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O95551 (TYDP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosyl-DNA phosphodiesterase 2

Short name=Tyr-DNA phosphodiesterase 2
Short name=hTDP2
EC=3.1.4.-
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 names
Name:TDP2
Synonyms:EAP2, TTRAP
ORF Names:AD-022
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length362 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.10 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16 Ref.19

Cofactor

Magnesium. Can use other divalent cations as cofactor in vitro, such as manganese. Ref.10 Ref.14 Ref.16

Subunit structure

Interacts with TRAF2, TRAF3, TRAF5, TRAF6, TNFRSF8/CD30, TNFRSF5/CD40, TNFRSF1B/TNF-R75, ETS1, ETS2, FLI1, SMAD3 and ACVR1B/ALK4. Ref.1 Ref.2 Ref.8

Subcellular location

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. Ref.2 Ref.10 Ref.15 Ref.19

Tissue specificity

Widely expressed. Ref.1

Post-translational modification

Ubiquitinated by TRAF6. Ref.13

Sequence similarities

Belongs to the CCR4/nocturin family.

Biophysicochemical properties

Kinetic parameters:

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

KM=8 µM for single-stranded 5'-tyrosyl DNA Ref.16

Sequence caution

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.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   LigandMagnesium
Metal-binding
   Molecular functionHydrolase
Nuclease
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell surface receptor signaling pathway

Traceable author statement Ref.1. Source: ProtInc

double-strand break repair

Inferred from direct assay Ref.10. Source: UniProtKB

regulation of RNA biosynthetic process

Traceable author statement Ref.1. Source: GOC

   Cellular_componentPML body

Inferred from direct assay Ref.10. Source: UniProtKB

cytoplasm

Inferred from direct assay Ref.19. Source: UniProtKB

intercellular bridge

Inferred from direct assay. Source: HPA

nucleolus

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay Ref.19. Source: UniProtKB

   Molecular_function5'-tyrosyl-DNA phosphodiesterase activity

Inferred from direct assay Ref.10Ref.14Ref.16. Source: UniProtKB

magnesium ion binding

Inferred from direct assay Ref.14Ref.16. Source: UniProtKB

manganese ion binding

Inferred from direct assay Ref.16. Source: UniProtKB

nuclease activity

Inferred from electronic annotation. Source: UniProtKB-KW

single-stranded DNA binding

Inferred from direct assay Ref.16. Source: UniProtKB

transcription corepressor activity

Traceable author statement Ref.1. Source: ProtInc

tyrosyl-RNA phosphodiesterase activity

Inferred from direct assay Ref.19. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O95551-1)

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.
Isoform 2 (identifier: O95551-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MRERHDTGACAEPRVGLLFRLKGRCRGGRKM
Note: No experimental confirmation available.
Isoform 3 (identifier: O95551-3)

The sequence of this isoform differs from the canonical sequence as follows:
     60-137: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 362362Tyrosyl-DNA phosphodiesterase 2
PRO_0000065678

Sites

Active site3511Proton acceptor Probable
Metal binding1201Magnesium Probable
Metal binding1521Magnesium By similarity
Metal binding2621Magnesium Probable
Metal binding2641Magnesium By similarity
Metal binding3501Magnesium By similarity
Metal binding3511Magnesium Probable

Amino acid modifications

Modified residue11N-acetylmethionine Ref.9 Ref.17 Ref.18
Modified residue881Phosphothreonine; by ACVR1B Ref.8
Modified residue921Phosphothreonine; by ACVR1B Ref.8

Natural variations

Alternative sequence11M → MRERHDTGACAEPRVGLLFR LKGRCRGGRKM in isoform 2.
VSP_038523
Alternative sequence60 – 13778Missing in isoform 3.
VSP_038524
Natural variant1661S → G.
Corresponds to variant rs35977478 [ dbSNP | Ensembl ].
VAR_051464
Natural variant2491Q → E. Ref.5
Corresponds to variant rs2294689 [ dbSNP | Ensembl ].
VAR_022634
Natural variant2681R → Q. Ref.5
Corresponds to variant rs17249952 [ dbSNP | Ensembl ].
VAR_022635

Experimental info

Mutagenesis881T → A: Abolishes function, but retains ability to interact with SMAD3; when associated with A-92. Ref.8
Mutagenesis921T → A: Abolishes function, but retains ability to interact with SMAD3; when associated with A-88. Ref.8
Mutagenesis1201N → A: Strongly reduced phosphodiesterase activity. Ref.16
Mutagenesis1521E → A: Loss of phosphodiesterase activity. Ref.10 Ref.16
Mutagenesis2621D → A: Loss of phosphodiesterase activity. Ref.10 Ref.16
Mutagenesis3511H → A: Loss of phosphodiesterase activity. Ref.16
Sequence conflict311E → R in AAF64144. Ref.3
Sequence conflict611Y → C in BAA92119. Ref.4
Sequence conflict721E → G in BAG60857. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 37892E125DB64410

FASTA36240,930
        10         20         30         40         50         60 
MELGSCLEGG REAAEEEGEP EVKKRRLLCV EFASVASCDA AVAQCFLAEN DWEMERALNS 

        70         80         90        100        110        120 
YFEPPVEESA LERRPETISE PKTYVDLTNE ETTDSTTSKI SPSEDTQQEN GSMFSLITWN 

       130        140        150        160        170        180 
IDGLDLNNLS ERARGVCSYL ALYSPDVIFL QEVIPPYYSY LKKRSSNYEI ITGHEEGYFT 

       190        200        210        220        230        240 
AIMLKKSRVK LKSQEIIPFP STKMMRNLLC VHVNVSGNEL CLMTSHLEST RGHAAERMNQ 

       250        260        270        280        290        300 
LKMVLKKMQE APESATVIFA GDTNLRDREV TRCGGLPNNI VDVWEFLGKP KHCQYTWDTQ 

       310        320        330        340        350        360 
MNSNLGITAA CKLRFDRIFF RAAAEEGHII PRSLDLLGLE KLDCGRFPSD HWGLLCNLDI 


IL 

« Hide

Isoform 2 [UniParc].

Checksum: 6B822134BDD395F3
Show »

FASTA39244,339
Isoform 3 [UniParc].

Checksum: 3FBF514CDDECB196
Show »

FASTA28432,176

References

« Hide 'large scale' references
[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]"Gene expression profiling in the human hypothalamus-pituitary-adrenal axis and full-length cDNA cloning."
Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X., Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M. expand/collapse author list , Zhou J., Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.
Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[19]"An RNA virus hijacks an incognito function of a DNA repair enzyme."
Virgen-Slane R., Rozovics J.M., Fitzgerald K.D., Ngo T., Chou W., van der Heden van Noort G.J., Filippov D.V., Gershon P.D., Semler B.L.
Proc. Natl. Acad. Sci. U.S.A. 109:14634-14639(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS TYROSYL-RNA PHOSPHODIESTERASE, SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_057698.2. NM_016614.2.
UniGeneHs.403010.

3D structure databases

ProteinModelPortalO95551.
SMRO95551. Positions 26-362.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119615. 30 interactions.
IntActO95551. 17 interactions.
MINTMINT-5005899.

Chemistry

ChEMBLCHEMBL2169736.

PTM databases

PhosphoSiteO95551.

Proteomic databases

PaxDbO95551.
PRIDEO95551.

Protocols and materials databases

DNASU51567.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000378198; ENSP00000367440; ENSG00000111802. [O95551-1]
ENST00000545995; ENSP00000437637; ENSG00000111802. [O95551-2]
GeneID51567.
KEGGhsa:51567.
UCSCuc003nej.3. human. [O95551-1]

Organism-specific databases

CTD51567.
GeneCardsGC06M024651.
HGNCHGNC:17768. TDP2.
HPAHPA054272.
MIM605764. gene.
neXtProtNX_O95551.
PharmGKBPA165618310.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG277021.
HOVERGENHBG079625.
InParanoidO95551.
OMARLLCVEF.
OrthoDBEOG7XPZ5W.
PhylomeDBO95551.
TreeFamTF314813.

Gene expression databases

ArrayExpressO95551.
BgeeO95551.
CleanExHS_TTRAP.
GenevestigatorO95551.

Family and domain databases

Gene3D3.60.10.10. 1 hit.
InterProIPR005135. Endo/exonuclease/phosphatase.
IPR009060. UBA-like.
[Graphical view]
PfamPF03372. Exo_endo_phos. 1 hit.
[Graphical view]
SUPFAMSSF46934. SSF46934. 1 hit.
SSF56219. SSF56219. 1 hit.
ProtoNetSearch...

Other

GeneWikiTTRAP.
GenomeRNAi51567.
NextBio55388.
PROO95551.
SOURCESearch...

Entry information

Entry nameTYDP2_HUMAN
AccessionPrimary (citable) accession number: O95551
Secondary accession number(s): B4DKL8 expand/collapse secondary AC list , B4DQ95, Q2TBE2, Q5JYM0, Q7Z6U5, Q9NUK5, Q9NYY9
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 115 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

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SIMILARITY comments

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