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Gene Review

TNKS  -  tankyrase, TRF1-interacting ankyrin...

Homo sapiens

Synonyms: ADP-ribosyltransferase diphtheria toxin-like 5, ARTD5, PARP-5a, PARP5A, PARPL, ...
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Disease relevance of TNKS


High impact information on TNKS


Biological context of TNKS


Anatomical context of TNKS


Associations of TNKS with chemical compounds

  • Using a tetracycline-sensitive promoter to regulate tankyrase-1 expression in Madin-Darby canine kidney (MDCK) cells, we found that a 40-fold induction of tankyrase-1 (from 1,500 to 60,000 copies per cell) lowers steady-state NAD(+) levels but does not affect basal cellular viability [9].
  • Herein we report that mitotic phosphorylation of tankyrase is abrogated in cells treated with the GSK3 inhibitors LiCl and indirubin [12].
  • The levels of tankyrase in breast cancers were significantly higher in comparison to normal tissues (P<0.0001) and significantly related to the status of progesterone receptors [13].
  • We show that in the framework of Hopfield and Tank (1985), changes in GABA suppression correspond to changes in the effective temperature and the relative energy of data terms and constraints of an analog network [14].
  • A radioactive tank waste sample from Hanford Tank 241-C-112 was determined to be 1.0 mM in ferrocyanide using the spectroelectrochemical sensor [15].

Physical interactions of TNKS


Regulatory relationships of TNKS


Other interactions of TNKS


Analytical, diagnostic and therapeutic context of TNKS


  1. Inhibition of Epstein-Barr virus OriP function by tankyrase, a telomere-associated poly-ADP ribose polymerase that binds and modifies EBNA1. Deng, Z., Atanasiu, C., Zhao, K., Marmorstein, R., Sbodio, J.I., Chi, N.W., Lieberman, P.M. J. Virol. (2005) [Pubmed]
  2. 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. (2001) [Pubmed]
  3. Cloning and characterization of TNKL, a member of tankyrase gene family. Kuimov, A.N., Kuprash, D.V., Petrov, V.N., Vdovichenko, K.K., Scanlan, M.J., Jongeneel, C.V., Lagarkova, M.A., Nedospasov, S.A. Genes Immun. (2001) [Pubmed]
  4. Telomerase subunits expression variation between biopsy samples and cell lines derived from malignant glioma. Shervington, A., Patel, R., Lu, C., Cruickshanks, N., Lea, R., Roberts, G., Dawson, T., Shervington, L. Brain Res. (2007) [Pubmed]
  5. Achieving healthy weight in African-American communities: research perspectives and priorities. Kumanyika, S.K., Gary, T.L., Lancaster, K.J., Samuel-Hodge, C.D., Banks-Wallace, J., Beech, B.M., Hughes-Halbert, C., Karanja, N., Odoms-Young, A.M., Prewitt, T.E., Whitt-Glover, M.C. Obes. Res. (2005) [Pubmed]
  6. TIN2 is a tankyrase 1 PARP modulator in the TRF1 telomere length control complex. Ye, J.Z., de Lange, T. Nat. Genet. (2004) [Pubmed]
  7. Tankyrase, a poly(ADP-ribose) polymerase at human telomeres. Smith, S., Giriat, I., Schmitt, A., de Lange, T. Science (1998) [Pubmed]
  8. 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. (2001) [Pubmed]
  9. Tankyrase-1 overexpression reduces genotoxin-induced cell death by inhibiting PARP1. Yeh, T.Y., Sbodio, J.I., Nguyen, M.T., Meyer, T.N., Lee, R.M., Chi, N.W. Mol. Cell. Biochem. (2005) [Pubmed]
  10. 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. (2000) [Pubmed]
  11. Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes. Smith, S., de Lange, T. J. Cell. Sci. (1999) [Pubmed]
  12. Mitotic phosphorylation of tankyrase, a PARP that promotes spindle assembly, by GSK3. Yeh, T.Y., Sbodio, J.I., Chi, N.W. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  13. Tankyrase, a positive regulator of telomere elongation, is over expressed in human breast cancer. Gelmini, S., Poggesi, M., Distante, V., Bianchi, S., Simi, L., Luconi, M., Raggi, C.C., Cataliotti, L., Pazzagli, M., Orlando, C. Cancer Lett. (2004) [Pubmed]
  14. Changes in GABAB modulation during a theta cycle may be analogous to the fall of temperature during annealing. Sohal, V.S., Hasselmo, M.E. Neural computation. (1998) [Pubmed]
  15. Spectroelectrochemical sensing based on multimode selectivity simultaneously achievable in a single device. 11. Design and evaluation of a small portable sensor for the determination of ferrocyanide in Hanford waste samples. Stegemiller, M.L., Heineman, W.R., Seliskar, C.J., Ridgway, T.H., Bryan, S.A., Hubler, T., Sell, R.L. Environ. Sci. Technol. (2003) [Pubmed]
  16. The formin-binding protein 17, FBP17, binds via a TNKS binding motif to tankyrase, a protein involved in telomere maintenance. Fuchs, U., Rehkamp, G.F., Slany, R., Follo, M., Borkhardt, A. FEBS Lett. (2003) [Pubmed]
  17. The telomeric poly(ADP-ribose) polymerase, tankyrase 1, contains multiple binding sites for telomeric repeat binding factor 1 (TRF1) and a novel acceptor, 182-kDa tankyrase-binding protein (TAB182). Seimiya, H., Smith, S. J. Biol. Chem. (2002) [Pubmed]
  18. Protection of internal (TTAGGG)n repeats in Chinese hamster cells by telomeric protein TRF1. Krutilina, R.I., Smirnova, A.N., Mudrak, O.S., Pleskach, N.M., Svetlova, M.P., Oei, S.L., Yau, P.M., Bradbury, E.M., Zalensky, A.O., Tomilin, N.V. Oncogene (2003) [Pubmed]
  19. Antisense inhibition of Bcr-Abl/c-Abl synthesis promotes telomerase activity and upregulates tankyrase in human leukemia cells. Bakalova, R., Ohba, H., Zhelev, Z., Kubo, T., Fujii, M., Ishikawa, M., Shinohara, Y., Baba, Y. FEBS Lett. (2004) [Pubmed]
  20. Identification of a tankyrase-binding motif shared by IRAP, TAB182, and human TRF1 but not mouse TRF1. NuMA contains this RXXPDG motif and is a novel tankyrase partner. Sbodio, J.I., Chi, N.W. J. Biol. Chem. (2002) [Pubmed]
  21. 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., Sanderson, G.M., Eyre, H.J., Sutherland, G.R., Daly, R.J. J. Biol. Chem. (2001) [Pubmed]
  22. NuMA is a major acceptor of poly(ADP-ribosyl)ation by tankyrase 1 in mitosis. Chang, W., Dynek, J.N., Smith, S. Biochem. J. (2005) [Pubmed]
  23. 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. (2002) [Pubmed]
  24. Identification of a novel gene (ADPRTL1) encoding a potential Poly(ADP-ribosyl)transferase protein. Still, I.H., Vince, P., Cowell, J.K. Genomics (1999) [Pubmed]
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