A dual specificity tyrosine-phosphorylation-regulated kinase 4 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9NR20]
EC 2.7.12.1
| 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 | 4 (100.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| harmine | Homo sapiens (human) | IC50 | 54.5000 | 3 | 3 |
| gw-5074 | Homo sapiens (human) | IC50 | 4.3800 | 1 | 1 |
| leucettamine b | Homo sapiens (human) | IC50 | 10.0000 | 1 | 1 |
| ((5z)5-(1,3-benzodioxol-5-yl)methylene-2-phenylamino-3,5-dihydro-4h-imidazol-4-one) | Homo sapiens (human) | IC50 | 0.5200 | 1 | 1 |
This protein enables 7 target(s):
| Target | Category | Definition |
|---|---|---|
| protein serine/threonine/tyrosine kinase activity | molecular function | Catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; ATP + a protein threonine = ADP + protein threonine phosphate; and ATP + a protein tyrosine = ADP + protein tyrosine phosphate. [GOC:mah] |
| protein tyrosine kinase activity | molecular function | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. [RHEA:10596] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| ATP binding | molecular function | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
| protein serine/threonine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. [GOC:bf, MetaCyc:PROTEIN-KINASE-RXN, PMID:2956925] |
This protein is located in 1 target(s):
| Target | Category | Definition |
|---|---|---|
| intracellular membrane-bounded organelle | cellular component | Organized structure of distinctive morphology and function, bounded by a single or double lipid bilayer membrane and occurring within the cell. Includes the nucleus, mitochondria, plastids, vacuoles, and vesicles. Excludes the plasma membrane. [GOC:go_curators] |
This protein is active in 3 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] |
| cytoskeleton | cellular component | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. [GOC:mah, PMID:16959967, PMID:27419875] |
| 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] |
This protein is involved in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| peptidyl-threonine phosphorylation | biological process | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038] |
| peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |