney cancer; diminished activity. Ref.26

VAR_009519

Natural variant

85

1

A → S in lung cancer. dbSNP rs17050550. Ref.24

VAR_024832

Natural variant

131

1

R → Q in lung cancer; loss of activity. Ref.24

VAR_024833

Natural variant

154

1

R → H in gastric cancer; No effect on base-excision activity. Alters substrate specificity and strongly increases mutagenic mis-repair. dbSNP rs56053615. Ref.26 Ref.17 Ref.23

VAR_009520

Natural variant

229

1

R → Q: dbSNP rs1805373. Ref.13

VAR_014487

Natural variant

232

1

S → T in kidney cancer. Ref.24

VAR_024834

Natural variant

288

1

A → V: dbSNP rs3219012. Ref.13

VAR_018890

Natural variant

320

1

S → T: dbSNP rs1801128.

VAR_014488

Natural variant

322

1

D → N: dbSNP rs3219014. Ref.13

VAR_018891

Natural variant

326

1

S → C Common polymorphism in the Japanese population. dbSNP rs1052133. Ref.13 Ref.12 Ref.15 Ref.25

VAR_009521

Experimental info

Mutagenesis

249

1

K → Q: Loss of activity. Ref.5

Mutagenesis

268

1

D → E or Q: No effect on activity. Ref.19

Mutagenesis

268

1

D → N: Decreases activity about 65-fold. Ref.19

Sequence conflict

47

1

W → WW in CAA10351. Ref.9

Sequence conflict

308

1

G → E in CAA10351. Ref.9

Sequence conflict

316

1

A → ATPPSLQ Ref.2

Secondary structure

1

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345

Helix Strand Turn

Details...

Turn

16 – 18

3

Helix

20 – 22

3

Beta strand

24 – 27

4

Turn

30 – 32

3

Helix

35 – 38

4

Turn

39 – 42

4

Beta strand

48 – 51

4

Beta strand

54 – 58

5

Beta strand

60 – 68

9

Beta 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

Beta strand

169 – 173

5

Beta 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

Beta strand

284 – 287

4

Helix

293 – 307

15

Helix

311 – 323

13

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1A (Alpha) [UniParc]. Last modified December 1, 2000. Version 2. Checksum: C284106ADEEC1FDD	FASTA	345	38,782
	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
	Isoform 1B. Checksum: FB6DAF62F162C353	FASTA	324	36,433
	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 NFFRSLWGPY AGWAQAVSVP RCPP
	Isoform 1C. Checksum: CA01660C056A09F0	FASTA	410	45,761
	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 310 320 330 340 350 360 NFFRSLWGPY AGWAQATPPS YRCCSVPTCA NPAMLRSHQQ SAERVPKGRK ARWGTLDKEI 370 380 390 400 410 PQAPSPPFPT SLSPSPPSLM LGRGLPVTTS KARHPQIKQS VCTTRWGGGY
	Isoform 2A (Beta). Checksum: 0013B0F2D51FD316	FASTA	424	47,237
	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 310 320 330 340 350 360 NFFRSLWGPY AGWAQAGLLG NAFDGHQLLR PLIFCQDHLR EGPPIGRGDS QGEELEPQLP 370 380 390 400 410 420 SSLSSIPYGF CDHCWTKDVD DPPLVTHPSP GSRDGHMTQA WPVKVVSPLA TVIGHVMQAS LLAL
	Isoform 2B. Checksum: 0FAA63310FC13ADB	FASTA	357	39,729
	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 CILPGVGTKG LLGNAFDGHQ LLRPLIFCQD HLREGPPIGR GDSQGEELEP QLPSSLSSIP 310 320 330 340 350 YGFCDHCWTK DVDDPPLVTH PSPGSRDGHM TQAWPVKVVS PLATVIGHVM QASLLAL
	Isoform 2C. Checksum: 16628F612964E282	FASTA	195	22,210
	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 FPSLQALAGP PWQCI
	Isoform 2D. Checksum: 40D1E4783F042C8F	FASTA	356	40,095
	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 310 320 330 340 350 NFFRSLWGPY AGWAQALCQV ITTFMTFLGP HRLDQMPPEE LQTSSSRLGG PPWQCI
	Isoform 2E. Checksum: E47B3CA5AE8CFABB	FASTA	322	36,085
	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 NFFRSLWGPY AGWAQAAGSD AS

References

	« Hide 'large scale' referencesShow '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: 9187114] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1A; 1B AND 2). 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: 9207108] [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: 9223306] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[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: 9223305] [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: 9197244] [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: 9190902] [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: 9348312] [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: 9321410] [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: 10449904] [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: 10233168] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], ALTERNATIVE SPLICING.
[12]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1A), VARIANT CYS-326. Tissue: Brain.
[13]	NIEHS SNPs program Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLN-229; VAL-288; ASN-322 AND CYS-326.
[14]	"The DNA sequence, annotation and analysis of human chromosome 3." Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J. , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A. Nature 440:1194-1198(2006) [PubMed: 16641997] [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: 15489334] [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: 10775435] [Abstract] Cited for: REVIEW.
[17]	"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: 10706276] [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.
[18]	"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: 11902834] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) IN COMPLEX WITH DNA AND 8-OXO-GUANINE.
[19]	"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: 12578369] [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.
[20]	"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: 12592398] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 12-327 IN COMPLEX WITH DNA AND 8-OXO-GUANINE.
[21]	"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: 15610848] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 12-325 OF MUTANT GLU-268 IN COMPLEX WITH DNA.
[22]	"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: 17114185] [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.
[23]	"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: 9765618] [Abstract] Cited for: VARIANT HIS-154.
[24]	"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: 9662341] [Abstract] Cited for: VARIANTS SER-85; GLN-131 AND THR-232, CHARACTERIZATION OF VARIANT GLN-131.
[25]	"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: 10497264] [Abstract] Cited for: CHARACTERIZATION OF VARIANT CYS-326.
[26]	"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: 10908322] [Abstract] Cited for: CHARACTERIZATION OF VARIANTS GLN-46 AND HIS-154.
[27]	"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: 12509224] [Abstract] Cited for: CHARACTERIZATION OF VARIANT GLU-12.
+	Additional computationally mapped references.

Web resources

NIEHS-SNPs

Cross-references

Sequence databases

EMBLGenBankDDBJ

U96710 mRNA. Translation: AAB81132.1.
Y11838 mRNA. Translation: CAA72536.1.
Y11731 mRNA. Translation: CAA72414.1.
AB000410 mRNA. Translation: BAA19103.1.
AF003595 mRNA. Translation: AAB61340.1.
U88527 mRNA. Translation: AAB68614.1.
U88620 mRNA. Translation: AAB68615.1.
Y13277 mRNA. Translation: CAA73726.1.
AF026691 mRNA. Translation: AAB84013.1.
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.

IPI

IPI00007312.
IPI00025730.
IPI00026574.
IPI00220178.
IPI00220179.
IPI00220180.
IPI00294126.
IPI00303869.

PIR

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

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1EBM	X-ray	2.10	A	12-325	[»]
1FN7	X-ray	2.60	A	12-325	[»]
1HU0	X-ray	2.35	A	12-327	[»]
1KO9	X-ray	2.15	A	1-345	[»]
1LWV	X-ray	2.30	A	12-327	[»]
1LWW	X-ray	2.10	A	12-327	[»]
1LWY	X-ray	2.01	A	12-327	[»]
1M3H	X-ray	2.05	A	12-325	[»]
1M3Q	X-ray	1.90	A	12-325	[»]
1N39	X-ray	2.20	A	12-325	[»]
1N3A	X-ray	2.20	A	12-325	[»]
1N3C	X-ray	2.70	A	12-325	[»]
1YQK	X-ray	2.50	A	12-327	[»]
1YQL	X-ray	2.60	A	12-327	[»]
1YQM	X-ray	2.50	A	12-327	[»]
1YQR	X-ray	2.43	A	12-327	[»]
2I5W	X-ray	2.60	A	12-323	[»]
2NOB	X-ray	2.10	A	12-327	[»]
2NOE	X-ray	2.20	A	12-327	[»]
2NOF	X-ray	2.35	A	12-327	[»]
2NOH	X-ray	2.01	A	12-327	[»]
2NOI	X-ray	2.35	A	12-327	[»]
2NOL	X-ray	2.57	A	12-327	[»]
2NOZ	X-ray	2.43	A	12-327	[»]

ModBase

Search...

Protein-protein interaction databases

IntAct

O15527. 3 interactions.

Proteomic databases

PRIDE

O15527.

Genome annotation databases

Ensembl

ENSG00000114026. Homo sapiens. [Contig view]

GeneID

4968.

KEGG

hsa:4968.

Organism-specific databases

GeneCards

GC03P009772.

H-InvDB

HIX0003031.

HGNC

HGNC:8125. OGG1.

MIM

144700. phenotype.
601982. gene.

Orphanet

151. Renal cell carcinoma, familial.

PharmGKB

PA31912.

GenAtlas

Search...

Phylogenomic databases

HOVERGEN

O15527.

OMA

O15527. GLRLIRQ.

Enzyme and pathway databases

BRENDA

4.2.99.18. 247.

Reactome

REACT_216. DNA Repair.

Gene expression databases

ArrayExpress

O15527.

Bgee

O15527.

GermOnline

ENSG00000114026. Homo sapiens.

Family and domain databases

InterPro

IPR003265. HhH-GPD_domain.
IPR004577. Ogg.
IPR012904. OGG_N.
[Graphical view]

Pfam

PF00730. HhH-GPD. 1 hit.
PF07934. OGG_N. 1 hit.
[Graphical view]

SMART

SM00478. ENDO3c. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00588. ogg. 1 hit.

ProtoNet

Search...

Other Resources

NextBio

19116.

SOURCE

Search...

Entry information

Entry name

OGG1_HUMAN

Accession

Primary (citable) accession number: O15527
Secondary accession number(s): A8K1E3 , O00390, O00670, O00705, O14876, O95488, P78554, Q9BW42, Q9UIK0, Q9UIK1, Q9UIK2, Q9UL34, Q9Y2C0, Q9Y2C1, Q9Y6C3, Q9Y6C4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 106 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)