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MGMT

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.


NCBI GenPept GI number(s): 127069
4505177
51247522
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot P16455 P16455
PFAM: PF01035
PF02870
PF01035
PF02870
InterPro: IPR001497
IPR014048
IPR008332
IPR011991
IPR001497
IPR014048
IPR008332
IPR011991
CATH: - -
SCOP: - -
PDB: - -


Protein sequence:
MDKDCEMKRTTLDSPLGKLELSGCEQGLHEIKLLGKGTSAADAVEVPAPA
AVLGGPEPLMQCTAWLNAYFHQPEAIEEFPVPALHHPVFQQESFTRQVLW
KLLKVVKFGEVISYQQLAALAGNPKAARAVGGAMRGNPVPILIPCHRVVC
SSGAVGNYSGGLAVKEWLLAHEGHRLGKPGLGGSSGLAGAWLKGAGATSG
SPPAGRN

MGMT (Homo sapiens) is able to recognize following damages:
MGMT (Homo sapiens) belongs to following protein families:
References:

Title Authors Journal
Isolation and structural characterization of a cDNA clone encoding the human DNA repair protein for O6-alkylguanine. Tano K, Shiota S, Collier J, Foote RS, Mitra S Proc Natl Acad Sci U S A Feb. 1, 1990
cDNA cloning and chromosomal assignment of the human O6-methylguanine-DNA methyltransferase. cDNA expression in Escherichia coli and gene expression in human cells. Rydberg B, Spurr N, Karran P J Biol Chem June 5, 1990
Expression and cloning of complementary DNA for a human enzyme that repairs O6-methylguanine in DNA. Hayakawa H, Koike G, Sekiguchi M J Mol Biol June 20, 1990
Purification, structure, and biochemical properties of human O6-methylguanine-DNA methyltransferase. Koike G, Maki H, Takeya H, Hayakawa H, Sekiguchi M J Biol Chem Sept. 5, 1990
Structural and immunological comparison of indigenous human O6-methylguanine-DNA methyltransferase with that encoded by a cloned cDNA. von Wronski MA, Shiota S, Tano K, Mitra S, Bigner DD, Brent TP J Biol Chem Feb. 15, 1991
Specificities of human, rat and E. coli O6-methylguanine-DNA methyltransferases towards the repair of O6-methyl and O6-ethylguanine in DNA. Liem LK, Lim A, Li BF Nucleic Acids Res May 11, 1994
Mutations in human O6-alkylguanine-DNA alkyltransferase imparting resistance to O6-benzylguanine. Crone TM, Goodtzova K, Edara S, Pegg AE Cancer Res Dec. 1, 1994
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. Kanugula S, Goodtzova K, Edara S, Pegg AE Biochemistry May 1, 1995
The role of tyrosine-158 in O6-alkylguanine-DNA alkyltransferase activity. Edara S, Goodtzova K, Pegg AE Carcinogenesis July 1, 1995
Crystal structure of the human O(6)-alkylguanine-DNA alkyltransferase. Wibley JE, Pegg AE, Moody PC Nucleic Acids Res Feb. 15, 2000
Active and alkylated human AGT structures: a novel zinc site, inhibitor and extrahelical base binding. Daniels DS, Mol CD, Arvai AS, Kanugula S, Pegg AE, Tainer JA EMBO J April 3, 2000
The DNA sequence and comparative analysis of human chromosome 10. 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 Nature May 27, 2004
Large-scale characterization of HeLa cell nuclear phosphoproteins. Beausoleil SA, Jedrychowski M, Schwartz D, Elias JE, Villen J, Li J, Cohn MA, Cantley LC, Gygi SP Proc Natl Acad Sci U S A Aug. 17, 2004
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). 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 Genome Res Oct. 1, 2004
The structure of the human AGT protein bound to DNA and its implications for damage detection. Duguid EM, Rice PA, He C J Mol Biol July 22, 2005
Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column. Imami K, Sugiyama N, Kyono Y, Tomita M, Ishihama Y Anal Sci Feb. 1, 2008


Last modification of this entry: Nov. 11, 2010.

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