SMUG1

Single-strand-selective monofunctional uracil-DNA glycosylase 1, also known as SMUG1, is a human gene.cite web | title = Entrez Gene: SMUG1 single-strand-selective monofunctional uracil-DNA glycosylase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23583| accessdate = ]

PBB_Summary
section_title =
summary_text = SMUG1 is a glycosylase that removes uracil from single- and double-stranded DNA in nuclear chromatin, thus contributing to base excision repair. [supplied by OMIM] cite web | title = Entrez Gene: SMUG1 single-strand-selective monofunctional uracil-DNA glycosylase 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=23583| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Maruyama K, Sugano S |title=Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. |journal=Gene |volume=138 |issue= 1-2 |pages= 171–4 |year= 1994 |pmid= 8125298 |doi=
*cite journal | author=Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, "et al." |title=Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library. |journal=Gene |volume=200 |issue= 1-2 |pages= 149–56 |year= 1997 |pmid= 9373149 |doi=
*cite journal | author=Haushalter KA, Todd Stukenberg MW, Kirschner MW, Verdine GL |title=Identification of a new uracil-DNA glycosylase family by expression cloning using synthetic inhibitors. |journal=Curr. Biol. |volume=9 |issue= 4 |pages= 174–85 |year= 1999 |pmid= 10074426 |doi=
*cite journal | author=Boorstein RJ, Cummings A, Marenstein DR, "et al." |title=Definitive identification of mammalian 5-hydroxymethyluracil DNA N-glycosylase activity as SMUG1. |journal=J. Biol. Chem. |volume=276 |issue= 45 |pages= 41991–7 |year= 2001 |pmid= 11526119 |doi= 10.1074/jbc.M106953200
*cite journal | author=Kavli B, Sundheim O, Akbari M, "et al." |title=hUNG2 is the major repair enzyme for removal of uracil from U:A matches, U:G mismatches, and U in single-stranded DNA, with hSMUG1 as a broad specificity backup. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39926–36 |year= 2002 |pmid= 12161446 |doi= 10.1074/jbc.M207107200
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Masaoka A, Matsubara M, Hasegawa R, "et al." |title=Mammalian 5-formyluracil-DNA glycosylase. 2. Role of SMUG1 uracil-DNA glycosylase in repair of 5-formyluracil and other oxidized and deaminated base lesions. |journal=Biochemistry |volume=42 |issue= 17 |pages= 5003–12 |year= 2003 |pmid= 12718543 |doi= 10.1021/bi0273213
*cite journal | author=Wibley JE, Waters TR, Haushalter K, "et al." |title=Structure and specificity of the vertebrate anti-mutator uracil-DNA glycosylase SMUG1. |journal=Mol. Cell |volume=11 |issue= 6 |pages= 1647–59 |year= 2003 |pmid= 12820976 |doi=
*cite journal | author=Ota T, Suzuki Y, Nishikawa T, "et al." |title=Complete sequencing and characterization of 21,243 full-length human cDNAs. |journal=Nat. Genet. |volume=36 |issue= 1 |pages= 40–5 |year= 2004 |pmid= 14702039 |doi= 10.1038/ng1285
*cite journal | author=Matsubara M, Tanaka T, Terato H, "et al." |title=Mutational analysis of the damage-recognition and catalytic mechanism of human SMUG1 DNA glycosylase. |journal=Nucleic Acids Res. |volume=32 |issue= 17 |pages= 5291–302 |year= 2004 |pmid= 15466595 |doi= 10.1093/nar/gkh859
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504
*cite journal | author=Schröfelbauer B, Yu Q, Zeitlin SG, Landau NR |title=Human immunodeficiency virus type 1 Vpr induces the degradation of the UNG and SMUG uracil-DNA glycosylases. |journal=J. Virol. |volume=79 |issue= 17 |pages= 10978–87 |year= 2005 |pmid= 16103149 |doi= 10.1128/JVI.79.17.10978-10987.2005
*cite journal | author=Rual JF, Venkatesan K, Hao T, "et al." |title=Towards a proteome-scale map of the human protein-protein interaction network. |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209
*cite journal | author=Di Noia JM, Rada C, Neuberger MS |title=SMUG1 is able to excise uracil from immunoglobulin genes: insight into mutation versus repair. |journal=EMBO J. |volume=25 |issue= 3 |pages= 585–95 |year= 2006 |pmid= 16407970 |doi= 10.1038/sj.emboj.7600939
*cite journal | author=Broderick P, Bagratuni T, Vijayakrishnan J, "et al." |title=Evaluation of NTHL1, NEIL1, NEIL2, MPG, TDG, UNG and SMUG1 genes in familial colorectal cancer predisposition. |journal=BMC Cancer |volume=6 |issue= |pages= 243 |year= 2006 |pmid= 17029639 |doi= 10.1186/1471-2407-6-243
*cite journal | author=Matsubara M, Tanaka T, Terato H, Ide H |title=Action mechanism of human SMUG1 uracil-DNA glycosylase. |journal=Nucleic Acids Symp Ser (Oxf) |volume= |issue= 49 |pages= 295–6 |year= 2007 |pmid= 17150750 |doi= 10.1093/nass/49.1.295
*cite journal | author=Pettersen HS, Sundheim O, Gilljam KM, "et al." |title=Uracil-DNA glycosylases SMUG1 and UNG2 coordinate the initial steps of base excision repair by distinct mechanisms. |journal=Nucleic Acids Res. |volume=35 |issue= 12 |pages= 3879–92 |year= 2007 |pmid= 17537817 |doi= 10.1093/nar/gkm372

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