Protein: Poly [ADP-ribose] polymerase tankyrase-2 (EC 2.4.2.30) (ADP-ribosyltransferase diphtheria toxin-like 6) (ARTD6) (Protein poly-ADP-ribosyltransferase tankyrase-2) (EC 2.4.2.-) (TNKS-2) (TRF1-interacting ankyrin-related ADP-ribose polymerase 2) (Tankyrase II) (Tankyrase-2) (TANK2) (Q3UES3)
Organism: Mus musculus (Mouse)
Function: 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. Stimulates 26S proteasome activity.
Subcellular location: Cytoplasm {ECO:0000250|UniProtKB:Q9H2K2}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9H2K2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9H2K2}. Nucleus {ECO:0000250|UniProtKB:Q9H2K2}. Chromosome, telomere {ECO:0000250|UniProtKB:Q9H2K2}. Note=Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (By similarity). Also found around the pericentriolar matrix of mitotic centromeres (By similarity). During interphase, a small fraction of TNKS2 is found in the nucleus, associated with TRF1 (By similarity). {ECO:0000250|UniProtKB:Q9H2K2}.
Interaction partners:
- Telomeric repeat-binding factor 1
- Axin-1
- SH3 domain-binding protein 2
- Axin-2
- E3 ubiquitin-protein ligase RNF146
- Hypoxia-inducible factor 1-alpha inhibitor
- Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN
- Induced myeloid leukemia cell differentiation protein Mcl-1 homolog
- 182 kDa tankyrase-1-binding protein
- Glycogen synthase kinase-3 beta
Sequence:
MSGRRCAGGGAACASAGAEAVEPSARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLAPTAQLKERLSYEFKGHSLLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNENVQQLLQEGASLGHSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGDAALLDAAKKGCLARVKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSADDVSALLTAAMPPSALPTCYKPQVLSGVRGPGATADALSSGPSSPSSLSAASSLDNLSGSFSELSAVVSSSAAEGATGLQRKEDSGIDFSITQFIRNLGLEHLMDIFEREQITLDVLVEMGHKELKEIGINAYGHRHKLIKGVERLISGQQGLNPYLTLNNSGSGTILIDLSPDDKEFQSVEEEMQSTVREHRDGGHAGGVFNRYNILKIQKVCNKKLWERYTHRRKEVSEENHNHANERMLFHGSPFVNAIIHKGFDERHAYIGGMFGAGIYFAENSSKSNQYVYGIGGGTGCPIHKDRSCYICHRQLLFCRVTLGKSFLQFSAMKMAHSPPGHHSVTGRPSVNGLALAEYVIYRGEQAYPEYLITYQIVRPEGMVDG