Proteins > Rho-associated protein kinase 2
Page last updated: 2024-08-07 15:27:23
Rho-associated protein kinase 2
A Rho-associated protein kinase 2 that is encoded in the genome of human. [PRO:CNA, UniProtKB:O75116]
Synonyms
EC 2.7.11.1;
Rho kinase 2;
Rho-associated, coiled-coil-containing protein kinase 2;
Rho-associated, coiled-coil-containing protein kinase II;
ROCK-II;
p164 ROCK-2
Research
Bioassay Publications (47)
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 10 (21.28) | 29.6817 |
| 2010's | 26 (55.32) | 24.3611 |
| 2020's | 11 (23.40) | 2.80 |
Compounds (247)
Drugs with Inhibition Measurements
Drugs with Activation Measurements
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|
| fasudil | Homo sapiens (human) | Kd | 0.5105 | 2 | 2 |
| 4-(4'-hydroxyphenyl)-amino-6,7-dimethoxyquinazoline | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| imatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| triciribine phosphate | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| staurosporine | Homo sapiens (human) | Kd | 0.0002 | 1 | 1 |
| picropodophyllin | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gefitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| lestaurtinib | Homo sapiens (human) | Kd | 10.0473 | 3 | 3 |
| perifosine | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vatalanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ruboxistaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| canertinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| birb 796 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| cyc 202 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sb 203580 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| enzastaurin | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| erlotinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| lapatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| sorafenib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| pd 173955 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| h 89 | Homo sapiens (human) | Kd | 0.0260 | 2 | 3 |
| s 1033 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| xl147 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 387032 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| sf 2370 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tandutinib | Homo sapiens (human) | Kd | 16.6667 | 3 | 3 |
| vx-745 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| dasatinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ha 1100 | Homo sapiens (human) | Kd | 1.3490 | 1 | 1 |
| 7-epi-hydroxystaurosporine | Homo sapiens (human) | Kd | 1.0960 | 1 | 1 |
| zd 6474 | Homo sapiens (human) | Kd | 16.8000 | 2 | 2 |
| imd 0354 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sirolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| alvocidib | Homo sapiens (human) | Kd | 15.7500 | 2 | 2 |
| bosutinib | Homo sapiens (human) | Kd | 15.1800 | 2 | 2 |
| orantinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| su 11248 | Homo sapiens (human) | Kd | 10.0933 | 3 | 3 |
| palbociclib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| vx680 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| cyc 116 | Homo sapiens (human) | Kd | 8.8850 | 1 | 1 |
| everolimus | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ekb 569 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| axitinib | Homo sapiens (human) | Kd | 20.0000 | 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) | EC50 | 0.1500 | 1 | 1 |
| y-39983 | Homo sapiens (human) | Kd | 0.0090 | 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 | 11.5333 | 3 | 3 |
| px-866 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| ripasudil | Homo sapiens (human) | Kd | 0.0830 | 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 | 30.0000 | 1 | 1 |
| pi103 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| 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 | 20.0000 | 2 | 2 |
| tofacitinib | Homo sapiens (human) | Kd | 1.6985 | 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 | 23.3333 | 2 | 3 |
| masitinib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| ly-2157299 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pazopanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| azd 6244 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| su 14813 | Homo sapiens (human) | Kd | 20.2200 | 2 | 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 | 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 | 30.0000 | 1 | 1 |
| volasertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pha 665752 | Homo sapiens (human) | Kd | 8.7000 | 1 | 1 |
| azd 7762 | Homo sapiens (human) | Kd | 30.0000 | 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 | 15.2800 | 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 | 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 | 30.0000 | 1 | 1 |
| bi 2536 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| inno-406 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| nvp-ast487 | Homo sapiens (human) | Kd | 0.3900 | 1 | 1 |
| kw 2449 | Homo sapiens (human) | Kd | 15.1250 | 2 | 2 |
| danusertib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| abt 869 | Homo sapiens (human) | Kd | 15.3150 | 2 | 2 |
| 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 |
| cortistatin a | Homo sapiens (human) | Kd | 0.2200 | 1 | 1 |
| cc-930 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| gw 2580 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
| tak 285 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| idelalisib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| crizotinib | Homo sapiens (human) | Kd | 16.6500 | 2 | 2 |
| osi 906 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir-265 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| motesanib | Homo sapiens (human) | Kd | 20.0000 | 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 | 20.0000 | 2 | 2 |
| 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 | 30.0000 | 1 | 2 |
| 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 | 2 | 2 |
| nvp-tae684 | Homo sapiens (human) | Kd | 0.1300 | 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 | 2 |
| tak-901 | Homo sapiens (human) | Kd | 30.0000 | 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 | 30.0000 | 1 | 1 |
| ro5126766 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| fedratinib | Homo sapiens (human) | Kd | 16.1000 | 2 | 2 |
| gsk690693 | Homo sapiens (human) | Kd | 0.5780 | 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 | 58.9770 | 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 | 10.0000 | 1 | 1 |
| mk 5108 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| cx 4945 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| cudc 101 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| arry-614 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| tak 593 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mln 8237 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| sgx 523 | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bms 754807 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| bms 777607 | 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 | 1 |
| ponatinib | Homo sapiens (human) | Kd | 30.0000 | 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 | 0.0260 | 1 | 1 |
| tak 733 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| mk 2206 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| 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 | 0.2190 | 1 | 1 |
| dcc-2036 | 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 |
| ly2584702 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| incb-018424 | Homo sapiens (human) | Kd | 2.9995 | 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 | 1 |
| pexidartinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| TAK-580 | Homo sapiens (human) | Kd | 30.0000 | 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 | 30.0000 | 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 | 15.9000 | 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 | 0.7560 | 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 | 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 | 1 |
| afuresertib | Homo sapiens (human) | Kd | 4.7330 | 1 | 1 |
| gsk 1070916 | Homo sapiens (human) | Kd | 2.4020 | 1 | 1 |
| jnj38877605 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| 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 | 2.2770 | 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 | 30.0000 | 1 | 1 |
| ceritinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| azd1208 | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| vx-509 | Homo sapiens (human) | Kd | 56.0660 | 1 | 1 |
| debio 1347 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| volitinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 2 |
| osimertinib | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| at 9283 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| otssp167 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| chir 258 | Homo sapiens (human) | Kd | 16.5500 | 2 | 2 |
| osi 027 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| nintedanib | Homo sapiens (human) | Kd | 20.0000 | 2 | 2 |
| bay 80-6946 | Homo sapiens (human) | Kd | 30.0000 | 1 | 1 |
| pp242 | Homo sapiens (human) | Kd | 10.0000 | 1 | 1 |
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Cyclizidine-Type Alkaloids from Streptomyces sp. HNA39.Journal of natural products, , 02-23, Volume: 81, Issue:2, 2018
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
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
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
Identification of a Potent, Selective, and Brain-Penetrant Rho Kinase Inhibitor and its Activity in a Mouse Model of Huntington's Disease.Journal of medicinal chemistry, , 07-28, Volume: 65, Issue:14, 2022
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Identification of Novel Rho-Kinase-II Inhibitors with Vasodilatory Activity.ACS medicinal chemistry letters, , Sep-10, Volume: 11, Issue:9, 2020
Design, synthesis, and biological evaluation of novel, highly active soft ROCK inhibitors.Journal of medicinal chemistry, , May-28, Volume: 58, Issue:10, 2015
Novel ROCK inhibitors for the treatment of pulmonary arterial hypertension.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 24, Issue:20, 2014
3-[2-(Aminomethyl)-5-[(pyridin-4-yl)carbamoyl]phenyl] benzoates as soft ROCK inhibitors.Bioorganic & medicinal chemistry letters, , Dec-01, Volume: 23, Issue:23, 2013
Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2).MedChemComm, , Jun-01, Volume: 3, Issue:6, 2012
Fragment-based discovery of 6-substituted isoquinolin-1-amine based ROCK-I inhibitors.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 21, Issue:1, 2011
Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
Kinase inhibitors: not just for kinases anymore.Journal of medicinal chemistry, , Apr-10, Volume: 46, Issue:8, 2003
A review on ROCK-II inhibitors: From molecular modelling to synthesis.Bioorganic & medicinal chemistry letters, , 05-15, Volume: 26, Issue:10, 2016
Novel ROCK inhibitors for the treatment of pulmonary arterial hypertension.Bioorganic & medicinal chemistry letters, , Oct-15, Volume: 24, Issue:20, 2014
Hit to lead account of the discovery of bisbenzamide and related ureidobenzamide inhibitors of Rho kinase.Journal of medicinal chemistry, , Jan-28, Volume: 53, Issue:2, 2010
Conjugates of 5-isoquinolinesulfonylamides and oligo-D-arginine possess high affinity and selectivity towards Rho kinase (ROCK).Bioorganic & medicinal chemistry letters, , May-15, Volume: 22, Issue:10, 2012
Structural analysis of ARC-type inhibitor (ARC-1034) binding to protein kinase A catalytic subunit and rational design of bisubstrate analogue inhibitors of basophilic protein kinases.Journal of medicinal chemistry, , Jan-22, Volume: 52, Issue:2, 2009
A systematic interaction map of validated kinase inhibitors with Ser/Thr kinases.Proceedings of the National Academy of Sciences of the United States of America, , Dec-18, Volume: 104, Issue:51, 2007
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
Identification of a Potent, Selective, and Brain-Penetrant Rho Kinase Inhibitor and its Activity in a Mouse Model of Huntington's Disease.Journal of medicinal chemistry, , 07-28, Volume: 65, Issue:14, 2022
Dual-target inhibitors of poly (ADP-ribose) polymerase-1 for cancer therapy: Advances, challenges, and opportunities.European journal of medicinal chemistry, , Feb-15, Volume: 230, 2022
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Fragment-based discovery of 6-substituted isoquinolin-1-amine based ROCK-I inhibitors.Bioorganic & medicinal chemistry letters, , Jan-01, Volume: 21, Issue:1, 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
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
In vivo optimization of 2,3-diaminopyrazine Rho Kinase inhibitors for the treatment of glaucoma.Bioorganic & medicinal chemistry letters, , Apr-15, Volume: 24, Issue:8, 2014
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
Small-Molecule Kinase Inhibitors for the Treatment of Nononcologic Diseases.Journal of medicinal chemistry, , 02-11, Volume: 64, Issue:3, 2021
Identification of 5H-chromeno[3,4-c]pyridine and 6H-isochromeno[3,4-c]pyridine derivatives as potent and selective dual ROCK inhibitors.Bioorganic & medicinal chemistry letters, , 11-01, Volume: 30, Issue:21, 2020
p62/SQSTM1, a Central but Unexploited Target: Advances in Its Physiological/Pathogenic Functions and Small Molecular Modulators.Journal of medicinal chemistry, , 09-24, Volume: 63, Issue:18, 2020
Ocular Disease Therapeutics: Design and Delivery of Drugs for Diseases of the Eye.Journal of medicinal chemistry, , 10-08, Volume: 63, Issue:19, 2020
The target landscape of clinical kinase drugs.Science (New York, N.Y.), , 12-01, Volume: 358, Issue:6367, 2017
Discovery of Molecular Therapeutics for Glaucoma: Challenges, Successes, and Promising Directions.Journal of medicinal chemistry, , Feb-11, Volume: 59, Issue:3, 2016
Design, synthesis, and biological evaluation of novel, highly active soft ROCK inhibitors.Journal of medicinal chemistry, , May-28, Volume: 58, Issue:10, 2015
Identification of 5H-chromeno[3,4-c]pyridine and 6H-isochromeno[3,4-c]pyridine derivatives as potent and selective dual ROCK inhibitors.Bioorganic & medicinal chemistry letters, , 11-01, Volume: 30, Issue:21, 2020
Substituted 2H-isoquinolin-1-one as potent Rho-Kinase inhibitors. Part 1: Hit-to-lead account.Bioorganic & medicinal chemistry letters, , Jun-01, Volume: 20, Issue:11, 2010
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
Examining the chirality, conformation and selective kinase inhibition of 3-((3R,4R)-4-methyl-3-(methyl(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino)piperidin-1-yl)-3-oxopropanenitrile (CP-690,550).Journal of medicinal chemistry, , Dec-25, Volume: 51, Issue:24, 2008
Prevention of organ allograft rejection by a specific Janus kinase 3 inhibitor.Science (New York, N.Y.), , Oct-31, Volume: 302, Issue:5646, 2003
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
Discovery of 3-(1H-indol-3-yl)-4-[2-(4-methylpiperazin-1-yl)quinazolin-4-yl]pyrrole-2,5-dione (AEB071), a potent and selective inhibitor of protein kinase C isotypes.Journal of medicinal chemistry, , Oct-22, Volume: 52, Issue:20, 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
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
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
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
Synthesis, structure-activity relationships, and in vivo efficacy of the novel potent and selective anaplastic lymphoma kinase (ALK) inhibitor 5-chloro-N2-(2-isopropoxy-5-methyl-4-(piperidin-4-yl)phenyl)-N4-(2-(isopropylsulfonyl)phenyl)pyrimidine-2,4-diamJournal of medicinal chemistry, , Jul-25, Volume: 56, Issue:14, 2013
Medulloblastoma drugs in development: Current leads, trials and drawbacks.European journal of medicinal chemistry, , Apr-05, Volume: 215, 2021
Pyridylthiazole-based ureas as inhibitors of Rho associated protein kinases (ROCK1 and 2).MedChemComm, , Jun-01, Volume: 3, Issue:6, 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
Enables
This protein enables 13 target(s):
| Target | Category | Definition |
|---|
| protease binding | molecular function | Binding to a protease or a peptidase. [GOC:hjd] |
| RNA binding | molecular function | Binding to an RNA molecule or a portion thereof. [GOC:jl, GOC:mah] |
| 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] |
| structural molecule activity | molecular function | The action of a molecule that contributes to the structural integrity of a complex. [GOC:mah, GOC:vw] |
| 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] |
| small GTPase binding | molecular function | Binding to a small monomeric GTPase. [GOC:mah, PMID:27218782] |
| metal ion binding | molecular function | Binding to a metal ion. [GOC:ai] |
| tau protein binding | molecular function | Binding to tau protein. tau is a microtubule-associated protein, implicated in Alzheimer's disease, Down Syndrome and ALS. [GOC:jid] |
| tau-protein kinase activity | molecular function | Catalysis of the reaction: ATP + tau-protein = ADP + O-phospho-tau-protein. [EC:2.7.11.26, MetaCyc:TAU-PROTEIN-KINASE-RXN] |
| endopeptidase activator activity | molecular function | Binds to and increases the activity of an endopeptidase. [GOC:dph, GOC:tb] |
| Rho-dependent protein serine/threonine kinase activity | molecular function | Rho GTPase-dependent catalysis of the reaction: ATP + a protein = ADP + a phosphoprotein. [GOC:ecd, PMID:12778124, PMID:20230755] |
| protein serine kinase activity | molecular function | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. [RHEA:17989] |
Located In
This protein is located in 5 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] |
| centrosome | cellular component | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. [GOC:mah, ISBN:0198547684] |
| 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] |
| 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] |
| cytoplasmic ribonucleoprotein granule | cellular component | A ribonucleoprotein granule located in the cytoplasm. [GOC:bf, GOC:PARL, PMID:15121898] |
Active In
This protein is active in 3 target(s):
| Target | Category | Definition |
|---|
| centrosome | cellular component | A structure comprised of a core structure (in most organisms, a pair of centrioles) and peripheral material from which a microtubule-based structure, such as a spindle apparatus, is organized. Centrosomes occur close to the nucleus during interphase in many eukaryotic cells, though in animal cells it changes continually during the cell-division cycle. [GOC:mah, ISBN:0198547684] |
| cytoskeleton | cellular component | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. [GOC:mah, PMID:16959967, PMID:27419875] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
Involved In
This protein is involved in 57 target(s):
| Target | Category | Definition |
|---|
| epithelial to mesenchymal transition | biological process | A transition where an epithelial cell loses apical/basolateral polarity, severs intercellular adhesive junctions, degrades basement membrane components and becomes a migratory mesenchymal cell. [GOC:dph, PMID:14701881] |
| positive regulation of protein phosphorylation | biological process | Any process that activates or increases the frequency, rate or extent of addition of phosphate groups to amino acids within a protein. [GOC:hjd] |
| response to ischemia | biological process | Any process that results in a change in state or activity of an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a inadequate blood supply. [GOC:hjd] |
| aortic valve morphogenesis | biological process | The process in which the structure of the aortic valve is generated and organized. [GOC:mtg_heart] |
| protein phosphorylation | biological process | The process of introducing a phosphate group on to a protein. [GOC:hb] |
| smooth muscle contraction | biological process | A process in which force is generated within smooth muscle tissue, resulting in a change in muscle geometry. Force generation involves a chemo-mechanical energy conversion step that is carried out by the actin/myosin complex activity, which generates force through ATP hydrolysis. Smooth muscle differs from striated muscle in the much higher actin/myosin ratio, the absence of conspicuous sarcomeres and the ability to contract to a much smaller fraction of its resting length. [GOC:ef, GOC:jl, GOC:mtg_muscle, ISBN:0198506732] |
| canonical NF-kappaB signal transduction | biological process | An intracellular signaling cassette characterized by the I-kappaB-kinase (IKK)-dependent activation of NF-kappaB, also known as the canonical NF-kappaB signaling cascade. The cascade begins with activation of a trimeric IKK complex (consisting of catalytic kinase subunits IKKalpha and/or IKKbeta, and the regulatory scaffold protein NEMO) and ends with the regulation of transcription of target genes by NF-kappaB. In a resting state, NF-kappaB dimers are bound to I-kappaB proteins, sequestering NF-kappaB in the cytoplasm. Phosphorylation of I-kappaB targets I-kappaB for ubiquitination and proteasomal degradation, thus releasing the NF-kappaB dimers, which can translocate to the nucleus to bind DNA and regulate transcription. The canonical NF-kappaB pathway is mainly stimulated by proinflammatory cytokines such as IL-1beta, tumor necrosis factor (TNF)-alpha, antigen ligands, and toll-like receptors (TLRs). [GOC:bf, PMID:12773372, PMID:34659217] |
| positive regulation of endothelial cell migration | biological process | Any process that increases the rate, frequency, or extent of the orderly movement of an endothelial cell into the extracellular matrix to form an endothelium. [GOC:BHF, GOC:dph, GOC:tb] |
| positive regulation of cardiac muscle hypertrophy | biological process | Any process that increases the rate, frequency or extent of the enlargement or overgrowth of all or part of the heart due to an increase in size (not length) of individual cardiac muscle fibers, without cell division. [GOC:BHF, GOC:dph, GOC:tb] |
| positive regulation of gene expression | biological process | Any process that increases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). [GOC:txnOH-2018] |
| negative regulation of gene expression | biological process | Any process that decreases the frequency, rate or extent of gene expression. Gene expression is the process in which a gene's coding sequence is converted into a mature gene product (protein or RNA). [GOC:txnOH-2018] |
| positive regulation of centrosome duplication | biological process | Any process that increases the frequency, rate or extent of centrosome duplication. Centrosome duplication is the replication of a centrosome, a structure comprised of a pair of centrioles and peri-centriolar material from which a microtubule spindle apparatus is organized. [GOC:dph, GOC:tb] |
| negative regulation of angiogenesis | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of angiogenesis. [GOC:go_curators] |
| actin cytoskeleton organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins. [GOC:dph, GOC:jl, GOC:mah] |
| 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] |
| positive regulation of cell migration | biological process | Any process that activates or increases the frequency, rate or extent of cell migration. [GOC:go_curators] |
| cortical actin cytoskeleton organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of actin-based cytoskeletal structures in the cell cortex, i.e. just beneath the plasma membrane. [GOC:dph, GOC:jl, GOC:mah, GOC:pf] |
| regulation of nervous system process | biological process | Any process that modulates the frequency, rate or extent of a neurophysiological process, an organ system process carried out by any of the organs or tissues of the nervous system. [GOC:dph, GOC:mah, GOC:tb] |
| positive regulation of connective tissue growth factor production | biological process | Any process that activates or increases the frequency, rate, or extent of connective tissue growth factor production. [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] |
| negative regulation of myosin-light-chain-phosphatase activity | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of myosin-light-chain-phosphatase activity. [GOC:bf, GOC:go_curators] |
| regulation of circadian rhythm | biological process | Any process that modulates the frequency, rate or extent of a circadian rhythm. A circadian rhythm is a biological process in an organism that recurs with a regularity of approximately 24 hours. [GOC:dph, GOC:jl, GOC:tb] |
| positive regulation of MAPK cascade | biological process | Any process that activates or increases the frequency, rate or extent of signal transduction mediated by the MAPK cascade. [GOC:go_curators] |
| modulation by host of viral process | biological process | A process in which a host organism modulates the frequency, rate or extent of any of a process being mediated by a virus with which it is infected. [GOC:jl] |
| negative regulation of nitric oxide biosynthetic process | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of the chemical reactions and pathways resulting in the formation of nitric oxide. [GOC:go_curators] |
| regulation of keratinocyte differentiation | biological process | Any process that modulates the frequency, rate or extent of keratinocyte differentiation. [GOC:go_curators] |
| rhythmic process | biological process | Any process pertinent to the generation and maintenance of rhythms in the physiology of an organism. [GOC:jid] |
| centrosome duplication | biological process | The replication of a centrosome, a structure comprised of a pair of centrioles and peri-centriolar material from which a microtubule spindle apparatus is organized. [GOC:ai] |
| regulation of stress fiber assembly | biological process | Any process that modulates the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts. [GOC:ai] |
| positive regulation of stress fiber assembly | biological process | Any process that activates or increases the frequency, rate or extent of the assembly of a stress fiber, a bundle of microfilaments and other proteins found in fibroblasts. [GOC:ai] |
| regulation of focal adhesion assembly | biological process | Any process that modulates the frequency, rate or extent of focal adhesion formation, the establishment and maturation of focal adhesions. [GOC:ai] |
| mRNA destabilization | biological process | Any process that decreases the stability of an mRNA molecule, making it more vulnerable to degradative processes. Messenger RNA is the intermediate molecule between DNA and protein. It includes UTR and coding sequences. It does not contain introns. [GOC:dph, GOC:jh] |
| negative regulation of biomineral tissue development | biological process | Any process that stops, prevents, or reduces the frequency, rate or extent of biomineral tissue development, the formation of hard tissues that consist mainly of inorganic compounds. [GOC:mah] |
| cellular response to testosterone stimulus | 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 testosterone stimulus. [GOC:mah] |
| response to transforming growth factor beta | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a transforming growth factor beta stimulus. [GOC:mah] |
| protein localization to plasma membrane | biological process | A process in which a protein is transported to, or maintained in, a specific location in the plasma membrane. [GOC:mah] |
| positive regulation of fibroblast growth factor production | biological process | Any process that increases the rate, frequency or extent of the appearance of a fibroblast growth factor due to biosynthesis or secretion following a cellular stimulus, resulting in an increase in its intracellular or extracellular levels. [GOC:BHF] |
| blood vessel diameter maintenance | biological process | Any process that modulates the diameter of blood vessels. [GOC:pr] |
| regulation of angiotensin-activated signaling pathway | biological process | Any process that modulates the frequency, rate or extent of the angiotensin-activated signaling pathway. [GOC:lf, PMID:28784619] |
| negative regulation of protein localization to lysosome | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of protein localization to lysosome. [GOC:aruk, GOC:bc, PMID:24305806] |
| regulation of cellular response to hypoxia | biological process | Any process that modulates the frequency, rate or extent of cellular response to hypoxia. [GOC:TermGenie, GOC:yaf] |
| positive regulation of amyloid-beta formation | biological process | Any process that activates or increases the frequency, rate or extent of amyloid-beta formation. [GOC:dph, GOC:TermGenie, PMID:17098871] |
| positive regulation of protein localization to early endosome | biological process | Any process that activates or increases the frequency, rate or extent of protein localization to early endosome. [GO_REF:0000058, GOC:sjp, GOC:TermGenie, PMID:22621900] |
| positive regulation of amyloid precursor protein catabolic process | biological process | Any process that activates or increases the frequency, rate or extent of amyloid precursor protein catabolic process. [GO_REF:0000058, GOC:PARL, GOC:rl, GOC:TermGenie, PMID:24499793] |
| regulation of establishment of endothelial barrier | biological process | Any process that modulates the frequency, rate or extent of establishment of endothelial barrier. [GO_REF:0000058, GOC:als, GOC:TermGenie, PMID:24851274] |
| negative regulation of bicellular tight junction assembly | biological process | Any process that stops, prevents or reduces the frequency, rate or extent of tight junction assembly. [GO_REF:0000058, GOC:jz, GOC:TermGenie, PMID:25050009] |
| cellular response to acetylcholine | 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 an acetylcholine stimulus. [GO_REF:0000071, GOC:TermGenie, PMID:21238497] |
| positive regulation of connective tissue replacement | biological process | Any process that activates or increases the frequency, rate or extent of connective tissue replacement. [GO_REF:0000058, GOC:bc, GOC:BHF, GOC:BHF_miRNA, GOC:TermGenie, PMID:25590961] |
| response to angiotensin | biological process | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an angiotensin stimulus. Angiotensin is any of three physiologically active peptides (angiotensin II, III, or IV) processed from angiotensinogen. [PMID:22982863] |
| regulation of establishment of cell polarity | biological process | Any process that modulates the frequency, rate or extent of establishment of cell polarity. [GOC:dph] |
| regulation of cell motility | biological process | Any process that modulates the frequency, rate or extent of cell motility. [GOC:mah] |
| actomyosin structure organization | biological process | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures containing both actin and myosin or paramyosin. The myosin may be organized into filaments. [GOC:dph, GOC:jl, GOC:mah] |
| peptidyl-threonine phosphorylation | biological process | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. [RESID:AA0038] |
| mitotic cytokinesis | biological process | A cell cycle process that results in the division of the cytoplasm of a cell after mitosis, resulting in the separation of the original cell into two daughter cells. [GOC:mtg_cell_cycle] |
| embryonic morphogenesis | biological process | The process in which anatomical structures are generated and organized during the embryonic phase. The embryonic phase begins with zygote formation. The end of the embryonic phase is organism-specific. For example, it would be at birth for mammals, larval hatching for insects and seed dormancy in plants. [GOC:jid, GOC:mtg_sensu] |
| regulation of cell junction assembly | biological process | Any process that modulates the frequency, rate or extent of cell junction assembly. [GOC:TermGenie] |
| Rho protein signal transduction | biological process | An intracellular signaling cassette in which a small monomeric GTPase of the Rho subfamily relays a signal. [GOC:bf] |