Page last updated: 2024-08-07 23:47:30

Myotonin-protein kinase

A myotonin-protein kinase that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q09013]

Synonyms

MT-PK;
EC 2.7.11.1;
DM-kinase;
DMK;
DM1 protein kinase;
DMPK;
Myotonic dystrophy protein kinase

Research

Bioassay Publications (7)

TimeframeStudies on this Protein(%)All Drugs %
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's2 (28.57)29.6817
2010's5 (71.43)24.3611
2020's0 (0.00)2.80

Compounds (77)

Drugs with Inhibition Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
fasudilHomo sapiens (human)IC508.000011
staurosporineHomo sapiens (human)IC500.173522
sb 203580Homo sapiens (human)IC501.000011
y 27632, dihydrochloride, (4(r)-trans)-isomerHomo sapiens (human)IC508.000011

Drugs with Activation Measurements

DrugTaxonomyMeasurementAverage (mM)Bioassay(s)Publication(s)
sb 202190Homo sapiens (human)Kd10.000011
imatinibHomo sapiens (human)Kd10.000022
staurosporineHomo sapiens (human)Kd0.003522
gefitinibHomo sapiens (human)Kd6.900022
lestaurtinibHomo sapiens (human)Kd0.240022
vatalanibHomo sapiens (human)Kd10.000022
ruboxistaurinHomo sapiens (human)Kd0.280022
canertinibHomo sapiens (human)Kd8.500022
birb 796Homo sapiens (human)Kd10.000022
cyc 202Homo sapiens (human)Kd10.000011
sb 203580Homo sapiens (human)Kd10.000022
enzastaurinHomo sapiens (human)Kd2.200011
erlotinibHomo sapiens (human)Kd2.900022
lapatinibHomo sapiens (human)Kd10.000022
sorafenibHomo sapiens (human)Kd10.000033
pd 173955Homo sapiens (human)Kd10.000011
s 1033Homo sapiens (human)Kd10.000011
bms 387032Homo sapiens (human)Kd10.000022
tandutinibHomo sapiens (human)Kd10.000033
vx-745Homo sapiens (human)Kd10.000022
dasatinibHomo sapiens (human)Kd1.300022
zd 6474Homo sapiens (human)Kd10.000022
4-(5-benzo(1,3)dioxol-5-yl-4-pyridin-2-yl-1h-imidazol-2-yl)benzamideHomo sapiens (human)Kd10.000011
alvocidibHomo sapiens (human)Kd0.650022
bosutinibHomo sapiens (human)Kd0.091011
su 11248Homo sapiens (human)Kd10.000033
jnj-7706621Homo sapiens (human)Kd1.200011
vx680Homo sapiens (human)Kd10.000022
ekb 569Homo sapiens (human)Kd0.059011
axitinibHomo sapiens (human)Kd10.000011
pd 184352Homo sapiens (human)Kd10.000011
bms345541Homo sapiens (human)Kd10.000011
midostaurinHomo sapiens (human)Kd3.800033
ki 20227Homo sapiens (human)Kd10.000011
cp 724714Homo sapiens (human)Kd10.000011
pi103Homo sapiens (human)Kd10.000022
hki 272Homo sapiens (human)Kd10.000011
tofacitinibHomo sapiens (human)Kd5.600022
n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamideHomo sapiens (human)Kd10.000011
cediranibHomo sapiens (human)Kd10.000011
masitinibHomo sapiens (human)Kd10.000011
pazopanibHomo sapiens (human)Kd10.000022
azd 6244Homo sapiens (human)Kd10.000011
su 14813Homo sapiens (human)Kd10.000022
bibw 2992Homo sapiens (human)Kd10.000011
tg100-115Homo sapiens (human)Kd10.000011
pha 665752Homo sapiens (human)Kd10.000011
6-[[5-fluoro-2-(3,4,5-trimethoxyanilino)-4-pyrimidinyl]amino]-2,2-dimethyl-4H-pyrido[3,2-b][1,4]oxazin-3-oneHomo sapiens (human)Kd10.000011
brivanibHomo sapiens (human)Kd10.000011
at 7519Homo sapiens (human)Kd1.100011
bi 2536Homo sapiens (human)Kd2.900011
nvp-ast487Homo sapiens (human)Kd10.000022
kw 2449Homo sapiens (human)Kd3.800011
abt 869Homo sapiens (human)Kd10.000022
gw 2580Homo sapiens (human)Kd10.000022
crizotinibHomo sapiens (human)Kd1.400011
chir-265Homo sapiens (human)Kd10.000022
motesanibHomo sapiens (human)Kd10.000022
mln8054Homo sapiens (human)Kd10.000022
GDC-0879Homo sapiens (human)Kd10.000011
gsk 461364Homo sapiens (human)Kd10.000011
azd 1152-hqpaHomo sapiens (human)Kd10.000022
nvp-tae684Homo sapiens (human)Kd2.100011
fedratinibHomo sapiens (human)Kd1.000011
gsk690693Homo sapiens (human)Kd10.000011
gdc 0941Homo sapiens (human)Kd10.000011
plx 4720Homo sapiens (human)Kd10.000011
sgx 523Homo sapiens (human)Kd10.000011
quizartinibHomo sapiens (human)Kd10.000022
incb-018424Homo sapiens (human)Kd3.500011
gsk 1838705aHomo sapiens (human)Kd10.000011
gsk 1363089Homo sapiens (human)Kd10.000011
chir 258Homo sapiens (human)Kd10.000022
nintedanibHomo sapiens (human)Kd10.000011
pp242Homo sapiens (human)Kd0.140011

Enables

This protein enables 6 target(s):

TargetCategoryDefinition
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 bindingmolecular functionBinding to a protein. [GOC:go_curators]
ATP bindingmolecular functionBinding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. [ISBN:0198506732]
myosin phosphatase regulator activitymolecular functionBinds to and modulates of the activity of myosin phosphatase. [GOC:ai, PMID:10491107]
metal ion bindingmolecular functionBinding to a metal ion. [GOC:ai]
protein serine kinase activitymolecular functionCatalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989]

Located In

This protein is located in 7 target(s):

TargetCategoryDefinition
nuclear outer membranecellular componentThe outer, i.e. cytoplasm-facing, lipid bilayer of the nuclear envelope; continuous with the endoplasmic reticulum of the cell and sometimes studded with ribosomes. [ISBN:0198547684]
mitochondrial outer membranecellular componentThe outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope. [GOC:ai]
endoplasmic reticulum membranecellular componentThe lipid bilayer surrounding the endoplasmic reticulum. [GOC:mah]
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]
plasma membranecellular componentThe membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363]
nuclear membranecellular componentEither of the lipid bilayers that surround the nucleus and form the nuclear envelope; excludes the intermembrane space. [GOC:mah, GOC:pz]
sarcoplasmic reticulum membranecellular componentThe lipid bilayer surrounding the sarcoplasmic reticulum. [GOC:rph]

Involved In

This protein is involved in 11 target(s):

TargetCategoryDefinition
regulation of sodium ion transportbiological processAny process that modulates the frequency, rate or extent of the directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:dph]
protein phosphorylationbiological processThe process of introducing a phosphate group on to a protein. [GOC:hb]
intracellular calcium ion homeostasisbiological processA homeostatic process involved in the maintenance of a steady state level of calcium ions within a cell. [GOC:ceb, GOC:mah]
nuclear envelope organizationbiological processA process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the nuclear envelope. [GOC:dph, GOC:ems, GOC:jl, GOC:mah]
regulation of heart contractionbiological processAny process that modulates the frequency, rate or extent of heart contraction. Heart contraction is the process in which the heart decreases in volume in a characteristic way to propel blood through the body. [GOC:dph, GOC:go_curators, GOC:tb]
muscle cell apoptotic processbiological processA form of programmed cell death induced by external or internal signals that trigger the activity of proteolytic caspases, whose actions dismantle a muscle cell and result in its death. A muscle cell is a mature contractile cell, commonly known as a myocyte, that forms one of three kinds of muscle. [CL:0000187, GOC:dph, GOC:mtg_apoptosis, GOC:tb]
regulation of myotube differentiationbiological processAny process that modulates the frequency, rate or extent of myotube differentiation. Myotube differentiation is the process in which a relatively unspecialized cell acquires specialized features of a myotube cell. Myotubes are multinucleated cells that are formed when proliferating myoblasts exit the cell cycle, differentiate and fuse. [GOC:dph, GOC:tb]
regulation of excitatory postsynaptic membrane potential involved in skeletal muscle contractionbiological processAny process, involved in skeletal muscle contraction, that modulates the establishment or extent of the excitatory postsynaptic potential (EPSP). Excitatory postsynaptic potential (EPSP) is a temporay increase in postsynaptic potential due to the flow of positively charged ions into the postsynaptic cell. The flow of ions that causes an EPSP is an excitatory postsynaptic current (EPSC) and makes it easier for the neuron to fire an action potential. [GOC:ef, GOC:mtg_muscle]
regulation of synapse structural plasticitybiological processAny process that modulates the frequency, rate or extent of synapse structural plasticity. Synapse structural plasticity is a type of cytoskeletal remodeling; this remodeling is induced by stimuli that can lead to long term potentiation and it can be activity-dependent or -independent. Examples of cytoskeletal changes include the formation of new spines and increase in spine size; this can be accompanied by the insertion of greater numbers of glutamate (or other neurotransmitter) receptors into the post-synaptic membrane. [PMID:11063967, PMID:14976517, PMID:9884123]
peptidyl-serine phosphorylationbiological processThe phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. [RESID:AA0037]
regulation of skeletal muscle contraction by calcium ion signalingbiological processAny process that modulates the frequency, rate or extent of skeletal muscle contraction by changing the calcium ion signals that trigger contraction. [GOC:mtg_muscle]