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Q9H2K2

- TNKS2_HUMAN

UniProt

Q9H2K2 - TNKS2_HUMAN

Protein

Tankyrase-2

Gene

TNKS2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      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 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 poly-ADP-ribosylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination. Mediates poly-ADP-ribosylation of TERF1, thereby contributing to the regulation of telomere length. May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles. Stimulates 26S proteasome activity.5 Publications

    Catalytic activityi

    NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor.2 PublicationsPROSITE-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 bindingi1081 – 10811ZincBy similarity
    Metal bindingi1084 – 10841ZincBy similarity
    Metal bindingi1089 – 10891ZincBy similarity
    Metal bindingi1092 – 10921ZincBy similarity

    GO - Molecular functioni

    1. enzyme binding Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. NAD+ ADP-ribosyltransferase activity Source: UniProtKB
    4. protein binding Source: UniProtKB

    GO - Biological processi

    1. multicellular organism growth Source: Ensembl
    2. positive regulation of canonical Wnt signaling pathway Source: UniProtKB
    3. positive regulation of telomere maintenance via telomerase Source: BHF-UCL
    4. protein ADP-ribosylation Source: BHF-UCL
    5. protein auto-ADP-ribosylation Source: UniProtKB
    6. protein localization to chromosome, telomeric region Source: BHF-UCL
    7. protein polyubiquitination Source: UniProtKB
    8. regulation of multicellular organism growth Source: Ensembl
    9. Wnt signaling pathway Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosyltransferase, Transferase

    Keywords - Biological processi

    Wnt signaling pathway

    Keywords - Ligandi

    Metal-binding, NAD, Zinc

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tankyrase-2 (EC:2.4.2.30)
    Short name:
    TANK2
    Alternative name(s):
    ADP-ribosyltransferase diphtheria toxin-like 6
    Short name:
    ARTD6
    Poly [ADP-ribose] polymerase 5B
    TNKS-2
    TRF1-interacting ankyrin-related ADP-ribose polymerase 2
    Tankyrase II
    Tankyrase-like protein
    Tankyrase-related protein
    Gene namesi
    Name:TNKS2
    Synonyms:PARP5B, TANK2, TNKL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:15677. TNKS2.

    Subcellular locationi

    Cytoplasm. Golgi apparatus membrane; Peripheral membrane protein. Nucleus. Chromosometelomere Curated
    Note: Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles. Also found around the pericentriolar matrix of mitotic centromeres. During interphase, a small fraction of TNKS2 is found in the nucleus, associated with TRF1.

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. Golgi membrane Source: UniProtKB-SubCell
    3. nuclear chromosome, telomeric region Source: BHF-UCL
    4. nuclear envelope Source: BHF-UCL
    5. nucleus Source: BHF-UCL
    6. pericentriolar material Source: BHF-UCL
    7. perinuclear region of cytoplasm Source: BHF-UCL

    Keywords - Cellular componenti

    Chromosome, Cytoplasm, Golgi apparatus, Membrane, Nucleus, Telomere

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi553 – 5531H → D: Enhanced hydroxylation by HIF1AN. 1 Publication
    Mutagenesisi553 – 5531H → N: Enhanced hydroxylation by HIF1AN. 1 Publication
    Mutagenesisi1054 – 10541M → V: Loss of activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA38019.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 11661166Tankyrase-2PRO_0000211334Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei203 – 2031(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei238 – 2381(3S)-3-hydroxyhistidine; by HIF1AN; partial1 Publication
    Modified residuei271 – 2711(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei427 – 4271(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei518 – 5181(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei553 – 5531(3S)-3-hydroxyhistidine; by HIF1AN; partial1 Publication
    Modified residuei586 – 5861(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei671 – 6711(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei706 – 7061(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication
    Modified residuei739 – 7391(3S)-3-hydroxyasparagine; by HIF1AN; partial1 Publication

    Post-translational modificationi

    Ubiquitinated at 'Lys-48' and 'Lys-63' by RNF146 when auto-poly-ADP-ribosylated; this leads to degradation.
    ADP-ribosylated (-auto). Poly-ADP-ribosylated protein is recognized by RNF146, followed by ubiquitination.
    The crystallographic evidence suggests that the 3-hydroxyhistidine may be the (3S) stereoisomer.

    Keywords - PTMi

    ADP-ribosylation, Hydroxylation, Ubl conjugation

    Proteomic databases

    MaxQBiQ9H2K2.
    PaxDbiQ9H2K2.
    PRIDEiQ9H2K2.

    PTM databases

    PhosphoSiteiQ9H2K2.

    Expressioni

    Tissue specificityi

    Highly expressed in placenta, skeletal muscle, liver, brain, kidney, heart, thymus, spinal cord, lung, peripheral blood leukocytes, pancreas, lymph nodes, spleen, prostate, testis, ovary, small intestine, colon, mammary gland, breast and breast carcinoma, and in common-type meningioma. Highly expressed in fetal liver, heart and brain.

    Gene expression databases

    BgeeiQ9H2K2.
    CleanExiHS_TNKS2.
    GenevestigatoriQ9H2K2.

    Organism-specific databases

    HPAiHPA036606.

    Interactioni

    Subunit structurei

    Oligomerizes and associates with TNKS. Interacts with the cytoplasmic domain of LNPEP/Otase in SLC2A4/GLUT4-vesicles. Binds to the N-terminus of Grb14 and TRF1 with its ankyrin repeat region. Interacts with HIF1AN. Interacts with RNF146; this interaction leads to ubiquitination and proteasomal degradation.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ANKRD28O150843EBI-4398527,EBI-359567
    AXIN1O151692EBI-4398527,EBI-710484
    BABAM1Q9NWV84EBI-4398527,EBI-745725
    BCRP112743EBI-4398527,EBI-712838
    FAT4Q6V0I72EBI-4398527,EBI-948985
    HIF1ANQ9NWT63EBI-4398527,EBI-745632
    RAD54LQ926983EBI-4398527,EBI-5333483
    SH3BP2P783145EBI-4398527,EBI-727062
    Sh3bp2Q066496EBI-4398527,EBI-5323518From a different organism.
    STRNO438152EBI-4398527,EBI-1046642
    TERF1P542742EBI-4398527,EBI-710997

    Protein-protein interaction databases

    BioGridi123257. 11 interactions.
    DIPiDIP-42098N.
    IntActiQ9H2K2. 32 interactions.
    MINTiMINT-1183420.
    STRINGi9606.ENSP00000360689.

    Structurei

    Secondary structure

    1
    1166
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi491 – 50212
    Helixi505 – 5117
    Turni514 – 5185
    Turni522 – 5254
    Helixi529 – 5357
    Helixi539 – 5479
    Helixi562 – 5687
    Helixi572 – 5809
    Helixi595 – 6017
    Helixi605 – 6139
    Helixi629 – 6313
    Helixi637 – 6448
    Beta strandi954 – 9574
    Helixi963 – 97412
    Turni980 – 9867
    Beta strandi992 – 100110
    Helixi1003 – 101816
    Turni1019 – 10224
    Beta strandi1026 – 10316
    Helixi1036 – 10427
    Helixi1046 – 10483
    Beta strandi1057 – 10648
    Helixi1065 – 10695
    Turni1070 – 10734
    Helixi1075 – 10773
    Turni1082 – 10843
    Beta strandi1090 – 10923
    Beta strandi1094 – 11029
    Beta strandi1105 – 11117
    Beta strandi1115 – 11173
    Beta strandi1123 – 11319
    Beta strandi1138 – 11425
    Helixi1144 – 11463
    Beta strandi1147 – 115711

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2Y0IX-ray2.28S538-558[»]
    3KR7X-ray1.95A946-1162[»]
    3KR8X-ray2.10A/C946-1162[»]
    3MHJX-ray1.80A/B946-1162[»]
    3MHKX-ray2.30A952-1166[»]
    3P0NX-ray1.90A/C946-1162[»]
    3P0PX-ray2.49A/C946-1162[»]
    3P0QX-ray1.90A/C946-1162[»]
    3TWQX-ray2.15A/B484-655[»]
    3TWRX-ray1.55A/B/C/D488-649[»]
    3TWSX-ray1.70A/B/C/D488-649[»]
    3TWTX-ray1.85A/B/C/D488-649[»]
    3TWUX-ray1.80A488-649[»]
    3TWVX-ray2.30A/B/C/D488-649[»]
    3TWWX-ray2.00A/B488-649[»]
    3TWXX-ray1.80A/B488-649[»]
    3U9HX-ray1.75A/B946-1162[»]
    3U9YX-ray2.30A946-1162[»]
    3UA9X-ray2.15A/B946-1162[»]
    3W51X-ray2.00A/B952-1161[»]
    4AVUX-ray2.40A/B946-1162[»]
    4AVWX-ray2.15A/B946-1162[»]
    4BFPX-ray2.40A/B946-1162[»]
    4BJ9X-ray2.05A/B946-1162[»]
    4BJBX-ray2.30A946-1162[»]
    4BJCX-ray2.20A946-1162[»]
    4BS4X-ray1.89A/B946-1162[»]
    4BU3X-ray2.15A/B946-1162[»]
    4BU5X-ray1.80A/B946-1162[»]
    4BU6X-ray1.80A/B946-1162[»]
    4BU7X-ray2.05A/C946-1162[»]
    4BU8X-ray1.85A/C946-1162[»]
    4BU9X-ray1.65A/B946-1162[»]
    4BUAX-ray1.85A/C946-1162[»]
    4BUDX-ray2.50A/C946-1162[»]
    4BUEX-ray1.60A/B946-1162[»]
    4BUFX-ray2.50A/B946-1162[»]
    4BUIX-ray1.95A/C946-1162[»]
    4BUSX-ray1.90A/B946-1162[»]
    4BUTX-ray1.90A/B946-1162[»]
    4BUUX-ray1.60A/B946-1162[»]
    4BUVX-ray1.80A/C946-1162[»]
    4BUWX-ray1.85A/B946-1162[»]
    4BUXX-ray1.95A/C946-1162[»]
    4BUYX-ray1.90A/B946-1162[»]
    4HKIX-ray2.15A/H946-1113[»]
    C/D1114-1162[»]
    4HKKX-ray1.95A/C946-1113[»]
    B/D1114-1162[»]
    4HKNX-ray2.05A946-1113[»]
    C1114-1162[»]
    4HL5X-ray2.20A946-1113[»]
    C1114-1162[»]
    4HLFX-ray2.15A/B946-1113[»]
    C/D1114-1162[»]
    4HLGX-ray2.00A/B946-1113[»]
    C/D1114-1162[»]
    4HLHX-ray1.75A/B946-1113[»]
    C/D1114-1162[»]
    4HLKX-ray2.00A/B946-1113[»]
    C/D1114-1162[»]
    4HLMX-ray1.95A/B946-1113[»]
    C/D1114-1162[»]
    4HMHX-ray2.30A946-1113[»]
    C1114-1162[»]
    4HYFX-ray2.80A/B/C946-1162[»]
    4IUEX-ray2.38A952-1161[»]
    4J1ZX-ray2.00A/B952-1161[»]
    4J21X-ray1.93A952-1161[»]
    4J22X-ray2.12A/B952-1161[»]
    4J3LX-ray2.09A952-1161[»]
    4J3MX-ray1.90A/B952-1161[»]
    4KZLX-ray2.00A/B946-1113[»]
    C/D1114-1162[»]
    4KZQX-ray2.25A/B946-1113[»]
    C/D1114-1162[»]
    4KZUX-ray2.10A/B946-1113[»]
    C/D1114-1162[»]
    4L09X-ray2.05A/B946-1113[»]
    C/D1114-1162[»]
    4L0BX-ray1.80A/B946-1113[»]
    C/D1114-1162[»]
    4L0IX-ray2.30A/B946-1113[»]
    C/D1114-1162[»]
    4L0SX-ray1.90A/B946-1113[»]
    C/D1114-1162[»]
    4L0TX-ray2.10A/B946-1113[»]
    C/D1114-1162[»]
    4L0VX-ray1.70A/B946-1113[»]
    C/D1114-1162[»]
    4L10X-ray1.70A/B946-1113[»]
    C/D1114-1162[»]
    4L2FX-ray2.05A/B946-1113[»]
    C/D1114-1162[»]
    4L2GX-ray2.05A/B946-1113[»]
    C/D1114-1162[»]
    4L2KX-ray2.10A/B946-1113[»]
    C/D1114-1162[»]
    4L31X-ray2.00A/B946-1113[»]
    C/D1114-1162[»]
    4L32X-ray1.85A/B946-1113[»]
    C/D1114-1162[»]
    4L33X-ray2.10A/B946-1113[»]
    C/D1114-1162[»]
    4L34X-ray1.80A/B946-1113[»]
    C/D1114-1162[»]
    4M7BX-ray1.95A/C946-1162[»]
    ProteinModelPortaliQ9H2K2.
    SMRiQ9H2K2. Positions 24-826, 876-938, 952-1161.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9H2K2.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati57 – 8933ANK 1Add
    BLAST
    Repeati90 – 12233ANK 2Add
    BLAST
    Repeati123 – 15533ANK 3Add
    BLAST
    Repeati210 – 24233ANK 4Add
    BLAST
    Repeati243 – 27533ANK 5Add
    BLAST
    Repeati276 – 30833ANK 6Add
    BLAST
    Repeati363 – 39836ANK 7Add
    BLAST
    Repeati399 – 43133ANK 8Add
    BLAST
    Repeati432 – 46433ANK 9Add
    BLAST
    Repeati525 – 55733ANK 10Add
    BLAST
    Repeati558 – 59033ANK 11Add
    BLAST
    Repeati591 – 62333ANK 12Add
    BLAST
    Repeati678 – 71033ANK 13Add
    BLAST
    Repeati711 – 74333ANK 14Add
    BLAST
    Repeati744 – 77633ANK 15Add
    BLAST
    Domaini873 – 93664SAMPROSITE-ProRule annotationAdd
    BLAST
    Domaini959 – 1164206PARP catalyticPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni545 – 5539HIF1AN-binding

    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.
    InParanoidiQ9H2K2.
    KOiK10799.
    OMAiPYLTLNN.
    OrthoDBiEOG7N8ZTP.
    PhylomeDBiQ9H2K2.
    TreeFamiTF326036.

    Family and domain databases

    Gene3Di1.10.150.50. 1 hit.
    1.25.40.20. 7 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.
    [Graphical view]
    PfamiPF00023. Ank. 2 hits.
    PF12796. Ank_2. 5 hits.
    PF00644. PARP. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view]
    PRINTSiPR01415. ANKYRIN.
    SMARTiSM00248. ANK. 15 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]

    Sequencei

    Sequence statusi: Complete.

    Q9H2K2-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSGRRCAGGG AACASAAAEA VEPAARELFE ACRNGDVERV KRLVTPEKVN     50
    SRDTAGRKST PLHFAAGFGR KDVVEYLLQN GANVQARDDG GLIPLHNACS 100
    FGHAEVVNLL LRHGADPNAR DNWNYTPLHE AAIKGKIDVC IVLLQHGAEP 150
    TIRNTDGRTA LDLADPSAKA VLTGEYKKDE LLESARSGNE EKMMALLTPL 200
    NVNCHASDGR KSTPLHLAAG YNRVKIVQLL LQHGADVHAK DKGDLVPLHN 250
    ACSYGHYEVT ELLVKHGACV NAMDLWQFTP LHEAASKNRV EVCSLLLSYG 300
    ADPTLLNCHN KSAIDLAPTP QLKERLAYEF KGHSLLQAAR EADVTRIKKH 350
    LSLEMVNFKH PQTHETALHC AAASPYPKRK QICELLLRKG ANINEKTKEF 400
    LTPLHVASEK AHNDVVEVVV KHEAKVNALD NLGQTSLHRA AYCGHLQTCR 450
    LLLSYGCDPN IISLQGFTAL QMGNENVQQL LQEGISLGNS EADRQLLEAA 500
    KAGDVETVKK LCTVQSVNCR DIEGRQSTPL HFAAGYNRVS VVEYLLQHGA 550
    DVHAKDKGGL VPLHNACSYG HYEVAELLVK HGAVVNVADL WKFTPLHEAA 600
    AKGKYEICKL LLQHGADPTK KNRDGNTPLD LVKDGDTDIQ DLLRGDAALL 650
    DAAKKGCLAR VKKLSSPDNV NCRDTQGRHS TPLHLAAGYN NLEVAEYLLQ 700
    HGADVNAQDK GGLIPLHNAA SYGHVDVAAL LIKYNACVNA TDKWAFTPLH 750
    EAAQKGRTQL CALLLAHGAD PTLKNQEGQT PLDLVSADDV SALLTAAMPP 800
    SALPSCYKPQ VLNGVRSPGA TADALSSGPS SPSSLSAASS LDNLSGSFSE 850
    LSSVVSSSGT EGASSLEKKE VPGVDFSITQ FVRNLGLEHL MDIFEREQIT 900
    LDVLVEMGHK ELKEIGINAY GHRHKLIKGV ERLISGQQGL NPYLTLNTSG 950
    SGTILIDLSP DDKEFQSVEE EMQSTVREHR DGGHAGGIFN RYNILKIQKV 1000
    CNKKLWERYT HRRKEVSEEN HNHANERMLF HGSPFVNAII HKGFDERHAY 1050
    IGGMFGAGIY FAENSSKSNQ YVYGIGGGTG CPVHKDRSCY ICHRQLLFCR 1100
    VTLGKSFLQF SAMKMAHSPP GHHSVTGRPS VNGLALAEYV IYRGEQAYPE 1150
    YLITYQIMRP EGMVDG 1166
    Length:1,166
    Mass (Da):126,918
    Last modified:March 1, 2001 - v1
    Checksum:i4C8B3B8D97CEF704
    GO

    Sequence cautioni

    The sequence AAG25674.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.
    The sequence BAB14665.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti115 – 1151A → T in BAG37180. (PubMed:14702039)Curated
    Sequence conflicti331 – 3377KGHSLLQ → QRPLVAA in AAG25674. (PubMed:11205898)Curated
    Sequence conflicti357 – 3615NFKHP → IQAS in AAG25674. (PubMed:11205898)Curated
    Sequence conflicti966 – 9661Q → P in BAB14665. (PubMed:14702039)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305081 mRNA. Translation: AAG25674.1. Different initiation.
    AF264912 mRNA. Translation: AAG44694.1.
    AF329696 mRNA. Translation: AAK13463.1.
    AF342982 mRNA. Translation: AAK25811.1.
    AF309033 mRNA. Translation: AAK82330.1.
    AF438201 mRNA. Translation: AAL40795.1.
    AK023746 mRNA. Translation: BAB14665.1. Different initiation.
    AK314612 mRNA. Translation: BAG37180.1.
    AL359707 Genomic DNA. Translation: CAC78760.1.
    CCDSiCCDS7417.1.
    RefSeqiNP_079511.1. NM_025235.3.
    UniGeneiHs.329327.

    Genome annotation databases

    EnsembliENST00000371627; ENSP00000360689; ENSG00000107854.
    GeneIDi80351.
    KEGGihsa:80351.
    UCSCiuc001khp.3. human.

    Polymorphism databases

    DMDMi20140805.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF305081 mRNA. Translation: AAG25674.1 . Different initiation.
    AF264912 mRNA. Translation: AAG44694.1 .
    AF329696 mRNA. Translation: AAK13463.1 .
    AF342982 mRNA. Translation: AAK25811.1 .
    AF309033 mRNA. Translation: AAK82330.1 .
    AF438201 mRNA. Translation: AAL40795.1 .
    AK023746 mRNA. Translation: BAB14665.1 . Different initiation.
    AK314612 mRNA. Translation: BAG37180.1 .
    AL359707 Genomic DNA. Translation: CAC78760.1 .
    CCDSi CCDS7417.1.
    RefSeqi NP_079511.1. NM_025235.3.
    UniGenei Hs.329327.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2Y0I X-ray 2.28 S 538-558 [» ]
    3KR7 X-ray 1.95 A 946-1162 [» ]
    3KR8 X-ray 2.10 A/C 946-1162 [» ]
    3MHJ X-ray 1.80 A/B 946-1162 [» ]
    3MHK X-ray 2.30 A 952-1166 [» ]
    3P0N X-ray 1.90 A/C 946-1162 [» ]
    3P0P X-ray 2.49 A/C 946-1162 [» ]
    3P0Q X-ray 1.90 A/C 946-1162 [» ]
    3TWQ X-ray 2.15 A/B 484-655 [» ]
    3TWR X-ray 1.55 A/B/C/D 488-649 [» ]
    3TWS X-ray 1.70 A/B/C/D 488-649 [» ]
    3TWT X-ray 1.85 A/B/C/D 488-649 [» ]
    3TWU X-ray 1.80 A 488-649 [» ]
    3TWV X-ray 2.30 A/B/C/D 488-649 [» ]
    3TWW X-ray 2.00 A/B 488-649 [» ]
    3TWX X-ray 1.80 A/B 488-649 [» ]
    3U9H X-ray 1.75 A/B 946-1162 [» ]
    3U9Y X-ray 2.30 A 946-1162 [» ]
    3UA9 X-ray 2.15 A/B 946-1162 [» ]
    3W51 X-ray 2.00 A/B 952-1161 [» ]
    4AVU X-ray 2.40 A/B 946-1162 [» ]
    4AVW X-ray 2.15 A/B 946-1162 [» ]
    4BFP X-ray 2.40 A/B 946-1162 [» ]
    4BJ9 X-ray 2.05 A/B 946-1162 [» ]
    4BJB X-ray 2.30 A 946-1162 [» ]
    4BJC X-ray 2.20 A 946-1162 [» ]
    4BS4 X-ray 1.89 A/B 946-1162 [» ]
    4BU3 X-ray 2.15 A/B 946-1162 [» ]
    4BU5 X-ray 1.80 A/B 946-1162 [» ]
    4BU6 X-ray 1.80 A/B 946-1162 [» ]
    4BU7 X-ray 2.05 A/C 946-1162 [» ]
    4BU8 X-ray 1.85 A/C 946-1162 [» ]
    4BU9 X-ray 1.65 A/B 946-1162 [» ]
    4BUA X-ray 1.85 A/C 946-1162 [» ]
    4BUD X-ray 2.50 A/C 946-1162 [» ]
    4BUE X-ray 1.60 A/B 946-1162 [» ]
    4BUF X-ray 2.50 A/B 946-1162 [» ]
    4BUI X-ray 1.95 A/C 946-1162 [» ]
    4BUS X-ray 1.90 A/B 946-1162 [» ]
    4BUT X-ray 1.90 A/B 946-1162 [» ]
    4BUU X-ray 1.60 A/B 946-1162 [» ]
    4BUV X-ray 1.80 A/C 946-1162 [» ]
    4BUW X-ray 1.85 A/B 946-1162 [» ]
    4BUX X-ray 1.95 A/C 946-1162 [» ]
    4BUY X-ray 1.90 A/B 946-1162 [» ]
    4HKI X-ray 2.15 A/H 946-1113 [» ]
    C/D 1114-1162 [» ]
    4HKK X-ray 1.95 A/C 946-1113 [» ]
    B/D 1114-1162 [» ]
    4HKN X-ray 2.05 A 946-1113 [» ]
    C 1114-1162 [» ]
    4HL5 X-ray 2.20 A 946-1113 [» ]
    C 1114-1162 [» ]
    4HLF X-ray 2.15 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4HLG X-ray 2.00 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4HLH X-ray 1.75 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4HLK X-ray 2.00 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4HLM X-ray 1.95 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4HMH X-ray 2.30 A 946-1113 [» ]
    C 1114-1162 [» ]
    4HYF X-ray 2.80 A/B/C 946-1162 [» ]
    4IUE X-ray 2.38 A 952-1161 [» ]
    4J1Z X-ray 2.00 A/B 952-1161 [» ]
    4J21 X-ray 1.93 A 952-1161 [» ]
    4J22 X-ray 2.12 A/B 952-1161 [» ]
    4J3L X-ray 2.09 A 952-1161 [» ]
    4J3M X-ray 1.90 A/B 952-1161 [» ]
    4KZL X-ray 2.00 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4KZQ X-ray 2.25 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4KZU X-ray 2.10 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L09 X-ray 2.05 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L0B X-ray 1.80 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L0I X-ray 2.30 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L0S X-ray 1.90 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L0T X-ray 2.10 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L0V X-ray 1.70 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L10 X-ray 1.70 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L2F X-ray 2.05 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L2G X-ray 2.05 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L2K X-ray 2.10 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L31 X-ray 2.00 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L32 X-ray 1.85 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L33 X-ray 2.10 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4L34 X-ray 1.80 A/B 946-1113 [» ]
    C/D 1114-1162 [» ]
    4M7B X-ray 1.95 A/C 946-1162 [» ]
    ProteinModelPortali Q9H2K2.
    SMRi Q9H2K2. Positions 24-826, 876-938, 952-1161.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123257. 11 interactions.
    DIPi DIP-42098N.
    IntActi Q9H2K2. 32 interactions.
    MINTi MINT-1183420.
    STRINGi 9606.ENSP00000360689.

    Chemistry

    BindingDBi Q9H2K2.
    ChEMBLi CHEMBL6154.

    PTM databases

    PhosphoSitei Q9H2K2.

    Polymorphism databases

    DMDMi 20140805.

    Proteomic databases

    MaxQBi Q9H2K2.
    PaxDbi Q9H2K2.
    PRIDEi Q9H2K2.

    Protocols and materials databases

    DNASUi 80351.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371627 ; ENSP00000360689 ; ENSG00000107854 .
    GeneIDi 80351.
    KEGGi hsa:80351.
    UCSCi uc001khp.3. human.

    Organism-specific databases

    CTDi 80351.
    GeneCardsi GC10P093548.
    HGNCi HGNC:15677. TNKS2.
    HPAi HPA036606.
    MIMi 607128. gene.
    neXtProti NX_Q9H2K2.
    PharmGKBi PA38019.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0666.
    HOGENOMi HOG000246964.
    HOVERGENi HBG059472.
    InParanoidi Q9H2K2.
    KOi K10799.
    OMAi PYLTLNN.
    OrthoDBi EOG7N8ZTP.
    PhylomeDBi Q9H2K2.
    TreeFami TF326036.

    Enzyme and pathway databases

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

    Miscellaneous databases

    ChiTaRSi TNKS2. human.
    EvolutionaryTracei Q9H2K2.
    GeneWikii TNKS2.
    GenomeRNAii 80351.
    NextBioi 70966.
    PROi Q9H2K2.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q9H2K2.
    CleanExi HS_TNKS2.
    Genevestigatori Q9H2K2.

    Family and domain databases

    Gene3Di 1.10.150.50. 1 hit.
    1.25.40.20. 7 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.
    [Graphical view ]
    Pfami PF00023. Ank. 2 hits.
    PF12796. Ank_2. 5 hits.
    PF00644. PARP. 1 hit.
    PF07647. SAM_2. 1 hit.
    [Graphical view ]
    PRINTSi PR01415. ANKYRIN.
    SMARTi SM00248. ANK. 15 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. "Novel tankyrase-related gene detected with meningioma-specific sera."
      Monz D., Munnia A., Comtesse N., Fischer U., Steudel W.-I., Feiden W., Glass B., Meese E.U.
      Clin. Cancer Res. 7:113-119(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal brain.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Mammary carcinoma.
    3. "Identification of a novel human tankyrase through its interaction with the adaptor protein Grb14."
      Lyons R.J., Deane R., Lynch D.K., Ye Z.-S.J., Sanderson G.M., Eyre H.J., Sutherland G.R., Daly R.J.
      J. Biol. Chem. 276:17172-17180(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Tissue: Liver.
    4. "TANK2, a new TRF1-associated poly(ADP-ribose) polymerase, causes rapid induction of cell death upon overexpression."
      Kaminker P.G., Kim S.-H., Taylor R.D., Zebarjadian Y., Funk W.D., Morin G.B., Yaswen P., Campisi J.
      J. Biol. Chem. 276:35891-35899(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
      Tissue: Placenta.
    5. "Tankyrase-2 oligomerizes with tankyrase-1 and binds to both TRF1 (telomere-repeat-binding factor 1) and IRAP (insulin-responsive aminopeptidase)."
      Sbodio J.I., Lodish H.F., Chi N.-W.
      Biochem. J. 361:451-459(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH TRF1 AND LNPEP/OTASE.
      Tissue: Skeletal muscle.
    6. Yin Y., Gelmann E.P.
      Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    7. "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].
      Tissue: Placenta and Testis.
    8. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. "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, ADP-RIBOSYLATION.
    10. "Proteomics-based identification of novel factor inhibiting hypoxia-inducible factor (FIH) substrates indicates widespread asparaginyl hydroxylation of ankyrin repeat domain-containing proteins."
      Cockman M.E., Webb J.D., Kramer H.B., Kessler B.M., Ratcliffe P.J.
      Mol. Cell. Proteomics 8:535-546(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HIF1AN, HYDROXYLATION AT ASN-203; ASN-271; ASN-427; ASN-518; ASN-586; ASN-671; ASN-706 AND ASN-739.
    11. Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, INTERACTION WITH AXIN1 AND AXIN2, MUTAGENESIS OF MET-1054.
    12. "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.
    13. "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, CATALYTIC ACTIVITY, INTERACTION WITH AXIN1; AXIN2; BLZF1 AND CASC3, UBIQUITINATION.
    14. Cited for: INTERACTION WITH RNF146, UBIQUITINATION, SUBCELLULAR LOCATION.
    15. "Proteasome regulation by ADP-ribosylation."
      Cho-Park P.F., Steller H.
      Cell 153:614-627(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    16. "Factor-inhibiting hypoxia-inducible factor (FIH) catalyses the post-translational hydroxylation of histidinyl residues within ankyrin repeat domains."
      Yang M., Chowdhury R., Ge W., Hamed R.B., McDonough M.A., Claridge T.D., Kessler B.M., Cockman M.E., Ratcliffe P.J., Schofield C.J.
      FEBS J. 278:1086-1097(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 538-558 IN COMPLEX WITH HIF1AN; IRON AND 2-OXOGLUTARATE, HYDROXYLATION AT HIS-238 AND HIS-553, MUTAGENESIS OF HIS-553.

    Entry informationi

    Entry nameiTNKS2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H2K2
    Secondary accession number(s): B2RBD3, Q9H8F2, Q9HAS4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 139 of the entry and version 1 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 10
      Human chromosome 10: 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