Proteins > Protein mono-ADP-ribosyltransferase PARP4
Page last updated: 2024-08-08 00:40:53
Protein mono-ADP-ribosyltransferase PARP4
A protein mono-ADP-ribosyltransferase PARP4 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9UKK3]
Synonyms
EC 2.4.2.-;
193 kDa vault protein;
ADP-ribosyltransferase diphtheria toxin-like 4;
ARTD4;
PARP-related/IalphaI-related H5/proline-rich;
PH5P;
Poly [ADP-ribose] polymerase 4;
PARP-4;
Vault poly(ADP-ribose) polymerase;
V
Research
Bioassay Publications (5)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 1 (20.00) | 29.6817 |
| 2010's | 3 (60.00) | 24.3611 |
| 2020's | 1 (20.00) | 2.80 |
Compounds (8)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| pj-34 | Homo sapiens (human) | IC50 | 0.7586 | 1 | 1 |
| 4-Methoxybenzamide | Homo sapiens (human) | IC50 | 65.0000 | 1 | 1 |
| rucaparib | Homo sapiens (human) | IC50 | 0.8354 | 1 | 2 |
| veliparib | Homo sapiens (human) | IC50 | 3.4837 | 1 | 2 |
| olaparib | Homo sapiens (human) | IC50 | 0.4087 | 1 | 2 |
| niraparib | Homo sapiens (human) | IC50 | 0.4076 | 2 | 3 |
| xav939 | Homo sapiens (human) | IC50 | 4.5890 | 2 | 3 |
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| rucaparib | Homo sapiens (human) | Kd | 0.5030 | 1 | 1 |
| veliparib | Homo sapiens (human) | Kd | 0.1050 | 1 | 1 |
| olaparib | Homo sapiens (human) | Kd | 0.1410 | 1 | 1 |
| niraparib | Homo sapiens (human) | Kd | 0.2720 | 1 | 1 |
| bmn 673 | Homo sapiens (human) | Kd | 0.0007 | 1 | 1 |
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 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 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 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
Discovery of a Highly Selective Tankyrase Inhibitor Displaying Growth Inhibition Effects against a Diverse Range of Tumor Derived Cell Lines.Journal of medicinal chemistry, , 07-13, Volume: 60, Issue:13, 2017
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
Enables
This protein enables 6 target(s):
| Target | Category | Definition |
|---|
| DNA binding | molecular function | Any molecular function by which a gene product interacts selectively and non-covalently with DNA (deoxyribonucleic acid). [GOC:dph, GOC:jl, GOC:tb, GOC:vw] |
| 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] |
| enzyme binding | molecular function | Binding to an enzyme, a protein with catalytic activity. [GOC:jl] |
| 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 |
|---|
| 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] |
| 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] |
| 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] |
| spindle microtubule | cellular component | Any microtubule that is part of a mitotic or meiotic spindle; anchored at one spindle pole. [ISBN:0815316194] |
| membrane | cellular component | A lipid bilayer along with all the proteins and protein complexes embedded in it and attached to it. [GOC:dos, GOC:mah, ISBN:0815316194] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
Active In
This protein is active in 1 target(s):
| Target | Category | Definition |
|---|
| 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 |
|---|
| ribonucleoprotein complex | cellular component | A macromolecular complex that contains both RNA and protein molecules. [GOC:krc, GOC:vesicles] |
Involved In
This protein is involved in 6 target(s):
| Target | Category | Definition |
|---|
| DNA repair | biological process | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. [PMID:11563486] |
| inflammatory response | biological process | The immediate defensive reaction (by vertebrate tissue) to infection or injury caused by chemical or physical agents. The process is characterized by local vasodilation, extravasation of plasma into intercellular spaces and accumulation of white blood cells and macrophages. [GO_REF:0000022, ISBN:0198506732] |
| DNA damage response | biological process | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. [GOC:go_curators] |
| response to xenobiotic stimulus | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus from a xenobiotic, a compound foreign to the organim exposed to it. It may be synthesized by another organism (like ampicilin) or it can be a synthetic chemical. [GOC:jl, GOC:krc] |
| protein modification process | biological process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl] |
| regulation of telomerase activity | biological process | Any process that modulates the frequency, rate or extent of telomerase activity, the catalysis of the reaction: deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1). Telomerases catalyze extension of the 3'- end of a DNA strand by one deoxynucleotide at a time using an internal RNA template that encodes the telomeric repeat sequence. [EC:2.-.-.-, GOC:ai] |