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Q9NUW8

- TYDP1_HUMAN

UniProt

Q9NUW8 - TYDP1_HUMAN

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Protein

Tyrosyl-DNA phosphodiesterase 1

Gene

TDP1

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 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.5 Publications

Kineticsi

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

  1. KM=0.08 µM for 14-mer single-stranded oligo with a 3'-phosphotyrosine1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei263 – 2631Nucleophile
Binding sitei265 – 2651Substrate
Active sitei493 – 4931Proton donor
Binding sitei495 – 4951Substrate
Sitei518 – 5181Interaction with DNA

GO - Molecular functioni

  1. 3'-tyrosyl-DNA phosphodiesterase activity Source: UniProtKB
  2. double-stranded DNA binding Source: UniProtKB
  3. exonuclease activity Source: UniProtKB-KW
  4. single-stranded DNA binding Source: UniProtKB

GO - Biological processi

  1. cell death Source: UniProtKB-KW
  2. DNA repair Source: UniProtKB
  3. double-strand break repair Source: UniProtKB
  4. single strand break repair Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Exonuclease, Hydrolase, Nuclease

Keywords - Biological processi

DNA damage, DNA repair

Enzyme and pathway databases

ReactomeiREACT_1201. Processing of DNA ends prior to end rejoining.
SABIO-RKQ9NUW8.

Names & Taxonomyi

Protein namesi
Recommended name:
Tyrosyl-DNA phosphodiesterase 1 (EC:3.1.4.-)
Short name:
Tyr-DNA phosphodiesterase 1
Gene namesi
Name:TDP1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:18884. TDP1.

Subcellular locationi

Nucleus 1 Publication. Cytoplasm 1 Publication

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. nucleus Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti493 – 4931H → R in SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA. 1 Publication
VAR_017144

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi263 – 2631H → A: Loss of activity. 2 Publications
Mutagenesisi265 – 2651K → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 2 Publications
Mutagenesisi265 – 2651K → S: Reduces the activity to nearly undetectable levels. 2 Publications
Mutagenesisi283 – 2831N → A: No effect. 1 Publication
Mutagenesisi294 – 2941Q → A: Slightly reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 1 Publication
Mutagenesisi493 – 4931H → A: 3000-fold reduction in activity; abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 2 Publications
Mutagenesisi493 – 4931H → N: 15000-fold reduction in activity. 2 Publications
Mutagenesisi495 – 4951K → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 2 Publications
Mutagenesisi495 – 4951K → S: 125-fold reduction in activity. 2 Publications
Mutagenesisi516 – 5161N → A: Reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 1 Publication
Mutagenesisi538 – 5381E → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 1 Publication

Keywords - Diseasei

Disease mutation, Neurodegeneration

Organism-specific databases

MIMi607250. phenotype.
Orphaneti94124. Spinocerebellar ataxia type 1 with axonal neuropathy.
PharmGKBiPA421.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 608608Tyrosyl-DNA phosphodiesterase 1PRO_0000212486Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei61 – 611Phosphoserine1 Publication
Modified residuei147 – 1471Phosphothreonine1 Publication
Modified residuei148 – 1481Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated on serine and/or threonine residues, but not on tyrosine residues.3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9NUW8.
PaxDbiQ9NUW8.
PRIDEiQ9NUW8.

PTM databases

PhosphoSiteiQ9NUW8.

Expressioni

Tissue specificityi

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.2 Publications

Gene expression databases

BgeeiQ9NUW8.
CleanExiHS_TDP1.
ExpressionAtlasiQ9NUW8. baseline and differential.
GenevestigatoriQ9NUW8.

Interactioni

Subunit structurei

Monomer.1 Publication

Protein-protein interaction databases

BioGridi120890. 8 interactions.
IntActiQ9NUW8. 4 interactions.
MINTiMINT-3074488.
STRINGi9606.ENSP00000337353.

Structurei

Secondary structure

1
608
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni149 – 1513Combined sources
Helixi154 – 1563Combined sources
Beta strandi166 – 1694Combined sources
Helixi176 – 1794Combined sources
Helixi185 – 1884Combined sources
Helixi191 – 1933Combined sources
Beta strandi196 – 2027Combined sources
Beta strandi204 – 2063Combined sources
Helixi208 – 2147Combined sources
Helixi217 – 2193Combined sources
Beta strandi224 – 2285Combined sources
Helixi232 – 24211Combined sources
Beta strandi248 – 2525Combined sources
Beta strandi266 – 2738Combined sources
Beta strandi275 – 2806Combined sources
Helixi286 – 2894Combined sources
Beta strandi291 – 2933Combined sources
Beta strandi295 – 2984Combined sources
Helixi319 – 32810Combined sources
Helixi333 – 3353Combined sources
Helixi336 – 3438Combined sources
Beta strandi352 – 3576Combined sources
Beta strandi359 – 3635Combined sources
Helixi364 – 3696Combined sources
Helixi371 – 38212Combined sources
Helixi389 – 3913Combined sources
Beta strandi394 – 3974Combined sources
Turni408 – 4158Combined sources
Helixi416 – 4205Combined sources
Beta strandi437 – 4404Combined sources
Helixi444 – 4485Combined sources
Beta strandi450 – 4523Combined sources
Helixi454 – 4596Combined sources
Helixi464 – 4674Combined sources
Helixi471 – 4766Combined sources
Helixi483 – 4853Combined sources
Beta strandi495 – 5006Combined sources
Beta strandi504 – 51411Combined sources
Helixi519 – 5224Combined sources
Beta strandi524 – 5263Combined sources
Turni527 – 5304Combined sources
Beta strandi531 – 5344Combined sources
Beta strandi536 – 5438Combined sources
Helixi545 – 5484Combined sources
Beta strandi553 – 5553Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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/B149-608[»]
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[»]
ProteinModelPortaliQ9NUW8.
SMRiQ9NUW8. Positions 161-608.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9NUW8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni400 – 4034Interaction with DNA

Sequence similaritiesi

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG274417.
GeneTreeiENSGT00390000002211.
HOGENOMiHOG000067775.
HOVERGENiHBG061242.
InParanoidiQ9NUW8.
KOiK10862.
OMAiNISLCQA.
PhylomeDBiQ9NUW8.
TreeFamiTF105989.

Family and domain databases

Gene3Di3.30.870.20. 1 hit.
InterProiIPR010347. Tdp1.
IPR027415. TDP_C.
[Graphical view]
PANTHERiPTHR12415. PTHR12415. 1 hit.
PfamiPF06087. Tyr-DNA_phospho. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9NUW8-1) [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
MSQEGDYGRW TISSSDESEE EKPKPDKPST SSLLCARQGA ANEPRYTCSE
60 70 80 90 100
AQKAAHKRKI SPVKFSNTDS VLPPKRQKSG SQEDLGWCLS SSDDELQPEM
110 120 130 140 150
PQKQAEKVVI KKEKDISAPN DGTAQRTENH GAPACHRLKE EEDEYETSGE
160 170 180 190 200
GQDIWDMLDK GNPFQFYLTR VSGVKPKYNS GALHIKDILS PLFGTLVSSA
210 220 230 240 250
QFNYCFDVDW LVKQYPPEFR KKPILLVHGD KREAKAHLHA QAKPYENISL
260 270 280 290 300
CQAKLDIAFG THHTKMMLLL YEEGLRVVIH TSNLIHADWH QKTQGIWLSP
310 320 330 340 350
LYPRIADGTH KSGESPTHFK ADLISYLMAY NAPSLKEWID VIHKHDLSET
360 370 380 390 400
NVYLIGSTPG RFQGSQKDNW GHFRLKKLLK DHASSMPNAE SWPVVGQFSS
410 420 430 440 450
VGSLGADESK WLCSEFKESM LTLGKESKTP GKSSVPLYLI YPSVENVRTS
460 470 480 490 500
LEGYPAGGSL PYSIQTAEKQ NWLHSYFHKW SAETSGRSNA MPHIKTYMRP
510 520 530 540 550
SPDFSKIAWF LVTSANLSKA AWGALEKNGT QLMIRSYELG VLFLPSAFGL
560 570 580 590 600
DSFKVKQKFF AGSQEPMATF PVPYDLPPEL YGSKDRPWIW NIPYVKAPDT

HGNMWVPS
Length:608
Mass (Da):68,420
Last modified:October 24, 2003 - v2
Checksum:iF30202BD8329E5CE
GO
Isoform 2 (identifier: Q9NUW8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-25: MSQEGDYGRWTISSSDESEEEKPKP → MVISERLRLTSMPRPSLTRTSLSAR
     26-264: Missing.

Note: No experimental confirmation available.

Show »
Length:369
Mass (Da):41,630
Checksum:i8674BAEED98FA149
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti389 – 3891A → P in BAA91997. (PubMed:14702039)Curated
Sequence conflicti511 – 5111L → R in AAF65624. (PubMed:10521354)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951E → D.1 Publication
Corresponds to variant rs35114462 [ dbSNP | Ensembl ].
VAR_025817
Natural varianti101 – 1011P → L.1 Publication
Corresponds to variant rs35455108 [ dbSNP | Ensembl ].
VAR_025818
Natural varianti134 – 1341A → T.1 Publication
Corresponds to variant rs28365054 [ dbSNP | Ensembl ].
VAR_025819
Natural varianti187 – 1871D → G.1 Publication
Corresponds to variant rs35271143 [ dbSNP | Ensembl ].
VAR_025820
Natural varianti304 – 3041R → Q.1 Publication
Corresponds to variant rs34452707 [ dbSNP | Ensembl ].
VAR_025821
Natural varianti493 – 4931H → R in SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA. 1 Publication
VAR_017144
Natural varianti566 – 5661P → L in autosomal recessive or sporadic spinocerebellar ataxia affected Japanese individuals. 1 Publication
VAR_017145
Natural varianti569 – 5691T → A.1 Publication
Corresponds to variant rs35973343 [ dbSNP | Ensembl ].
VAR_025822

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 2525MSQEG…EKPKP → MVISERLRLTSMPRPSLTRT SLSAR in isoform 2. 1 PublicationVSP_055765Add
BLAST
Alternative sequencei26 – 264239Missing in isoform 2. 1 PublicationVSP_055766Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX161451 mRNA. Translation: CAD61915.1.
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.
CCDSiCCDS9888.1. [Q9NUW8-1]
RefSeqiNP_001008744.1. NM_001008744.1. [Q9NUW8-1]
NP_060789.2. NM_018319.3. [Q9NUW8-1]
XP_005267904.1. XM_005267847.1. [Q9NUW8-1]
XP_005267905.1. XM_005267848.1. [Q9NUW8-1]
XP_006720260.1. XM_006720197.1. [Q9NUW8-1]
XP_006720261.1. XM_006720198.1. [Q9NUW8-1]
UniGeneiHs.209945.

Genome annotation databases

EnsembliENST00000335725; ENSP00000337353; ENSG00000042088. [Q9NUW8-1]
ENST00000393454; ENSP00000377099; ENSG00000042088. [Q9NUW8-1]
GeneIDi55775.
KEGGihsa:55775.
UCSCiuc001xxy.3. human. [Q9NUW8-1]

Polymorphism databases

DMDMi37999797.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BX161451 mRNA. Translation: CAD61915.1 .
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 .
CCDSi CCDS9888.1. [Q9NUW8-1 ]
RefSeqi NP_001008744.1. NM_001008744.1. [Q9NUW8-1 ]
NP_060789.2. NM_018319.3. [Q9NUW8-1 ]
XP_005267904.1. XM_005267847.1. [Q9NUW8-1 ]
XP_005267905.1. XM_005267848.1. [Q9NUW8-1 ]
XP_006720260.1. XM_006720197.1. [Q9NUW8-1 ]
XP_006720261.1. XM_006720198.1. [Q9NUW8-1 ]
UniGenei Hs.209945.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1JY1 X-ray 1.69 A 149-608 [» ]
1MU7 X-ray 2.00 A/B 149-608 [» ]
1MU9 X-ray 2.05 A/B 149-608 [» ]
1NOP X-ray 2.30 A/B 149-608 [» ]
1QZQ X-ray 2.40 A/B 149-608 [» ]
1RFF X-ray 1.70 A/B 149-608 [» ]
1RFI X-ray 2.20 A/B 149-608 [» ]
1RG1 X-ray 2.10 A/B 149-608 [» ]
1RG2 X-ray 2.10 A/B 149-608 [» ]
1RGT X-ray 2.00 A/B 149-608 [» ]
1RGU X-ray 2.22 A/B 149-608 [» ]
1RH0 X-ray 2.30 A/B 149-608 [» ]
ProteinModelPortali Q9NUW8.
SMRi Q9NUW8. Positions 161-608.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 120890. 8 interactions.
IntActi Q9NUW8. 4 interactions.
MINTi MINT-3074488.
STRINGi 9606.ENSP00000337353.

Chemistry

BindingDBi Q9NUW8.
ChEMBLi CHEMBL1075138.

PTM databases

PhosphoSitei Q9NUW8.

Polymorphism databases

DMDMi 37999797.

Proteomic databases

MaxQBi Q9NUW8.
PaxDbi Q9NUW8.
PRIDEi Q9NUW8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000335725 ; ENSP00000337353 ; ENSG00000042088 . [Q9NUW8-1 ]
ENST00000393454 ; ENSP00000377099 ; ENSG00000042088 . [Q9NUW8-1 ]
GeneIDi 55775.
KEGGi hsa:55775.
UCSCi uc001xxy.3. human. [Q9NUW8-1 ]

Organism-specific databases

CTDi 55775.
GeneCardsi GC14P090422.
GeneReviewsi TDP1.
HGNCi HGNC:18884. TDP1.
MIMi 607198. gene.
607250. phenotype.
neXtProti NX_Q9NUW8.
Orphaneti 94124. Spinocerebellar ataxia type 1 with axonal neuropathy.
PharmGKBi PA421.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG274417.
GeneTreei ENSGT00390000002211.
HOGENOMi HOG000067775.
HOVERGENi HBG061242.
InParanoidi Q9NUW8.
KOi K10862.
OMAi NISLCQA.
PhylomeDBi Q9NUW8.
TreeFami TF105989.

Enzyme and pathway databases

Reactomei REACT_1201. Processing of DNA ends prior to end rejoining.
SABIO-RK Q9NUW8.

Miscellaneous databases

EvolutionaryTracei Q9NUW8.
GeneWikii TDP1.
GenomeRNAii 55775.
NextBioi 60841.
PROi Q9NUW8.
SOURCEi Search...

Gene expression databases

Bgeei Q9NUW8.
CleanExi HS_TDP1.
ExpressionAtlasi Q9NUW8. baseline and differential.
Genevestigatori Q9NUW8.

Family and domain databases

Gene3Di 3.30.870.20. 1 hit.
InterProi IPR010347. Tdp1.
IPR027415. TDP_C.
[Graphical view ]
PANTHERi PTHR12415. PTHR12415. 1 hit.
Pfami PF06087. Tyr-DNA_phospho. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Full-length cDNA libraries and normalization."
    Li W.B., Gruber C., Jessee J., Polayes D.
    Submitted (JUL-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Placenta.
  2. "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] (ISOFORM 1).
    Tissue: Placenta.
  3. 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.
  4. "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.
    , 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].
  5. "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: Pancreas.
  6. "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 (ISOFORM 1).
  7. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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.
  12. "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.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-61, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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, BIOPHYSICOCHEMICAL PROPERTIES.
  17. "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.
  18. "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.
  19. "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.
  20. "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.
  21. "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.
  22. "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.
  23. "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.
  24. Cited for: CHARACTERIZATION OF VARIANT SCAN1 ARG-493, TISSUE SPECIFICITY.

Entry informationi

Entry nameiTYDP1_HUMAN
AccessioniPrimary (citable) accession number: Q9NUW8
Secondary accession number(s): Q2HXX4
, Q86TV8, Q96BK7, Q9NZM7, Q9NZM8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2003
Last sequence update: October 24, 2003
Last modified: November 26, 2014
This is version 124 of the entry and version 2 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3