Proteins > Poly [ADP-ribose] polymerase tankyrase-1
Page last updated: 2024-08-07 23:08:28
Poly [ADP-ribose] polymerase tankyrase-1
A poly [ADP-ribose] polymerase tankyrase-1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O95271]
Synonyms
EC 2.4.2.30;
ADP-ribosyltransferase diphtheria toxin-like 5;
ARTD5;
Poly [ADP-ribose] polymerase 5A;
Protein poly-ADP-ribosyltransferase tankyrase-1;
2.4.2.-;
TNKS-1;
TRF1-interacting ankyrin-related ADP-ribose polymerase;
Research
Bioassay Publications (35)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 2 (5.71) | 29.6817 |
2010's | 28 (80.00) | 24.3611 |
2020's | 5 (14.29) | 2.80 |
Compounds (34)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
From PARP1 to TNKS2 Inhibition: A Structure-Based Approach.ACS medicinal chemistry letters, , May-14, Volume: 11, Issue:5, 2020
Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.Journal of medicinal chemistry, , 02-23, Volume: 60, Issue:4, 2017
Evaluation and Structural Basis for the Inhibition of Tankyrases by PARP Inhibitors.ACS medicinal chemistry letters, , Jan-09, Volume: 5, Issue:1, 2014
Discovery of tankyrase inhibiting flavones with increased potency and isoenzyme selectivity.Journal of medicinal chemistry, , Oct-24, Volume: 56, Issue:20, 2013
Screening and structural analysis of flavones inhibiting tankyrases.Journal of medicinal chemistry, , May-09, Volume: 56, Issue:9, 2013
From PARP1 to TNKS2 Inhibition: A Structure-Based Approach.ACS medicinal chemistry letters, , May-14, Volume: 11, Issue:5, 2020
Discovery of novel, induced-pocket binding oxazolidinones as potent, selective, and orally bioavailable tankyrase inhibitors.Journal of medicinal chemistry, , Jun-13, Volume: 56, Issue:11, 2013
Discovery of 5-{4-[(7-Ethyl-6-oxo-5,6-dihydro-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl}-Journal of medicinal chemistry, , 10-14, Volume: 64, Issue:19, 2021
Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.Journal of medicinal chemistry, , 02-23, Volume: 60, Issue:4, 2017
Evaluation and Structural Basis for the Inhibition of Tankyrases by PARP Inhibitors.ACS medicinal chemistry letters, , Jan-09, Volume: 5, Issue:1, 2014
Discovery of 5-{4-[(7-Ethyl-6-oxo-5,6-dihydro-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl}-Journal of medicinal chemistry, , 10-14, Volume: 64, Issue:19, 2021
Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.Journal of medicinal chemistry, , 02-23, Volume: 60, Issue:4, 2017
Evaluation and Structural Basis for the Inhibition of Tankyrases by PARP Inhibitors.ACS medicinal chemistry letters, , Jan-09, Volume: 5, Issue:1, 2014
Rational design, synthesis and biological evaluation of dual PARP-1/2 and TNKS1/2 inhibitors for cancer therapy.European journal of medicinal chemistry, , Jul-05, Volume: 237, 2022
Discovery of 5-{4-[(7-Ethyl-6-oxo-5,6-dihydro-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl}-Journal of medicinal chemistry, , 10-14, Volume: 64, Issue:19, 2021
Examination of Diazaspiro Cores as Piperazine Bioisosteres in the Olaparib Framework Shows Reduced DNA Damage and Cytotoxicity.Journal of medicinal chemistry, , 06-28, Volume: 61, Issue:12, 2018
Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.Journal of medicinal chemistry, , 02-23, Volume: 60, Issue:4, 2017
Discovery of AZ0108, an orally bioavailable phthalazinone PARP inhibitor that blocks centrosome clustering.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 25, Issue:24, 2015
4-[3-(4-cyclopropanecarbonylpiperazine-1-carbonyl)-4-fluorobenzyl]-2H-phthalazin-1-one: a novel bioavailable inhibitor of poly(ADP-ribose) polymerase-1.Journal of medicinal chemistry, , Oct-23, Volume: 51, Issue:20, 2008
Discovery of 5-{4-[(7-Ethyl-6-oxo-5,6-dihydro-1,5-naphthyridin-3-yl)methyl]piperazin-1-yl}-Journal of medicinal chemistry, , 10-14, Volume: 64, Issue:19, 2021
Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.Journal of medicinal chemistry, , 02-23, Volume: 60, Issue:4, 2017
Discovery of 2-{4-[(3S)-piperidin-3-yl]phenyl}-2H-indazole-7-carboxamide (MK-4827): a novel oral poly(ADP-ribose)polymerase (PARP) inhibitor efficacious in BRCA-1 and -2 mutant tumors.Journal of medicinal chemistry, , Nov-26, Volume: 52, Issue:22, 2009
Small-Molecule Inhibitors of Tankyrases as Prospective Therapeutics for Cancer.Journal of medicinal chemistry, , 04-14, Volume: 65, Issue:7, 2022
Discovery of a class of novel tankyrase inhibitors that bind to both the nicotinamide pocket and the induced pocket.Journal of medicinal chemistry, , Feb-14, Volume: 56, Issue:3, 2013
Discovery of novel, induced-pocket binding oxazolidinones as potent, selective, and orally bioavailable tankyrase inhibitors.Journal of medicinal chemistry, , Jun-13, Volume: 56, Issue:11, 2013
Structural basis of selective inhibition of human tankyrases.Journal of medicinal chemistry, , Feb-09, Volume: 55, Issue:3, 2012
Design and Discovery of an Orally Efficacious Spiroindolinone-Based Tankyrase Inhibitor for the Treatment of Colon Cancer.Journal of medicinal chemistry, , 04-23, Volume: 63, Issue:8, 2020
Discovery of Novel Spiroindoline Derivatives as Selective Tankyrase Inhibitors.Journal of medicinal chemistry, , 04-11, Volume: 62, Issue:7, 2019
Structural basis and SAR for G007-LK, a lead stage 1,2,4-triazole based specific tankyrase 1/2 inhibitor.Journal of medicinal chemistry, , Apr-11, Volume: 56, Issue:7, 2013
Small-Molecule Inhibitors of Tankyrases as Prospective Therapeutics for Cancer.Journal of medicinal chemistry, , 04-14, Volume: 65, Issue:7, 2022
Rational design, synthesis and biological evaluation of dual PARP-1/2 and TNKS1/2 inhibitors for cancer therapy.European journal of medicinal chemistry, , Jul-05, Volume: 237, 2022
Discovery of Novel Spiroindoline Derivatives as Selective Tankyrase Inhibitors.Journal of medicinal chemistry, , 04-11, Volume: 62, Issue:7, 2019
[no title available]Journal of medicinal chemistry, , 06-13, Volume: 62, Issue:11, 2019
Fibrogenic Disorders in Human Diseases: From Inflammation to Organ Dysfunction.Journal of medicinal chemistry, , 11-21, Volume: 61, Issue:22, 2018
Structural Basis for Potency and Promiscuity in Poly(ADP-ribose) Polymerase (PARP) and Tankyrase Inhibitors.Journal of medicinal chemistry, , 02-23, Volume: 60, Issue:4, 2017
Targeting Wnt-driven cancers: Discovery of novel tankyrase inhibitors.European journal of medicinal chemistry, , Dec-15, Volume: 142, 2017
Structure-activity relationships of 2-arylquinazolin-4-ones as highly selective and potent inhibitors of the tankyrases.European journal of medicinal chemistry, , Aug-08, Volume: 118, 2016
Structure-based design, synthesis and evaluation in vitro of arylnaphthyridinones, arylpyridopyrimidinones and their tetrahydro derivatives as inhibitors of the tankyrases.Bioorganic & medicinal chemistry, , Jul-01, Volume: 23, Issue:13, 2015
Scaffold hopping approach on the route to selective tankyrase inhibitors.European journal of medicinal chemistry, , Nov-24, Volume: 87, 2014
Design, synthesis, crystallographic studies, and preliminary biological appraisal of new substituted triazolo[4,3-b]pyridazin-8-amine derivatives as tankyrase inhibitors.Journal of medicinal chemistry, , Mar-27, Volume: 57, Issue:6, 2014
Identification of NVP-TNKS656: the use of structure-efficiency relationships to generate a highly potent, selective, and orally active tankyrase inhibitor.Journal of medicinal chemistry, , Aug-22, Volume: 56, Issue:16, 2013
Fragment-based ligand design of novel potent inhibitors of tankyrases.Journal of medicinal chemistry, , Jun-13, Volume: 56, Issue:11, 2013
Discovery of a class of novel tankyrase inhibitors that bind to both the nicotinamide pocket and the induced pocket.Journal of medicinal chemistry, , Feb-14, Volume: 56, Issue:3, 2013
Design and Discovery of 2-Arylquinazolin-4-ones as Potent and Selective Inhibitors of Tankyrases.ACS medicinal chemistry letters, , Dec-12, Volume: 4, Issue:12, 2013
[1,2,4]triazol-3-ylsulfanylmethyl)-3-phenyl-[1,2,4]oxadiazoles: antagonists of the Wnt pathway that inhibit tankyrases 1 and 2 via novel adenosine pocket binding.Journal of medicinal chemistry, , Feb-09, Volume: 55, Issue:3, 2012
Structural basis of selective inhibition of human tankyrases.Journal of medicinal chemistry, , Feb-09, Volume: 55, Issue:3, 2012
Structural basis for the interaction between tankyrase-2 and a potent Wnt-signaling inhibitor.Journal of medicinal chemistry, , Jul-22, Volume: 53, Issue:14, 2010
Small-Molecule Inhibitors of Tankyrases as Prospective Therapeutics for Cancer.Journal of medicinal chemistry, , 04-14, Volume: 65, Issue:7, 2022
Discovery and Optimization of 2-Arylquinazolin-4-ones into a Potent and Selective Tankyrase Inhibitor Modulating Wnt Pathway Activity.Journal of medicinal chemistry, , 09-12, Volume: 62, Issue:17, 2019
Structure-activity relationships of 2-arylquinazolin-4-ones as highly selective and potent inhibitors of the tankyrases.European journal of medicinal chemistry, , Aug-08, Volume: 118, 2016
Enables
This protein enables 6 target(s):
Target | Category | Definition |
NAD+ ADP-ribosyltransferase activity | molecular function | Catalysis of the reaction: NAD+ + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D-ribosyl)(n+1)-acceptor. [EC:2.4.2.30] |
protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
zinc ion binding | molecular function | Binding to a zinc ion (Zn). [GOC:ai] |
nucleotidyltransferase activity | molecular function | Catalysis of the transfer of a nucleotidyl group to a reactant. [ISBN:0198506732] |
histone binding | molecular function | Binding to a histone, any of a group of water-soluble proteins found in association with the DNA of eukaryotic or archaeal chromosomes. They are involved in the condensation and coiling of chromosomes during cell division and have also been implicated in gene regulation and DNA replication. They may be chemically modified (methylated, acetlyated and others) to regulate gene transcription. [GOC:jl, PMID:16209651, PMID:30212449, PMID:9305837] |
NAD+-protein ADP-ribosyltransferase activity | molecular function | Catalysis of the reaction: amino acyl-[protein] + NAD+ = H+ + (ADP-D-ribosyl)-amino acyl-[protein] + nicotinamide. [PMID:1899243] |
Located In
This protein is located in 9 target(s):
Target | Category | Definition |
Golgi membrane | cellular component | The lipid bilayer surrounding any of the compartments of the Golgi apparatus. [GOC:mah] |
pericentriolar material | cellular component | A network of small fibers that surrounds the centrioles in cells; contains the microtubule nucleating activity of the centrosome. [GOC:clt, ISBN:0815316194] |
chromosome, telomeric region | cellular component | The end of a linear chromosome, required for the integrity and maintenance of the end. A chromosome telomere usually includes a region of telomerase-encoded repeats the length of which rarely exceeds 20 bp each and that permits the formation of a telomeric loop (T-loop). The telomeric repeat region is usually preceded by a sub-telomeric region that is gene-poor but rich in repetitive elements. Some telomeres only consist of the latter part (for eg. D. melanogaster telomeres). [GOC:elh] |
nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
Golgi apparatus | cellular component | A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways. [ISBN:0198506732] |
cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
nuclear body | cellular component | Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. [GOC:ma, PMID:10330182] |
nuclear membrane | cellular component | Either of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. [GOC:mah, GOC:pz] |
mitotic spindle pole | cellular component | Either of the ends of a mitotic spindle, a spindle that forms as part of mitosis, where spindle microtubules are organized; usually contains a microtubule organizing center and accessory molecules, spindle microtubules and astral microtubules. [GOC:vw] |
Active In
This protein is active in 2 target(s):
Target | Category | Definition |
nucleus | cellular component | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. [GOC:go_curators] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Part Of
This protein is part of 1 target(s):
Target | Category | Definition |
nuclear pore | cellular component | A protein complex providing a discrete opening in the nuclear envelope of a eukaryotic cell, where the inner and outer nuclear membranes are joined. [ISBN:0198547684] |
Involved In
This protein is involved in 19 target(s):
Target | Category | Definition |
protein polyubiquitination | biological process | Addition of multiple ubiquitin groups to a protein, forming a ubiquitin chain. [ISBN:0815316194] |
mitotic spindle organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the microtubule spindle during a mitotic cell cycle. [GOC:go_curators, GOC:mah] |
protein transport | biological process | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:ai] |
Wnt signaling pathway | biological process | The series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of a target cell and ending with a change in cell state. [PMID:11532397] |
regulation of telomere maintenance via telomerase | biological process | Any process that modulates the frequency, rate or extent of the addition of telomeric repeats by telomerase. [GOC:mah] |
positive regulation of telomere maintenance via telomerase | biological process | Any process that activates or increases the frequency, rate or extent of the addition of telomeric repeats by telomerase. [GOC:mah] |
positive regulation of transcription by RNA polymerase II | biological process | Any process that activates or increases the frequency, rate or extent of transcription from an RNA polymerase II promoter. [GOC:go_curators, GOC:txnOH] |
mRNA transport | biological process | The directed movement of mRNA, messenger ribonucleic acid, into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:ai] |
spindle assembly | biological process | The aggregation, arrangement and bonding together of a set of components to form the spindle, the array of microtubules and associated molecules that serves to move duplicated chromosomes apart. [GOC:ai, GOC:expert_rg, GOC:mtg_sensu, GOC:tb] |
cell division | biological process | The process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. [GOC:di, GOC:go_curators, GOC:pr] |
positive regulation of telomerase activity | biological process | Any process that activates or increases the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). [GOC:ai] |
protein localization to chromosome, telomeric region | biological process | Any process in which a protein is transported to, or maintained at, the telomeric region of a chromosome. [GOC:BHF, GOC:mah] |
protein poly-ADP-ribosylation | biological process | The transfer of multiple ADP-ribose residues from NAD to a protein amino acid, forming a poly(ADP-ribose) chain. [GOC:BHF, GOC:mah, GOC:rl, PMID:25043379] |
protein auto-ADP-ribosylation | biological process | The ADP-ribosylation by a protein of one or more of its own amino acid residues, or residues on an identical protein. [GOC:BHF, GOC:rl] |
positive regulation of canonical Wnt signaling pathway | biological process | Any process that increases the rate, frequency, or extent of the Wnt signaling pathway through beta-catenin, the series of molecular signals initiated by binding of a Wnt protein to a frizzled family receptor on the surface of the target cell, followed by propagation of the signal via beta-catenin, and ending with a change in transcription of target genes. [GOC:tb] |
positive regulation of telomere capping | biological process | Any process that activates or increases the frequency, rate or extent of telomere capping. [GO_REF:0000058, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:23959892] |
negative regulation of telomere maintenance via telomere lengthening | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of telomere maintenance via telomere lengthening. [GO_REF:0000058, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:23959892] |
negative regulation of telomeric DNA binding | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of telomeric DNA binding. [GO_REF:0000059, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:24415760] |
negative regulation of maintenance of mitotic sister chromatid cohesion, telomeric | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of maintenance of mitotic sister chromatid cohesion, telomeric. [GO_REF:0000058, GOC:BHF, GOC:BHF_telomere, GOC:rph, GOC:TermGenie, PMID:26373281] |