DNA-3-methyladenine glycosylase

Details

Name
DNA-3-methyladenine glycosylase
Synonyms
  • 3-alkyladenine DNA glycosylase
  • 3-methyladenine DNA glycosidase
  • 3.2.2.21
  • AAG
  • ADPG
  • ANPG
  • MID1
  • N-methylpurine-DNA glycosylase
Gene Name
MPG
Organism
Humans
Amino acid sequence
>lcl|BSEQ0049624|DNA-3-methyladenine glycosylase
MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRER
CLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGR
IVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVL
LRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDE
AVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
Number of residues
298
Molecular Weight
32868.365
Theoretical pI
Not Available
GO Classification
Functions
alkylbase DNA N-glycosylase activity / damaged DNA binding / DNA N-glycosylase activity / DNA-3-methyladenine glycosylase activity / DNA-3-methylguanine glycosylase activity / DNA-7-methyladenine glycosylase activity / DNA-7-methylguanine glycosylase activity
Processes
base-excision repair / depurination / DNA dealkylation involved in DNA repair
Components
mitochondrial nucleoid / nucleoplasm
General Function
Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions.
Specific Function
Alkylbase dna n-glycosylase activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0049625|DNA-3-methyladenine glycosylase (MPG)
ATGGTCACCCCCGCTTTGCAGATGAAGAAACCAAAGCAGTTTTGCCGACGGATGGGGCAA
AAGAAGCAGCGACCAGCTAGAGCAGGGCAGCCACACAGCTCGTCCGACGCAGCCCAGGCA
CCTGCAGAGCAGCCACACAGCTCGTCCGATGCAGCCCAGGCACCTTGCCCCAGGGAGCGC
TGCTTGGGACCGCCCACCACTCCGGGCCCATACCGCAGCATCTATTTCTCAAGCCCAAAG
GGCCACCTTACCCGACTGGGGTTGGAGTTCTTCGACCAGCCGGCAGTCCCCCTGGCCCGG
GCATTTCTGGGACAGGTCCTAGTCCGGCGACTTCCTAATGGCACAGAACTCCGAGGCCGC
ATCGTGGAGACCGAGGCATACCTGGGGCCAGAGGATGAAGCCGCCCACTCAAGGGGTGGC
CGGCAGACCCCCCGCAACCGAGGCATGTTCATGAAGCCGGGGACCCTGTACGTGTACATC
ATTTACGGCATGTACTTCTGCATGAACATCTCCAGCCAGGGGGACGGGGCTTGCGTCTTG
CTGCGAGCACTGGAGCCCCTGGAAGGTCTGGAGACCATGCGTCAGCTTCGCAGCACCCTC
CGGAAAGGCACCGCCAGCCGTGTCCTCAAGGACCGCGAGCTCTGCAGTGGCCCCTCCAAG
CTGTGCCAGGCCCTGGCCATCAACAAGAGCTTTGACCAGAGGGACCTGGCACAGGATGAA
GCTGTATGGCTGGAGCGTGGTCCCCTGGAGCCCAGTGAGCCGGCTGTAGTGGCAGCAGCC
CGGGTGGGCGTCGGCCATGCAGGGGAGTGGGCCCGGAAACCCCTCCGCTTCTATGTCCGG
GGCAGCCCCTGGGTCAGTGTGGTCGACAGAGTGGCTGAGCAGGACACACAGGCCTGA
Chromosome Location
16
Locus
16p13.3
External Identifiers
ResourceLink
UniProtKB IDP29372
UniProtKB Entry Name3MG_HUMAN
HGNC IDHGNC:7211
General References
  1. Samson L, Derfler B, Boosalis M, Call K: Cloning and characterization of a 3-methyladenine DNA glycosylase cDNA from human cells whose gene maps to chromosome 16. Proc Natl Acad Sci U S A. 1991 Oct 15;88(20):9127-31. [PubMed:1924375]
  2. Vickers MA, Vyas P, Harris PC, Simmons DL, Higgs DR: Structure of the human 3-methyladenine DNA glycosylase gene and localization close to the 16p telomere. Proc Natl Acad Sci U S A. 1993 Apr 15;90(8):3437-41. [PubMed:8475094]
  3. Daniels RJ, Peden JF, Lloyd C, Horsley SW, Clark K, Tufarelli C, Kearney L, Buckle VJ, Doggett NA, Flint J, Higgs DR: Sequence, structure and pathology of the fully annotated terminal 2 Mb of the short arm of human chromosome 16. Hum Mol Genet. 2001 Feb 15;10(4):339-52. [PubMed:11157797]
  4. Martin J, Han C, Gordon LA, Terry A, Prabhakar S, She X, Xie G, Hellsten U, Chan YM, Altherr M, Couronne O, Aerts A, Bajorek E, Black S, Blumer H, Branscomb E, Brown NC, Bruno WJ, Buckingham JM, Callen DF, Campbell CS, Campbell ML, Campbell EW, Caoile C, Challacombe JF, Chasteen LA, Chertkov O, Chi HC, Christensen M, Clark LM, Cohn JD, Denys M, Detter JC, Dickson M, Dimitrijevic-Bussod M, Escobar J, Fawcett JJ, Flowers D, Fotopulos D, Glavina T, Gomez M, Gonzales E, Goodstein D, Goodwin LA, Grady DL, Grigoriev I, Groza M, Hammon N, Hawkins T, Haydu L, Hildebrand CE, Huang W, Israni S, Jett J, Jewett PB, Kadner K, Kimball H, Kobayashi A, Krawczyk MC, Leyba T, Longmire JL, Lopez F, Lou Y, Lowry S, Ludeman T, Manohar CF, Mark GA, McMurray KL, Meincke LJ, Morgan J, Moyzis RK, Mundt MO, Munk AC, Nandkeshwar RD, Pitluck S, Pollard M, Predki P, Parson-Quintana B, Ramirez L, Rash S, Retterer J, Ricke DO, Robinson DL, Rodriguez A, Salamov A, Saunders EH, Scott D, Shough T, Stallings RL, Stalvey M, Sutherland RD, Tapia R, Tesmer JG, Thayer N, Thompson LS, Tice H, Torney DC, Tran-Gyamfi M, Tsai M, Ulanovsky LE, Ustaszewska A, Vo N, White PS, Williams AL, Wills PL, Wu JR, Wu K, Yang J, Dejong P, Bruce D, Doggett NA, Deaven L, Schmutz J, Grimwood J, Richardson P, Rokhsar DS, Eichler EE, Gilna P, Lucas SM, Myers RM, Rubin EM, Pennacchio LA: The sequence and analysis of duplication-rich human chromosome 16. Nature. 2004 Dec 23;432(7020):988-94. [PubMed:15616553]
  5. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334]
  6. Chakravarti D, Ibeanu GC, Tano K, Mitra S: Cloning and expression in Escherichia coli of a human cDNA encoding the DNA repair protein N-methylpurine-DNA glycosylase. J Biol Chem. 1991 Aug 25;266(24):15710-5. [PubMed:1874728]
  7. O'Connor TR, Laval J: Human cDNA expressing a functional DNA glycosylase excising 3-methyladenine and 7-methylguanine. Biochem Biophys Res Commun. 1991 May 15;176(3):1170-7. [PubMed:1645538]
  8. Kielman MF, Smits R, Devi TS, Fodde R, Bernini LF: Homology of a 130-kb region enclosing the alpha-globin gene cluster, the alpha-locus controlling region, and two non-globin genes in human and mouse. Mamm Genome. 1993;4(6):314-23. [PubMed:8318735]
  9. Watanabe S, Ichimura T, Fujita N, Tsuruzoe S, Ohki I, Shirakawa M, Kawasuji M, Nakao M: Methylated DNA-binding domain 1 and methylpurine-DNA glycosylase link transcriptional repression and DNA repair in chromatin. Proc Natl Acad Sci U S A. 2003 Oct 28;100(22):12859-64. Epub 2003 Oct 10. [PubMed:14555760]
  10. 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. [PubMed:18669648]
  11. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [PubMed:21269460]
  12. van Loon B, Samson LD: Alkyladenine DNA glycosylase (AAG) localizes to mitochondria and interacts with mitochondrial single-stranded binding protein (mtSSB). DNA Repair (Amst). 2013 Mar 1;12(3):177-87. doi: 10.1016/j.dnarep.2012.11.009. Epub 2013 Jan 3. [PubMed:23290262]
  13. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [PubMed:23186163]
  14. Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T: Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision. Cell. 1998 Oct 16;95(2):249-58. [PubMed:9790531]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB00515CisplatinapprovedunknownDetails
DB01593Zincapproved, investigationalunknownDetails
DB14487Zinc acetateapproved, investigationalunknownDetails
DB14533Zinc chlorideapproved, investigationalunknownDetails