Proteins > Protein mono-ADP-ribosyltransferase PARP16
Page last updated: 2024-08-07 20:41:55
Protein mono-ADP-ribosyltransferase PARP16
A protein mono-ADP-ribosyltransferase PARP16 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q8N5Y8]
Synonyms
EC 2.4.2.-;
ADP-ribosyltransferase diphtheria toxin-like 15;
Poly [ADP-ribose] polymerase 16;
PARP-16
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 | 0 (0.00) | 29.6817 |
| 2010's | 3 (60.00) | 24.3611 |
| 2020's | 2 (40.00) | 2.80 |
Compounds (8)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| 4-Methoxybenzamide | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| latonduine a | Homo sapiens (human) | IC50 | 0.4270 | 1 | 1 |
| olaparib | Homo sapiens (human) | IC50 | 5.1143 | 1 | 2 |
| xav939 | Homo sapiens (human) | IC50 | 5.0119 | 1 | 1 |
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| rucaparib | Homo sapiens (human) | Kd | 2.9000 | 1 | 1 |
| veliparib | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| olaparib | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| niraparib | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| bmn 673 | Homo sapiens (human) | Kd | 1.0000 | 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
Enables
This protein enables 9 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] |
| kinase binding | molecular function | Binding to a kinase, any enzyme that catalyzes the transfer of a phosphate group. [GOC:jl] |
| protein serine/threonine kinase activator activity | molecular function | Binds to and increases the activity of a protein serine/threonine kinase. [GOC:go_curators] |
| 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 6 target(s):
| Target | Category | Definition |
|---|
| nuclear envelope | cellular component | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). [ISBN:0198547684] |
| endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
| endoplasmic reticulum membrane | cellular component | The lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah] |
| 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] |
| 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] |
| endoplasmic reticulum tubular network | cellular component | A subcompartment of the endoplasmic reticulum consisting of tubules having membranes with high curvature in cross-section. [GOC:vw, PMID:16469703, PMID:20434336] |
Active In
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|
| nuclear envelope | cellular component | The double lipid bilayer enclosing the nucleus and separating its contents from the rest of the cytoplasm; includes the intermembrane space, a gap of width 20-40 nm (also called the perinuclear space). [ISBN:0198547684] |
| endoplasmic reticulum tubular network | cellular component | A subcompartment of the endoplasmic reticulum consisting of tubules having membranes with high curvature in cross-section. [GOC:vw, PMID:16469703, PMID:20434336] |
Involved In
This protein is involved in 7 target(s):
| Target | Category | Definition |
|---|
| 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] |
| endoplasmic reticulum unfolded protein response | biological process | The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation. [GOC:mah, PMID:12042763] |
| 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] |
| IRE1-mediated unfolded protein response | biological process | The series of molecular signals mediated by the endoplasmic reticulum stress sensor IRE1 (Inositol-requiring transmembrane kinase/endonuclease). Begins with activation of IRE1 in response to endoplasmic reticulum (ER) stress, and ends with regulation of a downstream cellular process, e.g. transcription. One target of activated IRE1 is the transcription factor HAC1 in yeast, or XBP1 in mammals; IRE1 cleaves an intron of a mRNA coding for HAC1/XBP1 to generate an activated HAC1/XBP1 transcription factor, which controls the up regulation of UPR-related genes. At least in mammals, IRE1 can also signal through additional intracellular pathways including JNK and NF-kappaB. [GOC:bf, GOC:PARL, PMID:22013210] |
| 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] |
| cellular response to leukemia inhibitory factor | 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 leukemia inhibitory factor stimulus. [PMID:12801913] |
| negative regulation of cytoplasmic translation | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of cytoplasmic translation. [GOC:obol] |