Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q13569

- TDG_HUMAN

UniProt

Q13569 - TDG_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

G/T mismatch-specific thymine DNA glycosylase

Gene

TDG

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.7 Publications

Catalytic activityi

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

GO - Molecular functioni

  1. damaged DNA binding Source: ProtInc
  2. DNA N-glycosylase activity Source: UniProtKB
  3. double-stranded DNA binding Source: UniProtKB
  4. mismatched DNA binding Source: UniProtKB
  5. protein homodimerization activity Source: UniProtKB
  6. pyrimidine-specific mismatch base pair DNA N-glycosylase activity Source: UniProtKB
  7. RNA polymerase II transcription cofactor activity Source: Ensembl
  8. structure-specific DNA binding Source: UniProtKB

GO - Biological processi

  1. base-excision repair Source: UniProtKB
  2. base-excision repair, AP site formation Source: Reactome
  3. chromatin modification Source: UniProtKB-KW
  4. depyrimidination Source: Reactome
  5. DNA demethylation Source: UniProtKB
  6. DNA repair Source: Reactome
  7. embryo development Source: UniProtKB
  8. mismatch repair Source: UniProtKB
  9. negative regulation of chromatin binding Source: Ensembl
  10. negative regulation of protein binding Source: Ensembl
  11. negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  12. regulation of gene expression, epigenetic Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator, Glycosidase, Hydrolase

Keywords - Biological processi

DNA damage, DNA repair, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_1064. Displacement of DNA glycosylase by APE1.
REACT_200682. TET1,2,3 and TDG demethylate DNA.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Names & Taxonomyi

Protein namesi
Recommended name:
G/T mismatch-specific thymine DNA glycosylase (EC:3.2.2.29)
Alternative name(s):
Thymine-DNA glycosylase
Short name:
hTDG
Gene namesi
Name:TDG
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 12

Organism-specific databases

HGNCiHGNC:11700. TDG.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nucleoplasm Source: Reactome
  2. nucleus Source: UniProtKB
  3. plasma membrane Source: HPA
  4. PML body Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi140 – 1401N → A: Loss of DNA glycosylase activity but still able to bind DNA. 1 Publication
Mutagenesisi145 – 1451A → G: Increased DNA glycosylase activity on G/T mispairs. 1 Publication
Mutagenesisi151 – 1511H → A or Q: Increased DNA glycosylase activity on G/T mispairs. 1 Publication
Mutagenesisi191 – 1911N → A: Reduced DNA glycosylase activity on G/T and G/U mispairs. 1 Publication
Mutagenesisi197 – 1971T → A: Reduced DNA glycosylase activity on G/T mispairs. 1 Publication
Mutagenesisi281 – 2811R → A: Restores the DNA-binding ability of the sumoylated form. 1 Publication
Mutagenesisi310 – 3101E → Q: Restores the DNA-binding ability of the sumoylated form. 2 Publications
Mutagenesisi315 – 3151F → A: Restores the DNA-binding ability of the sumoylated form. 1 Publication

Organism-specific databases

PharmGKBiPA36419.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 410410G/T mismatch-specific thymine DNA glycosylasePRO_0000185777Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki330 – 330Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modificationi

Sumoylation on Lys-330 by either SUMO1 or SUMO2 induces dissociation of the product DNA.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

MaxQBiQ13569.
PaxDbiQ13569.
PRIDEiQ13569.

PTM databases

PhosphoSiteiQ13569.

Expressioni

Gene expression databases

BgeeiQ13569.
CleanExiHS_TDG.
ExpressionAtlasiQ13569. baseline and differential.
GenevestigatoriQ13569.

Organism-specific databases

HPAiHPA052263.

Interactioni

Subunit structurei

Homodimer. Interacts with AICDA and GADD45A.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AICDAQ9GZX75EBI-348333,EBI-3834328
GADD45AP245223EBI-348333,EBI-448167

Protein-protein interaction databases

BioGridi112855. 28 interactions.
DIPiDIP-32709N.
IntActiQ13569. 10 interactions.
MINTiMINT-1182514.
STRINGi9606.ENSP00000376611.

Structurei

Secondary structure

1
410
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi119 – 1213Combined sources
Beta strandi133 – 1408Combined sources
Helixi143 – 1486Combined sources
Beta strandi150 – 1523Combined sources
Beta strandi154 – 1574Combined sources
Helixi159 – 1657Combined sources
Beta strandi168 – 1714Combined sources
Helixi175 – 1806Combined sources
Helixi181 – 1855Combined sources
Beta strandi186 – 1927Combined sources
Helixi200 – 2023Combined sources
Helixi205 – 22218Combined sources
Beta strandi225 – 2317Combined sources
Helixi232 – 24110Combined sources
Beta strandi252 – 2543Combined sources
Beta strandi265 – 2695Combined sources
Beta strandi272 – 2743Combined sources
Beta strandi277 – 2793Combined sources
Helixi282 – 2843Combined sources
Helixi286 – 29914Combined sources
Beta strandi308 – 3147Combined sources
Helixi317 – 32913Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1WYWX-ray2.10A112-339[»]
2D07X-ray2.10A112-339[»]
2RBAX-ray2.79A/B111-308[»]
3UFJX-ray2.97A/B111-308[»]
3UO7X-ray3.00A/B111-308[»]
3UOBX-ray3.01A/B111-308[»]
4FNCX-ray2.49A111-308[»]
4JGCX-ray2.58A111-308[»]
DisProtiDP00719.
ProteinModelPortaliQ13569.
SMRiQ13569. Positions 117-332.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13569.

Family & Domainsi

Sequence similaritiesi

Belongs to the TDG/mug DNA glycosylase family.Curated

Phylogenomic databases

eggNOGiCOG3663.
GeneTreeiENSGT00390000000987.
HOGENOMiHOG000220820.
HOVERGENiHBG003685.
InParanoidiQ13569.
KOiK03649.
OMAiNGQWMTQ.
OrthoDBiEOG790G1Z.
PhylomeDBiQ13569.
TreeFamiTF328764.

Family and domain databases

Gene3Di3.40.470.10. 1 hit.
InterProiIPR015637. DNA_glycosylase_G/T-mismatch.
IPR003310. Thymine-DNA_glycosylase.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view]
PANTHERiPTHR12159. PTHR12159. 1 hit.
PfamiPF03167. UDG. 1 hit.
[Graphical view]
SMARTiSM00986. UDG. 1 hit.
[Graphical view]
SUPFAMiSSF52141. SSF52141. 1 hit.
TIGRFAMsiTIGR00584. mug. 1 hit.

Sequencei

Sequence statusi: Complete.

Q13569-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MEAENAGSYS LQQAQAFYTF PFQQLMAEAP NMAVVNEQQM PEEVPAPAPA
60 70 80 90 100
QEPVQEAPKG RKRKPRTTEP KQPVEPKKPV ESKKSGKSAK SKEKQEKITD
110 120 130 140 150
TFKVKRKVDR FNGVSEAELL TKTLPDILTF NLDIVIIGIN PGLMAAYKGH
160 170 180 190 200
HYPGPGNHFW KCLFMSGLSE VQLNHMDDHT LPGKYGIGFT NMVERTTPGS
210 220 230 240 250
KDLSSKEFRE GGRILVQKLQ KYQPRIAVFN GKCIYEIFSK EVFGVKVKNL
260 270 280 290 300
EFGLQPHKIP DTETLCYVMP SSSARCAQFP RAQDKVHYYI KLKDLRDQLK
310 320 330 340 350
GIERNMDVQE VQYTFDLQLA QEDAKKMAVK EEKYDPGYEA AYGGAYGENP
360 370 380 390 400
CSSEPCGFSS NGLIESVELR GESAFSGIPN GQWMTQSFTD QIPSFSNHCG
410
TQEQEEESHA
Length:410
Mass (Da):46,053
Last modified:April 13, 2004 - v2
Checksum:i33752B26EBC789AE
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti91 – 911S → P in AAC50540. (PubMed:8662714)Curated
Sequence conflicti268 – 2681V → G in AAH37557. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti199 – 1991G → S.1 Publication
Corresponds to variant rs4135113 [ dbSNP | Ensembl ].
VAR_018892
Natural varianti367 – 3671V → L.
Corresponds to variant rs2888805 [ dbSNP | Ensembl ].
VAR_059450
Natural varianti367 – 3671V → M.1 Publication
Corresponds to variant rs2888805 [ dbSNP | Ensembl ].
VAR_018893
Natural varianti381 – 3811G → E.
Corresponds to variant rs3953597 [ dbSNP | Ensembl ].
VAR_050140

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51166 mRNA. Translation: AAC50540.1.
AF545435 Genomic DNA. Translation: AAN16399.1.
AC078819 Genomic DNA. No translation available.
BC037557 mRNA. Translation: AAH37557.1.
CCDSiCCDS9095.1.
RefSeqiNP_003202.3. NM_003211.4.
UniGeneiHs.584809.

Genome annotation databases

EnsembliENST00000392872; ENSP00000376611; ENSG00000139372.
GeneIDi6996.
KEGGihsa:6996.
UCSCiuc001tkg.3. human.

Polymorphism databases

DMDMi46397791.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U51166 mRNA. Translation: AAC50540.1 .
AF545435 Genomic DNA. Translation: AAN16399.1 .
AC078819 Genomic DNA. No translation available.
BC037557 mRNA. Translation: AAH37557.1 .
CCDSi CCDS9095.1.
RefSeqi NP_003202.3. NM_003211.4.
UniGenei Hs.584809.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1WYW X-ray 2.10 A 112-339 [» ]
2D07 X-ray 2.10 A 112-339 [» ]
2RBA X-ray 2.79 A/B 111-308 [» ]
3UFJ X-ray 2.97 A/B 111-308 [» ]
3UO7 X-ray 3.00 A/B 111-308 [» ]
3UOB X-ray 3.01 A/B 111-308 [» ]
4FNC X-ray 2.49 A 111-308 [» ]
4JGC X-ray 2.58 A 111-308 [» ]
DisProti DP00719.
ProteinModelPortali Q13569.
SMRi Q13569. Positions 117-332.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 112855. 28 interactions.
DIPi DIP-32709N.
IntActi Q13569. 10 interactions.
MINTi MINT-1182514.
STRINGi 9606.ENSP00000376611.

PTM databases

PhosphoSitei Q13569.

Polymorphism databases

DMDMi 46397791.

Proteomic databases

MaxQBi Q13569.
PaxDbi Q13569.
PRIDEi Q13569.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000392872 ; ENSP00000376611 ; ENSG00000139372 .
GeneIDi 6996.
KEGGi hsa:6996.
UCSCi uc001tkg.3. human.

Organism-specific databases

CTDi 6996.
GeneCardsi GC12P104359.
H-InvDB HIX0026376.
HGNCi HGNC:11700. TDG.
HPAi HPA052263.
MIMi 601423. gene.
neXtProti NX_Q13569.
PharmGKBi PA36419.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG3663.
GeneTreei ENSGT00390000000987.
HOGENOMi HOG000220820.
HOVERGENi HBG003685.
InParanoidi Q13569.
KOi K03649.
OMAi NGQWMTQ.
OrthoDBi EOG790G1Z.
PhylomeDBi Q13569.
TreeFami TF328764.

Enzyme and pathway databases

Reactomei REACT_1064. Displacement of DNA glycosylase by APE1.
REACT_200682. TET1,2,3 and TDG demethylate DNA.
REACT_702. Recognition and association of DNA glycosylase with site containing an affected pyrimidine.

Miscellaneous databases

ChiTaRSi TDG. human.
EvolutionaryTracei Q13569.
GeneWikii Thymine-DNA_glycosylase.
GenomeRNAii 6996.
NextBioi 27327.
PROi Q13569.
SOURCEi Search...

Gene expression databases

Bgeei Q13569.
CleanExi HS_TDG.
ExpressionAtlasi Q13569. baseline and differential.
Genevestigatori Q13569.

Family and domain databases

Gene3Di 3.40.470.10. 1 hit.
InterProi IPR015637. DNA_glycosylase_G/T-mismatch.
IPR003310. Thymine-DNA_glycosylase.
IPR005122. Uracil-DNA_glycosylase-like.
[Graphical view ]
PANTHERi PTHR12159. PTHR12159. 1 hit.
Pfami PF03167. UDG. 1 hit.
[Graphical view ]
SMARTi SM00986. UDG. 1 hit.
[Graphical view ]
SUPFAMi SSF52141. SSF52141. 1 hit.
TIGRFAMsi TIGR00584. mug. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and expression of human G/T mismatch-specific thymine-DNA glycosylase."
    Neddermann P., Gallinari P., Lettieri T., Schmid D., Truong O., Hsuan J.J., Wiebauer K., Jiricny J.
    J. Biol. Chem. 271:12767-12774(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION.
  2. NIEHS SNPs program
    Submitted (SEP-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-199 AND MET-367.
  3. "The finished DNA sequence of human chromosome 12."
    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.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Colon.
  5. "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. 91:1642-1646(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "The purification of a mismatch-specific thymine-DNA glycosylase from HeLa cells."
    Neddermann P., Jiricny J.
    J. Biol. Chem. 268:21218-21224(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover."
    Hardeland U., Steinacher R., Jiricny J., Schaer P.
    EMBO J. 21:1456-1464(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION AT LYS-330.
  8. Cited for: INTERACTION WITH AICDA AND GADD45A.
  9. "Thymine DNA glycosylase can rapidly excise 5-formylcytosine and 5-carboxylcytosine: potential implications for active demethylation of CpG sites."
    Maiti A., Drohat A.C.
    J. Biol. Chem. 286:35334-35338(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO1, MUTAGENESIS OF ARG-281; GLU-310 AND PHE-315.
  12. Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 112-339 CONJUGATED TO SUMO2, MUTAGENESIS OF GLU-310.
  13. "Crystal structure of human thymine DNA glycosylase bound to DNA elucidates sequence-specific mismatch recognition."
    Maiti A., Morgan M.T., Pozharski E., Drohat A.C.
    Proc. Natl. Acad. Sci. U.S.A. 105:8890-8895(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, SUBUNIT.
  14. "Thymine DNA glycosylase specifically recognizes 5-carboxylcytosine-modified DNA."
    Zhang L., Lu X., Lu J., Liang H., Dai Q., Xu G.L., Luo C., Jiang H., He C.
    Nat. Chem. Biol. 8:328-330(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.01 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, SUBUNIT, MUTAGENESIS OF ASN-140.
  15. "Excision of 5-hydroxymethyluracil and 5-carboxylcytosine by the thymine DNA glycosylase domain: its structural basis and implications for active DNA demethylation."
    Hashimoto H., Hong S., Bhagwat A.S., Zhang X., Cheng X.
    Nucleic Acids Res. 40:10203-10214(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.49 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION.
  16. "Lesion processing by a repair enzyme is severely curtailed by residues needed to prevent aberrant activity on undamaged DNA."
    Maiti A., Noon M.S., MacKerell A.D. Jr., Pozharski E., Drohat A.C.
    Proc. Natl. Acad. Sci. U.S.A. 109:8091-8096(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.97 ANGSTROMS) OF 111-308 IN COMPLEX WITH DNA, FUNCTION, MUTAGENESIS OF ALA-145; HIS-151; ASN-191 AND THR-197.

Entry informationi

Entry nameiTDG_HUMAN
AccessioniPrimary (citable) accession number: Q13569
Secondary accession number(s): Q8IUZ6, Q8IZM3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: April 13, 2004
Last modified: November 26, 2014
This is version 129 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3