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HUMAN:OGG1

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Species (Taxon ID) Homo sapiens (Human). (9606)
Gene Name(s) OGG1 (synonyms: MMH, MUTM, OGH1)
Protein Name(s) N-glycosylase/DNA lyase

8-oxoguanine DNA glycosylase DNA-(apurinic or apyrimidinic site) lyase AP lyase

External Links
UniProt O15527
EMBL U88527
U88620
U96710
Y13277
Y11731
AF003595
AB000410
AF026691
Y11838
AJ131341
AF088282
AF088282
AF088282
AB019528
AB019529
AB019530
AB019531
AB019532
AK289858
AF521807
AC022382
BC000657
CCDS CCDS2576.1
CCDS2577.1
CCDS2578.1
CCDS2579.1
CCDS2580.1
CCDS2581.1
CCDS43046.1
CCDS46742.1
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
PDB 1EBM
1FN7
1HU0
1KO9
1LWV
1LWW
1LWY
1M3H
1M3Q
1N39
1N3A
1N3C
1YQK
1YQL
1YQM
1YQR
2I5W
2NOB
2NOE
2NOF
2NOH
2NOI
2NOL
2NOZ
2XHI
3IH7
3KTU
5AN4
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
2XHI
3IH7
3KTU
5AN4
ProteinModelPortal O15527
SMR O15527
BioGrid 111018
IntAct O15527
MINT O15527
BindingDB O15527
ChEMBL CHEMBL3396944
iPTMnet O15527
PhosphoSitePlus O15527
BioMuta OGG1
MaxQB O15527
PeptideAtlas O15527
PRIDE O15527
DNASU 4968
Ensembl ENST00000302003
ENST00000302008
ENST00000302036
ENST00000339511
ENST00000344629
ENST00000349503
ENST00000383826
ENST00000449570
GeneID 4968
KEGG hsa:4968
UCSC uc003bsh.4
CTD 4968
DisGeNET 4968
EuPathDB HostDB:ENSG00000114026.21
GeneCards OGG1
HGNC HGNC:8125
HPA CAB047301
HPA027514
MalaCards OGG1
MIM 144700
601982
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
4.2.99.18
Reactome R-HSA-110328
R-HSA-110329
R-HSA-110330
R-HSA-110331
R-HSA-110357
R-HSA-5649702
SIGNOR O15527
ChiTaRS OGG1
EvolutionaryTrace O15527
GeneWiki Oxoguanine_glycosylase
GenomeRNAi 4968
PRO PR:O15527
Proteomes UP000005640
Bgee ENSG00000114026
ExpressionAtlas O15527
Genevisible O15527
GO GO:0005739
GO:0016363
GO:0016607
GO:0005654
GO:0005634
GO:0043234
GO:0034039
GO:0140078
GO:0140080
GO:0003684
GO:0019104
GO:0004519
GO:0008017
GO:0032357
GO:0008534
GO:0002526
GO:0007568
GO:0006284
GO:0071276
GO:0006974
GO:0045007
GO:0045008
GO:0043066
GO:1901291
GO:0033683
GO:0033158
GO:0006355
GO:0032355
GO:0045471
GO:0051593
GO:0009416
GO:0006979
GO:0009314
CDD cd00056
Gene3D 1.10.1670.10
InterPro IPR011257
IPR003265
IPR023170
IPR004577
IPR012904
Pfam PF00730
PF07934
SMART SM00478
SUPFAM SSF48150
TIGRFAMs TIGR00588

Annotations

Qualifier GO ID GO term name Reference ECO ID ECO term name with/from Aspect Extension Notes Status
GO:0034039

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

PMID:10987279[1]

ECO:0000315

F

Figure 1 shows the repair activity of mutant OGG1 proteins.

complete
CACAO 13258

enables

GO:0003684

damaged DNA binding

PMID:14706345[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0032357

oxidized purine DNA binding

PMID:14706345[2]

ECO:0000314

direct assay evidence used in manual assertion

F

Seeded From UniProt

complete

part_of

GO:0016607

nuclear speck

PMID:17148573[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0016363

nuclear matrix

PMID:17148573[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0009314

response to radiation

PMID:17148573[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006979

response to oxidative stress

PMID:17148573[3]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0006355

regulation of transcription, DNA-templated

PMID:8621488[4]

ECO:0000315

mutant phenotype evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

PMID:17148573[3]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0034039

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

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1097693
PANTHER:PTN000028426

F

Seeded From UniProt

complete

involved_in

GO:0006285

base-excision repair, AP site formation

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

PANTHER:PTN000028426
SGD:S000004525

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:21873635[5]

ECO:0000318

biological aspect of ancestor evidence used in manual assertion

MGI:MGI:1097693
PANTHER:PTN000028426
RGD:621168
SGD:S000004525
UniProtKB:O15527

C

Seeded From UniProt

complete

involved_in

GO:1901291

negative regulation of double-strand break repair via single-strand annealing

PMID:19506022[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

involved_in

GO:0033683

nucleotide-excision repair, DNA incision

PMID:19506022[6]

ECO:0000314

direct assay evidence used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0032991

protein-containing complex

PMID:19506022[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

PMID:19506022[6]

ECO:0000316

genetic interaction evidence used in manual assertion

UniProtKB:P43351

P

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

PMID:19506022[6]

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000052

ECO:0000314

direct assay evidence used in manual assertion

C

Seeded From UniProt

complete

enables

GO:0034039

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

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

F

Seeded From UniProt

complete

enables

GO:0008534

oxidized purine nucleobase lesion DNA N-glycosylase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

F

Seeded From UniProt

complete

enables

GO:0008017

microtubule binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

F

Seeded From UniProt

complete

involved_in

GO:0006284

base-excision repair

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

C

Seeded From UniProt

complete

enables

GO:0003677

DNA binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O08760
ensembl:ENSMUSP00000032406

F

Seeded From UniProt

complete

involved_in

GO:0071276

cellular response to cadmium ion

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

involved_in

GO:0051593

response to folic acid

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

involved_in

GO:0045471

response to ethanol

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

involved_in

GO:0043066

negative regulation of apoptotic process

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

involved_in

GO:0042493

response to drug

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

involved_in

GO:0032355

response to estradiol

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

enables

GO:0019104

DNA N-glycosylase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

F

Seeded From UniProt

complete

involved_in

GO:0009416

response to light stimulus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

enables

GO:0008534

oxidized purine nucleobase lesion DNA N-glycosylase activity

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

F

Seeded From UniProt

complete

involved_in

GO:0007568

aging

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

involved_in

GO:0006284

base-excision repair

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

C

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

C

Seeded From UniProt

complete

enables

GO:0003684

damaged DNA binding

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

F

Seeded From UniProt

complete

involved_in

GO:0002526

acute inflammatory response

GO_REF:0000107

ECO:0000265

sequence orthology evidence used in automatic assertion

UniProtKB:O70249
ensembl:ENSRNOP00000070483

P

Seeded From UniProt

complete

enables

GO:0003684

damaged DNA binding

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012904

F

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011257

F

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR011257

P

Seeded From UniProt

complete

involved_in

GO:0006284

base-excision repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR003265
InterPro:IPR004577

P

Seeded From UniProt

complete

involved_in

GO:0006289

nucleotide-excision repair

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR012904

P

Seeded From UniProt

complete

enables

GO:0008534

oxidized purine nucleobase lesion DNA N-glycosylase activity

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004577
InterPro:IPR012904

F

Seeded From UniProt

complete

enables

GO:0034039

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

GO_REF:0000002

ECO:0000256

match to sequence model evidence used in automatic assertion

InterPro:IPR004577

F

Seeded From UniProt

complete

enables

GO:0140078

class I DNA-(apurinic or apyrimidinic site) endonuclease activity

GO_REF:0000003

ECO:0000501

evidence used in automatic assertion

EC:4.2.99.18

F

Seeded From UniProt

complete

enables

GO:0008534

oxidized purine nucleobase lesion DNA N-glycosylase activity

PMID:9190902[7]
Reactome:R-HSA-110244
Reactome:R-HSA-110243

ECO:0000304

author statement supported by traceable reference used in manual assertion



F

Seeded From UniProt

complete

involved_in

GO:0006284

base-excision repair

PMID:9190902[7]

ECO:0000304

author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

PMID:9223305[8]
Reactome:R-HSA-5649701
Reactome:R-HSA-110354
Reactome:R-HSA-110244
Reactome:R-HSA-110243
Reactome:R-HSA-110236
Reactome:R-HSA-110235

ECO:0000304

author statement supported by traceable reference used in manual assertion







C

Seeded From UniProt

complete

enables

GO:0004519

endonuclease activity

PMID:9223305[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

enables

GO:0003684

damaged DNA binding

PMID:9223305[8]

ECO:0000304

author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

involved_in

GO:0045008

depyrimidination

Reactome:R-HSA-110329
Reactome:R-HSA-110328

ECO:0000304

author statement supported by traceable reference used in manual assertion


P

Seeded From UniProt

complete

involved_in

GO:0045007

depurination

Reactome:R-HSA-110331
Reactome:R-HSA-110330

ECO:0000304

author statement supported by traceable reference used in manual assertion


P

Seeded From UniProt

complete

involved_in

GO:0006281

DNA repair

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0234

P

Seeded From UniProt

complete

enables

GO:0016829

lyase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0456

F

Seeded From UniProt

complete

enables

GO:0016798

hydrolase activity, acting on glycosyl bonds

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326

F

Seeded From UniProt

complete

involved_in

GO:0006974

cellular response to DNA damage stimulus

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0227

P

Seeded From UniProt

complete

involved_in

GO:0008152

metabolic process

GO_REF:0000037
GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0326
UniProtKB-KW:KW-0511

P

Seeded From UniProt

complete

enables

GO:0016787

hydrolase activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0378

F

Seeded From UniProt

complete

part_of

GO:0005634

nucleus

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0539
UniProtKB-SubCell:SL-0191

C

Seeded From UniProt

complete

enables

GO:0003824

catalytic activity

GO_REF:0000037

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0511

F

Seeded From UniProt

complete

part_of

GO:0005739

mitochondrion

GO_REF:0000037
GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-KW:KW-0496
UniProtKB-SubCell:SL-0173

C

Seeded From UniProt

complete

part_of

GO:0005654

nucleoplasm

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0190

C

Seeded From UniProt

complete

part_of

GO:0016363

nuclear matrix

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0181

C

Seeded From UniProt

complete

part_of

GO:0016607

nuclear speck

GO_REF:0000039

ECO:0000322

imported manually asserted information used in automatic assertion

UniProtKB-SubCell:SL-0186

C

Seeded From UniProt

complete

Notes

References

See Help:References for how to manage references in GONUTS.

  1. Audebert, M et al. (2000) Alterations of the DNA repair gene OGG1 in human clear cell carcinomas of the kidney. Cancer Res. 60 4740-4 PubMed GONUTS page
  2. 2.0 2.1 Hegde, V et al. (2004) Characterization of human ribosomal protein S3 binding to 7,8-dihydro-8-oxoguanine and abasic sites by surface plasmon resonance. DNA Repair (Amst.) 3 121-6 PubMed GONUTS page
  3. 3.0 3.1 3.2 3.3 3.4 Campalans, A et al. (2007) UVA irradiation induces relocalisation of the DNA repair protein hOGG1 to nuclear speckles. J. Cell. Sci. 120 23-32 PubMed GONUTS page
  4. Chung, U et al. (1996) The interaction between Ku antigen and REF1 protein mediates negative gene regulation by extracellular calcium. J. Biol. Chem. 271 8593-8 PubMed GONUTS page
  5. 5.0 5.1 5.2 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
  6. 6.0 6.1 6.2 6.3 6.4 de Souza-Pinto, NC et al. (2009) The recombination protein RAD52 cooperates with the excision repair protein OGG1 for the repair of oxidative lesions in mammalian cells. Mol. Cell. Biol. 29 4441-54 PubMed GONUTS page
  7. 7.0 7.1 Arai, K et al. (1997) Cloning of a human homolog of the yeast OGG1 gene that is involved in the repair of oxidative DNA damage. Oncogene 14 2857-61 PubMed GONUTS page
  8. 8.0 8.1 8.2 Radicella, JP et al. (1997) Cloning and characterization of hOGG1, a human homolog of the OGG1 gene of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. U.S.A. 94 8010-5 PubMed GONUTS page