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Protein FULL name: Methylated-DNA--protein-cysteine methyltransferase, 6-O-methylguanine-DNA methyltransferase, O-6-methylguanine-DNA-alkyltransferase.,
Protein SHORT name: MGMT
MGMT (Homo sapiens) is product of expression of
MGMT
gene.
MGMT is involved in:
DRR in Homo sapiens
Keywords:
FUNCTION: Involved in the cellular defense against the biological
effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated
guanine in DNA by stoichiometrically transferring the alkyl group
at the O-6 position to a cysteine residue in the enzyme. This is a
suicide reaction: the enzyme is irreversibly inactivated.
CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein
L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-
cysteine.
COFACTOR: Binds 1 zinc ion.
SUBCELLULAR LOCATION: Nucleus.
MISCELLANEOUS: This enzyme catalyzes only one turnover and
therefore is not strictly catalytic. According to one definition,
an enzyme is a biocytalyst that acts repeatedly and over many
reaction cycles.
SIMILARITY: Belongs to the MGMT family.
Links to other databases:
Protein sequence:
MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPA
AVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLW
KLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVC
SSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSG
SPPAGRN
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MGMT (Homo sapiens) is able to recognize following damages:
MGMT (Homo sapiens) belongs to following protein families:
References:
Title
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Authors
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Journal
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Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine.
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Tano K, Shiota S, Collier J, Foote RS, Mitra S
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Proc Natl Acad Sci U S A
Feb. 1, 1990
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cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA methyltransferase. cDNA expression in Escherichia coli and gene expression in human cells.
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Rydberg B, Spurr N, Karran P
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J Biol Chem
June 5, 1990
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Expression and cloning of complementary DNA for a human enzyme that repairs O6-methylguanine in DNA.
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Hayakawa H, Koike G, Sekiguchi M
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J Mol Biol
June 20, 1990
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Purification, structure, and biochemical properties of human O6-methylguanine-DNA methyltransferase.
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Koike G, Maki H, Takeya H, Hayakawa H, Sekiguchi M
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J Biol Chem
Sept. 5, 1990
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Structural and immunological comparison of indigenous human O6-methylguanine-DNA methyltransferase with that encoded by a cloned cDNA.
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von Wronski MA, Shiota S, Tano K, Mitra S, Bigner DD, Brent TP
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J Biol Chem
Feb. 15, 1991
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Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA.
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Liem LK, Lim A, Li BF
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Nucleic Acids Res
May 11, 1994
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Mutations in human O6-alkylguanine-DNA alkyltransferase imparting resistance to O6-benzylguanine.
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Crone TM, Goodtzova K, Edara S, Pegg AE
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Cancer Res
Dec. 1, 1994
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Alteration of arginine-128 to alanine abolishes the ability of human O6-alkylguanine-DNA alkyltransferase to repair methylated DNA but has no effect on its reaction with O6-benzylguanine.
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Kanugula S, Goodtzova K, Edara S, Pegg AE
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Biochemistry
May 1, 1995
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The role of tyrosine-158 in O6-alkylguanine-DNA alkyltransferase activity.
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Edara S, Goodtzova K, Pegg AE
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Carcinogenesis
July 1, 1995
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Crystal structure of the human O(6)-alkylguanine-DNA alkyltransferase.
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Wibley JE, Pegg AE, Moody PC
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Nucleic Acids Res
Feb. 15, 2000
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Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding.
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Daniels DS, Mol CD, Arvai AS, Kanugula S, Pegg AE, Tainer JA
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EMBO J
April 3, 2000
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The DNA sequence and comparative analysis of human chromosome 10.
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Deloukas P, Earthrowl ME, Grafham DV, Rubenfield M, French L, Steward CA, Sims SK, Jones MC, Searle S, Scott C, Howe K, Hunt SE, Andrews TD, Gilbert JG, Swarbreck D, Ashurst JL, Taylor A, Battles J, Bird CP, Ainscough R, Almeida JP, Ashwell RI, Ambrose KD, Babbage AK, Bagguley CL, Bailey J, Banerjee R, Bates K, Beasley H, Bray-Allen S, Brown AJ, Brown JY, Burford DC, Burrill W, Burton J, Cahill P, Camire D, Carter NP, Chapman JC, Clark SY, Clarke G, Clee CM, Clegg S, Corby N, Coulson A, Dhami P, Dutta I, Dunn M, Faulkner L, Frankish A, Frankland JA, Garner P, Garnett J, Gribble S, Griffiths C, Grocock R, Gustafson E, Hammond S, Harley JL, Hart E, Heath PD, Ho TP, Hopkins B, Horne J, Howden PJ, Huckle E, Hynds C, Johnson C, Johnson D, Kana A, Kay M, Kimberley AM, Kershaw JK, Kokkinaki M, Laird GK, Lawlor S, Lee HM, Leongamornlert DA, Laird G, Lloyd C, Lloyd DM, Loveland J, Lovell J, McLaren S, McLay KE, McMurray A, Mashreghi-Mohammadi M, Matthews L, Milne S, Nickerson T, Nguyen M, Overton-Larty E, Palmer SA, Pearce AV, Peck AI, Pelan S, Phillimore B, Porter K, Rice CM, Rogosin A, Ross MT, Sarafidou T, Sehra HK, Shownkeen R, Skuce CD, Smith M, Standring L, Sycamore N, Tester J, Thorpe A, Torcasso W, Tracey A, Tromans A, Tsolas J, Wall M, Walsh J, Wang H, Weinstock K, West AP, Willey DL, Whitehead SL, Wilming L, Wray PW, Young L, Chen Y, Lovering RC, Moschonas NK, Siebert R, Fechtel K, Bentley D, Durbin R, Hubbard T, Doucette-Stamm L, Beck S, Smith DR, Rogers J
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Nature
May 27, 2004
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Large-scale characterization of HeLa cell nuclear phosphoproteins.
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Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP
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Proc Natl Acad Sci U S A
Aug. 17, 2004
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
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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
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Genome Res
Oct. 1, 2004
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The structure of the human AGT protein bound to DNA and its implications for damage detection.
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Duguid EM, Rice PA, He C
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J Mol Biol
July 22, 2005
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Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.
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Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y
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Anal Sci
Feb. 1, 2008
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Last modification of this entry: Nov. 14, 2020.
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