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Q13569

- TDG_HUMAN

UniProt

Q13569 - TDG_HUMAN

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
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    • History
      Entry version 127 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    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 binding Source: IntAct
    6. protein homodimerization activity Source: UniProtKB
    7. pyrimidine-specific mismatch base pair DNA N-glycosylase activity Source: UniProtKB
    8. RNA polymerase II transcription cofactor activity Source: Ensembl
    9. 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

    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

    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

    ArrayExpressiQ13569.
    BgeeiQ13569.
    CleanExiHS_TDG.
    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. 26 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 – 1213
    Beta strandi133 – 1408
    Helixi143 – 1486
    Beta strandi150 – 1523
    Beta strandi154 – 1574
    Helixi159 – 1657
    Beta strandi168 – 1714
    Helixi175 – 1806
    Helixi181 – 1855
    Beta strandi186 – 1927
    Helixi200 – 2023
    Helixi205 – 22218
    Beta strandi225 – 2317
    Helixi232 – 24110
    Beta strandi252 – 2543
    Beta strandi265 – 2695
    Beta strandi272 – 2743
    Beta strandi277 – 2793
    Helixi282 – 2843
    Helixi286 – 29914
    Beta strandi308 – 3147
    Helixi317 – 32913

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MEAENAGSYS LQQAQAFYTF PFQQLMAEAP NMAVVNEQQM PEEVPAPAPA    50
    QEPVQEAPKG RKRKPRTTEP KQPVEPKKPV ESKKSGKSAK SKEKQEKITD 100
    TFKVKRKVDR FNGVSEAELL TKTLPDILTF NLDIVIIGIN PGLMAAYKGH 150
    HYPGPGNHFW KCLFMSGLSE VQLNHMDDHT LPGKYGIGFT NMVERTTPGS 200
    KDLSSKEFRE GGRILVQKLQ KYQPRIAVFN GKCIYEIFSK EVFGVKVKNL 250
    EFGLQPHKIP DTETLCYVMP SSSARCAQFP RAQDKVHYYI KLKDLRDQLK 300
    GIERNMDVQE VQYTFDLQLA QEDAKKMAVK EEKYDPGYEA AYGGAYGENP 350
    CSSEPCGFSS NGLIESVELR GESAFSGIPN GQWMTQSFTD QIPSFSNHCG 400
    TQEQEEESHA 410
    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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. 26 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.
    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

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

    Gene expression databases

    ArrayExpressi Q13569.
    Bgeei Q13569.
    CleanExi HS_TDG.
    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

    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: October 1, 2014
    This is version 127 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