Uracil-DNA glycosylase

From Wikipedia, the free encyclopedia

PDB rendering based on 1akz.

Available structures: 1akz, 1emh, 1emj, 1q3f, 1ssp, 1ugh, 1yuo, 2hxm, 2ssp, 4skn

Identifiers

Symbol(s)

UNG; DGU; DKFZp781L1143; HIGM4; UDG; UNG1; UNG15

External IDs

OMIM: 191525 MGI: 109352 HomoloGene: 6585

Gene ontology
Molecular Function:	• uracil DNA N-glycosylase activity • protein binding • hydrolase activity, acting on glycosyl bonds
Cellular Component:	• nucleus • mitochondrion
Biological Process:	• base-excision repair • metabolic process • somatic hypermutation of immunoglobulin genes • somatic recombination of immunoglobulin gene segments

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_003362 (mRNA)
NP_003353 (protein)

NM_001040691 (mRNA)
NP_001035781 (protein)

Location

Chr 12: 108.02 - 108.03 Mb

Chr 5: 114.39 - 114.4 Mb

Pubmed search

[1]

[2]

Uracil-DNA glycosylase, also known as UNG, is a human gene.^[1]

This gene encodes one of several uracil-DNA glycosylases. One important function of uracil-DNA glycosylases is to prevent mutagenesis by eliminating uracil from DNA molecules by cleaving the N-glycosylic bond and initiating the base-excision repair (BER) pathway. Uracil bases occur from cytosine deamination or misincorporation of dUMP residues. Alternative promoter usage and splicing of this gene leads to two different isoforms: the mitochondrial UNG1 and the nuclear UNG2.^[1]

[edit] References

^ ^a ^b Entrez Gene: UNG uracil-DNA glycosylase.

[edit] Further reading

Caradonna S, Muller-Weeks S (2002). "The nature of enzymes involved in uracil-DNA repair: isoform characteristics of proteins responsible for nuclear and mitochondrial genomic integrity.". Curr. Protein Pept. Sci. 2 (4): 335-47. PMID 12369930.
Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193-205. doi:10.1089/104454904773819789. PMID 15142377.
Van Maele B, Debyser Z (2005). "HIV-1 integration: an interplay between HIV-1 integrase, cellular and viral proteins.". AIDS reviews 7 (1): 26-43. PMID 15875659.
Slupphaug G, Olsen LC, Helland D, et al. (1991). "Cell cycle regulation and in vitro hybrid arrest analysis of the major human uracil-DNA glycosylase.". Nucleic Acids Res. 19 (19): 5131-7. PMID 1923798.
Muller SJ, Caradonna S (1991). "Isolation and characterization of a human cDNA encoding uracil-DNA glycosylase.". Biochim. Biophys. Acta 1088 (2): 197-207. PMID 2001396.
Olsen LC, Aasland R, Wittwer CU, et al. (1990). "Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme.". EMBO J. 8 (10): 3121-5. PMID 2555154.
Nagelhus TA, Slupphaug G, Lindmo T, Krokan HE (1995). "Cell cycle regulation and subcellular localization of the major human uracil-DNA glycosylase.". Exp. Cell Res. 220 (2): 292-7. doi:10.1006/excr.1995.1318. PMID 7556436.
Mol CD, Arvai AS, Sanderson RJ, et al. (1995). "Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA.". Cell 82 (5): 701-8. PMID 7671300.
Mol CD, Arvai AS, Slupphaug G, et al. (1995). "Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis.". Cell 80 (6): 869-78. PMID 7697717.
Haug T, Skorpen F, Lund H, Krokan HE (1994). "Structure of the gene for human uracil-DNA glycosylase and analysis of the promoter function.". FEBS Lett. 353 (2): 180-4. PMID 7926048.
Slupphaug G, Markussen FH, Olsen LC, et al. (1993). "Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene.". Nucleic Acids Res. 21 (11): 2579-84. PMID 8332455.
Bouhamdan M, Benichou S, Rey F, et al. (1996). "Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme.". J. Virol. 70 (2): 697-704. PMID 8551605.
Kavli B, Slupphaug G, Mol CD, et al. (1996). "Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase.". EMBO J. 15 (13): 3442-7. PMID 8670846.
Haug T, Skorpen F, Kvaløy K, et al. (1997). "Human uracil-DNA glycosylase gene: sequence organization, methylation pattern, and mapping to chromosome 12q23-q24.1.". Genomics 36 (3): 408-16. doi:10.1006/geno.1996.0485. PMID 8884263.
Slupphaug G, Mol CD, Kavli B, et al. (1996). "A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA.". Nature 384 (6604): 87-92. doi:10.1038/384087a0. PMID 8900285.
Nilsen H, Otterlei M, Haug T, et al. (1997). "Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene.". Nucleic Acids Res. 25 (4): 750-5. PMID 9016624.
Nagelhus TA, Haug T, Singh KK, et al. (1997). "A sequence in the N-terminal region of human uracil-DNA glycosylase with homology to XPA interacts with the C-terminal part of the 34-kDa subunit of replication protein A.". J. Biol. Chem. 272 (10): 6561-6. PMID 9045683.
Selig L, Benichou S, Rogel ME, et al. (1997). "Uracil DNA glycosylase specifically interacts with Vpr of both human immunodeficiency virus type 1 and simian immunodeficiency virus of sooty mangabeys, but binding does not correlate with cell cycle arrest.". J. Virol. 71 (6): 4842-6. PMID 9151883.
Withers-Ward ES, Jowett JB, Stewart SA, et al. (1997). "Human immunodeficiency virus type 1 Vpr interacts with HHR23A, a cellular protein implicated in nucleotide excision DNA repair.". J. Virol. 71 (12): 9732-42. PMID 9371639.
Haug T, Skorpen F, Aas PA, et al. (1998). "Regulation of expression of nuclear and mitochondrial forms of human uracil-DNA glycosylase.". Nucleic Acids Res. 26 (6): 1449-57. PMID 9490791.