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O95551

- TYDP2_HUMAN

UniProt

O95551 - TYDP2_HUMAN

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Protein

Tyrosyl-DNA phosphodiesterase 2

Gene

TDP2

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

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. single-stranded DNA binding Source: UniProtKB
  6. transcription corepressor activity Source: ProtInc
  7. 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
Complete GO annotation...

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. nucleus Source: UniProtKB
  4. PML body Source: UniProtKB
Complete GO annotation...

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

Orphaneti404493. Autosomal recessive cerebellar ataxia-epilepsy-intellectual disability syndrome due to TUD deficiency.
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

BgeeiO95551.
CleanExiHS_TTRAP.
ExpressionAtlasiO95551. baseline and differential.
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. 32 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.
GeneTreeiENSGT00390000014242.
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

        10         20         30         40         50
MELGSCLEGG REAAEEEGEP EVKKRRLLCV EFASVASCDA AVAQCFLAEN
60 70 80 90 100
DWEMERALNS YFEPPVEESA LERRPETISE PKTYVDLTNE ETTDSTTSKI
110 120 130 140 150
SPSEDTQQEN GSMFSLITWN IDGLDLNNLS ERARGVCSYL ALYSPDVIFL
160 170 180 190 200
QEVIPPYYSY LKKRSSNYEI ITGHEEGYFT AIMLKKSRVK LKSQEIIPFP
210 220 230 240 250
STKMMRNLLC VHVNVSGNEL CLMTSHLEST RGHAAERMNQ LKMVLKKMQE
260 270 280 290 300
APESATVIFA GDTNLRDREV TRCGGLPNNI VDVWEFLGKP KHCQYTWDTQ
310 320 330 340 350
MNSNLGITAA CKLRFDRIFF RAAAEEGHII PRSLDLLGLE KLDCGRFPSD
360
HWGLLCNLDI IL
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. 32 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.
Orphaneti 404493. Autosomal recessive cerebellar ataxia-epilepsy-intellectual disability syndrome due to TUD deficiency.
PharmGKBi PA165618310.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG277021.
GeneTreei ENSGT00390000014242.
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

Bgeei O95551.
CleanExi HS_TTRAP.
ExpressionAtlasi O95551. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 120 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