Proteins > Protein mono-ADP-ribosyltransferase PARP3
Page last updated: 2024-08-08 00:27:31
Protein mono-ADP-ribosyltransferase PARP3
A protein mono-ADP-ribosyltransferase PARP3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9Y6F1]
Synonyms
EC 2.4.2.-;
ADP-ribosyltransferase diphtheria toxin-like 3;
ARTD3;
DNA ADP-ribosyltransferase PARP3;
2.4.2.-;
IRT1;
NAD(+) ADP-ribosyltransferase 3;
ADPRT-3;
Poly [ADP-ribose] polymerase 3;
PARP-3;
hPARP-3;
Pol
Research
Bioassay Publications (13)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (15.38) | 29.6817 |
| 2010's | 9 (69.23) | 24.3611 |
| 2020's | 2 (15.38) | 2.80 |
Compounds (12)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| pj-34 | Homo sapiens (human) | IC50 | 1.4377 | 1 | 2 |
| 4-Methoxybenzamide | Homo sapiens (human) | IC50 | 100.0000 | 1 | 1 |
| rucaparib | Homo sapiens (human) | IC50 | 0.4597 | 1 | 2 |
| latonduine a | Homo sapiens (human) | IC50 | 3.4000 | 1 | 1 |
| veliparib | Homo sapiens (human) | IC50 | 2.0890 | 1 | 2 |
| olaparib | Homo sapiens (human) | IC50 | 0.1315 | 3 | 4 |
| niraparib | Homo sapiens (human) | IC50 | 0.3797 | 4 | 5 |
| xav939 | Homo sapiens (human) | IC50 | 3.8903 | 2 | 3 |
| me0328 | Homo sapiens (human) | IC50 | 2.6967 | 2 | 3 |
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| pj-34 | Homo sapiens (human) | Kd | 0.7000 | 1 | 1 |
| 3-aminobenzoic acid | Homo sapiens (human) | Kd | 2.0000 | 1 | 1 |
| rucaparib | Homo sapiens (human) | EC50 | 0.0047 | 1 | 1 |
| rucaparib | Homo sapiens (human) | Kd | 0.2670 | 1 | 1 |
| veliparib | Homo sapiens (human) | EC50 | 0.0059 | 1 | 1 |
| veliparib | Homo sapiens (human) | Kd | 0.2310 | 1 | 1 |
| olaparib | Homo sapiens (human) | EC50 | 0.0036 | 1 | 1 |
| olaparib | Homo sapiens (human) | Kd | 0.0058 | 1 | 1 |
| niraparib | Homo sapiens (human) | EC50 | 0.0240 | 2 | 2 |
| niraparib | Homo sapiens (human) | EC50 | 0.0040 | 2 | 2 |
| bmn 673 | Homo sapiens (human) | EC50 | 0.0025 | 2 | 2 |
| bmn 673 | Homo sapiens (human) | Kd | 0.0240 | 1 | 1 |
Drugs with Other Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| niraparib | Homo sapiens (human) | EC90 | 0.2200 | 1 | 1 |
| niraparib | Homo sapiens (human) | EC90 | 0.0450 | 1 | 1 |
| niraparib | Homo sapiens (human) | IC90 | 0.0493 | 3 | 3 |
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
Structural basis for inhibitor specificity in human poly(ADP-ribose) polymerase-3.Journal of medicinal chemistry, , May-14, Volume: 52, Issue:9, 2009
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 and Characterization of (8S,9R)-5-Fluoro-8-(4-fluorophenyl)-9-(1-methyl-1H-1,2,4-triazol-5-yl)-2,7,8,9-tetrahydro-3H-pyrido[4,3,2-de]phthalazin-3-one (BMN 673, Talazoparib), a Novel, Highly Potent, and Orally Efficacious Poly(ADP-ribose) PolymerJournal of medicinal chemistry, , Jan-14, Volume: 59, Issue:1, 2016
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 and Characterization of (8S,9R)-5-Fluoro-8-(4-fluorophenyl)-9-(1-methyl-1H-1,2,4-triazol-5-yl)-2,7,8,9-tetrahydro-3H-pyrido[4,3,2-de]phthalazin-3-one (BMN 673, Talazoparib), a Novel, Highly Potent, and Orally Efficacious Poly(ADP-ribose) PolymerJournal of medicinal chemistry, , Jan-14, Volume: 59, Issue:1, 2016
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 and Characterization of (8S,9R)-5-Fluoro-8-(4-fluorophenyl)-9-(1-methyl-1H-1,2,4-triazol-5-yl)-2,7,8,9-tetrahydro-3H-pyrido[4,3,2-de]phthalazin-3-one (BMN 673, Talazoparib), a Novel, Highly Potent, and Orally Efficacious Poly(ADP-ribose) PolymerJournal of medicinal chemistry, , Jan-14, Volume: 59, Issue:1, 2016
Discovery of AZ0108, an orally bioavailable phthalazinone PARP inhibitor that blocks centrosome clustering.Bioorganic & medicinal chemistry letters, , Dec-15, Volume: 25, Issue:24, 2015
Design, synthesis, and biological evaluation of a series of benzo[de][1,7]naphthyridin-7(8H)-ones bearing a functionalized longer chain appendage as novel PARP1 inhibitors.Journal of medicinal chemistry, , Apr-11, Volume: 56, Issue:7, 2013
Niraparib: A Poly(ADP-ribose) Polymerase (PARP) Inhibitor for the Treatment of Tumors with Defective Homologous Recombination.Journal of medicinal chemistry, , Apr-23, Volume: 58, Issue:8, 2015
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
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
Niraparib: A Poly(ADP-ribose) Polymerase (PARP) Inhibitor for the Treatment of Tumors with Defective Homologous Recombination.Journal of medicinal chemistry, , Apr-23, Volume: 58, Issue:8, 2015
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
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
Fragment-based ligand design of novel potent inhibitors of tankyrases.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
Discovery and Characterization of (8S,9R)-5-Fluoro-8-(4-fluorophenyl)-9-(1-methyl-1H-1,2,4-triazol-5-yl)-2,7,8,9-tetrahydro-3H-pyrido[4,3,2-de]phthalazin-3-one (BMN 673, Talazoparib), a Novel, Highly Potent, and Orally Efficacious Poly(ADP-ribose) PolymerJournal of medicinal chemistry, , Jan-14, Volume: 59, Issue:1, 2016
Niraparib: A Poly(ADP-ribose) Polymerase (PARP) Inhibitor for the Treatment of Tumors with Defective Homologous Recombination.Journal of medicinal chemistry, , Apr-23, Volume: 58, Issue:8, 2015
Chemical probes to study ADP-ribosylation: synthesis and biochemical evaluation of inhibitors of the human ADP-ribosyltransferase ARTD3/PARP3.Journal of medicinal chemistry, , Dec-12, Volume: 56, Issue:23, 2013
PARP inhibitor with selectivity toward ADP-ribosyltransferase ARTD3/PARP3.ACS chemical biology, , Aug-16, Volume: 8, Issue:8, 2013
Enables
This protein enables 9 target(s):
| Target | Category | Definition |
|---|
| catalytic activity | molecular function | Catalysis of a biochemical reaction at physiological temperatures. In biologically catalyzed reactions, the reactants are known as substrates, and the catalysts are naturally occurring macromolecular substances known as enzymes. Enzymes possess specific binding sites for substrates, and are usually composed wholly or largely of protein, but RNA that has catalytic activity (ribozyme) is often also regarded as enzymatic. [GOC:vw, ISBN:0198506732] |
| 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] |
| nucleotidyltransferase activity | molecular function | Catalysis of the transfer of a nucleotidyl group to a reactant. [ISBN:0198506732] |
| NAD DNA ADP-ribosyltransferase activity | molecular function | Catalysis of the transfer of the ADP-ribose group of NAD+ to a residue in double-stranded DNA. [PMID:27471034, PMID:29361132, PMID:29520010] |
| NAD+- protein-lysine ADP-ribosyltransferase activity | molecular function | Catalysis of the reaction: L-lysyl-[protein] + NAD+ = H+ + N(6)-(ADP-D-ribosyl)-L-lysyl-[protein] + nicotinamide. [PMID:25043379, RHEA:58220] |
| NAD+- protein-aspartate ADP-ribosyltransferase activity | molecular function | Catalysis of the reaction: L-aspartyl-[protein] + NAD+ = 4-O-(ADP-D-ribosyl)-L-aspartyl-[protein] + nicotinamide. [PMID:19764761, PMID:25043379, RHEA:54424] |
| NAD+-protein-glutamate ADP-ribosyltransferase activity | molecular function | Catalysis of the reaction: L-glutamyl-[protein] + NAD+ = 5-O-(ADP-D-ribosyl)-L-glutamyl-[protein] + nicotinamide. [PMID:19764761, PMID:25043379, RHEA:58224] |
| 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 7 target(s):
| Target | Category | Definition |
|---|
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
| centrosome | cellular component | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. [GOC:mah, ISBN:0198547684] |
| centriole | cellular component | A cellular organelle, found close to the nucleus in many eukaryotic cells, consisting of a small cylinder with microtubular walls, 300-500 nm long and 150-250 nm in diameter. It contains nine short, parallel, peripheral microtubular fibrils, each fibril consisting of one complete microtubule fused to two incomplete microtubules. Cells usually have two centrioles, lying at right angles to each other. At division, each pair of centrioles generates another pair and the twin pairs form the pole of the mitotic spindle. [ISBN:0198547684] |
| nuclear body | cellular component | Extra-nucleolar nuclear domains usually visualized by confocal microscopy and fluorescent antibodies to specific proteins. [GOC:ma, PMID:10330182] |
| site of double-strand break | cellular component | A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix. [GOC:bf, GOC:mah, GOC:vw, PMID:20096808, PMID:21035408] |
| intercellular bridge | cellular component | A direct connection between the cytoplasm of two cells that is formed following the completion of cleavage furrow ingression during cell division. They are usually present only briefly prior to completion of cytokinesis. However, in some cases, such as the bridges between germ cells during their development, they become stabilised. [PMID:9635420] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| nucleolus | cellular component | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. [ISBN:0198506732] |
| site of double-strand break | cellular component | A region of a chromosome at which a DNA double-strand break has occurred. DNA damage signaling and repair proteins accumulate at the lesion to respond to the damage and repair the DNA to form a continuous DNA helix. [GOC:bf, GOC:mah, GOC:vw, PMID:20096808, PMID:21035408] |
Involved In
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|
| DNA ADP-ribosylation | biological process | The covalent attachment of an ADP-ribosyl group to a residue in double-stranded DNA. [PMID:11592983, PMID:27471034, PMID:29361132, PMID:29520010] |
| negative regulation of isotype switching | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of isotype switching. [GOC:go_curators] |
| 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] |
| negative regulation of telomerase RNA reverse transcriptase activity | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of telomerase RNA reverse transcriptase activity. [GO_REF:0000059, GOC:BHF, GOC:BHF_telomere, GOC:nc, GOC:TermGenie, PMID:22633954] |
| positive regulation of double-strand break repair via nonhomologous end joining | biological process | Any process that activates or increases the frequency, rate or extent of double-strand break repair via nonhomologous end joining. [GOC:obol] |
| double-strand break repair | biological process | The repair of double-strand breaks in DNA via homologous and nonhomologous mechanisms to reform a continuous DNA helix. [GOC:elh] |