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G/T mismatch-specific thymine DNA glycosylase (EC 3.2.2.29) (Thymine-DNA glycosylase) (hTDG)

 TDG_HUMAN               Reviewed;         410 AA.
Q13569; Q8IUZ6; Q8IZM3;
15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
13-APR-2004, sequence version 2.
22-NOV-2017, entry version 161.
RecName: Full=G/T mismatch-specific thymine DNA glycosylase;
EC=3.2.2.29;
AltName: Full=Thymine-DNA glycosylase;
Short=hTDG;
Name=TDG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=8662714; DOI=10.1074/jbc.271.22.12767;
Neddermann P., Gallinari P., Lettieri T., Schmid D., Truong O.,
Hsuan J.J., Wiebauer K., Jiricny J.;
"Cloning and expression of human G/T mismatch-specific thymine-DNA
glycosylase.";
J. Biol. Chem. 271:12767-12774(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-199 AND MET-367.
NIEHS SNPs program;
Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
FUNCTION.
PubMed=8127859; DOI=10.1073/pnas.91.5.1642;
Neddermann P., Jiricny J.;
"Efficient removal of uracil from G.U mispairs by the mismatch-
specific thymine DNA glycosylase from HeLa cells.";
Proc. Natl. Acad. Sci. U.S.A. 91:1642-1646(1994).
[6]
FUNCTION.
PubMed=8407958;
Neddermann P., Jiricny J.;
"The purification of a mismatch-specific thymine-DNA glycosylase from
HeLa cells.";
J. Biol. Chem. 268:21218-21224(1993).
[7]
SUMOYLATION AT LYS-330.
PubMed=11889051; DOI=10.1093/emboj/21.6.1456;
Hardeland U., Steinacher R., Jiricny J., Schaer P.;
"Modification of the human thymine-DNA glycosylase by ubiquitin-like
proteins facilitates enzymatic turnover.";
EMBO J. 21:1456-1464(2002).
[8]
INTERACTION WITH AICDA AND GADD45A.
PubMed=21722948; DOI=10.1016/j.cell.2011.06.020;
Cortellino S., Xu J., Sannai M., Moore R., Caretti E., Cigliano A.,
Le Coz M., Devarajan K., Wessels A., Soprano D., Abramowitz L.K.,
Bartolomei M.S., Rambow F., Bassi M.R., Bruno T., Fanciulli M.,
Renner C., Klein-Szanto A.J., Matsumoto Y., Kobi D., Davidson I.,
Alberti C., Larue L., Bellacosa A.;
"Thymine DNA glycosylase is essential for active DNA demethylation by
linked deamination-base excision repair.";
Cell 146:67-79(2011).
[9]
FUNCTION.
PubMed=21862836; DOI=10.1074/jbc.C111.284620;
Maiti A., Drohat A.C.;
"Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-
carboxylcytosine: potential implications for active demethylation of
CpG sites.";
J. Biol. Chem. 286:35334-35338(2011).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-330, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[14]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-103; LYS-248 AND LYS-330,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[15]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1,
AND MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
PubMed=15959518; DOI=10.1038/nature03634;
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K.,
Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.;
"Crystal structure of thymine DNA glycosylase conjugated to SUMO-1.";
Nature 435:979-982(2005).
[16]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO2,
AND MUTAGENESIS OF GLU-310.
PubMed=16626738; DOI=10.1016/j.jmb.2006.03.036;
Baba D., Maita N., Jee J.-G., Uchimura Y., Saitoh H., Sugasawa K.,
Hanaoka F., Tochio H., Hiroaki H., Shirakawa M.;
"Crystal structure of SUMO-3-modified thymine-DNA glycosylase.";
J. Mol. Biol. 359:137-147(2006).
[17]
X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA,
AND SUBUNIT.
PubMed=18587051; DOI=10.1073/pnas.0711061105;
Maiti A., Morgan M.T., Pozharski E., Drohat A.C.;
"Crystal structure of human thymine DNA glycosylase bound to DNA
elucidates sequence-specific mismatch recognition.";
Proc. Natl. Acad. Sci. U.S.A. 105:8890-8895(2008).
[18]
X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA,
FUNCTION, SUBUNIT, AND MUTAGENESIS OF ASN-140.
PubMed=22327402; DOI=10.1038/nchembio.914;
Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H.,
He C.;
"Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-
modified DNA.";
Nat. Chem. Biol. 8:328-330(2012).
[19]
X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA,
AND FUNCTION.
PubMed=22962365; DOI=10.1093/nar/gks845;
Hashimoto H., Hong S., Bhagwat A.S., Zhang X., Cheng X.;
"Excision of 5-hydroxymethyluracil and 5-carboxylcytosine by the
thymine DNA glycosylase domain: its structural basis and implications
for active DNA demethylation.";
Nucleic Acids Res. 40:10203-10214(2012).
[20]
X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA,
FUNCTION, AND MUTAGENESIS OF ALA-145; HIS-151; ASN-191 AND THR-197.
PubMed=22573813; DOI=10.1073/pnas.1201010109;
Maiti A., Noon M.S., MacKerell A.D. Jr., Pozharski E., Drohat A.C.;
"Lesion processing by a repair enzyme is severely curtailed by
residues needed to prevent aberrant activity on undamaged DNA.";
Proc. Natl. Acad. Sci. U.S.A. 109:8091-8096(2012).
-!- FUNCTION: DNA glycosylase that plays a key role in active DNA
demethylation: specifically recognizes and binds 5-formylcytosine
(5fC) and 5-carboxylcytosine (5caC) in the context of CpG sites
and mediates their excision through base-excision repair (BER) to
install an unmethylated cytosine. Cannot remove 5-
hydroxymethylcytosine (5hmC). According to an alternative model,
involved in DNA demethylation by mediating DNA glycolase activity
toward 5-hydroxymethyluracil (5hmU) produced by deamination of
5hmC. Also involved in DNA repair by acting as a thymine-DNA
glycosylase that mediates correction of G/T mispairs to G/C pairs:
in the DNA of higher eukaryotes, hydrolytic deamination of 5-
methylcytosine to thymine leads to the formation of G/T
mismatches. Its role in the repair of canonical base damage is
however minor compared to its role in DNA demethylation. 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.
{ECO:0000269|PubMed:21862836, ECO:0000269|PubMed:22327402,
ECO:0000269|PubMed:22573813, ECO:0000269|PubMed:22962365,
ECO:0000269|PubMed:8127859, ECO:0000269|PubMed:8407958,
ECO:0000269|PubMed:8662714}.
-!- CATALYTIC ACTIVITY: Hydrolyzes mismatched double-stranded DNA and
polynucleotides, releasing free thymine.
-!- SUBUNIT: Homodimer. Interacts with AICDA and GADD45A.
{ECO:0000269|PubMed:18587051, ECO:0000269|PubMed:21722948,
ECO:0000269|PubMed:22327402, ECO:0000269|PubMed:22573813,
ECO:0000269|PubMed:22962365}.
-!- INTERACTION:
Q9GZX7:AICDA; NbExp=5; IntAct=EBI-348333, EBI-3834328;
P24522:GADD45A; NbExp=3; IntAct=EBI-348333, EBI-448167;
O88846:Rnf4 (xeno); NbExp=2; IntAct=EBI-348333, EBI-7258907;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8662714}.
-!- PTM: Sumoylation on Lys-330 by either SUMO1 or SUMO2 induces
dissociation of the product DNA. {ECO:0000269|PubMed:11889051}.
-!- SIMILARITY: Belongs to the uracil-DNA glycosylase (UDG)
superfamily. TDG/mug family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/tdg/";
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EMBL; U51166; AAC50540.1; -; mRNA.
EMBL; AF545435; AAN16399.1; -; Genomic_DNA.
EMBL; AC078819; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC037557; AAH37557.1; -; mRNA.
CCDS; CCDS9095.1; -.
RefSeq; NP_003202.3; NM_003211.4.
UniGene; Hs.584809; -.
PDB; 1WYW; X-ray; 2.10 A; A=112-339.
PDB; 2D07; X-ray; 2.10 A; A=112-339.
PDB; 2RBA; X-ray; 2.79 A; A/B=111-308.
PDB; 3UFJ; X-ray; 2.97 A; A/B=111-308.
PDB; 3UO7; X-ray; 3.00 A; A/B=111-308.
PDB; 3UOB; X-ray; 3.01 A; A/B=111-308.
PDB; 4FNC; X-ray; 2.49 A; A=111-308.
PDB; 4JGC; X-ray; 2.58 A; A=111-308.
PDB; 4XEG; X-ray; 1.72 A; A=111-308.
PDB; 4Z3A; X-ray; 1.72 A; A=111-308.
PDB; 4Z47; X-ray; 1.45 A; A=111-308.
PDB; 4Z7B; X-ray; 2.02 A; A=111-308.
PDB; 4Z7Z; X-ray; 1.83 A; A=111-308.
PDB; 5CYS; X-ray; 2.45 A; A=111-308.
PDB; 5FF8; X-ray; 1.70 A; A=82-308.
PDB; 5HF7; X-ray; 1.54 A; A=82-308.
PDB; 5JXY; X-ray; 1.71 A; A=111-308.
PDB; 5T2W; X-ray; 2.20 A; A=82-308.
PDBsum; 1WYW; -.
PDBsum; 2D07; -.
PDBsum; 2RBA; -.
PDBsum; 3UFJ; -.
PDBsum; 3UO7; -.
PDBsum; 3UOB; -.
PDBsum; 4FNC; -.
PDBsum; 4JGC; -.
PDBsum; 4XEG; -.
PDBsum; 4Z3A; -.
PDBsum; 4Z47; -.
PDBsum; 4Z7B; -.
PDBsum; 4Z7Z; -.
PDBsum; 5CYS; -.
PDBsum; 5FF8; -.
PDBsum; 5HF7; -.
PDBsum; 5JXY; -.
PDBsum; 5T2W; -.
DisProt; DP00719; -.
ProteinModelPortal; Q13569; -.
SMR; Q13569; -.
BioGrid; 112855; 38.
DIP; DIP-32709N; -.
ELM; Q13569; -.
IntAct; Q13569; 14.
MINT; MINT-1182514; -.
STRING; 9606.ENSP00000376611; -.
iPTMnet; Q13569; -.
PhosphoSitePlus; Q13569; -.
BioMuta; TDG; -.
DMDM; 46397791; -.
EPD; Q13569; -.
MaxQB; Q13569; -.
PaxDb; Q13569; -.
PeptideAtlas; Q13569; -.
PRIDE; Q13569; -.
Ensembl; ENST00000392872; ENSP00000376611; ENSG00000139372.
GeneID; 6996; -.
KEGG; hsa:6996; -.
UCSC; uc001tkg.4; human.
CTD; 6996; -.
DisGeNET; 6996; -.
EuPathDB; HostDB:ENSG00000139372.14; -.
GeneCards; TDG; -.
H-InvDB; HIX0026376; -.
HGNC; HGNC:11700; TDG.
HPA; HPA052263; -.
MIM; 601423; gene.
neXtProt; NX_Q13569; -.
OpenTargets; ENSG00000139372; -.
PharmGKB; PA36419; -.
eggNOG; KOG4120; Eukaryota.
eggNOG; COG3663; LUCA.
GeneTree; ENSGT00390000000987; -.
HOGENOM; HOG000220820; -.
HOVERGEN; HBG003685; -.
InParanoid; Q13569; -.
KO; K20813; -.
OMA; FPFQQMM; -.
OrthoDB; EOG091G0N58; -.
PhylomeDB; Q13569; -.
TreeFam; TF328764; -.
BRENDA; 3.2.2.29; 2681.
Reactome; R-HSA-110328; Recognition and association of DNA glycosylase with site containing an affected pyrimidine.
Reactome; R-HSA-110329; Cleavage of the damaged pyrimidine.
Reactome; R-HSA-110357; Displacement of DNA glycosylase by APEX1.
Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
Reactome; R-HSA-5221030; TET1,2,3 and TDG demethylate DNA.
ChiTaRS; TDG; human.
EvolutionaryTrace; Q13569; -.
GeneWiki; Thymine-DNA_glycosylase; -.
GenomeRNAi; 6996; -.
PRO; PR:Q13569; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000139372; -.
CleanEx; HS_TDG; -.
ExpressionAtlas; Q13569; baseline and differential.
Genevisible; Q13569; HS.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0016605; C:PML body; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IDA:CAFA.
GO; GO:0031404; F:chloride ion binding; IDA:CAFA.
GO; GO:0003684; F:damaged DNA binding; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; ISS:UniProtKB.
GO; GO:0019104; F:DNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0043739; F:G/U mismatch-specific uracil-DNA glycosylase activity; IMP:CAFA.
GO; GO:0000287; F:magnesium ion binding; IDA:CAFA.
GO; GO:0030983; F:mismatched DNA binding; IDA:UniProtKB.
GO; GO:0019904; F:protein domain specific binding; IEA:Ensembl.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0005080; F:protein kinase C binding; IEA:Ensembl.
GO; GO:0043621; F:protein self-association; IDA:CAFA.
GO; GO:0008263; F:pyrimidine-specific mismatch base pair DNA N-glycosylase activity; IDA:UniProtKB.
GO; GO:0001104; F:RNA polymerase II transcription cofactor activity; IEA:Ensembl.
GO; GO:0031402; F:sodium ion binding; IDA:CAFA.
GO; GO:0032183; F:SUMO binding; IPI:CAFA.
GO; GO:0008134; F:transcription factor binding; IEA:Ensembl.
GO; GO:0004844; F:uracil DNA N-glycosylase activity; IDA:CAFA.
GO; GO:0006284; P:base-excision repair; IDA:UniProtKB.
GO; GO:0006285; P:base-excision repair, AP site formation; IDA:CAFA.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0045008; P:depyrimidination; TAS:Reactome.
GO; GO:0080111; P:DNA demethylation; ISS:UniProtKB.
GO; GO:0009790; P:embryo development; ISS:UniProtKB.
GO; GO:0006298; P:mismatch repair; IDA:UniProtKB.
GO; GO:0035562; P:negative regulation of chromatin binding; IEA:Ensembl.
GO; GO:0032091; P:negative regulation of protein binding; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0035511; P:oxidative DNA demethylation; TAS:Reactome.
GO; GO:1902544; P:regulation of DNA N-glycosylase activity; IMP:CAFA.
GO; GO:0040029; P:regulation of gene expression, epigenetic; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd10028; UDG_F2_MUG; 1.
Gene3D; 3.40.470.10; -; 1.
InterPro; IPR015637; MUG/TDG.
InterPro; IPR003310; TDG.
InterPro; IPR005122; Uracil-DNA_glycosylase-like.
InterPro; IPR036895; Uracil-DNA_glycosylase-like_sf.
PANTHER; PTHR12159; PTHR12159; 1.
Pfam; PF03167; UDG; 1.
SUPFAM; SSF52141; SSF52141; 1.
TIGRFAMs; TIGR00584; mug; 1.
1: Evidence at protein level;
3D-structure; Activator; Chromatin regulator; Complete proteome;
Direct protein sequencing; DNA damage; DNA repair; Hydrolase;
Isopeptide bond; Nucleus; Polymorphism; Reference proteome;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 410 G/T mismatch-specific thymine DNA
glycosylase.
/FTId=PRO_0000185777.
CROSSLNK 103 103 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 248 248 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 330 330 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate.
CROSSLNK 330 330 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
VARIANT 199 199 G -> S (in dbSNP:rs4135113).
{ECO:0000269|Ref.2}.
/FTId=VAR_018892.
VARIANT 367 367 V -> L (in dbSNP:rs2888805).
/FTId=VAR_059450.
VARIANT 367 367 V -> M (in dbSNP:rs2888805).
{ECO:0000269|Ref.2}.
/FTId=VAR_018893.
VARIANT 381 381 G -> E (in dbSNP:rs3953597).
/FTId=VAR_050140.
MUTAGEN 140 140 N->A: Loss of DNA glycosylase activity
but still able to bind DNA.
{ECO:0000269|PubMed:22327402}.
MUTAGEN 145 145 A->G: Increased DNA glycosylase activity
on G/T mispairs.
{ECO:0000269|PubMed:22573813}.
MUTAGEN 151 151 H->A,Q: Increased DNA glycosylase
activity on G/T mispairs.
{ECO:0000269|PubMed:22573813}.
MUTAGEN 191 191 N->A: Reduced DNA glycosylase activity on
G/T and G/U mispairs.
{ECO:0000269|PubMed:22573813}.
MUTAGEN 197 197 T->A: Reduced DNA glycosylase activity on
G/T mispairs.
{ECO:0000269|PubMed:22573813}.
MUTAGEN 281 281 R->A: Restores the DNA-binding ability of
the sumoylated form.
{ECO:0000269|PubMed:15959518}.
MUTAGEN 310 310 E->Q: Restores the DNA-binding ability of
the sumoylated form.
{ECO:0000269|PubMed:15959518,
ECO:0000269|PubMed:16626738}.
MUTAGEN 315 315 F->A: Restores the DNA-binding ability of
the sumoylated form.
{ECO:0000269|PubMed:15959518}.
CONFLICT 91 91 S -> P (in Ref. 1; AAC50540).
{ECO:0000305}.
CONFLICT 268 268 V -> G (in Ref. 4; AAH37557).
{ECO:0000305}.
TURN 111 113 {ECO:0000244|PDB:5CYS}.
HELIX 116 119 {ECO:0000244|PDB:4Z47}.
STRAND 133 139 {ECO:0000244|PDB:4Z47}.
HELIX 143 148 {ECO:0000244|PDB:4Z47}.
STRAND 150 152 {ECO:0000244|PDB:4Z47}.
STRAND 154 157 {ECO:0000244|PDB:5HF7}.
HELIX 159 165 {ECO:0000244|PDB:4Z47}.
STRAND 168 171 {ECO:0000244|PDB:4Z47}.
HELIX 175 180 {ECO:0000244|PDB:4Z47}.
HELIX 181 185 {ECO:0000244|PDB:4Z47}.
STRAND 186 192 {ECO:0000244|PDB:4Z47}.
HELIX 200 202 {ECO:0000244|PDB:4Z47}.
HELIX 205 222 {ECO:0000244|PDB:4Z47}.
STRAND 225 231 {ECO:0000244|PDB:4Z47}.
HELIX 232 243 {ECO:0000244|PDB:4Z47}.
STRAND 252 254 {ECO:0000244|PDB:4Z47}.
STRAND 265 269 {ECO:0000244|PDB:4Z47}.
STRAND 272 274 {ECO:0000244|PDB:2RBA}.
STRAND 277 279 {ECO:0000244|PDB:2D07}.
HELIX 282 304 {ECO:0000244|PDB:4Z47}.
STRAND 308 314 {ECO:0000244|PDB:1WYW}.
HELIX 317 329 {ECO:0000244|PDB:1WYW}.
SEQUENCE 410 AA; 46053 MW; 33752B26EBC789AE CRC64;
MEAENAGSYS LQQAQAFYTF PFQQLMAEAP NMAVVNEQQM PEEVPAPAPA QEPVQEAPKG
RKRKPRTTEP KQPVEPKKPV ESKKSGKSAK SKEKQEKITD TFKVKRKVDR FNGVSEAELL
TKTLPDILTF NLDIVIIGIN PGLMAAYKGH HYPGPGNHFW KCLFMSGLSE VQLNHMDDHT
LPGKYGIGFT NMVERTTPGS KDLSSKEFRE GGRILVQKLQ KYQPRIAVFN GKCIYEIFSK
EVFGVKVKNL EFGLQPHKIP DTETLCYVMP SSSARCAQFP RAQDKVHYYI KLKDLRDQLK
GIERNMDVQE VQYTFDLQLA QEDAKKMAVK EEKYDPGYEA AYGGAYGENP CSSEPCGFSS
NGLIESVELR GESAFSGIPN GQWMTQSFTD QIPSFSNHCG TQEQEEESHA


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