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Q9NUW8 (TYDP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 117. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Tyrosyl-DNA phosphodiesterase 1

Short name=Tyr-DNA phosphodiesterase 1
EC=3.1.4.-
Gene names
Name:TDP1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length608 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 3'-phosphodiester bond, giving rise to DNA with a free 3' phosphate. Catalyzes the hydrolysis of dead-end complexes between DNA and the topoisomerase I active site tyrosine residue. Hydrolyzes 3'-phosphoglycolates on protruding 3' ends on DNA double-strand breaks due to DNA damage by radiation and free radicals. Acts on blunt-ended double-strand DNA breaks and on single-stranded DNA. Has low 3'exonuclease activity and can remove a single nucleoside from the 3'end of DNA and RNA molecules with 3'hydroxyl groups. Has no exonuclease activity towards DNA or RNA with a 3'phosphate. Ref.7 Ref.8 Ref.9 Ref.10 Ref.15

Subunit structure

Monomer. Ref.17

Subcellular location

Nucleus. Cytoplasm Ref.21.

Tissue specificity

Ubiquitously expressed. Similar expression throughout the central nervous system (whole brain, amygdala, caudate nucleus, cerebellum, cerebral cortex, frontal lobe, hippocampus, medulla oblongata, occipital lobe, putamen, substantia nigra, temporal lobe, thalamus, nucleus accumbens and spinal cord) and increased expression in testis and thymus. Ref.20 Ref.23

Post-translational modification

Phosphorylated on serine and/or threonine residues, but not on tyrosine residues. Ref.21

Involvement in disease

Spinocerebellar ataxia, autosomal recessive, with axonal neuropathy (SCAN1) [MIM:607250]: Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCAN1 is an autosomal recessive cerebellar ataxia (ARCA) associated with peripheral axonal motor and sensory neuropathy, distal muscular atrophy, pes cavus and steppage gait as seen in Charcot-Marie-Tooth neuropathy. All affected individuals have normal intelligence.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.20 Ref.21 Ref.22 Ref.23

Sequence similarities

Belongs to the tyrosyl-DNA phosphodiesterase family.

Biophysicochemical properties

Kinetic parameters:

kcat is 7 sec(-1) with single-stranded 5'-tyrosyl DNA as substrate.

KM=0.08 µM for 14-mer single-stranded oligo with a 3'-phosphotyrosine Ref.15

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 608608Tyrosyl-DNA phosphodiesterase 1
PRO_0000212486

Regions

Region400 – 4034Interaction with DNA

Sites

Active site2631Nucleophile
Active site4931Proton donor
Binding site2651Substrate
Binding site4951Substrate
Site5181Interaction with DNA

Amino acid modifications

Modified residue611Phosphoserine Ref.12
Modified residue1471Phosphothreonine Ref.13
Modified residue1481Phosphoserine Ref.13

Natural variations

Natural variant951E → D. Ref.2
Corresponds to variant rs35114462 [ dbSNP | Ensembl ].
VAR_025817
Natural variant1011P → L. Ref.2
Corresponds to variant rs35455108 [ dbSNP | Ensembl ].
VAR_025818
Natural variant1341A → T. Ref.2
Corresponds to variant rs28365054 [ dbSNP | Ensembl ].
VAR_025819
Natural variant1871D → G. Ref.2
Corresponds to variant rs35271143 [ dbSNP | Ensembl ].
VAR_025820
Natural variant3041R → Q. Ref.2
Corresponds to variant rs34452707 [ dbSNP | Ensembl ].
VAR_025821
Natural variant4931H → R in SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA. Ref.10 Ref.20 Ref.21 Ref.22 Ref.23
VAR_017144
Natural variant5661P → L in autosomal recessive or sporadic spinocerebellar ataxia affected Japanese individuals. Ref.20
VAR_017145
Natural variant5691T → A. Ref.2
Corresponds to variant rs35973343 [ dbSNP | Ensembl ].
VAR_025822

Experimental info

Mutagenesis2631H → A: Loss of activity. Ref.6 Ref.8
Mutagenesis2651K → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. Ref.6 Ref.8
Mutagenesis2651K → S: Reduces the activity to nearly undetectable levels. Ref.6 Ref.8
Mutagenesis2831N → A: No effect. Ref.8
Mutagenesis2941Q → A: Slightly reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA. Ref.8
Mutagenesis4931H → A: 3000-fold reduction in activity; abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. Ref.6 Ref.8
Mutagenesis4931H → N: 15000-fold reduction in activity. Ref.6 Ref.8
Mutagenesis4951K → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. Ref.6 Ref.8
Mutagenesis4951K → S: 125-fold reduction in activity. Ref.6 Ref.8
Mutagenesis5161N → A: Reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA. Ref.8
Mutagenesis5381E → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. Ref.8
Sequence conflict3891A → P in BAA91997. Ref.1
Sequence conflict5111L → R in AAF65624. Ref.5

Secondary structure

...................................................................................... 608
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9NUW8 [UniParc].

Last modified October 24, 2003. Version 2.
Checksum: F30202BD8329E5CE

FASTA60868,420
        10         20         30         40         50         60 
MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE AQKAAHKRKI 

        70         80         90        100        110        120 
SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM PQKQAEKVVI KKEKDISAPN 

       130        140        150        160        170        180 
DGTAQRTENH GAPACHRLKE EEDEYETSGE GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS 

       190        200        210        220        230        240 
GALHIKDILS PLFGTLVSSA QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA 

       250        260        270        280        290        300 
QAKPYENISL CQAKLDIAFG THHTKMMLLL YEEGLRVVIH TSNLIHADWH QKTQGIWLSP 

       310        320        330        340        350        360 
LYPRIADGTH KSGESPTHFK ADLISYLMAY NAPSLKEWID VIHKHDLSET NVYLIGSTPG 

       370        380        390        400        410        420 
RFQGSQKDNW GHFRLKKLLK DHASSMPNAE SWPVVGQFSS VGSLGADESK WLCSEFKESM 

       430        440        450        460        470        480 
LTLGKESKTP GKSSVPLYLI YPSVENVRTS LEGYPAGGSL PYSIQTAEKQ NWLHSYFHKW 

       490        500        510        520        530        540 
SAETSGRSNA MPHIKTYMRP SPDFSKIAWF LVTSANLSKA AWGALEKNGT QLMIRSYELG 

       550        560        570        580        590        600 
VLFLPSAFGL DSFKVKQKFF AGSQEPMATF PVPYDLPPEL YGSKDRPWIW NIPYVKAPDT 


HGNMWVPS 

« Hide

References

« Hide 'large scale' references
[1]"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].
Tissue: Placenta.
[2]NIEHS SNPs program
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASP-95; LEU-101; THR-134; GLY-187; GLN-304 AND ALA-569.
[3]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Pancreas.
[5]"Yeast gene for a Tyr-DNA phosphodiesterase that repairs topoisomerase I complexes."
Pouliot J.J., Yao K.C., Robertson C.A., Nash H.A.
Science 286:552-555(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-608.
[6]"The tyrosyl-DNA phosphodiesterase Tdp1 is a member of the phospholipase D superfamily."
Interthal H., Pouliot J.J., Champoux J.J.
Proc. Natl. Acad. Sci. U.S.A. 98:12009-12014(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: SIMILARITY TO PHOSPHOLIPASE D SUPERFAMILY, MUTAGENESIS OF HIS-263; LYS-265; HIS-493 AND LYS-495.
[7]"Conversion of phosphoglycolate to phosphate termini on 3' overhangs of DNA double strand breaks by the human tyrosyl-DNA phosphodiesterase hTdp1."
Inamdar K.V., Pouliot J.J., Zhou T., Lees-Miller S.P., Rasouli-Nia A., Povirk L.F.
J. Biol. Chem. 277:27162-27168(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[8]"Analysis of human tyrosyl-DNA phosphodiesterase I catalytic residues."
Raymond A.C., Rideout M.C., Staker B., Hjerrild K., Burgin A.B. Jr.
J. Mol. Biol. 338:895-906(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, ENZYME MECHANISM, MUTAGENESIS OF HIS-263; LYS-265; ASN-283; GLN-294; HIS-493; LYS-495; ASN-516 AND GLU-538.
[9]"Substrate specificity of tyrosyl-DNA phosphodiesterase I (Tdp1)."
Raymond A.C., Staker B.L., Burgin A.B. Jr.
J. Biol. Chem. 280:22029-22035(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"Human Tdp1 cleaves a broad spectrum of substrates, including phosphoamide linkages."
Interthal H., Chen H.J., Champoux J.J.
J. Biol. Chem. 280:36518-36528(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF VARIANT SCAN1 ARG-493.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-147 AND SER-148, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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].
[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, BIOPHYSICOCHEMICAL PROPERTIES.
[16]"Insights into substrate binding and catalytic mechanism of human tyrosyl-DNA phosphodiesterase (Tdp1) from vanadate and tungstate-inhibited structures."
Davies D.R., Interthal H., Champoux J.J., Hol W.G.J.
J. Mol. Biol. 324:917-932(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 149-608 IN COMPLEXES WITH SUBSTRATE; VANADATE AND TUNGSTATE.
[17]"The crystal structure of human tyrosyl-DNA phosphodiesterase, Tdp1."
Davies D.R., Interthal H., Champoux J.J., Hol W.G.J.
Structure 10:237-248(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.69 ANGSTROMS) OF 149-608, SUBUNIT.
[18]"Crystal structure of a transition state mimic for TDP1 assembled from vanadate, DNA, and a topoisomerase I-derived peptide."
Davies D.R., Interthal H., Champoux J.J., Hol W.G.J.
Chem. Biol. 10:139-147(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 149-608.
[19]"Explorations of peptide and oligonucleotide binding sites of tyrosyl-DNA phosphodiesterase using vanadate complexes."
Davies D.R., Interthal H., Champoux J.J., Hol W.G.J.
J. Med. Chem. 47:829-837(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 149-608 IN COMPLEXES WITH SUBSTRATES.
[20]"Mutation of TDP1, encoding a topoisomerase I-dependent DNA damage repair enzyme, in spinocerebellar ataxia with axonal neuropathy."
Takashima H., Boerkoel C.F., John J., Saifi G.M., Salih M.A.M., Armstrong D., Mao Y., Quiocho F.A., Roa B.B., Nakagawa M., Stockton D.W., Lupski J.R.
Nat. Genet. 32:267-272(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SCAN1 ARG-493, VARIANT LEU-566, TISSUE SPECIFICITY.
[21]"Deficiency in 3'-phosphoglycolate processing in human cells with a hereditary mutation in tyrosyl-DNA phosphodiesterase (TDP1)."
Zhou T., Lee J.W., Tatavarthi H., Lupski J.R., Valerie K., Povirk L.F.
Nucleic Acids Res. 33:289-297(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SCAN1 ARG-493, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[22]"SCAN1 mutant Tdp1 accumulates the enzyme-DNA intermediate and causes camptothecin hypersensitivity."
Interthal H., Chen H.J., Kehl-Fie T.E., Zotzmann J., Leppard J.B., Champoux J.J.
EMBO J. 24:2224-2233(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SCAN1 ARG-493.
[23]"Spinocerebellar ataxia with axonal neuropathy: consequence of a Tdp1 recessive neomorphic mutation?"
Hirano R., Interthal H., Huang C., Nakamura T., Deguchi K., Choi K., Bhattacharjee M.B., Arimura K., Umehara F., Izumo S., Northrop J.L., Salih M.A.M., Inoue K., Armstrong D.L., Champoux J.J., Takashima H., Boerkoel C.F.
EMBO J. 26:4732-4743(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT SCAN1 ARG-493, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Web resources

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK001952 mRNA. Translation: BAA91997.1.
DQ367843 Genomic DNA. Translation: ABC79301.1.
AL137128 Genomic DNA. No translation available.
BC015474 mRNA. Translation: AAH15474.1.
AF182002 mRNA. Translation: AAF65623.1.
AF182003 mRNA. Translation: AAF65624.1.
RefSeqNP_001008744.1. NM_001008744.1.
NP_060789.2. NM_018319.3.
XP_005267904.1. XM_005267847.1.
XP_005267905.1. XM_005267848.1.
UniGeneHs.209945.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JY1X-ray1.69A149-608[»]
1MU7X-ray2.00A/B149-608[»]
1MU9X-ray2.05A/B149-608[»]
1NOPX-ray2.30A/B149-608[»]
1QZQX-ray2.40A/B147-608[»]
1RFFX-ray1.70A/B149-608[»]
1RFIX-ray2.20A/B149-608[»]
1RG1X-ray2.10A/B149-608[»]
1RG2X-ray2.10A/B149-608[»]
1RGTX-ray2.00A/B149-608[»]
1RGUX-ray2.22A/B149-608[»]
1RH0X-ray2.30A/B149-608[»]
ProteinModelPortalQ9NUW8.
SMRQ9NUW8. Positions 161-608.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid120890. 5 interactions.
IntActQ9NUW8. 4 interactions.
MINTMINT-3074488.
STRING9606.ENSP00000337353.

Chemistry

BindingDBQ9NUW8.
ChEMBLCHEMBL1075138.

PTM databases

PhosphoSiteQ9NUW8.

Polymorphism databases

DMDM37999797.

Proteomic databases

PaxDbQ9NUW8.
PRIDEQ9NUW8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000335725; ENSP00000337353; ENSG00000042088.
ENST00000393454; ENSP00000377099; ENSG00000042088.
GeneID55775.
KEGGhsa:55775.
UCSCuc001xxy.3. human.

Organism-specific databases

CTD55775.
GeneCardsGC14P090422.
HGNCHGNC:18884. TDP1.
MIM607198. gene.
607250. phenotype.
neXtProtNX_Q9NUW8.
Orphanet94124. Spinocerebellar ataxia type 1 with axonal neuropathy.
PharmGKBPA421.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG274417.
HOGENOMHOG000067775.
HOVERGENHBG061242.
InParanoidQ9NUW8.
KOK10862.
OMANISLCQA.
PhylomeDBQ9NUW8.
TreeFamTF105989.

Enzyme and pathway databases

ReactomeREACT_216. DNA Repair.
SABIO-RKQ9NUW8.

Gene expression databases

ArrayExpressQ9NUW8.
BgeeQ9NUW8.
CleanExHS_TDP1.
GenevestigatorQ9NUW8.

Family and domain databases

Gene3D3.30.870.20. 1 hit.
InterProIPR010347. Tdp1.
IPR027415. TDP_C.
[Graphical view]
PANTHERPTHR12415. PTHR12415. 1 hit.
PfamPF06087. Tyr-DNA_phospho. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9NUW8.
GeneWikiTDP1.
GenomeRNAi55775.
NextBio60841.
PROQ9NUW8.
SOURCESearch...

Entry information

Entry nameTYDP1_HUMAN
AccessionPrimary (citable) accession number: Q9NUW8
Secondary accession number(s): Q2HXX4 expand/collapse secondary AC list , Q96BK7, Q9NZM7, Q9NZM8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: April 16, 2014
This is version 117 of the entry and version 2 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM