Proteins > Dual specificity protein kinase CLK1
Page last updated: 2024-08-07 18:37:07
Dual specificity protein kinase CLK1
A dual specificity protein kinase CLK1 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P49759]
Synonyms
EC 2.7.12.1;
CDC-like kinase 1
Research
Bioassay Publications (29)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 5 (17.24) | 29.6817 |
2010's | 22 (75.86) | 24.3611 |
2020's | 2 (6.90) | 2.80 |
Compounds (239)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
fasudil | Homo sapiens (human) | Kd | 0.1520 | 1 | 1 |
4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sb 202190 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
imatinib | Homo sapiens (human) | Kd | 10.8750 | 4 | 4 |
staurosporine | Homo sapiens (human) | Kd | 0.0303 | 3 | 3 |
gefitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
lestaurtinib | Homo sapiens (human) | Kd | 0.0661 | 3 | 3 |
perifosine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vatalanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
ruboxistaurin | Homo sapiens (human) | Kd | 0.9100 | 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 | 11.1000 | 3 | 3 |
sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
enzastaurin | Homo sapiens (human) | Kd | 0.5100 | 1 | 1 |
erlotinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
lapatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
sorafenib | Homo sapiens (human) | Kd | 14.3750 | 4 | 4 |
pd 173955 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
s 1033 | Homo sapiens (human) | Kd | 2.1000 | 2 | 2 |
tg 003 | Homo sapiens (human) | Kd | 0.0190 | 1 | 1 |
xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cgp 74514a | Homo sapiens (human) | EC50 | 4.2000 | 1 | 1 |
bms 387032 | Homo sapiens (human) | Kd | 0.8870 | 3 | 3 |
sf 2370 | Homo sapiens (human) | Kd | 0.0100 | 1 | 1 |
tandutinib | Homo sapiens (human) | Kd | 6.6580 | 5 | 5 |
vx-745 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
dasatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
ha 1100 | Homo sapiens (human) | Kd | 24.0560 | 1 | 1 |
7-epi-hydroxystaurosporine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
zd 6474 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
ml106 | Homo sapiens (human) | Kd | 0.0370 | 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 |
imd 0354 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alvocidib | Homo sapiens (human) | Kd | 8.9000 | 4 | 4 |
bosutinib | Homo sapiens (human) | Kd | 0.5993 | 3 | 3 |
orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
su 11248 | Homo sapiens (human) | Kd | 0.1040 | 7 | 7 |
palbociclib | Homo sapiens (human) | Kd | 0.2760 | 1 | 1 |
jnj-7706621 | Homo sapiens (human) | Kd | 0.6600 | 1 | 1 |
vx680 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
cyc 116 | Homo sapiens (human) | Kd | 0.5860 | 1 | 1 |
everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ekb 569 | Homo sapiens (human) | Kd | 11.4333 | 3 | 3 |
axitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
aminopurvalanol a | Homo sapiens (human) | EC50 | 12.0000 | 1 | 1 |
temsirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
pd 184352 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
on 01910 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
av 412 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
telatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
y-39983 | Homo sapiens (human) | Kd | 0.0180 | 1 | 1 |
cp 547632 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms345541 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
lenvatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pd 0325901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
midostaurin | Homo sapiens (human) | Kd | 7.7625 | 4 | 4 |
px-866 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
osi 930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ki 20227 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
scio-469 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cp 724714 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
pi103 | Homo sapiens (human) | Kd | 3.9000 | 2 | 2 |
hmn-214 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tivozanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
hki 272 | Homo sapiens (human) | Kd | 23.3333 | 2 | 3 |
tofacitinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
n-(6-chloro-7-methoxy-9h-beta-carbolin-8-yl)-2-methylnicotinamide | Homo sapiens (human) | Kd | 0.6400 | 1 | 1 |
cediranib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
pazopanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
azd 6244 | Homo sapiens (human) | Kd | 23.3333 | 2 | 3 |
su 14813 | Homo sapiens (human) | Kd | 10.2400 | 3 | 3 |
bibw 2992 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
binimetinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sotrastaurin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
aee 788 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
saracatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vx 702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
crenolanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tg100-115 | Homo sapiens (human) | Kd | 15.0700 | 2 | 2 |
cc 401 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms 599626 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
exel-7647 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 665752 | Homo sapiens (human) | Kd | 0.7300 | 1 | 1 |
azd 7762 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
regorafenib | Homo sapiens (human) | Kd | 2.1070 | 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 | 15.6000 | 2 | 2 |
brivanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
mp470 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
rgb 286638 | Homo sapiens (human) | Kd | 0.0020 | 1 | 1 |
np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
at 7519 | Homo sapiens (human) | Kd | 2.7280 | 2 | 2 |
bms-690514 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bi 2536 | Homo sapiens (human) | Kd | 15.4700 | 2 | 2 |
inno-406 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
nvp-ast487 | Homo sapiens (human) | Kd | 0.1100 | 2 | 2 |
kw 2449 | Homo sapiens (human) | Kd | 1.2075 | 2 | 2 |
danusertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
abt 869 | Homo sapiens (human) | Kd | 15.9333 | 3 | 3 |
azd 8931 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
arq 197 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd 1152 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pf 00299804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ridaforolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ch 4987655 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
6-(5-((cyclopropylamino)carbonyl)-3-fluoro-2-methylphenyl)-n-(2,2-dimethylprpyl)-3-pyridinecarboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cc-930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
tak 285 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
idelalisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
crizotinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
chir-265 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
motesanib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
fostamatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
trametinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mln8054 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
pf-562,271 | Homo sapiens (human) | Kd | 0.3630 | 1 | 1 |
GDC-0879 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
jnj-26483327 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ly2603618 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tg100801 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dactolisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bgt226 | Homo sapiens (human) | Kd | 0.2460 | 1 | 1 |
gsk 461364 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
azd 1152-hqpa | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
nvp-tae684 | Homo sapiens (human) | Kd | 0.0120 | 1 | 1 |
enmd 2076 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
e 7050 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
2-amino-8-ethyl-4-methyl-6-(1H-pyrazol-5-yl)-7-pyrido[2,3-d]pyrimidinone | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tak-901 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gdc-0973 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd 1480 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd8330 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 848125 | Homo sapiens (human) | Kd | 0.0080 | 1 | 1 |
ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
fedratinib | Homo sapiens (human) | Kd | 16.2500 | 2 | 2 |
gsk690693 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
14-methyl-20-oxa-5,7,14,26-tetraazatetracyclo(19.3.1.1(2,6).1(8,12))heptacosa-1(25),2(26),3,5,8(27),9,11,16,21,23-decaene | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pf 04217903 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gdc 0941 | Homo sapiens (human) | Kd | 15.5500 | 2 | 2 |
icotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ph 797804 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
kx-01 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
plx 4720 | Homo sapiens (human) | Kd | 6.6000 | 1 | 1 |
mk 5108 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cx 4945 | Homo sapiens (human) | Kd | 0.0140 | 1 | 1 |
cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
arry-614 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tak 593 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
mln 8237 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sgx 523 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bms 754807 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sgi 1776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pci 32765 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
ponatinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
amg 900 | Homo sapiens (human) | Kd | 2.4580 | 1 | 1 |
mk-1775 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
AMG-208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
quizartinib | Homo sapiens (human) | Kd | 20.0000 | 3 | 4 |
tak 733 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk 2206 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
sns 314 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
lucitanib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pf-04691502 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
n-(cyanomethyl)-4-(2-((4-(4-morpholinyl)phenyl)amino)-4-pyrimidinyl)benzamide | Homo sapiens (human) | Kd | 0.9180 | 1 | 1 |
dcc-2036 | Homo sapiens (human) | Kd | 2.1390 | 1 | 1 |
cabozantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
defactinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ly2584702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
incb-018424 | Homo sapiens (human) | Kd | 6.6165 | 2 | 2 |
poziotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
asp3026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
entrectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
pexidartinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
TAK-580 | Homo sapiens (human) | Kd | 0.9420 | 1 | 1 |
gsk 2126458 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
emd1214063 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1838705a | Homo sapiens (human) | Kd | 0.0210 | 1 | 1 |
pf 3758309 | Homo sapiens (human) | Kd | 0.0900 | 1 | 1 |
gdc 0980 | Homo sapiens (human) | Kd | 30.0000 | 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 | 1 |
gsk 1363089 | Homo sapiens (human) | Kd | 15.2750 | 2 | 2 |
arry-334543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
kin-193 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bay 869766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
as 703026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
baricitinib | Homo sapiens (human) | Kd | 0.7780 | 1 | 1 |
dabrafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pki 587 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
n-(3-fluoro-4-((1-methyl-6-(1h-pyrazol-4-yl)-1h-indazol-5 yl)oxy)phenyl)-1-(4-fluorophenyl)-6-methyl-2-oxo-1,2-dihydropyridine-3-carboxamide | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ribociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk-8033 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 793887 | Homo sapiens (human) | Kd | 2.1840 | 1 | 1 |
sb 1518 | Homo sapiens (human) | Kd | 0.1380 | 1 | 1 |
abemaciclib | Homo sapiens (human) | Kd | 0.0070 | 1 | 1 |
mk-8776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 1070916 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
jnj38877605 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dinaciclib | Homo sapiens (human) | Kd | 0.7140 | 1 | 1 |
gilteritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alectinib | Homo sapiens (human) | Kd | 29.8810 | 1 | 1 |
encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms-911543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd8186 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
byl719 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cep-32496 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
rociletinib | Homo sapiens (human) | Kd | 0.6510 | 1 | 1 |
ceritinib | Homo sapiens (human) | Kd | 1.0590 | 1 | 1 |
vx-509 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
volitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
osimertinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
at 9283 | Homo sapiens (human) | Kd | 2.0450 | 1 | 1 |
otssp167 | Homo sapiens (human) | Kd | 0.0110 | 1 | 1 |
chir 258 | Homo sapiens (human) | Kd | 14.5333 | 3 | 3 |
osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
((5z)5-(1,3-benzodioxol-5-yl)methylene-2-phenylamino-3,5-dihydro-4h-imidazol-4-one) | Homo sapiens (human) | Kd | 0.0750 | 1 | 1 |
nintedanib | Homo sapiens (human) | Kd | 15.0044 | 2 | 2 |
2-[(7-methoxy-4-methyl-2-quinazolinyl)amino]-5,6-dimethyl-1H-pyrimidin-4-one | Homo sapiens (human) | EC50 | 20.0000 | 1 | 1 |
bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pp242 | Homo sapiens (human) | Kd | 0.9100 | 1 | 1 |
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
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
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
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
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
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
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
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
Synthesis, biological evaluation and molecular modelling studies of 4-anilinoquinazoline derivatives as protein kinase inhibitors.Bioorganic & medicinal chemistry, , Mar-15, Volume: 22, Issue:6, 2014
Acridone alkaloids from Glycosmis chlorosperma as DYRK1A inhibitors.Journal of natural products, , May-23, Volume: 77, Issue:5, 2014
Recent advances in the development of active hybrid molecules in the treatment of cardiovascular diseases.Bioorganic & medicinal chemistry, , 05-15, Volume: 62, 2022
Discovery of Potent and Selective Inhibitors of Cdc2-Like Kinase 1 (CLK1) as a New Class of Autophagy Inducers.Journal of medicinal chemistry, , 07-27, Volume: 60, Issue:14, 2017
Development of Selective Clk1 and -4 Inhibitors for Cellular Depletion of Cancer-Relevant Proteins.Journal of medicinal chemistry, , 07-13, Volume: 60, Issue:13, 2017
Hydroxybenzothiophene Ketones Are Efficient Pre-mRNA Splicing Modulators Due to Dual Inhibition of Dyrk1A and Clk1/4.ACS medicinal chemistry letters, , Sep-11, Volume: 5, Issue:9, 2014
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
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
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
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
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
Further investigation of Paprotrain: Towards the conception of selective and multi-targeted CNS kinase inhibitors.European journal of medicinal chemistry, , Nov-29, Volume: 124, 2016
Synthesis, biological evaluation and molecular modeling studies of imidazo[1,2-a]pyridines derivatives as protein kinase inhibitors.European journal of medicinal chemistry, , Nov-10, Volume: 123, 2016
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
Synthesis and biological evaluation of N-aryl-7-methoxybenzo[b]furo[3,2-d]pyrimidin-4-amines and their N-arylbenzo[b]thieno[3,2-d]pyrimidin-4-amine analogues as dual inhibitors of CLK1 and DYRK1A kinases.European journal of medicinal chemistry, , Volume: 59, 2013
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
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Novel CLK1 inhibitors based on N-aryloxazol-2-amine skeleton - A possible way to dual VEGFR2 TK/CLK ligands.European journal of medicinal chemistry, , Jan-27, Volume: 126, 2017
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
Novel CLK1 inhibitors based on N-aryloxazol-2-amine skeleton - A possible way to dual VEGFR2 TK/CLK ligands.European journal of medicinal chemistry, , Jan-27, Volume: 126, 2017
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
Identification of genotype-correlated sensitivity to selective kinase inhibitors by using high-throughput tumor cell line profiling.Proceedings of the National Academy of Sciences of the United States of America, , Dec-11, Volume: 104, Issue:50, 2007
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
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
A quantitative analysis of kinase inhibitor selectivity.Nature biotechnology, , Volume: 26, Issue:1, 2008
A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
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
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
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
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
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
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
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
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
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
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
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
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
Exploring the roles of the Cdc2-like kinases in cancers.Bioorganic & medicinal chemistry, , 09-15, Volume: 70, 2022
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
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
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
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
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
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
Enables
This protein enables 7 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 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] |
non-membrane spanning protein tyrosine kinase activity | molecular function | Catalysis of the reaction: ATP + protein L-tyrosine = ADP + protein L-tyrosine phosphate by a non-membrane spanning protein. [EC:2.7.10.2] |
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 tyrosine kinase activity | molecular function | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. [RHEA:10596] |
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 2 target(s):
Target | Category | Definition |
regulation of RNA splicing | biological process | Any process that modulates the frequency, rate or extent of RNA splicing, the process of removing sections of the primary RNA transcript to remove sequences not present in the mature form of the RNA and joining the remaining sections to form the mature form of the RNA. [GOC:jl] |
peptidyl-tyrosine phosphorylation | biological process | The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. [RESID:AA0039] |