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O95271

- TNKS1_HUMAN

UniProt

O95271 - TNKS1_HUMAN

Protein

Tankyrase-1

Gene

TNKS

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 145 (01 Oct 2014)
      Sequence version 2 (14 Apr 2009)
      Previous versions | rss
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    Functioni

    Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking. Acts as an activator of the Wnt signaling pathway by mediating poly-ADP-ribosylation (PARsylation) of AXIN1 and AXIN2, 2 key components of the beta-catenin destruction complex: poly-ADP-ribosylated target proteins are recognized by RNF146, which mediates their ubiquitination and subsequent degradation. Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length. Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. May be involved in spindle pole assembly through PARsylation of NUMA1. Stimulates 26S proteasome activity.7 Publications

    Catalytic activityi

    NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.1 PublicationPROSITE-ProRule annotation

    Enzyme regulationi

    Specifically inhibited by XAV939, a small molecule, leading to inhibit the Wnt signaling pathway by stabilizing AXIN1 and AXIN2.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1234 – 12341Zinc
    Metal bindingi1237 – 12371Zinc
    Metal bindingi1242 – 12421Zinc
    Metal bindingi1245 – 12451Zinc

    GO - Molecular functioni

    1. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. zinc ion binding Source: BHF-UCL

    GO - Biological processi

    1. mitotic nuclear division Source: UniProtKB-KW
    2. mitotic spindle organization Source: BHF-UCL
    3. mRNA transport Source: UniProtKB-KW
    4. negative regulation of DNA binding Source: BHF-UCL
    5. peptidyl-serine phosphorylation Source: MGI
    6. peptidyl-threonine phosphorylation Source: MGI
    7. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    8. positive regulation of telomere maintenance via telomerase Source: BHF-UCL
    9. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    10. protein ADP-ribosylation Source: BHF-UCL
    11. protein auto-ADP-ribosylation Source: UniProtKB
    12. protein localization to chromosome, telomeric region Source: BHF-UCL
    13. protein poly-ADP-ribosylation Source: BHF-UCL
    14. protein polyubiquitination Source: UniProtKB
    15. protein transport Source: UniProtKB-KW
    16. regulation of telomere maintenance via telomerase Source: BHF-UCL
    17. spindle assembly Source: BHF-UCL
    18. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Cell cycle, Cell division, Mitosis, mRNA transport, Protein transport, Translocation, Transport, Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

    BRENDAi2.4.2.30. 2681.
    ReactomeiREACT_200766. degradation of AXIN.
    REACT_200777. TCF dependent signaling in response to WNT.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tankyrase-1 (EC:2.4.2.30)
    Short name:
    TANK1
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 5
    Short name:
    ARTD5
    Poly [ADP-ribose] polymerase 5A
    TNKS-1
    TRF1-interacting ankyrin-related ADP-ribose polymerase
    Tankyrase I
    Gene namesi
    Name:TNKS
    Synonyms:PARP5A, PARPL, TIN1, TINF1, TNKS1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:11941. TNKS.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Chromosomecentromere. Nucleusnuclear pore complex. Chromosometelomere Curated. Cytoplasmcytoskeletonspindle pole
    Note: Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1. Localizes to spindle poles at mitosis onset via interaction with NUMA1.

    GO - Cellular componenti

    1. chromosome, centromeric region Source: UniProtKB-SubCell
    2. chromosome, telomeric region Source: UniProtKB
    3. Golgi apparatus Source: UniProtKB
    4. Golgi membrane Source: UniProtKB-SubCell
    5. nuclear chromosome, telomeric region Source: BHF-UCL
    6. nuclear membrane Source: BHF-UCL
    7. nuclear pore Source: BHF-UCL
    8. nucleus Source: HPA
    9. pericentriolar material Source: BHF-UCL
    10. spindle pole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Centromere, Chromosome, Cytoplasm, Cytoskeleton, Golgi apparatus, Membrane, Nuclear pore complex, Nucleus, Telomere

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1184 – 11841H → A: Loss of activity; when associated with A-1291. 1 Publication
    Mutagenesisi1291 – 12911E → A: Loss of activity; when associated with A-1184. 1 Publication

    Organism-specific databases

    PharmGKBiPA36631.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 13271327Tankyrase-1PRO_0000211333Add
    BLAST

    Post-translational modificationi

    Phosphorylated on serine residues by MAPK kinases upon insulin stimulation. Phosphorylated during mitosis.1 Publication
    Ubiquitinated by RNF146 when auto-poly-ADP-ribosylated, leading to its degradation.1 Publication
    ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.1 Publication

    Keywords - PTMi

    ADP-ribosylation, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiO95271.
    PaxDbiO95271.
    PRIDEiO95271.

    PTM databases

    PhosphoSiteiO95271.

    Expressioni

    Tissue specificityi

    Ubiquitous; highest levels in testis.

    Gene expression databases

    ArrayExpressiO95271.
    BgeeiO95271.
    CleanExiHS_TNKS.
    GenevestigatoriO95271.

    Organism-specific databases

    HPAiHPA025690.

    Interactioni

    Subunit structurei

    Oligomerizes and associates with TNKS2. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of telomeric TERF1 via the ANK repeats. Found in a complex with POT1; TERF1 and TINF2. Interacts with AXIN1, AXIN2, BLZF1 and CASC3.4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Axin1O356254EBI-1105254,EBI-2365912From a different organism.
    CENPJQ9HC774EBI-1105254,EBI-946194
    FNBP1Q96RU34EBI-1105254,EBI-1111248
    HIF1ANQ9NWT62EBI-1105254,EBI-745632

    Protein-protein interaction databases

    BioGridi114207. 20 interactions.
    DIPiDIP-36652N.
    IntActiO95271. 14 interactions.
    MINTiMINT-7026707.
    STRINGi9606.ENSP00000311579.

    Structurei

    Secondary structure

    1
    1327
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi1107 – 11104
    Helixi1116 – 112611
    Turni1133 – 11397
    Beta strandi1143 – 115412
    Helixi1156 – 117116
    Turni1172 – 11754
    Beta strandi1179 – 11846
    Helixi1189 – 11957
    Helixi1199 – 12013
    Turni1203 – 12053
    Beta strandi1210 – 12178
    Helixi1218 – 12225
    Turni1223 – 12264
    Helixi1228 – 12303
    Turni1235 – 12373
    Beta strandi1243 – 12453
    Beta strandi1247 – 12559
    Beta strandi1258 – 12636
    Beta strandi1268 – 12703
    Beta strandi1276 – 12805
    Beta strandi1284 – 12863
    Beta strandi1287 – 12893
    Beta strandi1291 – 12966
    Helixi1297 – 12993
    Beta strandi1300 – 131112

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RF5X-ray2.30A1091-1325[»]
    3UDDX-ray1.95A/B1105-1327[»]
    3UH2X-ray2.00A/B1105-1327[»]
    3UH4X-ray2.00A/B1105-1327[»]
    4DVIX-ray1.90A/B1104-1314[»]
    4I9IX-ray2.40A/B/C/D1104-1314[»]
    4K4EX-ray2.30A/B1104-1314[»]
    4K4FX-ray2.90A/B1104-1314[»]
    4KRSX-ray2.29A/B1105-1327[»]
    4LI6X-ray2.05A/B1105-1327[»]
    4LI7X-ray2.20A/B1105-1327[»]
    4LI8X-ray2.52A/B1105-1327[»]
    4MSGX-ray1.80A/B1104-1314[»]
    4MSKX-ray2.30A/B/C/D1104-1314[»]
    4MT9X-ray2.00A/B1104-1314[»]
    4N3RX-ray1.90A/B1104-1314[»]
    4N4VX-ray2.00A/B1104-1314[»]
    ProteinModelPortaliO95271.
    SMRiO95271. Positions 144-986, 1030-1089, 1105-1314.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO95271.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati215 – 24733ANK 1Add
    BLAST
    Repeati248 – 28033ANK 2Add
    BLAST
    Repeati281 – 31333ANK 3Add
    BLAST
    Repeati368 – 40033ANK 4Add
    BLAST
    Repeati401 – 43333ANK 5Add
    BLAST
    Repeati434 – 46633ANK 6Add
    BLAST
    Repeati521 – 55636ANK 7Add
    BLAST
    Repeati557 – 58933ANK 8Add
    BLAST
    Repeati590 – 62233ANK 9Add
    BLAST
    Repeati683 – 71533ANK 10Add
    BLAST
    Repeati716 – 74833ANK 11Add
    BLAST
    Repeati749 – 78133ANK 12Add
    BLAST
    Repeati836 – 86833ANK 13Add
    BLAST
    Repeati869 – 90133ANK 14Add
    BLAST
    Repeati902 – 93433ANK 15Add
    BLAST
    Domaini1030 – 108960SAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini1112 – 1317206PARP catalyticPROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi9 – 146Poly-His
    Compositional biasi27 – 348Poly-Pro
    Compositional biasi128 – 1347Poly-Ser
    Compositional biasi137 – 1459Poly-Ser

    Sequence similaritiesi

    Contains 15 ANK repeats.PROSITE-ProRule annotation
    Contains 1 PARP catalytic domain.PROSITE-ProRule annotation
    Contains 1 SAM (sterile alpha motif) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    ANK repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG0666.
    HOGENOMiHOG000246964.
    HOVERGENiHBG059472.
    InParanoidiO95271.
    KOiK10799.
    OMAiDDKEYQS.
    PhylomeDBiO95271.
    TreeFamiTF326036.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    1.25.40.20. 8 hits.
    3.90.228.10. 1 hit.
    InterProiIPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR028731. TNKS.
    [Graphical view]
    PANTHERiPTHR24180:SF3. PTHR24180:SF3. 1 hit.
    PfamiPF00023. Ank. 12 hits.
    PF12796. Ank_2. 1 hit.
    PF00644. PARP. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 17 hits.
    SM00454. SAM. 1 hit.
    [Graphical view]
    SUPFAMiSSF47769. SSF47769. 1 hit.
    SSF48403. SSF48403. 4 hits.
    PROSITEiPS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 15 hits.
    PS51059. PARP_CATALYTIC. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O95271-1) [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

    MAASRRSQHH HHHHQQQLQP APGASAPPPP PPPPLSPGLA PGTTPASPTA     50
    SGLAPFASPR HGLALPEGDG SRDPPDRPRS PDPVDGTSCC STTSTICTVA 100
    AAPVVPAVST SSAAGVAPNP AGSGSNNSPS SSSSPTSSSS SSPSSPGSSL 150
    AESPEAAGVS STAPLGPGAA GPGTGVPAVS GALRELLEAC RNGDVSRVKR 200
    LVDAANVNAK DMAGRKSSPL HFAAGFGRKD VVEHLLQMGA NVHARDDGGL 250
    IPLHNACSFG HAEVVSLLLC QGADPNARDN WNYTPLHEAA IKGKIDVCIV 300
    LLQHGADPNI RNTDGKSALD LADPSAKAVL TGEYKKDELL EAARSGNEEK 350
    LMALLTPLNV NCHASDGRKS TPLHLAAGYN RVRIVQLLLQ HGADVHAKDK 400
    GGLVPLHNAC SYGHYEVTEL LLKHGACVNA MDLWQFTPLH EAASKNRVEV 450
    CSLLLSHGAD PTLVNCHGKS AVDMAPTPEL RERLTYEFKG HSLLQAAREA 500
    DLAKVKKTLA LEIINFKQPQ SHETALHCAV ASLHPKRKQV TELLLRKGAN 550
    VNEKNKDFMT PLHVAAERAH NDVMEVLHKH GAKMNALDTL GQTALHRAAL 600
    AGHLQTCRLL LSYGSDPSII SLQGFTAAQM GNEAVQQILS ESTPIRTSDV 650
    DYRLLEASKA GDLETVKQLC SSQNVNCRDL EGRHSTPLHF AAGYNRVSVV 700
    EYLLHHGADV HAKDKGGLVP LHNACSYGHY EVAELLVRHG ASVNVADLWK 750
    FTPLHEAAAK GKYEICKLLL KHGADPTKKN RDGNTPLDLV KEGDTDIQDL 800
    LRGDAALLDA AKKGCLARVQ KLCTPENINC RDTQGRNSTP LHLAAGYNNL 850
    EVAEYLLEHG ADVNAQDKGG LIPLHNAASY GHVDIAALLI KYNTCVNATD 900
    KWAFTPLHEA AQKGRTQLCA LLLAHGADPT MKNQEGQTPL DLATADDIRA 950
    LLIDAMPPEA LPTCFKPQAT VVSASLISPA STPSCLSAAS SIDNLTGPLA 1000
    ELAVGGASNA GDGAAGTERK EGEVAGLDMN ISQFLKSLGL EHLRDIFETE 1050
    QITLDVLADM GHEELKEIGI NAYGHRHKLI KGVERLLGGQ QGTNPYLTFH 1100
    CVNQGTILLD LAPEDKEYQS VEEEMQSTIR EHRDGGNAGG IFNRYNVIRI 1150
    QKVVNKKLRE RFCHRQKEVS EENHNHHNER MLFHGSPFIN AIIHKGFDER 1200
    HAYIGGMFGA GIYFAENSSK SNQYVYGIGG GTGCPTHKDR SCYICHRQML 1250
    FCRVTLGKSF LQFSTMKMAH APPGHHSVIG RPSVNGLAYA EYVIYRGEQA 1300
    YPEYLITYQI MKPEAPSQTA TAAEQKT 1327
    Length:1,327
    Mass (Da):142,039
    Last modified:April 14, 2009 - v2
    Checksum:i44BDE985C715BEFF
    GO
    Isoform 2 (identifier: O95271-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         641-643: EST → GHS
         644-1327: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:643
    Mass (Da):67,203
    Checksum:iFA67DE30C2A2F3B8
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti83 – 831P → Q in AAH98394. (PubMed:15489334)Curated
    Sequence conflicti802 – 8021R → K in AAC79841. (PubMed:9822378)Curated
    Sequence conflicti802 – 8021R → K in AAC79842. (PubMed:9822378)Curated
    Sequence conflicti1001 – 10011E → G in AAH98394. (PubMed:15489334)Curated
    Sequence conflicti1266 – 12661M → I in AAH98394. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei641 – 6433EST → GHS in isoform 2. 1 PublicationVSP_004538
    Alternative sequencei644 – 1327684Missing in isoform 2. 1 PublicationVSP_004539Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082556 mRNA. Translation: AAC79841.1.
    AF082557 mRNA. Translation: AAC79842.1.
    AF082558 mRNA. Translation: AAC79843.1.
    AF082559 mRNA. Translation: AAC79844.1.
    AC103834 Genomic DNA. No translation available.
    AC103877 Genomic DNA. No translation available.
    AC104052 Genomic DNA. No translation available.
    AC021242 Genomic DNA. No translation available.
    BC098394 mRNA. Translation: AAH98394.1.
    CCDSiCCDS5974.1. [O95271-1]
    RefSeqiNP_003738.2. NM_003747.2. [O95271-1]
    UniGeneiHs.370267.

    Genome annotation databases

    EnsembliENST00000310430; ENSP00000311579; ENSG00000173273. [O95271-1]
    ENST00000518635; ENSP00000431098; ENSG00000173273.
    GeneIDi8658.
    KEGGihsa:8658.
    UCSCiuc003wss.3. human. [O95271-1]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF082556 mRNA. Translation: AAC79841.1 .
    AF082557 mRNA. Translation: AAC79842.1 .
    AF082558 mRNA. Translation: AAC79843.1 .
    AF082559 mRNA. Translation: AAC79844.1 .
    AC103834 Genomic DNA. No translation available.
    AC103877 Genomic DNA. No translation available.
    AC104052 Genomic DNA. No translation available.
    AC021242 Genomic DNA. No translation available.
    BC098394 mRNA. Translation: AAH98394.1 .
    CCDSi CCDS5974.1. [O95271-1 ]
    RefSeqi NP_003738.2. NM_003747.2. [O95271-1 ]
    UniGenei Hs.370267.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RF5 X-ray 2.30 A 1091-1325 [» ]
    3UDD X-ray 1.95 A/B 1105-1327 [» ]
    3UH2 X-ray 2.00 A/B 1105-1327 [» ]
    3UH4 X-ray 2.00 A/B 1105-1327 [» ]
    4DVI X-ray 1.90 A/B 1104-1314 [» ]
    4I9I X-ray 2.40 A/B/C/D 1104-1314 [» ]
    4K4E X-ray 2.30 A/B 1104-1314 [» ]
    4K4F X-ray 2.90 A/B 1104-1314 [» ]
    4KRS X-ray 2.29 A/B 1105-1327 [» ]
    4LI6 X-ray 2.05 A/B 1105-1327 [» ]
    4LI7 X-ray 2.20 A/B 1105-1327 [» ]
    4LI8 X-ray 2.52 A/B 1105-1327 [» ]
    4MSG X-ray 1.80 A/B 1104-1314 [» ]
    4MSK X-ray 2.30 A/B/C/D 1104-1314 [» ]
    4MT9 X-ray 2.00 A/B 1104-1314 [» ]
    4N3R X-ray 1.90 A/B 1104-1314 [» ]
    4N4V X-ray 2.00 A/B 1104-1314 [» ]
    ProteinModelPortali O95271.
    SMRi O95271. Positions 144-986, 1030-1089, 1105-1314.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114207. 20 interactions.
    DIPi DIP-36652N.
    IntActi O95271. 14 interactions.
    MINTi MINT-7026707.
    STRINGi 9606.ENSP00000311579.

    Chemistry

    BindingDBi O95271.
    ChEMBLi CHEMBL6164.

    PTM databases

    PhosphoSitei O95271.

    Proteomic databases

    MaxQBi O95271.
    PaxDbi O95271.
    PRIDEi O95271.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000310430 ; ENSP00000311579 ; ENSG00000173273 . [O95271-1 ]
    ENST00000518635 ; ENSP00000431098 ; ENSG00000173273 .
    GeneIDi 8658.
    KEGGi hsa:8658.
    UCSCi uc003wss.3. human. [O95271-1 ]

    Organism-specific databases

    CTDi 8658.
    GeneCardsi GC08P009450.
    H-InvDB HIX0034248.
    HGNCi HGNC:11941. TNKS.
    HPAi HPA025690.
    MIMi 603303. gene.
    neXtProti NX_O95271.
    PharmGKBi PA36631.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000246964.
    HOVERGENi HBG059472.
    InParanoidi O95271.
    KOi K10799.
    OMAi DDKEYQS.
    PhylomeDBi O95271.
    TreeFami TF326036.

    Enzyme and pathway databases

    BRENDAi 2.4.2.30. 2681.
    Reactomei REACT_200766. degradation of AXIN.
    REACT_200777. TCF dependent signaling in response to WNT.

    Miscellaneous databases

    ChiTaRSi TNKS. human.
    EvolutionaryTracei O95271.
    GeneWikii TNKS.
    GenomeRNAii 8658.
    NextBioi 32469.
    PROi O95271.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O95271.
    Bgeei O95271.
    CleanExi HS_TNKS.
    Genevestigatori O95271.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    1.25.40.20. 8 hits.
    3.90.228.10. 1 hit.
    InterProi IPR002110. Ankyrin_rpt.
    IPR020683. Ankyrin_rpt-contain_dom.
    IPR012317. Poly(ADP-ribose)pol_cat_dom.
    IPR001660. SAM.
    IPR013761. SAM/pointed.
    IPR011510. SAM_2.
    IPR028731. TNKS.
    [Graphical view ]
    PANTHERi PTHR24180:SF3. PTHR24180:SF3. 1 hit.
    Pfami PF00023. Ank. 12 hits.
    PF12796. Ank_2. 1 hit.
    PF00644. PARP. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 17 hits.
    SM00454. SAM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47769. SSF47769. 1 hit.
    SSF48403. SSF48403. 4 hits.
    PROSITEi PS50297. ANK_REP_REGION. 1 hit.
    PS50088. ANK_REPEAT. 15 hits.
    PS51059. PARP_CATALYTIC. 1 hit.
    PS50105. SAM_DOMAIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Tankyrase, a poly(ADP-ribose) polymerase at human telomeres."
      Smith S., Giriat I., Schmitt A., de Lange T.
      Science 282:1484-1487(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Testis.
    2. "DNA sequence and analysis of human chromosome 8."
      Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
      , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
      Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. "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: Testis.
    4. "Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes."
      Smith S., de Lange T.
      J. Cell Sci. 112:3649-3656(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION.
    5. "Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles."
      Chi N.-W., Lodish H.F.
      J. Biol. Chem. 275:38437-38444(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PHOSPHORYLATION.
    6. "Role for the related poly(ADP-Ribose) polymerases tankyrase 1 and 2 at human telomeres."
      Cook B.D., Dynek J.N., Chang W., Shostak G., Smith S.
      Mol. Cell. Biol. 22:332-342(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF HIS-1184 AND GLU-1291.
    7. "POT1 as a terminal transducer of TRF1 telomere length control."
      Loayza D., De Lange T.
      Nature 423:1013-1018(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION IN A COMPLEX WITH POT1; TERF1 AND TINF2.
    8. "NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis."
      Chang W., Dynek J.N., Smith S.
      Biochem. J. 391:177-184(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH AXIN1 AND AXIN2.
    10. "Toward a unified nomenclature for mammalian ADP-ribosyltransferases."
      Hottiger M.O., Hassa P.O., Luscher B., Schuler H., Koch-Nolte F.
      Trends Biochem. Sci. 35:208-219(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: NOMENCLATURE.
    11. "RNF146 is a poly(ADP-ribose)-directed E3 ligase that regulates axin degradation and Wnt signalling."
      Zhang Y., Liu S., Mickanin C., Feng Y., Charlat O., Michaud G.A., Schirle M., Shi X., Hild M., Bauer A., Myer V.E., Finan P.M., Porter J.A., Huang S.M., Cong F.
      Nat. Cell Biol. 13:623-629(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND CASC3, UBIQUITINATION.
    12. Cited for: INTERACTION WITH AXIN1, SUBCELLULAR LOCATION.
    13. "Poly-ADP ribosylation of Miki by tankyrase-1 promotes centrosome maturation."
      Ozaki Y., Matsui H., Asou H., Nagamachi A., Aki D., Honda H., Yasunaga S., Takihara Y., Yamamoto T., Izumi S., Ohsugi M., Inaba T.
      Mol. Cell 47:694-706(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    14. "Proteasome regulation by ADP-ribosylation."
      Cho-Park P.F., Steller H.
      Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    15. Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1091-1325, ZINC-BINDING SITES.

    Entry informationi

    Entry nameiTNKS1_HUMAN
    AccessioniPrimary (citable) accession number: O95271
    Secondary accession number(s): O95272, Q4G0F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: April 14, 2009
    Last modified: October 1, 2014
    This is version 145 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 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3