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TargetRAC-alpha serine/threonine-protein kinase
LigandBDBM50399676
Substrate/Competitorn/a
Meas. Tech.ChEMBL_876557 (CHEMBL2188514)
IC50>10000±n/a nM
Citation Yang, JWang, LJLiu, JJZhong, LZheng, RLXu, YJi, PZhang, CHWang, WJLin, XDLi, LLWei, YQYang, SY Structural optimization and structure-activity relationships of N2-(4-(4-Methylpiperazin-1-yl)phenyl)-N8-phenyl-9H-purine-2,8-diamine derivatives, a new class of reversible kinase inhibitors targeting both EGFR-activating and resistance mutations. J Med Chem55:10685-99 (2012) [PubMed]  Article
More Info.:Get all data from this article,  Assay Method
 
RAC-alpha serine/threonine-protein kinase
Name:RAC-alpha serine/threonine-protein kinase
Synonyms:AKT phosphorylation (p-AKT) | AKT1 | AKT1/PPP1CA | AKT1_HUMAN | C-AKT | PKB | PKB alpha | Protein kinase Akt-1 | Protein kinase B | Protein kinase B (AKT1) | Protein kinase B (Akt 1) | Protein kinase B (Akt) | Protein kinase B alpha | Protein kinase B alpha (AKT1) | Proto-oncogene Akt (Akt1) | Proto-oncogene c-Akt (AKT) | Proto-oncogene c-Akt (AKT1) | RAC | RAC-PK-alpha | RAC-alpha serine/threonine-protein kinase (AKT) | RAC-alpha serine/threonine-protein kinase (AKT1) | RAC-alpha serine/threonine-protein kinase (pAKT)
Type:Enzyme
Mol. Mass.:55681.25
Organism:Homo sapiens (Human)
Description:P31749
Residue:480
Sequence:
MSDVAIVKEGWLHKRGEYIKTWRPRYFLLKNDGTFIGYKERPQDVDQREAPLNNFSVAQC
QLMKTERPRPNTFIIRCLQWTTVIERTFHVETPEEREEWTTAIQTVADGLKKQEEEEMDF
RSGSPSDNSGAEEMEVSLAKPKHRVTMNEFEYLKLLGKGTFGKVILVKEKATGRYYAMKI
LKKEVIVAKDEVAHTLTENRVLQNSRHPFLTALKYSFQTHDRLCFVMEYANGGELFFHLS
RERVFSEDRARFYGAEIVSALDYLHSEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGI
KDGATMKTFCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFEL
ILMEEIRFPRTLGPEAKSLLSGLLKKDPKQRLGGGSEDAKEIMQHRFFAGIVWQHVYEKK
LSPPFKPQVTSETDTRYFDEEFTAQMITITPPDQDDSMECVDSERRPHFPQFSYSASGTA
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  Blast E-value cutoff:
BDBM50399676
n/a
NameBDBM50399676
Synonyms:CHEMBL2178352 | US9096601, 8-26
TypeSmall organic molecule
Emp. Form.C27H32N8
Mol. Mass.468.5966
SMILESCN1CCN(CC1)c1ccc(Nc2ncc3nc(Nc4ccccc4)n(C4CCCC4)c3n2)cc1
Structure
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