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Protein FULL name:

G/T mismatch-specific thymine DNA glycosylase, Thymine-DNA glycosylase

TDG (Homo sapiens) is product of expression of TDG gene.

TDG is involved in:

BER in Homo sapiens


FUNCTION: In the DNA of higher eukaryotes, hydrolytic deamination of 5-methylcytosine to thymine leads to the formation of G/T mismatches. This enzyme corrects G/T mispairs to G/C pairs. It is capable of hydrolyzing the carbon-nitrogen bond between the sugar- phosphate backbone of the DNA and a mispaired thymine. In addition to the G/T, it can remove thymine also from C/T and T/T mispairs in the order G/T >> C/T > T/T. It has no detectable activity on apyrimidinic sites and does not catalyze the removal of thymine from A/T pairs or from single-stranded DNA. It can also remove uracil and 5-bromouracil from mispairs with guanine.

CATALYTIC ACTIVITY: Hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free thymine.

INTERACTION: Q13838:BAT1; NbExp=1; IntAct=EBI-348333, EBI-348622;


PTM: Sumoylation on Lys-330 by either SUMO1 or SUMO2 induces dissociation of the product DNA.

SIMILARITY: Belongs to the TDG/mug DNA glycosylase family.


NCBI GenPept GI number(s): 46397791
Species: Homo sapiens

Links to other databases:

Database ID Link
Uniprot Q13569 Q13569
PFAM: PF03167
InterPro: IPR015637
CATH: - -
SCOP: - -
PDB: - -

Protein sequence:

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

Title Authors Journal
The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells. Neddermann P, Jiricny J J Biol Chem Oct. 5, 1993
Efficient removal of uracil from G.U mispairs by the mismatch-specific thymine DNA glycosylase from HeLa cells. Neddermann P, Jiricny J Proc Natl Acad Sci U S A March 1, 1994
Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase. Neddermann P, Gallinari P, Lettieri T, Schmid D, Truong O, Hsuan JJ, Wiebauer K, Jiricny J J Biol Chem May 31, 1996
Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. Hardeland U, Steinacher R, Jiricny J, Schar P EMBO J March 15, 2002
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
Crystal structure of thymine DNA glycosylase conjugated to SUMO-1. Baba D, Maita N, Jee JG, Uchimura Y, Saitoh H, Sugasawa K, Hanaoka F, Tochio H, Hiroaki H, Shirakawa M Nature June 16, 2005
Crystal structure of SUMO-3-modified thymine-DNA glycosylase. Baba D, Maita N, Jee JG, Uchimura Y, Saitoh H, Sugasawa K, Hanaoka F, Tochio H, Hiroaki H, Shirakawa M J Mol Biol May 26, 2006

Last modification of this entry: Oct. 15, 2010.

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