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O95551

- TYDP2_HUMAN

UniProt

O95551 - TYDP2_HUMAN

Protein

Tyrosyl-DNA phosphodiesterase 2

Gene

TDP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 119 (01 Oct 2014)
      Sequence version 1 (01 May 1999)
      Previous versions | rss
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    Functioni

    DNA repair enzyme that can remove a variety of covalent adducts from DNA through hydrolysis of a 5'-phosphodiester bond, giving rise to DNA with a free 5' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase 2 (TOP2) active site tyrosine residue. Hydrolyzes 5'-phosphoglycolates on protruding 5' ends on DNA double-strand breaks (DSBs) due to DNA damage by radiation and free radicals. The 5'-tyrosyl DNA phosphodiesterase activity can enable the repair of TOP2-induced DSBs without the need for nuclease activity, creating a 'clean' DSB with 5'-phosphate termini that are ready for ligation. Has preference for single-stranded DNA or duplex DNA with a 4 base pair overhang as substrate. Has also 3'-tyrosyl DNA phosphodiesterase activity, but less efficiently and much slower than TDP1. Constitutes the major if not only 5'-tyrosyl-DNA phosphodiesterase in cells. Also acts as a 5'-tyrosyl-RNA phosphodiesterase following picornavirus infection: its activity is hijacked by picornavirus and acts by specifically cleaving the protein-RNA covalent linkage generated during the viral genomic RNA replication steps of a picornavirus infection, without impairing the integrity of viral RNA. Also acts as an adapter by participating in the specific activation of MAP3K7/TAK1 in response to TGF-beta: associates with components of the TGF-beta receptor-TRAF6-TAK1 signaling module and promotes their ubiquitination dependent complex formation. Involved in non-canonical TGF-beta induced signaling routes. May also act as a negative regulator of ETS1 and may inhibit NF-kappa-B activation. Acts as a regulator of ribosome biogenesis following stress.7 Publications

    Cofactori

    Magnesium. Can use other divalent cations as cofactor in vitro, such as manganese.3 Publications

    Kineticsi

    kcat is 3 sec(-1) with single-stranded 5'-tyrosyl DNA as substrate.

    1. KM=8 µM for single-stranded 5'-tyrosyl DNA1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi120 – 1201MagnesiumCurated
    Metal bindingi152 – 1521MagnesiumBy similarity
    Metal bindingi262 – 2621MagnesiumCurated
    Metal bindingi264 – 2641MagnesiumBy similarity
    Metal bindingi350 – 3501MagnesiumBy similarity
    Active sitei351 – 3511Proton acceptorCurated
    Metal bindingi351 – 3511MagnesiumCurated

    GO - Molecular functioni

    1. 5'-tyrosyl-DNA phosphodiesterase activity Source: UniProtKB
    2. magnesium ion binding Source: UniProtKB
    3. manganese ion binding Source: UniProtKB
    4. nuclease activity Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. single-stranded DNA binding Source: UniProtKB
    7. transcription corepressor activity Source: ProtInc
    8. tyrosyl-RNA phosphodiesterase activity Source: UniProtKB

    GO - Biological processi

    1. cell surface receptor signaling pathway Source: ProtInc
    2. double-strand break repair Source: UniProtKB
    3. regulation of RNA biosynthetic process Source: GOC

    Keywords - Molecular functioni

    Hydrolase, Nuclease

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Magnesium, Metal-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosyl-DNA phosphodiesterase 2 (EC:3.1.4.-)
    Short name:
    Tyr-DNA phosphodiesterase 2
    Short name:
    hTDP2
    Alternative name(s):
    5'-tyrosyl-DNA phosphodiesterase
    Short name:
    5'-Tyr-DNA phosphodiesterase
    ETS1-associated protein 2
    ETS1-associated protein II
    Short name:
    EAPII
    TRAF and TNF receptor-associated protein
    Tyrosyl-RNA phosphodiesterase
    VPg unlinkase
    Gene namesi
    Name:TDP2
    Synonyms:EAP2, TTRAP
    ORF Names:AD-022
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 6

    Organism-specific databases

    HGNCiHGNC:17768. TDP2.

    Subcellular locationi

    Nucleus. NucleusPML body. Nucleusnucleolus. Cytoplasm
    Note: Localizes to nucleolar cavities following stress; localization to nucleolus is dependent on PML protein. In case of infection by picornavirus, relocalizes to cytoplasmic sites distinct from those containing viral proteins associated with RNA replication or encapsidation.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. intercellular bridge Source: HPA
    3. nucleolus Source: UniProtKB-SubCell
    4. nucleus Source: UniProtKB
    5. PML body Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi88 – 881T → A: Abolishes function, but retains ability to interact with SMAD3; when associated with A-92. 1 Publication
    Mutagenesisi92 – 921T → A: Abolishes function, but retains ability to interact with SMAD3; when associated with A-88. 1 Publication
    Mutagenesisi120 – 1201N → A: Strongly reduced phosphodiesterase activity. 1 Publication
    Mutagenesisi152 – 1521E → A: Loss of phosphodiesterase activity. 2 Publications
    Mutagenesisi262 – 2621D → A: Loss of phosphodiesterase activity. 2 Publications
    Mutagenesisi351 – 3511H → A: Loss of phosphodiesterase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA165618310.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 362362Tyrosyl-DNA phosphodiesterase 2PRO_0000065678Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine3 Publications
    Modified residuei88 – 881Phosphothreonine; by ACVR1B1 Publication
    Modified residuei92 – 921Phosphothreonine; by ACVR1B1 Publication

    Post-translational modificationi

    Ubiquitinated by TRAF6.1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO95551.
    PaxDbiO95551.
    PRIDEiO95551.

    PTM databases

    PhosphoSiteiO95551.

    Expressioni

    Tissue specificityi

    Widely expressed.1 Publication

    Gene expression databases

    ArrayExpressiO95551.
    BgeeiO95551.
    CleanExiHS_TTRAP.
    GenevestigatoriO95551.

    Organism-specific databases

    HPAiHPA054272.

    Interactioni

    Subunit structurei

    Interacts with TRAF2, TRAF3, TRAF5, TRAF6, TNFRSF8/CD30, TNFRSF5/CD40, TNFRSF1B/TNF-R75, ETS1, ETS2, FLI1, SMAD3 and ACVR1B/ALK4.3 Publications

    Protein-protein interaction databases

    BioGridi119615. 30 interactions.
    IntActiO95551. 17 interactions.
    MINTiMINT-5005899.

    Structurei

    3D structure databases

    ProteinModelPortaliO95551.
    SMRiO95551. Positions 31-362.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the CCR4/nocturin family.Curated

    Phylogenomic databases

    eggNOGiNOG277021.
    HOVERGENiHBG079625.
    InParanoidiO95551.
    OMAiRLLCVEF.
    OrthoDBiEOG7XPZ5W.
    PhylomeDBiO95551.
    TreeFamiTF314813.

    Family and domain databases

    Gene3Di3.60.10.10. 1 hit.
    InterProiIPR005135. Endo/exonuclease/phosphatase.
    IPR009060. UBA-like.
    [Graphical view]
    PfamiPF03372. Exo_endo_phos. 1 hit.
    [Graphical view]
    SUPFAMiSSF46934. SSF46934. 1 hit.
    SSF56219. SSF56219. 1 hit.

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95551-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MELGSCLEGG REAAEEEGEP EVKKRRLLCV EFASVASCDA AVAQCFLAEN    50
    DWEMERALNS YFEPPVEESA LERRPETISE PKTYVDLTNE ETTDSTTSKI 100
    SPSEDTQQEN GSMFSLITWN IDGLDLNNLS ERARGVCSYL ALYSPDVIFL 150
    QEVIPPYYSY LKKRSSNYEI ITGHEEGYFT AIMLKKSRVK LKSQEIIPFP 200
    STKMMRNLLC VHVNVSGNEL CLMTSHLEST RGHAAERMNQ LKMVLKKMQE 250
    APESATVIFA GDTNLRDREV TRCGGLPNNI VDVWEFLGKP KHCQYTWDTQ 300
    MNSNLGITAA CKLRFDRIFF RAAAEEGHII PRSLDLLGLE KLDCGRFPSD 350
    HWGLLCNLDI IL 362
    Length:362
    Mass (Da):40,930
    Last modified:May 1, 1999 - v1
    Checksum:i37892E125DB64410
    GO
    Isoform 2 (identifier: O95551-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MRERHDTGACAEPRVGLLFRLKGRCRGGRKM

    Note: No experimental confirmation available.

    Show »
    Length:392
    Mass (Da):44,339
    Checksum:i6B822134BDD395F3
    GO
    Isoform 3 (identifier: O95551-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         60-137: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:284
    Mass (Da):32,176
    Checksum:i3FBF514CDDECB196
    GO

    Sequence cautioni

    The sequence BAG59230.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence CAD92510.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311E → R in AAF64144. (PubMed:10931946)Curated
    Sequence conflicti61 – 611Y → C in BAA92119. (PubMed:14702039)Curated
    Sequence conflicti72 – 721E → G in BAG60857. (PubMed:14702039)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti166 – 1661S → G.
    Corresponds to variant rs35977478 [ dbSNP | Ensembl ].
    VAR_051464
    Natural varianti249 – 2491Q → E.1 Publication
    Corresponds to variant rs2294689 [ dbSNP | Ensembl ].
    VAR_022634
    Natural varianti268 – 2681R → Q.1 Publication
    Corresponds to variant rs17249952 [ dbSNP | Ensembl ].
    VAR_022635

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 11M → MRERHDTGACAEPRVGLLFR LKGRCRGGRKM in isoform 2. 1 PublicationVSP_038523
    Alternative sequencei60 – 13778Missing in isoform 3. 1 PublicationVSP_038524Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ269473 mRNA. Translation: CAB92966.1.
    AF201687 mRNA. Translation: AAG35600.1.
    AF223469 mRNA. Translation: AAF64144.1.
    AK002168 mRNA. Translation: BAA92119.1.
    AK296623 mRNA. Translation: BAG59230.1. Different initiation.
    AK298699 mRNA. Translation: BAG60857.1.
    AY613922 Genomic DNA. Translation: AAT09764.1.
    AL031775 Genomic DNA. Translation: CAA21141.1.
    AL031775 Genomic DNA. Translation: CAD92510.1. Sequence problems.
    BC017553 mRNA. Translation: AAH17553.1.
    BC110375 mRNA. Translation: AAI10376.1.
    CCDSiCCDS4557.1. [O95551-1]
    RefSeqiNP_057698.2. NM_016614.2. [O95551-1]
    UniGeneiHs.403010.

    Genome annotation databases

    EnsembliENST00000378198; ENSP00000367440; ENSG00000111802. [O95551-1]
    GeneIDi51567.
    KEGGihsa:51567.
    UCSCiuc003nej.3. human. [O95551-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SeattleSNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ269473 mRNA. Translation: CAB92966.1 .
    AF201687 mRNA. Translation: AAG35600.1 .
    AF223469 mRNA. Translation: AAF64144.1 .
    AK002168 mRNA. Translation: BAA92119.1 .
    AK296623 mRNA. Translation: BAG59230.1 . Different initiation.
    AK298699 mRNA. Translation: BAG60857.1 .
    AY613922 Genomic DNA. Translation: AAT09764.1 .
    AL031775 Genomic DNA. Translation: CAA21141.1 .
    AL031775 Genomic DNA. Translation: CAD92510.1 . Sequence problems.
    BC017553 mRNA. Translation: AAH17553.1 .
    BC110375 mRNA. Translation: AAI10376.1 .
    CCDSi CCDS4557.1. [O95551-1 ]
    RefSeqi NP_057698.2. NM_016614.2. [O95551-1 ]
    UniGenei Hs.403010.

    3D structure databases

    ProteinModelPortali O95551.
    SMRi O95551. Positions 31-362.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119615. 30 interactions.
    IntActi O95551. 17 interactions.
    MINTi MINT-5005899.

    Chemistry

    ChEMBLi CHEMBL2169736.

    PTM databases

    PhosphoSitei O95551.

    Proteomic databases

    MaxQBi O95551.
    PaxDbi O95551.
    PRIDEi O95551.

    Protocols and materials databases

    DNASUi 51567.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000378198 ; ENSP00000367440 ; ENSG00000111802 . [O95551-1 ]
    GeneIDi 51567.
    KEGGi hsa:51567.
    UCSCi uc003nej.3. human. [O95551-1 ]

    Organism-specific databases

    CTDi 51567.
    GeneCardsi GC06M024651.
    HGNCi HGNC:17768. TDP2.
    HPAi HPA054272.
    MIMi 605764. gene.
    neXtProti NX_O95551.
    PharmGKBi PA165618310.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG277021.
    HOVERGENi HBG079625.
    InParanoidi O95551.
    OMAi RLLCVEF.
    OrthoDBi EOG7XPZ5W.
    PhylomeDBi O95551.
    TreeFami TF314813.

    Miscellaneous databases

    GeneWikii TTRAP.
    GenomeRNAii 51567.
    NextBioi 55388.
    PROi O95551.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95551.
    Bgeei O95551.
    CleanExi HS_TTRAP.
    Genevestigatori O95551.

    Family and domain databases

    Gene3Di 3.60.10.10. 1 hit.
    InterProi IPR005135. Endo/exonuclease/phosphatase.
    IPR009060. UBA-like.
    [Graphical view ]
    Pfami PF03372. Exo_endo_phos. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46934. SSF46934. 1 hit.
    SSF56219. SSF56219. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "TTRAP, a novel protein that associates with CD40, tumor necrosis factor (TNF) receptor-75 and TNF receptor-associated factors (TRAFs), and that inhibits nuclear factor-kappa B activation."
      Pype S., Declercq W., Ibrahimi A., Michiels C., Van Rietschoten J.G.I., Dewulf N., de Boer M., Vandenabeele P., Huylebroeck D., Remacle J.E.
      J. Biol. Chem. 275:18586-18593(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH TNFRSF5; TNFRSF8; TNFRSF1B; TRAF2; TRAF3; TRAF5 AND TRAF6, TISSUE SPECIFICITY.
      Tissue: Umbilical vein.
    2. "EAPII interacts with ETS1 and modulates its transcriptional function."
      Pei H., Yordy J.S., Leng Q., Zhao Q., Watson D.K., Li R.
      Oncogene 22:2699-2709(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH ETS1; ETS2 AND FLI1, SUBCELLULAR LOCATION.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Adrenal gland.
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 23-362 (ISOFORM 3).
      Tissue: Colon and Placenta.
    5. SeattleSNPs variation discovery resource
      Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-249 AND GLN-268.
    6. "The DNA sequence and analysis of human chromosome 6."
      Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
      , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
      Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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] (ISOFORM 1).
      Tissue: Duodenum and Skin.
    8. "Ttrap is an essential modulator of Smad3-dependent Nodal signaling during zebrafish gastrulation and left-right axis determination."
      Esguerra C.V., Nelles L., Vermeire L., Ibrahimi A., Crawford A.D., Derua R., Janssens E., Waelkens E., Carmeliet P., Collen D., Huylebroeck D.
      Development 134:4381-4393(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH ACVR1B AND SMAD3, PHOSPHORYLATION AT THR-88 AND THR-92, MUTAGENESIS OF THR-88 AND THR-92.
    9. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "A human 5'-tyrosyl DNA phosphodiesterase that repairs topoisomerase-mediated DNA damage."
      Ledesma F.C., El Khamisy S.F., Zuma M.C., Osborn K., Caldecott K.W.
      Nature 461:674-678(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION AS TYROSYL-DNA PHOSPHODIESTERASE, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, COFACTOR, MUTAGENESIS OF GLU-152 AND ASP-262.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. "TDP2/TTRAP is the major 5'-tyrosyl DNA phosphodiesterase activity in vertebrate cells and is critical for cellular resistance to topoisomerase II-induced DNA damage."
      Zeng Z., Cortes-Ledesma F., El Khamisy S.F., Caldecott K.W.
      J. Biol. Chem. 286:403-409(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    13. "TTRAP is a novel component of the non-canonical TRAF6-TAK1 TGF-beta signaling pathway."
      Varady G., Sarkadi B., Fatyol K.
      PLoS ONE 6:E25548-E25548(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, UBIQUITINATION.
    14. "Characterization of magnesium requirement of human 5'-tyrosyl DNA phosphodiesterase mediated reaction."
      Adhikari S., Karmahapatra S.K., Karve T.M., Bandyopadhyay S., Woodrick J., Manthena P.V., Glasgow E., Byers S., Saha T., Uren A.
      BMC Res. Notes 5:134-134(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR.
    15. "The PML nuclear bodies-associated protein TTRAP regulates ribosome biogenesis in nucleolar cavities upon proteasome inhibition."
      Vilotti S., Biagioli M., Foti R., Dal Ferro M., Lavina Z.S., Collavin L., Del Sal G., Zucchelli S., Gustincich S.
      Cell Death Differ. 19:488-500(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    16. "Biochemical characterization of human Tyrosyl DNA Phosphodiesterase 2 (TDP2/TTRAP): a Mg2+/Mn2+-dependent phosphodiesterase specific for the repair of topoisomerase cleavage complexes."
      Gao R., Huang S.Y., Marchand C., Pommier Y.
      J. Biol. Chem. 287:30842-30852(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF ASN-120; GLU-152; ASP-262 AND HIS-351.
    17. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
      Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
      Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. Cited for: FUNCTION AS TYROSYL-RNA PHOSPHODIESTERASE, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiTYDP2_HUMAN
    AccessioniPrimary (citable) accession number: O95551
    Secondary accession number(s): B4DKL8
    , B4DQ95, Q2TBE2, Q5JYM0, Q7Z6U5, Q9NUK5, Q9NYY9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2005
    Last sequence update: May 1, 1999
    Last modified: October 1, 2014
    This is version 119 of the entry and version 1 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 6
      Human chromosome 6: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3