Page last updated: 2024-08-07 18:26:45

Dual specificity tyrosine-phosphorylation-regulated kinase 3

A dual specificity tyrosine-phosphorylation-regulated kinase 3 that is encoded in the genome of human. [PRO:DNx, UniProtKB:O43781]

Synonyms

EC 2.7.12.1;
Regulatory erythroid kinase;
REDK

Research

Bioassay Publications (10)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (10.00)29.6817
2010's8 (80.00)24.3611
2020's1 (10.00)2.80

Compounds (6)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
staurosporineHomo sapiens (human)IC500.023122
cyc 202Homo sapiens (human)IC5010.000011
harmineHomo sapiens (human)IC500.604055
leucettamine bHomo sapiens (human)IC501.350022
cgp 57380Homo sapiens (human)IC503.200011
((5z)5-(1,3-benzodioxol-5-yl)methylene-2-phenylamino-3,5-dihydro-4h-imidazol-4-one)Homo sapiens (human)IC500.416733

Enables

This protein enables 7 target(s):

TargetCategoryDefinition
magnesium ion bindingmolecular functionBinding to a magnesium (Mg) ion. [GOC:ai]
protein kinase activitymolecular functionCatalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. [PMID:25399640]
protein serine/threonine kinase activitymolecular functionCatalysis 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]
protein serine/threonine/tyrosine kinase activitymolecular functionCatalysis 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 activitymolecular functionCatalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. [RHEA:10596]
ATP bindingmolecular functionBinding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
protein serine kinase activitymolecular functionCatalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989]

Located In

This protein is located in 8 target(s):

TargetCategoryDefinition
pericentriolar materialcellular componentA network of small fibers that surrounds the centrioles in cells; contains the microtubule nucleating activity of the centrosome. [GOC:clt, ISBN:0815316194]
nucleuscellular componentA 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]
nucleoplasmcellular componentThat part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
cytosolcellular componentThe part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
cytoplasmic stress granulecellular componentA dense aggregation in the cytosol composed of proteins and RNAs that appear when the cell is under stress. [GOC:ans, PMID:17284590, PMID:17601829, PMID:17967451, PMID:20368989]
nuclear speckcellular componentA discrete extra-nucleolar subnuclear domain, 20-50 in number, in which splicing factors are seen to be localized by immunofluorescence microscopy. [http://www.cellnucleus.com/]
intracellular membrane-bounded organellecellular componentOrganized 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]

Active In

This protein is active in 3 target(s):

TargetCategoryDefinition
nucleuscellular componentA 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]
cytoskeletoncellular componentA 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]
cytoplasmcellular componentThe contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]

Involved In

This protein is involved in 13 target(s):

TargetCategoryDefinition
protein phosphorylationbiological processThe process of introducing a phosphate group on to a protein. [GOC:hb]
erythrocyte differentiationbiological processThe process in which a myeloid precursor cell acquires specializes features of an erythrocyte. [GOC:mah]
nuclear speck organizationbiological processA process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of nuclear specks, a class of nuclear body in which splicing factors are localized. [GOC:bf, GOC:curators]
stress granule disassemblybiological processThe disaggregation of a stress granule into its constituent protein and RNA parts. [GOC:BHF, PMID:19825938]
negative regulation of apoptotic processbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of cell death by apoptotic process. [GOC:jl, GOC:mtg_apoptosis]
negative regulation of DNA damage response, signal transduction by p53 class mediatorbiological processAny process that stops, prevents, or reduces the frequency, rate or extent of the cascade of processes induced by the cell cycle regulator phosphoprotein p53, or an equivalent protein, in response to the detection of DNA damage. [GOC:jl]
cell divisionbiological processThe process resulting in division and partitioning of components of a cell to form more cells; may or may not be accompanied by the physical separation of a cell into distinct, individually membrane-bounded daughter cells. [GOC:di, GOC:go_curators, GOC:pr]
regulation of cellular response to stressbiological processAny process that modulates the frequency, rate or extent of a cellular response to stress. Cellular response to stress is 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 the organism is under stress. The stress is usually, but not necessarily, exogenous (e.g. temperature, humidity, ionizing radiation). [GOC:dhl]
positive regulation of cell cycle G2/M phase transitionbiological processAny signaling pathway that activates or increases the activity of a cell cycle cyclin-dependent protein kinase to modulate the switch from G2 phase to M phase of the cell cycle. [GO_REF:0000058, GOC:jl, GOC:TermGenie]
organelle disassemblybiological processThe disaggregation of an organelle into its constituent components. [GO_REF:0000079, GOC:TermGenie]
regulation of TORC1 signalingbiological processAny process that modulates the frequency, rate or extent of TORC1 signaling. [GO_REF:0000058, GOC:TermGenie]
peptidyl-serine phosphorylationbiological processThe phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037]
peptidyl-threonine phosphorylationbiological processThe phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038]