Page last updated: 2024-08-07 16:39:28
Tyrosine-protein kinase ABL2
A tyrosine-protein kinase ABL2 that is encoded in the genome of human. [PRO:DNx, UniProtKB:P42684]
Synonyms
EC 2.7.10.2;
Abelson murine leukemia viral oncogene homolog 2;
Abelson tyrosine-protein kinase 2;
Abelson-related gene protein;
Tyrosine-protein kinase ARG
Research
Bioassay Publications (27)
Timeframe | Studies on this Protein(%) | All Drugs % |
pre-1990 | 0 (0.00) | 18.7374 |
1990's | 3 (11.11) | 18.2507 |
2000's | 11 (40.74) | 29.6817 |
2010's | 12 (44.44) | 24.3611 |
2020's | 1 (3.70) | 2.80 |
Compounds (244)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
fasudil | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
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 | 0.0779 | 8 | 8 |
triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
staurosporine | Homo sapiens (human) | Kd | 0.1267 | 3 | 3 |
picropodophyllin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gefitinib | Homo sapiens (human) | Kd | 17.9000 | 3 | 4 |
lestaurtinib | Homo sapiens (human) | Kd | 15.5000 | 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 | 16.6667 | 3 | 3 |
canertinib | Homo sapiens (human) | Kd | 8.2600 | 4 | 4 |
birb 796 | Homo sapiens (human) | Kd | 5.6500 | 2 | 2 |
cyc 202 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 2 | 2 |
enzastaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
erlotinib | Homo sapiens (human) | Kd | 7.6750 | 4 | 4 |
lapatinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
sorafenib | Homo sapiens (human) | Kd | 11.6667 | 5 | 6 |
pd 173955 | Homo sapiens (human) | Kd | 0.0007 | 1 | 1 |
hts 466284 | Homo sapiens (human) | Kd | 1.8700 | 1 | 1 |
s 1033 | Homo sapiens (human) | Kd | 0.1585 | 2 | 2 |
xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms 387032 | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
sf 2370 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tandutinib | Homo sapiens (human) | Kd | 15.0000 | 4 | 4 |
vx-745 | Homo sapiens (human) | Kd | 1.3400 | 3 | 3 |
dasatinib | Homo sapiens (human) | Kd | 0.0014 | 3 | 3 |
ha 1100 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
7-epi-hydroxystaurosporine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
zd 6474 | Homo sapiens (human) | Kd | 7.5670 | 4 | 4 |
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 | 16.6667 | 3 | 3 |
bosutinib | Homo sapiens (human) | Kd | 0.0108 | 2 | 2 |
orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
su 11248 | Homo sapiens (human) | Kd | 6.8400 | 5 | 5 |
palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
jnj-7706621 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
vx680 | Homo sapiens (human) | Kd | 0.0898 | 4 | 4 |
cyc 116 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ekb 569 | Homo sapiens (human) | Kd | 10.1767 | 3 | 3 |
axitinib | Homo sapiens (human) | Kd | 0.5545 | 2 | 2 |
temsirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
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 | 30.0000 | 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 | 15.0000 | 4 | 4 |
px-866 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ripasudil | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
osi 930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ki 20227 | Homo sapiens (human) | Kd | 0.9500 | 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 | 10.0000 | 2 | 2 |
hmn-214 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
tivozanib | Homo sapiens (human) | Kd | 0.3020 | 1 | 1 |
hki 272 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
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 | 10.0000 | 1 | 1 |
cediranib | Homo sapiens (human) | Kd | 15.3650 | 2 | 2 |
masitinib | Homo sapiens (human) | Kd | 0.2320 | 2 | 2 |
ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pazopanib | Homo sapiens (human) | Kd | 12.0000 | 3 | 3 |
azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
su 14813 | Homo sapiens (human) | Kd | 16.6667 | 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 | 14.9240 | 1 | 1 |
saracatinib | Homo sapiens (human) | Kd | 0.0910 | 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 | 20.0000 | 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 | 0.6280 | 1 | 1 |
volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pha 665752 | Homo sapiens (human) | Kd | 6.9000 | 1 | 1 |
azd 7762 | Homo sapiens (human) | Kd | 0.8990 | 1 | 1 |
regorafenib | Homo sapiens (human) | Kd | 30.0000 | 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 | 15.3600 | 2 | 2 |
brivanib | Homo sapiens (human) | Kd | 15.9000 | 2 | 2 |
mp470 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
rgb 286638 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
np 031112 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
at 7519 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bms-690514 | Homo sapiens (human) | Kd | 0.1325 | 2 | 2 |
bi 2536 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
inno-406 | Homo sapiens (human) | Kd | 0.0100 | 1 | 1 |
nvp-ast487 | Homo sapiens (human) | Kd | 0.0034 | 2 | 2 |
kw 2449 | Homo sapiens (human) | Kd | 20.0833 | 2 | 3 |
danusertib | Homo sapiens (human) | Kd | 0.0100 | 1 | 1 |
abt 869 | Homo sapiens (human) | Kd | 16.6667 | 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 | 2 |
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 | 0.4435 | 2 | 2 |
osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
chir-265 | Homo sapiens (human) | Kd | 11.2667 | 3 | 3 |
motesanib | Homo sapiens (human) | Kd | 14.8333 | 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 | 2.6310 | 3 | 3 |
pf-562,271 | Homo sapiens (human) | Kd | 30.0000 | 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 | 1.0340 | 1 | 1 |
dactolisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bgt226 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk 461364 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
azd 1152-hqpa | Homo sapiens (human) | Kd | 20.0000 | 3 | 4 |
nvp-tae684 | Homo sapiens (human) | Kd | 0.3800 | 1 | 1 |
enmd 2076 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
e 7050 | Homo sapiens (human) | Kd | 0.7220 | 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 | 0.4220 | 1 | 1 |
gdc-0973 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
buparlisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
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 | 3.7540 | 1 | 1 |
ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
fedratinib | Homo sapiens (human) | Kd | 15.2850 | 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 |
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 | 20.0000 | 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 | 2.7000 | 1 | 1 |
mk 5108 | Homo sapiens (human) | Kd | 0.0770 | 1 | 1 |
cx 4945 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
arry-614 | Homo sapiens (human) | Kd | 0.3510 | 1 | 1 |
tak 593 | Homo sapiens (human) | Kd | 4.0580 | 1 | 1 |
mln 8237 | Homo sapiens (human) | Kd | 1.0090 | 1 | 1 |
sgx 523 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
bms 754807 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms 777607 | Homo sapiens (human) | Kd | 1.5080 | 1 | 1 |
sgi 1776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pci 32765 | Homo sapiens (human) | Kd | 0.9190 | 1 | 1 |
ponatinib | Homo sapiens (human) | Kd | 0.0200 | 1 | 1 |
amg 900 | Homo sapiens (human) | Kd | 30.0000 | 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 | 16.6667 | 3 | 3 |
at13148 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
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 | 2 |
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 | 30.0000 | 1 | 1 |
dcc-2036 | Homo sapiens (human) | Kd | 0.1350 | 1 | 1 |
cabozantinib | Homo sapiens (human) | Kd | 0.9180 | 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 | 20.0000 | 2 | 2 |
poziotinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
asp3026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
entrectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pexidartinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
TAK-580 | Homo sapiens (human) | Kd | 0.0990 | 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 | 10.0000 | 1 | 1 |
pf 3758309 | Homo sapiens (human) | Kd | 0.9390 | 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 | 0.0405 | 2 | 2 |
arry-334543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
kin-193 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk 2461 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bay 869766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
as 703026 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
baricitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
dabrafenib | Homo sapiens (human) | Kd | 0.3050 | 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 | 30.0000 | 1 | 1 |
sb 1518 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
abemaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
mk-8776 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
afuresertib | 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 | 2 |
dinaciclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gilteritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
alectinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
glpg0634 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
encorafenib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
bms-911543 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
gsk2141795 | 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 | 0.0300 | 1 | 1 |
rociletinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
ceritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
azd1208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
vx-509 | Homo sapiens (human) | Kd | 7.0710 | 1 | 1 |
debio 1347 | 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 | 1.0820 | 1 | 1 |
otssp167 | Homo sapiens (human) | Kd | 0.1870 | 1 | 1 |
chir 258 | Homo sapiens (human) | Kd | 7.0140 | 3 | 3 |
osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
nintedanib | Homo sapiens (human) | Kd | 16.0000 | 2 | 2 |
bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
pp242 | Homo sapiens (human) | Kd | 1.2000 | 1 | 1 |
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Comprehensive analysis of kinase inhibitor selectivity.Nature biotechnology, , Oct-30, Volume: 29, Issue:11, 2011
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A small molecule-kinase interaction map for clinical kinase inhibitors.Nature biotechnology, , Volume: 23, Issue:3, 2005
Identification of orally active, potent, and selective 4-piperazinylquinazolines as antagonists of the platelet-derived growth factor receptor tyrosine kinase family.Journal of medicinal chemistry, , Aug-15, Volume: 45, Issue:17, 2002
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
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
Discovery of a novel class of non-ATP site DFG-out state p38 inhibitors utilizing computationally assisted virtual fragment-based drug design (vFBDD).Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 21, Issue:23, 2011
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
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
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
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
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 Selective and Brain Penetrant p38αMAPK Inhibitor Candidate for Neurologic and Neuropsychiatric Disorders That Attenuates Neuroinflammation and Cognitive Dysfunction.Journal of medicinal chemistry, , 06-13, Volume: 62, Issue:11, 2019
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
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
Global target profile of the kinase inhibitor bosutinib in primary chronic myeloid leukemia cells.Leukemia, , Volume: 23, Issue:3, 2009
Inhibition of Src kinase activity by 7-[(2,4-dichloro-5-methoxyphenyl)amino]-2-heteroaryl-thieno[3,2-b]pyridine-6-carbonitriles.Bioorganic & medicinal chemistry letters, , Nov-01, Volume: 15, Issue:21, 2005
7-Alkoxy-4-phenylamino-3-quinolinecar-bonitriles as dual inhibitors of Src and Abl kinases.Journal of medicinal chemistry, , Mar-25, Volume: 47, Issue:7, 2004
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
Discovery and development of aurora kinase inhibitors as anticancer agents.Journal of medicinal chemistry, , May-14, Volume: 52, Issue:9, 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
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
Design of a Cyclin G Associated Kinase (GAK)/Epidermal Growth Factor Receptor (EGFR) Inhibitor Set to Interrogate the Relationship of EGFR and GAK in Chordoma.Journal of medicinal chemistry, , 05-09, Volume: 62, Issue:9, 2019
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
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
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
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 10 target(s):
Target | Category | Definition |
magnesium ion binding | molecular function | Binding to a magnesium (Mg) ion. [GOC:ai] |
phosphotyrosine residue binding | molecular function | Binding to a phosphorylated tyrosine residue within a protein. [PMID:14636584] |
actin monomer binding | molecular function | Binding to monomeric actin, also known as G-actin. [GOC:ai] |
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 tyrosine kinase activity | molecular function | Catalysis of the reaction: ATP + a protein tyrosine = ADP + protein tyrosine phosphate. [RHEA:10596] |
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] |
manganese ion binding | molecular function | Binding to a manganese ion (Mn). [GOC:ai] |
actin filament binding | molecular function | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. [ISBN:0198506732] |
Located In
This protein is located in 2 target(s):
Target | Category | Definition |
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] |
actin cytoskeleton | cellular component | The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes. [GOC:jl, ISBN:0395825172, ISBN:0815316194] |
Active In
This protein is active in 1 target(s):
Target | Category | Definition |
plasma membrane | cellular component | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. [ISBN:0716731363] |
Involved In
This protein is involved in 16 target(s):
Target | Category | Definition |
cell adhesion | biological process | The attachment of a cell, either to another cell or to an underlying substrate such as the extracellular matrix, via cell adhesion molecules. [GOC:hb, GOC:pf] |
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] |
regulation of autophagy | biological process | Any process that modulates the frequency, rate or extent of autophagy. Autophagy is the process in which cells digest parts of their own cytoplasm. [GOC:dph, GOC:tb] |
positive regulation of neuron projection development | biological process | Any process that increases the rate, frequency or extent of neuron projection development. Neuron projection development is the process whose specific outcome is the progression of a neuron projection over time, from its formation to the mature structure. A neuron projection is any process extending from a neural cell, such as axons or dendrites (collectively called neurites). [GOC:dph, GOC:tb] |
peptidyl-tyrosine phosphorylation | biological process | The phosphorylation of peptidyl-tyrosine to form peptidyl-O4'-phospho-L-tyrosine. [RESID:AA0039] |
regulation of endocytosis | biological process | Any process that modulates the frequency, rate or extent of endocytosis. [GOC:go_curators] |
regulation of cell adhesion | biological process | Any process that modulates the frequency, rate or extent of attachment of a cell to another cell or to the extracellular matrix. [GOC:mah] |
regulation of actin cytoskeleton organization | biological process | Any process that modulates the frequency, rate or extent of the formation, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. [GOC:mah] |
protein modification process | biological process | The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl] |
positive regulation of oxidoreductase activity | biological process | Any process that activates or increases the frequency, rate or extent of oxidoreductase activity, the catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. [GOC:ai] |
cellular response to retinoic acid | 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 a retinoic acid stimulus. [GOC:mah] |
positive regulation of establishment of T cell polarity | biological process | Any process that activates or increases the frequency, rate or extent of establishment of T cell polarity. [GO_REF:0000058, GOC:als, GOC:TermGenie, PMID:23575248] |
regulation of cell motility | biological process | Any process that modulates the frequency, rate or extent of cell motility. [GOC:mah] |
positive regulation of T cell migration | biological process | Any process that activates or increases the frequency, rate or extent of T cell migration. [GOC:mah] |
epidermal growth factor receptor signaling pathway | biological process | The series of molecular signals initiated by binding of a ligand to the tyrosine kinase receptor EGFR (ERBB1) on the surface of a cell. The pathway ends with regulation of a downstream cellular process, e.g. transcription. [GOC:ceb] |
protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |