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Protein

Tyrosyl-DNA phosphodiesterase 1

Gene

TDP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
    Active sitei263Nucleophile2 Publications1
    Binding sitei265Substrate1 Publication1
    Active sitei493Proton donor/acceptor2 Publications1
    Binding sitei495Substrate1 Publication1

    GO - Molecular functioni

    • 3'-tyrosyl-DNA phosphodiesterase activity Source: UniProtKB
    • double-stranded DNA binding Source: UniProtKB
    • exonuclease activity Source: UniProtKB-KW
    • single-stranded DNA binding Source: UniProtKB

    GO - Biological processi

    • DNA repair Source: UniProtKB
    • double-strand break repair Source: UniProtKB
    • 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

    ReactomeiR-HSA-5693571. Nonhomologous End-Joining (NHEJ).
    SABIO-RKQ9NUW8.
    SIGNORiQ9NUW8.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tyrosyl-DNA phosphodiesterase 1 (EC:3.1.4.-3 Publications)
    Short name:
    Tyr-DNA phosphodiesterase 1
    Gene namesi
    Name:TDP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:18884. TDP1.

    Subcellular locationi

    GO - Cellular componenti

    • cytoplasm Source: UniProtKB
    • intracellular membrane-bounded organelle Source: HPA
    • nucleus Source: HPA
    • plasma membrane Source: HPA
    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Spinocerebellar ataxia, autosomal recessive, with axonal neuropathy (SCAN1)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionSpinocerebellar 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.
    See also OMIM:607250
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_017144493H → R in SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA. 5 PublicationsCorresponds to variant rs119467003dbSNPEnsembl.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi263H → A: Loss of activity. 2 Publications1
    Mutagenesisi265K → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 2 Publications1
    Mutagenesisi265K → S: Reduces the activity to nearly undetectable levels. 2 Publications1
    Mutagenesisi283N → A: No effect. 1 Publication1
    Mutagenesisi294Q → A: Slightly reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 1 Publication1
    Mutagenesisi493H → A: 3000-fold reduction in activity; abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 2 Publications1
    Mutagenesisi493H → N: 15000-fold reduction in activity. 2 Publications1
    Mutagenesisi495K → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 2 Publications1
    Mutagenesisi495K → S: 125-fold reduction in activity. 2 Publications1
    Mutagenesisi516N → A: Reduced hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 1 Publication1
    Mutagenesisi538E → A: Abolishes hydrolysis of the covalent intermediate between the active site nucleophile and DNA. 1 Publication1

    Keywords - Diseasei

    Disease mutation, Neurodegeneration

    Organism-specific databases

    DisGeNETi55775.
    MalaCardsiTDP1.
    MIMi607250. phenotype.
    OpenTargetsiENSG00000042088.
    Orphaneti94124. Spinocerebellar ataxia type 1 with axonal neuropathy.
    PharmGKBiPA421.

    Chemistry databases

    ChEMBLiCHEMBL1075138.

    Polymorphism and mutation databases

    BioMutaiTDP1.
    DMDMi37999797.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00002124861 – 608Tyrosyl-DNA phosphodiesterase 1Add BLAST608

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Modified residuei61PhosphoserineCombined sources1
    Modified residuei147PhosphothreonineCombined sources1
    Modified residuei148PhosphoserineCombined sources1

    Post-translational modificationi

    Phosphorylated on serine and/or threonine residues, but not on tyrosine residues.1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    EPDiQ9NUW8.
    MaxQBiQ9NUW8.
    PaxDbiQ9NUW8.
    PeptideAtlasiQ9NUW8.
    PRIDEiQ9NUW8.

    PTM databases

    iPTMnetiQ9NUW8.
    PhosphoSitePlusiQ9NUW8.

    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

    BgeeiENSG00000042088.
    CleanExiHS_TDP1.
    ExpressionAtlasiQ9NUW8. baseline and differential.
    GenevisibleiQ9NUW8. HS.

    Organism-specific databases

    HPAiHPA071317.

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Sitei518Interaction with DNA1 Publication1

    Protein-protein interaction databases

    BioGridi120890. 10 interactors.
    IntActiQ9NUW8. 4 interactors.
    MINTiMINT-3074488.
    STRINGi9606.ENSP00000337353.

    Chemistry databases

    BindingDBiQ9NUW8.

    Structurei

    Secondary structure

    1608
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Turni149 – 151Combined sources3
    Helixi154 – 156Combined sources3
    Beta strandi166 – 169Combined sources4
    Helixi176 – 179Combined sources4
    Helixi185 – 188Combined sources4
    Helixi191 – 193Combined sources3
    Beta strandi196 – 202Combined sources7
    Beta strandi204 – 206Combined sources3
    Helixi208 – 214Combined sources7
    Helixi217 – 219Combined sources3
    Beta strandi224 – 228Combined sources5
    Helixi232 – 242Combined sources11
    Beta strandi248 – 252Combined sources5
    Beta strandi266 – 273Combined sources8
    Beta strandi275 – 280Combined sources6
    Helixi286 – 289Combined sources4
    Beta strandi291 – 293Combined sources3
    Beta strandi295 – 298Combined sources4
    Helixi319 – 328Combined sources10
    Helixi333 – 335Combined sources3
    Helixi336 – 343Combined sources8
    Beta strandi352 – 357Combined sources6
    Beta strandi359 – 363Combined sources5
    Helixi364 – 369Combined sources6
    Helixi371 – 382Combined sources12
    Helixi389 – 391Combined sources3
    Beta strandi394 – 397Combined sources4
    Turni408 – 415Combined sources8
    Helixi416 – 420Combined sources5
    Beta strandi437 – 440Combined sources4
    Helixi444 – 448Combined sources5
    Beta strandi450 – 452Combined sources3
    Helixi454 – 459Combined sources6
    Helixi464 – 467Combined sources4
    Helixi471 – 476Combined sources6
    Helixi483 – 485Combined sources3
    Beta strandi495 – 500Combined sources6
    Beta strandi504 – 514Combined sources11
    Helixi519 – 522Combined sources4
    Beta strandi524 – 526Combined sources3
    Turni527 – 530Combined sources4
    Beta strandi531 – 534Combined sources4
    Beta strandi536 – 543Combined sources8
    Helixi545 – 548Combined sources4
    Beta strandi553 – 555Combined sources3
    Helixi566 – 568Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9NUW8.

    Family & Domainsi

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni400 – 403Interaction with DNA1 Publication4

    Sequence similaritiesi

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiKOG2031. Eukaryota.
    ENOG410XQPZ. LUCA.
    GeneTreeiENSGT00390000002211.
    HOGENOMiHOG000147157.
    HOVERGENiHBG061242.
    InParanoidiQ9NUW8.
    KOiK10862.
    OMAiNEPRYTC.
    OrthoDBiEOG091G0DQF.
    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. AlignAdd to basket

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti389A → P in BAA91997 (PubMed:14702039).Curated1
    Sequence conflicti511L → R in AAF65624 (PubMed:10521354).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_02581795E → D.1 PublicationCorresponds to variant rs35114462dbSNPEnsembl.1
    Natural variantiVAR_025818101P → L.1 PublicationCorresponds to variant rs35455108dbSNPEnsembl.1
    Natural variantiVAR_025819134A → T.1 PublicationCorresponds to variant rs28365054dbSNPEnsembl.1
    Natural variantiVAR_025820187D → G.1 PublicationCorresponds to variant rs35271143dbSNPEnsembl.1
    Natural variantiVAR_025821304R → Q.1 PublicationCorresponds to variant rs34452707dbSNPEnsembl.1
    Natural variantiVAR_017144493H → R in SCAN1; reduces enzyme activity and leads to the accumulation of covalent complexes between TDP1 and DNA. 5 PublicationsCorresponds to variant rs119467003dbSNPEnsembl.1
    Natural variantiVAR_017145566P → L in autosomal recessive or sporadic spinocerebellar ataxia affected Japanese individuals. 1 PublicationCorresponds to variant rs767298655dbSNPEnsembl.1
    Natural variantiVAR_025822569T → A.1 PublicationCorresponds to variant rs35973343dbSNPEnsembl.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Alternative sequenceiVSP_0557651 – 25MSQEG…EKPKP → MVISERLRLTSMPRPSLTRT SLSAR in isoform 2. 1 PublicationAdd BLAST25
    Alternative sequenceiVSP_05576626 – 264Missing in isoform 2. 1 PublicationAdd BLAST239

    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_005267847.2. [Q9NUW8-1]
    XP_005267905.1. XM_005267848.2. [Q9NUW8-1]
    XP_006720260.1. XM_006720197.3. [Q9NUW8-1]
    XP_006720261.1. XM_006720198.3. [Q9NUW8-1]
    XP_011535244.1. XM_011536942.2. [Q9NUW8-1]
    XP_011535245.1. XM_011536943.2. [Q9NUW8-1]
    XP_016876928.1. XM_017021439.1. [Q9NUW8-1]
    XP_016876931.1. XM_017021442.1. [Q9NUW8-2]
    XP_016876932.1. XM_017021443.1. [Q9NUW8-2]
    XP_016876933.1. XM_017021444.1. [Q9NUW8-2]
    UniGeneiHs.209945.

    Genome annotation databases

    EnsembliENST00000335725; ENSP00000337353; ENSG00000042088. [Q9NUW8-1]
    ENST00000393454; ENSP00000377099; ENSG00000042088. [Q9NUW8-1]
    GeneIDi55775.
    KEGGihsa:55775.
    UCSCiuc001xxy.4. human. [Q9NUW8-1]

    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.
    CCDSiCCDS9888.1. [Q9NUW8-1]
    RefSeqiNP_001008744.1. NM_001008744.1. [Q9NUW8-1]
    NP_060789.2. NM_018319.3. [Q9NUW8-1]
    XP_005267904.1. XM_005267847.2. [Q9NUW8-1]
    XP_005267905.1. XM_005267848.2. [Q9NUW8-1]
    XP_006720260.1. XM_006720197.3. [Q9NUW8-1]
    XP_006720261.1. XM_006720198.3. [Q9NUW8-1]
    XP_011535244.1. XM_011536942.2. [Q9NUW8-1]
    XP_011535245.1. XM_011536943.2. [Q9NUW8-1]
    XP_016876928.1. XM_017021439.1. [Q9NUW8-1]
    XP_016876931.1. XM_017021442.1. [Q9NUW8-2]
    XP_016876932.1. XM_017021443.1. [Q9NUW8-2]
    XP_016876933.1. XM_017021444.1. [Q9NUW8-2]
    UniGeneiHs.209945.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi120890. 10 interactors.
    IntActiQ9NUW8. 4 interactors.
    MINTiMINT-3074488.
    STRINGi9606.ENSP00000337353.

    Chemistry databases

    BindingDBiQ9NUW8.
    ChEMBLiCHEMBL1075138.

    PTM databases

    iPTMnetiQ9NUW8.
    PhosphoSitePlusiQ9NUW8.

    Polymorphism and mutation databases

    BioMutaiTDP1.
    DMDMi37999797.

    Proteomic databases

    EPDiQ9NUW8.
    MaxQBiQ9NUW8.
    PaxDbiQ9NUW8.
    PeptideAtlasiQ9NUW8.
    PRIDEiQ9NUW8.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000335725; ENSP00000337353; ENSG00000042088. [Q9NUW8-1]
    ENST00000393454; ENSP00000377099; ENSG00000042088. [Q9NUW8-1]
    GeneIDi55775.
    KEGGihsa:55775.
    UCSCiuc001xxy.4. human. [Q9NUW8-1]

    Organism-specific databases

    CTDi55775.
    DisGeNETi55775.
    GeneCardsiTDP1.
    GeneReviewsiTDP1.
    HGNCiHGNC:18884. TDP1.
    HPAiHPA071317.
    MalaCardsiTDP1.
    MIMi607198. gene.
    607250. phenotype.
    neXtProtiNX_Q9NUW8.
    OpenTargetsiENSG00000042088.
    Orphaneti94124. Spinocerebellar ataxia type 1 with axonal neuropathy.
    PharmGKBiPA421.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG2031. Eukaryota.
    ENOG410XQPZ. LUCA.
    GeneTreeiENSGT00390000002211.
    HOGENOMiHOG000147157.
    HOVERGENiHBG061242.
    InParanoidiQ9NUW8.
    KOiK10862.
    OMAiNEPRYTC.
    OrthoDBiEOG091G0DQF.
    PhylomeDBiQ9NUW8.
    TreeFamiTF105989.

    Enzyme and pathway databases

    ReactomeiR-HSA-5693571. Nonhomologous End-Joining (NHEJ).
    SABIO-RKQ9NUW8.
    SIGNORiQ9NUW8.

    Miscellaneous databases

    EvolutionaryTraceiQ9NUW8.
    GeneWikiiTDP1.
    GenomeRNAii55775.
    PROiQ9NUW8.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000042088.
    CleanExiHS_TDP1.
    ExpressionAtlasiQ9NUW8. baseline and differential.
    GenevisibleiQ9NUW8. HS.

    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]
    ProtoNetiSearch...

    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 2, 2016
    This is version 142 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.