Proteins > Dual specificity tyrosine-phosphorylation-regulated kinase 1B
Page last updated: 2024-08-07 18:54:02
Dual specificity tyrosine-phosphorylation-regulated kinase 1B
A dual specificity tyrosine-phosphorylation-regulated kinase 1B that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9Y463]
Synonyms
EC 2.7.12.1;
Minibrain-related kinase;
Mirk protein kinase
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 | 3 (14.29) | 29.6817 |
2010's | 16 (76.19) | 24.3611 |
2020's | 2 (9.52) | 2.80 |
Compounds (124)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
sb 202190 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
imatinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
staurosporine | Homo sapiens (human) | Kd | 0.0280 | 2 | 2 |
gefitinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
lestaurtinib | Homo sapiens (human) | Kd | 0.0290 | 2 | 2 |
vatalanib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
ruboxistaurin | Homo sapiens (human) | Kd | 5.4000 | 2 | 2 |
canertinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
birb 796 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
cyc 202 | Homo sapiens (human) | Kd | 1.1000 | 1 | 1 |
sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
enzastaurin | Homo sapiens (human) | Kd | 1.0000 | 1 | 1 |
erlotinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
lapatinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
sorafenib | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
pd 173955 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
s 1033 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
tg 003 | Homo sapiens (human) | Kd | 0.1300 | 1 | 1 |
bms 387032 | Homo sapiens (human) | Kd | 0.2000 | 2 | 2 |
sf 2370 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tandutinib | Homo sapiens (human) | Kd | 10.0000 | 3 | 3 |
vx-745 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
dasatinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
zd 6474 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
ml106 | Homo sapiens (human) | Kd | 0.4300 | 1 | 1 |
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1h-imidazol-2-yl)benzamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alvocidib | Homo sapiens (human) | Kd | 0.0840 | 2 | 2 |
bosutinib | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
su 11248 | Homo sapiens (human) | Kd | 2.3000 | 3 | 3 |
palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
jnj-7706621 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
vx680 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
ekb 569 | Homo sapiens (human) | Kd | 4.0000 | 1 | 1 |
axitinib | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
pd 184352 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
av 412 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms345541 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
midostaurin | Homo sapiens (human) | Kd | 0.3300 | 3 | 3 |
ki 20227 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
cp 724714 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
pi103 | Homo sapiens (human) | Kd | 7.8500 | 2 | 2 |
hki 272 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
tofacitinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamide | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
cediranib | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pazopanib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
azd 6244 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
su 14813 | Homo sapiens (human) | Kd | 2.6000 | 2 | 2 |
bibw 2992 | Homo sapiens (human) | Kd | 2.8000 | 1 | 1 |
tg100-115 | Homo sapiens (human) | Kd | 15.3650 | 2 | 2 |
cc 401 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 665752 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-one | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
brivanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
rgb 286638 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
at 7519 | Homo sapiens (human) | Kd | 0.2900 | 1 | 1 |
bi 2536 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
inno-406 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
nvp-ast487 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
kw 2449 | Homo sapiens (human) | Kd | 15.4700 | 2 | 2 |
abt 869 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
ridaforolimus | Homo sapiens (human) | Kd | 1.2620 | 1 | 1 |
cc-930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
idelalisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
crizotinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
chir-265 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
motesanib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
fostamatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
trametinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mln8054 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
GDC-0879 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
tg100801 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 461364 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
azd 1152-hqpa | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
nvp-tae684 | Homo sapiens (human) | Kd | 4.5000 | 1 | 1 |
e 7050 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
fedratinib | Homo sapiens (human) | Kd | 9.5000 | 1 | 1 |
gsk690693 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
azd5438 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pf 04217903 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gdc 0941 | Homo sapiens (human) | Kd | 16.9000 | 2 | 2 |
icotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
kx-01 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
plx 4720 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
mk 5108 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mln 8237 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sgx 523 | Homo sapiens (human) | Kd | 20.6000 | 2 | 3 |
pci 32765 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
AMG-208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
quizartinib | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
mk 2206 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sns 314 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
defactinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
incb-018424 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
TAK-580 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1838705a | Homo sapiens (human) | Kd | 0.9700 | 1 | 1 |
azd2014 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
(5-(2,4-bis((3s)-3-methylmorpholin-4-yl)pyrido(2,3-d)pyrimidin-7-yl)-2-methoxyphenyl)methanol | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
plx4032 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
gsk 1363089 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
dabrafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk-8033 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1070916 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
alectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ceritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
chir 258 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
((5z)5-(1,3-benzodioxol-5-yl)methylene-2-phenylamino-3,5-dihydro-4h-imidazol-4-one) | Homo sapiens (human) | Kd | 0.1400 | 1 | 1 |
nintedanib | Homo sapiens (human) | Kd | 1.6000 | 1 | 1 |
bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pp242 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
Synthesis of novel 1H-Pyrazolo[3,4-b]pyridine derivatives as DYRK 1A/1B inhibitors.Bioorganic & medicinal chemistry letters, , 09-01, Volume: 47, 2021
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
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
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
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
Potent and selective small molecule inhibitors of specific isoforms of Cdc2-like kinases (Clk) and dual specificity tyrosine-phosphorylation-regulated kinases (Dyrk).Bioorganic & medicinal chemistry letters, , May-15, Volume: 21, Issue:10, 2011
Evaluation of substituted 6-arylquinazolin-4-amines as potent and selective inhibitors of cdc2-like kinases (Clk).Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 19, Issue:23, 2009
Structural Optimization and Pharmacological Evaluation of Inhibitors Targeting Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases (DYRK) and CDC-like kinases (CLK) in Glioblastoma.Journal of medicinal chemistry, , 03-09, Volume: 60, Issue:5, 2017
Systematic diversification of benzylidene heterocycles yields novel inhibitor scaffolds selective for Dyrk1A, Clk1 and CK2.European journal of medicinal chemistry, , Apr-13, Volume: 112, 2016
An Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f] quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers High Selectivity for Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases.Journal of medicinal chemistry, , 11-23, Volume: 59, Issue:22, 2016
Discovery and optimization of a novel series of Dyrk1B kinase inhibitors to explore a MEK resistance hypothesis.Journal of medicinal chemistry, , Mar-26, Volume: 58, Issue:6, 2015
Small-molecule pyrimidine inhibitors of the cdc2-like (Clk) and dual specificity tyrosine phosphorylation-regulated (Dyrk) kinases: development of chemical probe ML315.Bioorganic & medicinal chemistry letters, , Jun-15, Volume: 23, Issue:12, 2013
Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B.Journal of medicinal chemistry, , Nov-08, Volume: 55, Issue:21, 2012
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
Structure-Activity Relationship in the Leucettine Family of Kinase Inhibitors.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B.Journal of medicinal chemistry, , Nov-08, Volume: 55, Issue:21, 2012
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
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
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
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
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
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
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
2-Aminothiazole Derivatives as Selective Allosteric Modulators of the Protein Kinase CK2. 2. Structure-Based Optimization and Investigation of Effects Specific to the Allosteric Mode of Action.Journal of medicinal chemistry, , 02-28, Volume: 62, Issue:4, 2019
2-Aminothiazole Derivatives as Selective Allosteric Modulators of the Protein Kinase CK2. 1. Identification of an Allosteric Binding Site.Journal of medicinal chemistry, , 02-28, Volume: 62, Issue:4, 2019
Dual-Specificity Tyrosine Phosphorylation-Regulated Kinase 1A (DYRK1A) Inhibitors as Potential Therapeutics.Journal of medicinal chemistry, , 11-21, Volume: 61, Issue:22, 2018
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
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
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
Structure-Activity Relationship in the Leucettine Family of Kinase Inhibitors.Journal of medicinal chemistry, , 01-27, Volume: 65, Issue:2, 2022
An Unusual Binding Model of the Methyl 9-Anilinothiazolo[5,4-f] quinazoline-2-carbimidates (EHT 1610 and EHT 5372) Confers High Selectivity for Dual-Specificity Tyrosine Phosphorylation-Regulated Kinases.Journal of medicinal chemistry, , 11-23, Volume: 59, Issue:22, 2016
Chemical synthesis and biological validation of immobilized protein kinase inhibitory Leucettines.European journal of medicinal chemistry, , Volume: 62, 2013
Selectivity, cocrystal structures, and neuroprotective properties of leucettines, a family of protein kinase inhibitors derived from the marine sponge alkaloid leucettamine B.Journal of medicinal chemistry, , Nov-08, Volume: 55, Issue:21, 2012
Enables
This protein enables 8 target(s):
Target | Category | Definition |
transcription coactivator activity | molecular function | A transcription coregulator activity that activates or increases the transcription of specific gene sets via binding to a DNA-bound DNA-binding transcription factor, either on its own or as part of a complex. Coactivators often act by altering chromatin structure and modifications. For example, one class of transcription coactivators modifies chromatin structure through covalent modification of histones. A second class remodels the conformation of chromatin in an ATP-dependent fashion. A third class modulates interactions of DNA-bound DNA-binding transcription factors with other transcription coregulators. A fourth class of coactivator activity is the bridging of a DNA-binding transcription factor to the general (basal) transcription machinery. The Mediator complex, which bridges sequence-specific DNA binding transcription factors and RNA polymerase, is also a transcription coactivator. [GOC:txnOH-2018, PMID:10213677, PMID:16858867] |
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 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] |
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 3 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] |
chromosome | cellular component | A structure composed of a very long molecule of DNA and associated proteins (e.g. histones) that carries hereditary information. [ISBN:0198547684] |
nucleolus | cellular component | A small, dense body one or more of which are present in the nucleus of eukaryotic cells. It is rich in RNA and protein, is not bounded by a limiting membrane, and is not seen during mitosis. Its prime function is the transcription of the nucleolar DNA into 45S ribosomal-precursor RNA, the processing of this RNA into 5.8S, 18S, and 28S components of ribosomal RNA, and the association of these components with 5S RNA and proteins synthesized outside the nucleolus. This association results in the formation of ribonucleoprotein precursors; these pass into the cytoplasm and mature into the 40S and 60S subunits of the ribosome. [ISBN:0198506732] |
Active In
This protein is active in 1 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] |
Involved In
This protein is involved in 7 target(s):
Target | Category | Definition |
DNA repair | biological process | The process of restoring DNA after damage. Genomes are subject to damage by chemical and physical agents in the environment (e.g. UV and ionizing radiations, chemical mutagens, fungal and bacterial toxins, etc.) and by free radicals or alkylating agents endogenously generated in metabolism. DNA is also damaged because of errors during its replication. A variety of different DNA repair pathways have been reported that include direct reversal, base excision repair, nucleotide excision repair, photoreactivation, bypass, double-strand break repair pathway, and mismatch repair pathway. [PMID:11563486] |
protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
myoblast fusion | biological process | A process in which non-proliferating myoblasts fuse to existing fibers or to myotubes to form new fibers. A myoblast is a mononucleate cell type that, by fusion with other myoblasts, gives rise to the myotubes that eventually develop into skeletal muscle fibers. [CL:0000056, GOC:mtg_muscle] |
positive regulation of DNA-templated transcription | biological process | Any process that activates or increases the frequency, rate or extent of cellular DNA-templated transcription. [GOC:go_curators, GOC:txnOH] |
adipose tissue development | biological process | The process whose specific outcome is the progression of adipose tissue over time, from its formation to the mature structure. Adipose tissue is specialized tissue that is used to store fat. [GOC:dph] |
peptidyl-serine phosphorylation | biological process | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037] |
peptidyl-threonine phosphorylation | biological process | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038] |