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Showing Protein DNA-3-methyladenine glycosylase (HMDBP02834)

IdentificationBiological propertiesGene propertiesProtein propertiesExternal linksReferencesXMLShow 5 metabolites
Identification
HMDB Protein ID HMDBP02834
Secondary Accession Numbers
  • 8341
Name DNA-3-methyladenine glycosylase
Synonyms
  1. 3-alkyladenine DNA glycosylase
  2. 3-methyladenine DNA glycosidase
  3. ADPG
  4. N-methylpurine-DNA glycosylase
Gene Name MPG
Protein Type Enzyme
Biological Properties
General Function Involved in catalytic activity
Specific Function Hydrolysis of the deoxyribose N-glycosidic bond to excise 3-methyladenine, and 7-methylguanine from the damaged DNA polymer formed by alkylation lesions
Pathways Not Available
Reactions Not Available
GO Classification
Function
dna n-glycosylase activity
binding
catalytic activity
hydrolase activity
hydrolase activity, acting on glycosyl bonds
hydrolase activity, hydrolyzing n-glycosyl compounds
alkylbase dna n-glycosylase activity
nucleic acid binding
dna binding
Process
base-excision repair
metabolic process
macromolecule metabolic process
cellular macromolecule metabolic process
dna metabolic process
dna repair
Cellular Location
  1. Nucleus (Potential)
Gene Properties
Chromosome Location Chromosome:1
Locus 16p13.3
SNPs MPG
Gene Sequence 
>897 bp
ATGGTCACCCCCGCTTTGCAGATGAAGAAACCAAAGCAGTTTTGCCGACGGATGGGGCAA
AAGAAGCAGCGACCAGCTAGAGCAGGGCAGCCACACAGCTCGTCCGACGCAGCCCAGGCA
CCTGCAGAGCAGCCACACAGCTCGTCCGATGCAGCCCAGGCACCTTGCCCCAGGGAGCGC
TGCTTGGGACCGCCCACCACTCCGGGCCCATACCGCAGCATCTATTTCTCAAGCCCAAAG
GGCCACCTTACCCGACTGGGGTTGGAGTTCTTCGACCAGCCGGCAGTCCCCCTGGCCCGG
GCATTTCTGGGACAGGTCCTAGTCCGGCGACTTCCTAATGGCACAGAACTCCGAGGCCGC
ATCGTGGAGACCGAGGCATACCTGGGGCCAGAGGATGAAGCCGCCCACTCAAGGGGTGGC
CGGCAGACCCCCCGCAACCGAGGCATGTTCATGAAGCCGGGGACCCTGTACGTGTACATC
ATTTACGGCATGTACTTCTGCATGAACATCTCCAGCCAGGGGGACGGGGCTTGCGTCTTG
CTGCGAGCACTGGAGCCCCTGGAAGGTCTGGAGACCATGCGTCAGCTTCGCAGCACCCTC
CGGAAAGGCACCGCCAGCCGTGTCCTCAAGGACCGCGAGCTCTGCAGTGGCCCCTCCAAG
CTGTGCCAGGCCCTGGCCATCAACAAGAGCTTTGACCAGAGGGACCTGGCACAGGATGAA
GCTGTATGGCTGGAGCGTGGTCCCCTGGAGCCCAGTGAGCCGGCTGTAGTGGCAGCAGCC
CGGGTGGGCGTCGGCCATGCAGGGGAGTGGGCCCGGAAACCCCTCCGCTTCTATGTCCGG
GGCAGCCCCTGGGTCAGTGTGGTCGACAGAGTGGCTGAGCAGGACACACAGGCCTGA
Protein Properties
Number of Residues 298
Molecular Weight 32868.4
Theoretical pI 10.0
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence 
>DNA-3-methyladenine glycosylase
MVTPALQMKKPKQFCRRMGQKKQRPARAGQPHSSSDAAQAPAEQPHSSSDAAQAPCPRER
CLGPPTTPGPYRSIYFSSPKGHLTRLGLEFFDQPAVPLARAFLGQVLVRRLPNGTELRGR
IVETEAYLGPEDEAAHSRGGRQTPRNRGMFMKPGTLYVYIIYGMYFCMNISSQGDGACVL
LRALEPLEGLETMRQLRSTLRKGTASRVLKDRELCSGPSKLCQALAINKSFDQRDLAQDE
AVWLERGPLEPSEPAVVAAARVGVGHAGEWARKPLRFYVRGSPWVSVVDRVAEQDTQA
GenBank ID Protein 62632769
UniProtKB/Swiss-Prot ID P29372
UniProtKB/Swiss-Prot Entry Name 3MG_HUMAN
PDB IDs
GenBank Gene ID NM_002434.2
GeneCard ID MPG
GenAtlas ID MPG
HGNC ID HGNC:7211
References
General References
  1. 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 ]
  2. 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 ]
  3. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP: Large-scale characterization of HeLa cell nuclear phosphoproteins. Proc Natl Acad Sci U S A. 2004 Aug 17;101(33):12130-5. Epub 2004 Aug 9. [PubMed:15302935 ]
  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. 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 ]
  6. 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 ]
  7. 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 ]
  8. 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 ]
  9. 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 ]
  10. 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 ]
  11. 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 ]
  12. 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 ]