Proteins > Serine/threonine-protein kinase 25
Page last updated: 2024-08-07 22:59:51
Serine/threonine-protein kinase 25
A serine/threonine-protein kinase 25 that is encoded in the genome of human. [PRO:WCB, UniProtKB:O00506]
Synonyms
EC 2.7.11.1;
Ste20-like kinase;
Sterile 20/oxidant stress-response kinase 1;
SOK-1;
Ste20/oxidant stress response kinase 1
Research
Bioassay Publications (6)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (33.33) | 29.6817 |
| 2010's | 4 (66.67) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
Compounds (75)
Drugs with Inhibition Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| staurosporine | Homo sapiens (human) | IC50 | 0.0029 | 3 | 3 |
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
Chemistry-oriented synthesis (ChOS) and target deconvolution on neuroprotective effect of a novel scaffold, oxaza spiroquinone.European journal of medicinal chemistry, , Feb-01, Volume: 163, 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
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
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
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
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 7 target(s):
| Target | Category | Definition |
|---|
| protein kinase activity | molecular function | Catalysis 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 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 homodimerization activity | molecular function | Binding to an identical protein to form a homodimer. [GOC:jl] |
| 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] |
Located In
This protein is located 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] |
| extracellular exosome | cellular component | A vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm. [GOC:BHF, GOC:mah, GOC:vesicles, PMID:15908444, PMID:17641064, PMID:19442504, PMID:19498381, PMID:22418571, PMID:24009894] |
Active In
This protein is active in 1 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] |
Part Of
This protein is part of 1 target(s):
| Target | Category | Definition |
|---|
| FAR/SIN/STRIPAK complex | cellular component | A conserved protein phosphatase type 2A complex which contains a protein phosphatase type 2A, a protein phosphatase regulatory subunit, a striatin, an FHA domain protein and other subunits (at least six proteins). In fission yeast this complex negatively regulate the septation initiation network at the spindle pole body. [GOC:vw, PMID:21561862, PMID:22119525] |
Involved In
This protein is involved in 13 target(s):
| Target | Category | Definition |
|---|
| protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
| response to oxidative stress | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:jl, PMID:12115731] |
| establishment or maintenance of cell polarity | biological process | Any cellular process that results in the specification, formation or maintenance of anisotropic intracellular organization or cell growth patterns. [GOC:mah] |
| signal transduction | biological process | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. [GOC:go_curators, GOC:mtg_signaling_feb11] |
| axonogenesis | biological process | De novo generation of a long process of a neuron, including the terminal branched region. Refers to the morphogenesis or creation of shape or form of the developing axon, which carries efferent (outgoing) action potentials from the cell body towards target cells. [GOC:dph, GOC:jid, GOC:pg, GOC:pr, ISBN:0198506732] |
| positive regulation of stress-activated MAPK cascade | biological process | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the stress-activated MAPK cascade. [GOC:mah] |
| cellular response to oxidative stress | 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 oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. [GOC:mah] |
| intrinsic apoptotic signaling pathway in response to hydrogen peroxide | biological process | The series of molecular signals in which an intracellular signal is conveyed to trigger the apoptotic death of a cell. The pathway is induced in response to hydrogen peroxide (H2O2). [GOC:bf, GOC:PARL] |
| 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] |
| positive regulation of axonogenesis | biological process | Any process that activates or increases the frequency, rate or extent of axonogenesis. [GOC:ai] |
| Golgi localization | biological process | Any process in which the Golgi is transported to, and/or maintained in, a specific location within the cell. [GOC:ai] |
| establishment of Golgi localization | biological process | The directed movement of the Golgi to a specific location. [GOC:ai] |
| Golgi reassembly | biological process | The reformation of the Golgi following its breakdown and partitioning contributing to Golgi inheritance. [GOC:ascb_2009, GOC:dph, GOC:tb] |