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NameUracil-DNA glycosylase
Synonyms
  • 3.2.2.27
  • DGU
  • UDG
  • UNG1
  • UNG15
Gene NameUNG
OrganismHuman
Amino acid sequence
>lcl|BSEQ0007234|Uracil-DNA glycosylase
MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGT
PPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAE
ERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLE
NIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVS
WLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELL
QKSGKKPIDWKEL
Number of residues313
Molecular Weight34645.27
Theoretical pI9.85
GO Classification
Functions
  • damaged DNA binding
  • uracil DNA N-glycosylase activity
Processes
  • base-excision repair
  • viral process
  • base-excision repair, AP site formation
  • depyrimidination
  • positive regulation of isotype switching
  • somatic hypermutation of immunoglobulin genes
  • somatic recombination of immunoglobulin gene segments
  • DNA repair
Components
  • nucleoplasm
  • mitochondrion
  • nucleus
General FunctionUracil dna n-glycosylase activity
Specific FunctionExcises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine.
Pfam Domain Function
Transmembrane RegionsNot Available
GenBank Protein ID37599
UniProtKB IDP13051
UniProtKB Entry NameUNG_HUMAN
Cellular LocationMitochondrion
Gene sequence
>lcl|BSEQ0012634|Uracil-DNA glycosylase (UNG)
ATGGGCGTCTTCTGCCTTGGGCCGTGGGGGTTGGGCCGGAAGCTGCGGACGCCTGGGAAG
GGGCCGCTGCAGCTCTTGAGCCGCCTCTGCGGGGACCACTTGCAGGCCATCCCAGCCAAG
AAGGCCCCGGCTGGGCAGGAGGAGCCTGGGACGCCGCCCTCCTCGCCGCTGAGTGCCGAG
CAGTTGGACCGGATCCAGAGGAACAAGGCCGCGGCCCTGCTCAGACTCGCGGCCCGCAAC
GTGCCCGTGGGCTTTGGAGAGAGCTGGAAGAAGCACCTCAGCGGGGAGTTCGGGAAACCG
TATTTTATCAAGCTAATGGGATTTGTTGCAGAAGAAAGAAAGCATTACACTGTTTATCCA
CCCCCACACCAAGTCTTCACCTGGACCCAGATGTGTGACATAAAAGATGTGAAGGTTGTC
ATCCTGGGACAGGATCCATATCATGGACCTAATCAAGCTCACGGGCTCTGCTTTAGTGTT
CAAAGGCCTGTTCCGCCTCCGCCCAGTTTGGAGAACATTTATAAAGAGTTGTCTACAGAC
ATAGAGGATTTTGTTCATCCTGGCCATGGAGATTTATCTGGGTGGGCCAAGCAAGGTGTT
CTCCTTCTCAACGCTGTCCTCACGGTTCGTGCCCATCAAGCCAACTCTCATAAGGAGCGA
GGCTGGGAGCAGTTCACTGATGCAGTTGTGTCCTGGCTAAATCAGAACTCGAATGGCCTT
GTTTTCTTGCTCTGGGGCTCTTATGCTCAGAAGAAGGGCAGTGCCATTGATAGGAAGCGG
CACCATGTACTACAGACGGCTCATCCCTCCCCTTTGTCAGTGTATAGAGGGTTCTTTGGA
TGTAGACACTTTTCAAAGACCAATGAGCTGCTGCAGAAGTCTGGCAAGAAGCCCATTGAC
TGGAAGGAGCTGTGA
GenBank Gene IDX15653
GeneCard IDNot Available
GenAtlas IDNot Available
HGNC IDHGNC:12572
Chromosome Location12
Locus12q23-q24.1
References
  1. Olsen LC, Aasland R, Wittwer CU, Krokan HE, Helland DE: Molecular cloning of human uracil-DNA glycosylase, a highly conserved DNA repair enzyme. EMBO J. 1989 Oct;8(10):3121-5. 2555154
  2. Haug T, Skorpen F, Lund H, Krokan HE: Structure of the gene for human uracil-DNA glycosylase and analysis of the promoter function. FEBS Lett. 1994 Oct 17;353(2):180-4. 7926048
  3. Nilsen H, Otterlei M, Haug T, Solum K, Nagelhus TA, Skorpen F, Krokan HE: Nuclear and mitochondrial uracil-DNA glycosylases are generated by alternative splicing and transcription from different positions in the UNG gene. Nucleic Acids Res. 1997 Feb 15;25(4):750-5. 9016624
  4. 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 TO, 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: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. 14702039
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  6. Slupphaug G, Markussen FH, Olsen LC, Aasland R, Aarsaether N, Bakke O, Krokan HE, Helland DE: Nuclear and mitochondrial forms of human uracil-DNA glycosylase are encoded by the same gene. Nucleic Acids Res. 1993 Jun 11;21(11):2579-84. 8332455
  7. Kavli B, Slupphaug G, Mol CD, Arvai AS, Peterson SB, Tainer JA, Krokan HE: Excision of cytosine and thymine from DNA by mutants of human uracil-DNA glycosylase. EMBO J. 1996 Jul 1;15(13):3442-7. 8670846
  8. Bouhamdan M, Benichou S, Rey F, Navarro JM, Agostini I, Spire B, Camonis J, Slupphaug G, Vigne R, Benarous R, Sire J: Human immunodeficiency virus type 1 Vpr protein binds to the uracil DNA glycosylase DNA repair enzyme. J Virol. 1996 Feb;70(2):697-704. 8551605
  9. Otterlei M, Haug T, Nagelhus TA, Slupphaug G, Lindmo T, Krokan HE: Nuclear and mitochondrial splice forms of human uracil-DNA glycosylase contain a complex nuclear localisation signal and a strong classical mitochondrial localisation signal, respectively. Nucleic Acids Res. 1998 Oct 15;26(20):4611-7. 9753728
  10. Olsen JV, Blagoev B, Gnad F, Macek B, Kumar C, Mortensen P, Mann M: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell. 2006 Nov 3;127(3):635-48. 17081983
  11. Guo C, Zhang X, Fink SP, Platzer P, Wilson K, Willson JK, Wang Z, Markowitz SD: Ugene, a newly identified protein that is commonly overexpressed in cancer and binds uracil DNA glycosylase. Cancer Res. 2008 Aug 1;68(15):6118-26. doi: 10.1158/0008-5472.CAN-08-1259. 18676834
  12. Cantin GT, Yi W, Lu B, Park SK, Xu T, Lee JD, Yates JR 3rd: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. J Proteome Res. 2008 Mar;7(3):1346-51. doi: 10.1021/pr0705441. Epub 2008 Jan 26. 18220336
  13. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. 18669648
  14. Gauci S, Helbig AO, Slijper M, Krijgsveld J, Heck AJ, Mohammed S: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. Anal Chem. 2009 Jun 1;81(11):4493-501. doi: 10.1021/ac9004309. 19413330
  15. Mayya V, Lundgren DH, Hwang SI, Rezaul K, Wu L, Eng JK, Rodionov V, Han DK: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. Sci Signal. 2009 Aug 18;2(84):ra46. doi: 10.1126/scisignal.2000007. 19690332
  16. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. 19608861
  17. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. 20068231
  18. Rigbolt KT, Prokhorova TA, Akimov V, Henningsen J, Johansen PT, Kratchmarova I, Kassem M, Mann M, Olsen JV, Blagoev B: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. Sci Signal. 2011 Mar 15;4(164):rs3. doi: 10.1126/scisignal.2001570. 21406692
  19. Mol CD, Arvai AS, Slupphaug G, Kavli B, Alseth I, Krokan HE, Tainer JA: Crystal structure and mutational analysis of human uracil-DNA glycosylase: structural basis for specificity and catalysis. Cell. 1995 Mar 24;80(6):869-78. 7697717
  20. Mol CD, Arvai AS, Sanderson RJ, Slupphaug G, Kavli B, Krokan HE, Mosbaugh DW, Tainer JA: Crystal structure of human uracil-DNA glycosylase in complex with a protein inhibitor: protein mimicry of DNA. Cell. 1995 Sep 8;82(5):701-8. 7671300
  21. Slupphaug G, Mol CD, Kavli B, Arvai AS, Krokan HE, Tainer JA: A nucleotide-flipping mechanism from the structure of human uracil-DNA glycosylase bound to DNA. Nature. 1996 Nov 7;384(6604):87-92. 8900285
  22. Parikh SS, Mol CD, Slupphaug G, Bharati S, Krokan HE, Tainer JA: Base excision repair initiation revealed by crystal structures and binding kinetics of human uracil-DNA glycosylase with DNA. EMBO J. 1998 Sep 1;17(17):5214-26. 9724657
  23. Imai K, Slupphaug G, Lee WI, Revy P, Nonoyama S, Catalan N, Yel L, Forveille M, Kavli B, Krokan HE, Ochs HD, Fischer A, Durandy A: Human uracil-DNA glycosylase deficiency associated with profoundly impaired immunoglobulin class-switch recombination. Nat Immunol. 2003 Oct;4(10):1023-8. Epub 2003 Sep 7. 12958596
  24. Kavli B, Andersen S, Otterlei M, Liabakk NB, Imai K, Fischer A, Durandy A, Krokan HE, Slupphaug G: B cells from hyper-IgM patients carrying UNG mutations lack ability to remove uracil from ssDNA and have elevated genomic uracil. J Exp Med. 2005 Jun 20;201(12):2011-21. 15967827