Proteins > cAMP-dependent protein kinase catalytic subunit PRKX
Page last updated: 2024-08-07 23:35:00
cAMP-dependent protein kinase catalytic subunit PRKX
A serine/threonine-protein kinase PRKX that is encoded in the genome of human. [PRO:DNx, UniProtKB:P51817]
Synonyms
PrKX;
Protein kinase X;
Protein kinase X-linked;
Serine/threonine-protein kinase PRKX;
EC 2.7.11.1;
Protein kinase PKX1
Research
Bioassay Publications (8)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 3 (37.50) | 29.6817 |
| 2010's | 5 (62.50) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Compounds (76)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| staurosporine | Homo sapiens (human) | IC50 | 0.0014 | 2 | 2 |
| birb 796 | Homo sapiens (human) | IC50 | 30.0000 | 1 | 1 |
| gsk690693 | Homo sapiens (human) | IC50 | 0.0050 | 1 | 1 |
Drugs with Activation Measurements
ASR352, A potent anticancer agent: Synthesis, preliminary SAR, and biological activities against colorectal cancer bulk, 5-fluorouracil/oxaliplatin resistant and stem cells.European journal of medicinal chemistry, , Jan-01, Volume: 161, 2019
Novel quinazoline derivatives bearing various 6-benzamide moieties as highly selective and potent EGFR inhibitors.Bioorganic & medicinal chemistry, , 05-01, Volume: 26, Issue:8, 2018
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD).Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 21, Issue:23, 2011
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
Identification of 4-(2-(4-amino-1,2,5-oxadiazol-3-yl)-1-ethyl-7-{[(3S)-3-piperidinylmethyl]oxy}-1H-imidazo[4,5-c]pyridin-4-yl)-2-methyl-3-butyn-2-ol (GSK690693), a novel inhibitor of AKT kinase.Journal of medicinal chemistry, , Sep-25, Volume: 51, Issue:18, 2008
Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML).Blood, , Oct-01, Volume: 114, Issue:14, 2009
Enables
This protein enables 4 target(s):
| Target | Category | Definition |
|---|
| cAMP-dependent protein kinase activity | molecular function | cAMP-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. [EC:2.7.11.11] |
| 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] |
| protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
Located In
This protein is located in 3 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] |
Involved In
This protein is involved in 14 target(s):
| Target | Category | Definition |
|---|
| angiogenesis | biological process | Blood vessel formation when new vessels emerge from the proliferation of pre-existing blood vessels. [ISBN:0878932453] |
| endothelial cell proliferation | biological process | The multiplication or reproduction of endothelial cells, resulting in the expansion of a cell population. Endothelial cells are thin flattened cells which line the inside surfaces of body cavities, blood vessels, and lymph vessels, making up the endothelium. [GOC:add, ISBN:0781735149] |
| cell adhesion | biological process | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. [GOC:hb, GOC:pf] |
| peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |
| myeloid cell differentiation | biological process | The process in which a relatively unspecialized myeloid precursor cell acquires the specialized features of any cell of the myeloid leukocyte, megakaryocyte, thrombocyte, or erythrocyte lineages. [GOC:add, ISBN:0781735149] |
| regulation of cell adhesion | biological process | Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix. [GOC:mah] |
| regulation of cell migration | biological process | Any process that modulates the frequency, rate or extent of cell migration. [GOC:go_curators] |
| cell-substrate adhesion | biological process | The attachment of a cell to the underlying substrate via adhesion molecules. [GOC:mah, GOC:pf] |
| endothelial cell migration | biological process | The orderly movement of an endothelial cell into the extracellular matrix to form an endothelium. [GOC:go_curators] |
| protein autophosphorylation | biological process | The phosphorylation by a protein of one or more of its own amino acid residues (cis-autophosphorylation), or residues on an identical protein (trans-autophosphorylation). [ISBN:0198506732] |
| epithelial tube morphogenesis | biological process | The process in which the anatomical structures of a tube are generated and organized from an epithelium. Epithelial tubes transport gases, liquids and cells from one site to another and form the basic structure of many organs and tissues, with tube shape and organization varying from the single-celled excretory organ in Caenorhabditis elegans to the branching trees of the mammalian kidney and insect tracheal system. [GOC:dph] |
| kidney morphogenesis | biological process | Morphogenesis of a kidney. A kidney is an organ that filters the blood and excretes the end products of body metabolism in the form of urine. [GOC:dph, GOC:mtg_kidney_jan10] |
| regulation of epithelial cell differentiation involved in kidney development | biological process | Any process that modulates the frequency, rate or extent of epithelial cell differentiation involved in kidney development. [GOC:mtg_kidney_jan10, GOC:yaf] |
| protein kinase A signaling | biological process | An intracellular signaling cassette that starts with the activation of protein kinase A (PKA), and ends with the regulation of a downstream cellular process, e.g. transcription. The PKA catalytic subunit (PKA-C) is normally present in a complex with its regulatory subunit, PKA-R. The inhibitory action of PKA-R is released upon cAMP binding, which results in the activation of PKA-C. [PMID:35252178, PMID:36431013] |