OGG1
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "OGG1".

8-oxoguanine DNA glycosylase
PDB rendering based on 1ebm.
Available structures: 1ebm, 1fn7, 1hu0, 1ko9, 1lwv, 1lww, 1lwy, 1m3h, 1m3q, 1n39, 1n3a, 1n3c, 1yqk, 1yql, 1yqm, 1yqr, 2i5w, 2nob, 2noe, 2nof, 2noh, 2noi, 2nol, 2noz
Identifiers
Symbols	OGG1; HMMH; HOGG1; MUTM; OGH1
External IDs	OMIM: 601982 MGI: 1097693 HomoloGene: 1909
Gene ontology Molecular function: • damaged DNA binding • endonuclease activity • oxidized purine base lesion DNA N-glycosylase activity • hydrolase activity, acting on glycosyl bonds • lyase activity Cellular component: • cellular_component • intracellular • nucleus • nucleoplasm • mitochondrion Biological process: • base-excision repair • metabolic process
RNA expression pattern
More reference expression data
Orthologs
	Human	Mouse
Entrez	4968	18294
Ensembl	ENSG00000114026	ENSMUSG00000030271
Uniprot	O15527	Q3UIL3
Refseq	NM_002542 (mRNA) NP_002533 (protein)	NM_010957 (mRNA) NP_035087 (protein)
Location	Chr 3: 9.77 - 9.78 Mb	Chr 6: 113.29 - 113.3 Mb
Pubmed search	[1]	[2]

8-oxoguanine glycosylase is a DNA glycosylase enzyme. It is involved in base excision repair.

It is the primary enzyme responsible for the excision of 7,8-dihydro-8-oxoguanine (8-oxoG), a mutagenic base byproduct which occurs as a result of exposure to reactive oxygen species (ROS). The action of this enzyme includes lyase activity for chain cleavage. Alternative splicing of the C-terminal region of this gene classifies splice variants into two major groups, type 1 and type 2, depending on the last exon of the sequence. Type 1 alternative splice variants end with exon 7 and type 2 end with exon 8. All variants share the N-terminal region in common. Many alternative splice variants for this gene have been described, but the full-length nature for every variant has not been determined. The N-terminus of this gene contains a mitochondrial targetting signal, essential for mitochondrial localization.¹

References

Further reading

External links

• MeSH oxoguanine+glycosylase+1,+human

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