Proteins > Protein mono-ADP-ribosyltransferase PARP10
Page last updated: 2024-08-07 21:15:47
Protein mono-ADP-ribosyltransferase PARP10
A protein mono-ADP-ribosyltransferase PARP10 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q53GL7]
Synonyms
EC 2.4.2.-;
ADP-ribosyltransferase diphtheria toxin-like 10;
ARTD10;
Poly [ADP-ribose] polymerase 10;
PARP-10
Research
Bioassay Publications (7)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 0 (0.00) | 29.6817 |
2010's | 5 (71.43) | 24.3611 |
2020's | 2 (28.57) | 2.80 |
Compounds (10)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
rucaparib | Homo sapiens (human) | Kd | 3.1000 | 1 | 1 |
veliparib | Homo sapiens (human) | Kd | 6.8000 | 1 | 1 |
olaparib | Homo sapiens (human) | Kd | 9.7000 | 1 | 1 |
niraparib | Homo sapiens (human) | Kd | 5.0000 | 1 | 1 |
bmn 673 | Homo sapiens (human) | Kd | 5.7000 | 1 | 1 |
Rational Design of Cell-Active Inhibitors of PARP10.ACS medicinal chemistry letters, , Jan-10, Volume: 10, Issue:1, 2019
Selective inhibition of PARP10 using a chemical genetics strategy.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 25, Issue:21, 2015
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
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
Enables
This protein enables 8 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] |
nucleotidyltransferase activity | molecular function | Catalysis of the transfer of a nucleotidyl group to a reactant. [ISBN:0198506732] |
K63-linked polyubiquitin modification-dependent protein binding | molecular function | Binding to a protein upon poly-ubiquitination formed by linkages between lysine residues at position 63 in the target protein. [GOC:mah, PMID:15556404, PMID:17525341] |
DNA-binding transcription factor binding | molecular function | Binding to a DNA-binding transcription factor, a protein that interacts with a specific DNA sequence (sometimes referred to as a motif) within the regulatory region of a gene to modulate transcription. [GOC:txnOH-2018] |
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 ADP-ribosyltransferase activity | molecular function | Catalysis of the reaction: amino acyl-[protein] + NAD+ = H+ + (ADP-D-ribosyl)-amino acyl-[protein] + nicotinamide. [PMID:1899243] |
transcription corepressor activity | molecular function | A transcription coregulator activity that represses or decreases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Corepressors often act by altering chromatin structure and modifications. For example, one class of transcription corepressors modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. [GOC:txnOH-2018, PMID:10213677, PMID:16858867] |
Located In
This protein is located in 5 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] |
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] |
cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
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] |
Active In
This protein is active in 2 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] |
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] |
Involved In
This protein is involved in 11 target(s):
Target | Category | Definition |
chromatin organization | biological process | The assembly or remodeling of chromatin composed of DNA complexed with histones, other associated proteins, and sometimes RNA. [PMID:20404130] |
negative regulation of gene expression | biological process | Any process that decreases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). [GOC:txnOH-2018] |
viral protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a viral protein. [GOC:bf, GOC:jl, ISBN:0781702534] |
translesion synthesis | biological process | The replication of damaged DNA by synthesis across a lesion in the template strand; a specialized DNA polymerase or replication complex inserts a defined nucleotide across from the lesion which allows DNA synthesis to continue beyond the lesion. This process can be mutagenic depending on the damaged nucleotide and the inserted nucleotide. [GOC:elh, GOC:vw, PMID:10535901] |
negative regulation of NF-kappaB transcription factor activity | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the activity of the transcription factor NF-kappaB. [GOC:dph, GOC:rl, GOC:tb] |
NAD biosynthesis via nicotinamide riboside salvage pathway | biological process | The chemical reactions and pathways resulting in the formation of nicotinamide adenine dinucleotide (NAD) from the vitamin precursor nicotinamide riboside. [PMID:17482543] |
negative regulation of DNA-templated transcription | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
negative regulation of fibroblast proliferation | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of multiplication or reproduction of fibroblast cells. [GOC:jid] |
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] |
negative regulation of protein K63-linked ubiquitination | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of protein K63-linked ubiquitination. [GOC:TermGenie] |