Molecular cloning and identification of a serine/threonine protein kinase of the second-messenger subfamily.Jones P.F., Jakubowicz T., Pitossi F.J., Maurer F., Hemmings B.A.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CATALYTIC ACTIVITYCategoriesFunction, SequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 88:4171-4175 (1991)Cited in1
Isolation and characterization of the human AKT1 gene, identification of 13 single nucleotide polymorphisms (SNPs), and their lack of association with Type II diabetes.Matsubara A., Wasson J.C., Donelan S.S., Welling C.M., Glaser B., Permutt M.A.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCDiabetologia 44:910-913 (2001)Cited in1Mapped to7
Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families.Coffer P.J., Woodgett J.R.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA] OF 63-480 (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITYTissueForeskinCategoriesFunction, Sequences, ExpressionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 201:475-481 (1991)Cited in2
No title available.Coffer P.J., Woodgett J.R.Cited forERRATUM OF PUBMED:1718748, SEQUENCE REVISIONCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEur. J. Biochem. 205:1217-1218 (1992)Cited in2
CREB is a regulatory target for the protein kinase Akt/PKB.Du K., Montminy M.View abstractCited forFUNCTION IN PHOSPHORYLATION OF CREB1CategoriesFunction, PTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 273:32377-32379 (1998)Cited in2Mapped to2
Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase.Delcommenne M., Tan C., Gray V., Rue L., Woodgett J.R., Dedhar S.View abstractCited forACTIVITY REGULATION, PHOSPHORYLATION AT SER-473CategoriesFunction, PTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 95:11211-11216 (1998)Cited in3Mapped to3
Mechanism of activation of protein kinase B by insulin and IGF-1.Alessi D.R., Andjelkovic M., Caudwell F.B., Cron P., Morrice N., Cohen P., Hemmings B.A.View abstractCited forMUTAGENESIS OF THR-308 AND SER-473, PHOSPHORYLATION AT THR-308 AND SER-473CategoriesPTM / Processing, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCEMBO J. 15:6541-6551 (1996)Cited in1
Activation of protein kinase B beta and gamma isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B alpha.Walker K.S., Deak M., Paterson A., Hudson K., Cohen P., Alessi D.R.View abstractCited forFUNCTION, ACTIVITY REGULATION, PHOSPHORYLATION AT THR-308 BY PDPK1CategoriesFunction, PTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. J. 331:299-308 (1998)Cited in4Mapped to1
Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B.Rena G., Guo S., Cichy S.C., Unterman T.G., Cohen P.View abstractCited forFUNCTION IN PHOSPHORYLATION OF FOXO1CategoriesFunction, PTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 274:17179-17183 (1999)Cited in2Mapped to5
Phosphorylation and regulation of Raf by Akt (protein kinase B).Zimmermann S., Moelling K.View abstractCited forFUNCTION IN PHOSPHORYLATION OF RAF1, INTERACTION WITH RAF1CategoriesFunction, PTM / Processing, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCScience 286:1741-1744 (1999)Cited in2
Inhibition of Akt and its anti-apoptotic activities by tumor necrosis factor-induced protein kinase C-related kinase 2 (PRK2) cleavage.Koh H., Lee K.H., Kim D., Kim S., Kim J.W., Chung J.View abstractCited forFUNCTION IN PHOSPHORYLATION OF BAD, INTERACTION WITH BAD AND PKN2CategoriesFunction, PTM / Processing, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 275:34451-34458 (2000)Cited in3
The protooncogene TCL1 is an Akt kinase coactivator.Laine J., Kuenstle G., Obata T., Sha M., Noguchi M.View abstractCited forINTERACTION WITH MTCP1; TCL1A AND TCL1BCategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 6:395-407 (2000)Cited in5Mapped to8
Tcl1 enhances Akt kinase activity and mediates its nuclear translocation.Pekarsky Y., Koval A., Hallas C., Bichi R., Tresini M., Malstrom S., Russo G., Tsichlis P., Croce C.M.View abstractCited forINTERACTION WITH TCL1ACategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCProc. Natl. Acad. Sci. U.S.A. 97:3028-3033 (2000)Cited in4
Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1.Kim A.H., Khursigara G., Sun X., Franke T.F., Chao M.V.View abstractCited forFUNCTION IN PHOSPHORYLATION OF MAP3K5, INTERACTION WITH MAP3K5CategoriesFunction, PTM / Processing, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 21:893-901 (2001)Cited in2Mapped to15
Carboxyl-terminal modulator protein (CTMP), a negative regulator of PKB/Akt and v-Akt at the plasma membrane.Maira S.-M., Galetic I., Brazil D.P., Kaech S., Ingley E., Thelen M., Hemmings B.A.View abstractCited forINTERACTION WITH THEM4, SUBCELLULAR LOCATIONCategoriesInteraction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCScience 294:374-380 (2001)Cited in5Mapped to10
A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain.Kane S., Sano H., Liu S.C.H., Asara J.M., Lane W.S., Garner C.C., Lienhard G.E.View abstractCited forFUNCTION IN PHOSPHORYLATION OF TBC1D4CategoriesFunction, PTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 277:22115-22118 (2002)Cited in4Mapped to5
Akt-dependent phosphorylation of p27Kip1 promotes binding to 14-3-3 and cytoplasmic localization.Fujita N., Sato S., Katayama K., Tsuruo T.View abstractCited forINTERACTION WITH CDKN1B, FUNCTIONCategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 277:28706-28713 (2002)Cited in4Mapped to25
Direct identification of tyrosine 474 as a regulatory phosphorylation site for the Akt protein kinase.Conus N.M., Hannan K.M., Cristiano B.E., Hemmings B.A., Pearson R.B.View abstractCited forPHOSPHORYLATION AT TYR-474, MUTAGENESIS OF TYR-474CategoriesPTM / Processing, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 277:38021-38028 (2002)Cited in1Mapped to7
Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway.Manning B.D., Tee A.R., Logsdon M.N., Blenis J., Cantley L.C.View abstractCited forFUNCTION IN PHOSPHORYLATION OF TSC2CategoriesFunction, PTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell 10:151-162 (2002)Cited in2Mapped to21
Identification of Akt association and oligomerization domains of the Akt kinase coactivator TCL1.Kuenstle G., Laine J., Pierron G., Kagami S., Nakajima H., Hoh F., Roumestand C., Stern M.H., Noguchi M.View abstractCited forINTERACTION WITH TCL1ACategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 22:1513-1525 (2002)Cited in3
TSC2 is phosphorylated and inhibited by Akt and suppresses mTOR signalling.Inoki K., Li Y., Zhu T., Wu J., Guan K.L.View abstractCited forFUNCTION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-179CategoriesFunction, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Cell Biol. 4:648-657 (2002)Cited in5Mapped to8
PKB/Akt mediates cell-cycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization.Shin I., Yakes F.M., Rojo F., Shin N.-Y., Bakin A.V., Baselga J., Arteaga C.L.View abstractCited forINTERACTION WITH CDKN1B, FUNCTION, MUTAGENESIS OF THR-308 AND SER-473CategoriesFunction, Disease & Variants, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCNat. Med. 8:1145-1152 (2002)Cited in2Mapped to16
Identification of Tyr900 in the kinase domain of c-Kit as a Src-dependent phosphorylation site mediating interaction with c-Crk.Lennartsson J., Wernstedt C., Engstrom U., Hellman U., Ronnstrand L.View abstractCited forFUNCTION IN PARTICIPATION IN KIT SIGNALINGCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCExp. Cell Res. 288:110-118 (2003)Cited in4Mapped to20
PIKE (phosphatidylinositol 3-kinase enhancer)-A GTPase stimulates Akt activity and mediates cellular invasion.Ahn J.-Y., Rong R., Kroll T.G., Van Meir E.G., Snyder S.H., Ye K.View abstractCited forINTERACTION WITH AGAP2, PHOSPHORYLATION AT SER-473CategoriesPTM / Processing, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 279:16441-16451 (2004)Cited in2Mapped to2
LGI1, a putative tumor metastasis suppressor gene, controls in vitro invasiveness and expression of matrix metalloproteinases in glioma cells through the ERK1/2 pathway.Kunapuli P., Kasyapa C.S., Hawthorn L., Cowell J.K.View abstractCited forPHOSPHORYLATION AT SER-473CategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 279:23151-23157 (2004)Cited in3Mapped to6