3-phosphoinositide-dependent protein kinase 1 (hPDK1) (EC 2.7.11.1)
1_MARTT 6_ SQLYD 11_ AVPIQ 16_ SSVVL 21_ CSCPS 26_ PSMVR 31_ TQTES 36_ STPPG 41_ IPGGS 46_ RQGPA 51_ MDGTA 56_ AEPRP 61_ GAGSL 66_ QHAQP 71_ PPQPR 76_ KKRPE 81_ DFKFG 86_ KILGE 91_ GSFST 96_ VVLAR 101_ ELATS 106_ REYAI 111_ KILEK 116_ RHIIK 121_ ENKVP 126_ YVTRE 131_ RDVMS 136_ RLDHP 141_ FFVKL 146_ YFTFQ 151_ DDEKL 156_ YFGLS 161_ YAKNG 166_ ELLKY 171_ IRKIG 176_ SFDET 181_ CTRFY 186_ TAEIV 191_ SALEY 196_ LHGKG 201_ IIHRD 206_ LKPEN 211_ ILLNE 216_ DMHIQ 221_ ITDFG 226_ TAKVL 231_ SPESK 236_ QARAN 241_ SFVGT 246_ AQYVS 251_ PELLT 256_ EKSAC 261_ KSSDL 266_ WALGC 271_ IIYQL 276_ VAGLP 281_ PFRAG 286_ NEYLI 291_ FQKII 296_ KLEYD 301_ FPEKF 306_ FPKAR 311_ DLVEK 316_ LLVLD 321_ ATKRL 326_ GCEEM 331_ EGYGP 336_ LKAHP 341_ FFESV 346_ TWENL 351_ HQQTP 356_ PKLTA 361_ YLPAM 366_ SEDDE 371_ DCYGN 376_ YDNLL 381_ SQFGC 386_ MQVSS 391_ SSSSH 396_ SLSAS 401_ DTGLP 406_ QRSGS 411_ NIEQY 416_ IHDLD 421_ SNSFE 426_ LDLQF 431_ SEDEK 436_ RLLLE 441_ KQAGG 446_ NPWHQ 451_ FVENN 456_ LILKM 461_ GPVDK 466_ RKGLF 471_ ARRRQ 476_ LLLTE 481_ GPHLY 486_ YVDPV 491_ NKVLK 496_ GEIPW 501_ SQELR 506_ PEAKN 511_ FKTFF 516_ VHTPN 521_ RTYYL 526_ MDPSG 531_ NAHKW 536_ CRKIQ 541_ EVWRQ 546_ RYQSH 551_PDAAV
1: Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases (PubMed:10226025, PubMed:10480933, PubMed:10995762, PubMed:12167717, PubMed:14585963, PubMed:14604990, PubMed:16207722, PubMed:16251192, PubMed:17327236, PubMed:17371830, PubMed:18835241, PubMed:9094314, PubMed:9368760, PubMed:9445476, PubMed:9445477, PubMed:9707564, PubMed:9768361). Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), TSSK3, protein kinase PKN (PKN1 and PKN2) (PubMed:10226025, PubMed:10480933, PubMed:10995762, PubMed:12167717, PubMed:14585963, PubMed:14604990, PubMed:16207722, PubMed:16251192, PubMed:17327236, PubMed:17371830, PubMed:18835241, PubMed:9094314, PubMed:9368760, PubMed:9445476, PubMed:9707564, PubMed:9768361). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage (PubMed:10226025, PubMed:12167717, PubMed:9094314). Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta (PubMed:17327236). Activates PPARG transcriptional activity and promotes adipocyte differentiation (By similarity). Activates the NF-kappa-B pathway via phosphorylation of IKKB (PubMed:16207722). The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II (PubMed:14585963). Controls proliferation, survival, and growth of developing pancreatic cells (By similarity). Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells (By similarity). Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis (PubMed:17371830). Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response (By similarity). Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses (By similarity). Provides negative feedback inhibition to toll-like receptor-mediated NF-kappa-B activation in macrophages (By similarity)
2: Catalytically inactive