O95551 (TYDP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	362 AA.
Sequence status	Complete.
Protein existence	Evidence 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 to 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.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Cofactor	Magnesium. Can use other divalent cations as cofactor in vitro, such as manganese. Ref.9 Ref.13 Ref.15
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. Nucleus › PML body. Nucleus › nucleolus. 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.9 Ref.14 Ref.16
Tissue specificity	Widely expressed. Ref.1
Post-translational modification	Ubiquitinated by TRAF6. Ref.12
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.15
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 process	DNA damage DNA repair
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	Magnesium Metal-binding
Molecular function	Hydrolase Nuclease
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell surface receptor signaling pathway Traceable author statement Ref.1. Source: ProtInc double-strand break repair Inferred from direct assay Ref.9. Source: UniProtKB nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	PML body Inferred from direct assay Ref.9. Source: UniProtKB cytoplasm Inferred from direct assay Ref.16. Source: UniProtKB nucleolus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	5'-tyrosyl-DNA phosphodiesterase activity Inferred from direct assay Ref.9Ref.13Ref.15. Source: UniProtKB magnesium ion binding Inferred from direct assay Ref.13Ref.15. Source: UniProtKB manganese ion binding Inferred from direct assay Ref.15. Source: UniProtKB nuclease activity Inferred from electronic annotation. Source: UniProtKB-KW single-stranded DNA binding Inferred from direct assay Ref.15. Source: UniProtKB transcription corepressor activity Traceable author statement Ref.1. Source: ProtInc tyrosyl-RNA phosphodiesterase activity Inferred from direct assay Ref.16. 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 362	362	Tyrosyl-DNA phosphodiesterase 2		PRO_0000065678
Sites
	Active site	351	1	Proton acceptor Probable
	Metal binding	120	1	Magnesium Probable
	Metal binding	152	1	Magnesium By similarity
	Metal binding	262	1	Magnesium Probable
	Metal binding	264	1	Magnesium By similarity
	Metal binding	350	1	Magnesium By similarity
	Metal binding	351	1	Magnesium Probable
Amino acid modifications
	Modified residue	88	1	Phosphothreonine; by ACVR1B Ref.8
	Modified residue	92	1	Phosphothreonine; by ACVR1B Ref.8
Natural variations
	Alternative sequence	1	1	M → MRERHDTGACAEPRVGLLFR LKGRCRGGRKM in isoform 2.		VSP_038523
	Alternative sequence	60 – 137	78	Missing in isoform 3.		VSP_038524
	Natural variant	166	1	S → G. Corresponds to variant rs35977478 [ dbSNP | Ensembl ].		VAR_051464
	Natural variant	249	1	Q → E. Ref.5 Corresponds to variant rs2294689 [ dbSNP | Ensembl ].		VAR_022634
	Natural variant	268	1	R → Q. Ref.5 Corresponds to variant rs17249952 [ dbSNP | Ensembl ].		VAR_022635
Experimental info
	Mutagenesis	88	1	T → A: Abolishes function, but retains ability to interact with SMAD3; when associated with A-92. Ref.8
	Mutagenesis	92	1	T → A: Abolishes function, but retains ability to interact with SMAD3; when associated with A-88. Ref.8
	Mutagenesis	120	1	N → A: Strongly reduced phosphodiesterase activity. Ref.15
	Mutagenesis	152	1	E → A: Loss of phosphodiesterase activity. Ref.9 Ref.15
	Mutagenesis	262	1	D → A: Loss of phosphodiesterase activity. Ref.9 Ref.15
	Mutagenesis	351	1	H → A: Loss of phosphodiesterase activity. Ref.15
	Sequence conflict	31	1	E → R in AAF64144. Ref.3
	Sequence conflict	61	1	Y → C in BAA92119. Ref.4
	Sequence conflict	72	1	E → G in BAG60857. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: 37892E125DB64410	FASTA	362	40,930
	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
	Isoform 2 [UniParc]. Checksum: 6B822134BDD395F3	FASTA	392	44,339
	10 20 30 40 50 60 MRERHDTGAC AEPRVGLLFR LKGRCRGGRK MELGSCLEGG REAAEEEGEP EVKKRRLLCV 70 80 90 100 110 120 EFASVASCDA AVAQCFLAEN DWEMERALNS YFEPPVEESA LERRPETISE PKTYVDLTNE 130 140 150 160 170 180 ETTDSTTSKI SPSEDTQQEN GSMFSLITWN IDGLDLNNLS ERARGVCSYL ALYSPDVIFL 190 200 210 220 230 240 QEVIPPYYSY LKKRSSNYEI ITGHEEGYFT AIMLKKSRVK LKSQEIIPFP STKMMRNLLC 250 260 270 280 290 300 VHVNVSGNEL CLMTSHLEST RGHAAERMNQ LKMVLKKMQE APESATVIFA GDTNLRDREV 310 320 330 340 350 360 TRCGGLPNNI VDVWEFLGKP KHCQYTWDTQ MNSNLGITAA CKLRFDRIFF RAAAEEGHII 370 380 390 PRSLDLLGLE KLDCGRFPSD HWGLLCNLDI IL
	Isoform 3 [UniParc]. Checksum: 3FBF514CDDECB196	FASTA	284	32,176
	10 20 30 40 50 60 MELGSCLEGG REAAEEEGEP EVKKRRLLCV EFASVASCDA AVAQCFLAEN DWEMERALNS 70 80 90 100 110 120 YLALYSPDVI FLQEVIPPYY SYLKKRSSNY EIITGHEEGY FTAIMLKKSR VKLKSQEIIP 130 140 150 160 170 180 FPSTKMMRNL LCVHVNVSGN ELCLMTSHLE STRGHAAERM NQLKMVLKKM QEAPESATVI 190 200 210 220 230 240 FAGDTNLRDR EVTRCGGLPN NIVDVWEFLG KPKHCQYTWD TQMNSNLGIT AACKLRFDRI 250 260 270 280 FFRAAAEEGH IIPRSLDLLG LEKLDCGRFP SDHWGLLCNL DIIL

References

	« Hide 'large scale' referencesShow '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. , 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. , 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]	"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.
[10]	"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].
[11]	"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.
[12]	"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.
[13]	"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.
[14]	"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.
[15]	"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.
[16]	"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

SeattleSNPs

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.
IPI	IPI00009913. IPI00954485. IPI00954580.
RefSeq	NP_057698.2. NM_016614.2.
UniGene	Hs.731481.
3D structure databases
ProteinModelPortal	O95551.
ModBase	Search...
Protein-protein interaction databases
IntAct	O95551. 13 interactions.
MINT	MINT-5005899.
PTM databases
PhosphoSite	O95551.
Proteomic databases
PaxDb	O95551.
PRIDE	O95551.
Protocols and materials databases
DNASU	51567.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341060; ENSP00000345345; ENSG00000111802. ENST00000378198; ENSP00000367440; ENSG00000111802. ENST00000545995; ENSP00000437637; ENSG00000111802.
GeneID	51567.
KEGG	hsa:51567.
UCSC	uc003nej.3. human.
Organism-specific databases
CTD	51567.
GeneCards	GC06M024651.
HGNC	HGNC:17768. TDP2.
MIM	605764. gene.
neXtProt	NX_O95551.
PharmGKB	PA165618310.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG277021.
HOVERGEN	HBG079625.
InParanoid	O95551.
OMA	LITWNID.
OrthoDB	EOG4HQDJR.
PhylomeDB	O95551.
Gene expression databases
Bgee	O95551.
CleanEx	HS_TTRAP.
Genevestigator	O95551.
GermOnline	ENSG00000111802. Homo sapiens.
Family and domain databases
InterPro	IPR005135. Endo/exonuclease/phosphatase. IPR009060. UBA-like. [Graphical view]
Pfam	PF03372. Exo_endo_phos. 1 hit. [Graphical view]
SUPFAM	SSF56219. Exo_endo_phos. 1 hit. SSF46934. UBA_like. 1 hit.
ProtoNet	Search...
Other
GenomeRNAi	51567.
NextBio	55388.
SOURCE	Search...

Entry information

Entry name

TYDP2_HUMAN

Accession

Primary (citable) accession number: O95551
Secondary accession number(s): B4DKL8 , B4DQ95, Q2TBE2, Q5JYM0, Q7Z6U5, Q9NUK5, Q9NYY9

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 7, 2005
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 104 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.