TNKS

TNKS (Tankyrase) is a Protein Coding gene. Diseases related to TNKS include Cherubism and Cornelia De Lange Syndrome. Among its related pathways are Metabolism of proteins and Regulation of Telomerase. Gene Ontology (GO) annotations related to TNKS include NAD+ ADP-ribosyltransferase activity. An important paralog of TNKS is TNKS2.

tankyrase, TRF1-interacting ankyrin-related ADP-ribose polymerase

Poly-ADP-ribosyltransferase involved in various processes such as Wnt signaling pathway, telomere length and vesicle trafficking (PubMed:10988299, PubMed:11739745, PubMed:16076287, PubMed:19759537, PubMed:21478859, PubMed:22864114, PubMed:23622245, PubMed:25043379).
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 (PubMed:19759537, PubMed:21478859).
Also mediates PARsylation of BLZF1 and CASC3, followed by recruitment of RNF146 and subsequent ubiquitination (PubMed:21478859).
Mediates PARsylation of TERF1, thereby contributing to the regulation of telomere length (PubMed:11739745).
Involved in centrosome maturation during prometaphase by mediating PARsylation of HEPACAM2/MIKI (PubMed:22864114).
May also regulate vesicle trafficking and modulate the subcellular distribution of SLC2A4/GLUT4-vesicles (PubMed:10988299).
May be involved in spindle pole assembly through PARsylation of NUMA1 (PubMed:16076287).
Stimulates 26S proteasome activity (PubMed:23622245).

Biological Process cell division Source:UniProtKB-KW
Biological Process mitotic spindle organization Source:BHF-UCL1 Publication
Biological Process mRNA transport Source:UniProtKB-KW
Biological Process negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric Source:BHF-UCL1 Publication
Biological Process negative regulation of telomere maintenance via telomere lengthening Source:BHF-UCL1 Publication
Biological Process negative regulation of telomeric DNA binding Source:BHF-UCL1 Publication
Biological Process peptidyl-serine phosphorylation Source:MGI1 Publication
Biological Process peptidyl-threonine phosphorylation Source:MGI1 Publication
Biological Process positive regulation of canonical Wnt signaling pathway Source:UniProtKB1 Publication
Biological Process positive regulation of telomerase activity Source:BHF-UCL1 Publication
Biological Process positive regulation of telomere capping Source:BHF-UCL1 Publication
Biological Process positive regulation of telomere maintenance via telomerase Source:BHF-UCL2 Publications
Biological Process positive regulation of transcription by RNA polymerase II Source:UniProtKB1 Publication
Biological Process protein ADP-ribosylation Source:BHF-UCL2 Publications
Biological Process protein auto-ADP-ribosylation Source:UniProtKB2 Publications
Biological Process protein localization to chromosome, telomeric region Source:BHF-UCL2 Publications
Biological Process protein poly-ADP-ribosylation Source:UniProtKB2 Publications
Biological Process protein polyubiquitination Source:UniProtKB2 Publications
Biological Process protein transport Source:UniProtKB-KW
Biological Process regulation of telomere maintenance via telomerase Source:BHF-UCL1 Publication
Biological Process spindle assembly Source:BHF-UCL1 Publication
Biological Process Wnt signaling pathway Source:UniProtKB-KW

Cytoplasm
Golgi apparatus membrane
Cytoplasm, cytoskeleton, microtubule organizing center, centrosome
Nucleus, nuclear pore complex
Chromosome, telomere
Cytoplasm, cytoskeleton, spindle pole
Associated with the Golgi and with juxtanuclear SLC2A4/GLUT4-vesicles (PubMed:22864114).
A minor proportion is also found at nuclear pore complexes and around the pericentriolar matrix of mitotic centromeres (PubMed:10523501).
During interphase, a small fraction of TNKS is found in the nucleus, associated with TERF1 (PubMed:12768206).
Localizes to spindle poles at mitosis onset via interaction with NUMA1 (PubMed:12080061).

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