Proteins > MAP kinase-interacting serine/threonine-protein kinase 1
Page last updated: 2024-08-07 18:48:33
MAP kinase-interacting serine/threonine-protein kinase 1
A MAP kinase-interacting serine/threonine-protein kinase 1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9BUB5]
Synonyms
EC 2.7.11.1;
MAP kinase signal-integrating kinase 1;
MAPK signal-integrating kinase 1;
Mnk1
Research
Bioassay Publications (21)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 4 (19.05) | 29.6817 |
| 2010's | 11 (52.38) | 24.3611 |
| 2020's | 6 (28.57) | 2.80 |
Compounds (90)
Drugs with Inhibition Measurements
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
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
Stepwise Evolution of Fragment Hits against MAPK Interacting Kinases 1 and 2.Journal of medicinal chemistry, , 01-23, Volume: 63, Issue:2, 2020
Structure-Activity Relationship Studies of Mitogen Activated Protein Kinase Interacting Kinase (MNK) 1 and 2 and BCR-ABL1 Inhibitors Targeting Chronic Myeloid Leukemic Cells.Journal of medicinal chemistry, , Apr-14, Volume: 59, Issue:7, 2016
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
Overcoming Paradoxical Kinase Priming by a Novel MNK1 Inhibitor.Journal of medicinal chemistry, , 04-28, Volume: 65, Issue:8, 2022
Update on the Development of MNK Inhibitors as Therapeutic Agents.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Optimization of 4,6-Disubstituted Pyrido[3,2-Journal of medicinal chemistry, , 09-23, Volume: 64, Issue:18, 2021
Progress in developing MNK inhibitors.European journal of medicinal chemistry, , Jul-05, Volume: 219, 2021
Targeting the immunity protein kinases for immuno-oncology.European journal of medicinal chemistry, , Feb-01, Volume: 163, 2019
Design, synthesis and biological evaluation of 4-aniline-thieno[2,3-d]pyrimidine derivatives as MNK1 inhibitors against renal cell carcinoma and nasopharyngeal carcinoma.Bioorganic & medicinal chemistry, , 06-01, Volume: 27, Issue:11, 2019
Design and synthesis of novel 6-hydroxy-4-methoxy-3-methylbenzofuran-7-carboxamide derivatives as potent Mnks inhibitors by fragment-based drug design.Bioorganic & medicinal chemistry, , 09-01, Volume: 26, Issue:16, 2018
Discovery of 4-(dihydropyridinon-3-yl)amino-5-methylthieno[2,3-d]pyrimidine derivatives as potent Mnk inhibitors: synthesis, structure-activity relationship analysis and biological evaluation.European journal of medicinal chemistry, , May-05, Volume: 95, 2015
An integrated approach for discovery of highly potent and selective Mnk inhibitors: Screening, synthesis and SAR analysis.European journal of medicinal chemistry, , Oct-20, Volume: 103, 2015
Discovery of mitogen-activated protein kinase-interacting kinase 1 inhibitors by a comprehensive fragment-oriented virtual screening approach.Journal of medicinal chemistry, , Sep-23, Volume: 53, Issue:18, 2010
The selectivity of protein kinase inhibitors: a further update.The Biochemical journal, , Dec-15, Volume: 408, Issue:3, 2007
Discovery of mitogen-activated protein kinase-interacting kinase 1 inhibitors by a comprehensive fragment-oriented virtual screening approach.Journal of medicinal chemistry, , Sep-23, Volume: 53, Issue:18, 2010
Pyrrolopyridine inhibitors of mitogen-activated protein kinase-activated protein kinase 2 (MK-2).Journal of medicinal chemistry, , May-31, Volume: 50, Issue:11, 2007
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 8 target(s):
| Target | Category | Definition |
|---|
| 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] |
| 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] |
| calmodulin-dependent protein kinase activity | molecular function | Calmodulin-dependent catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. [GOC:mah, PMID:11264466] |
| calcium-dependent protein serine/threonine kinase activity | molecular function | Calcium-dependent catalysis of the reactions: ATP + a protein serine = ADP + protein serine phosphate; and ATP + a protein threonine = ADP + protein threonine phosphate. [GOC:mah] |
| calmodulin binding | molecular function | Binding to calmodulin, a calcium-binding protein with many roles, both in the calcium-bound and calcium-free states. [GOC:krc] |
Located In
This protein is located in 2 target(s):
| Target | Category | Definition |
|---|
| nucleoplasm | cellular component | That part of the nuclear content other than the chromosomes or the nucleolus. [GOC:ma, ISBN:0124325653] |
| 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] |
Active In
This protein is active 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] |
| 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] |
Involved In
This protein is involved in 5 target(s):
| Target | Category | Definition |
|---|
| regulation of translation | biological process | Any process that modulates the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of proteins by the translation of mRNA or circRNA. [GOC:isa_complete] |
| protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
| peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |
| intracellular signal transduction | biological process | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. [GOC:bf, GOC:jl, GOC:signaling, ISBN:3527303782] |
| 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] |