The Eukaryote Linear Motif resource for Functional Sites in Proteins
Accession:
Functional site class:
PKB Phosphorylation site
Functional site description:
Motif phosphorylated by a subset of AGC group kinases including PKB that all have similar sequence specificity.
ELM Description:
Phosphorylation site preference R.R.(ST) targeted by some basophilic kinases of the AGC group, including PKB and p70S6K. AGC group kinases do not tolerate Pro at position +1. Lys at the Arg positions may be allowed in some weaker sites. Some specificity determinants may occur at the less conserved non-basic sites: e.g Phe at position +2 is reported to be an optimal PKB site but a poor one for p60S6K.
Pattern: R.R..([ST])[^P]..
Pattern Probability: 0.0006034
Present in taxons: Caenorhabditis elegans Dictyostelium discoideum Drosophila melanogaster Eukaryota Vertebrata
Interaction Domain:
Pkinase (PF00069) Protein kinase domain (Stochiometry: 1 : 1)
o See 20 Instances for MOD_PKB_1
o Abstract
Protein kinase B (PKB/Akt/Rac-protein kinase) belongs to the large set of related AGC kinases having a preference for phosphorylating basophilic sites. PKB is a key player in the signaling pathways of numerous essential eukaryotic cellular processes including glucose metabolism, cell proliferation, apoptosis, cell migration and transcription. Many targets of PKB have been identified in vitro, and many studies looking at in vivo roles are currently underway. Kinase activity of PKB is stimulated by a variety of growth factors, cytokines, chemokines, heat shock, hyperosmolarity, hypoxia, integrin engagement and T-cell receptor interactions. The N-termini of the protein contains a pleckstrin homology (PH) domain that binds lipid products of phosphoinositide 3'-kinase (PI3K) and mediates recruitment to the membrane in response to PI3K (Obata,2000). Translocation of PKB then allows phosphorylation at Thr-308 by another Ser/Thr protein kinase (3-phosphoinositide-dependent protein kinase 1 (PDK1)) and full activation occurs after phosphorylation of Ser-473 (Toker,2000). A serine (or less often a threonine) residue at the end of the motif in PKB substrates is then phosphorylated.
o 7 selected references:

o 2 GO-Terms:

o 20 Instances for MOD_PKB_1
(click table headers for sorting; Notes column: =Number of Switches, =Number of Interactions)
Protein NameGene NameStartEndSubsequenceLogic#Ev.OrganismNotes
NR4A1_MOUSE Nr4a1 349 357 SLKGRRGRLPSKPKQPPDAS TP 1 Mus musculus (House mouse)
TERT_HUMAN TERT 819 827 CHHAVRIRGKSYVQCQGIPQ TP 1 Homo sapiens (Human)
F262_BOVIN PFKFB2 462 470 SQTPVRMRRNSFTPLSSSNT TP 1 Bos taurus (Cattle)
FOXO4_HUMAN FOXO4 192 200 SGKAPRRRAASMDSSSKLLR TP 3 Homo sapiens (Human)
CDN1B_HUMAN CDKN1B 152 160 QCAGIRKRPATDDSSTQNKR TP 6 Homo sapiens (Human)
1 
CDN1A_HUMAN CDKN1A 140 148 GDSQGRKRRQTSMTDFYHSK TP 2 Homo sapiens (Human)
1 
BAD_MOUSE Bad 131 139 ELSPFRGRSRSAPPNLWAAQ TP 5 Mus musculus (House mouse)
1 
FOXO4_HUMAN FOXO4 27 35 FEPQSRPRSCTWPLPRPEIA TP 3 Homo sapiens (Human)
1 
GSK3B_MOUSE Gsk3b 4 12 MSGRPRTTSFAESCKPVQQP TP 2 Mus musculus (House mouse)
1 
NR4A1_HUMAN NR4A1 346 354 SLKGRRGRLPSKPKQPPDAS TP 2 Homo sapiens (Human)
1 
CASP9_HUMAN CASP9 191 199 DCEKLRRRFSSLHFMVEVKG TP 2 Homo sapiens (Human)
1 
IKKA_HUMAN CHUK 18 26 GPWEMRERLGTGGFGNVCLY TP 2 Homo sapiens (Human)
1 
MDM2_HUMAN MDM2 161 169 PSTSSRRRAISETEENSDEL TP 2 Homo sapiens (Human)
1 
MDM2_HUMAN MDM2 181 189 SGERQRKRHKSDSISLSFDE TP 2 Homo sapiens (Human)
1 
BRCA1_HUMAN BRCA1 504 512 TNKLKRKRRPTSGLHPEDFI TP 2 Homo sapiens (Human)
1 
RAF1_HUMAN RAF1 254 262 GSLSQRQRSTSTPNVHMVST TP 2 Homo sapiens (Human)
1 
TSC2_HUMAN TSC2 934 942 EKDSFRARSTSLNERPKSLR TP 1 Homo sapiens (Human)
1 
TSC2_HUMAN TSC2 976 984 AAEAFRCRSISVSEHVVRSR TP 1 Homo sapiens (Human)
1 
TSC2_HUMAN TSC2 1127 1135 RGARDRVRSMSGGHGLRVGA TP 1 Homo sapiens (Human)
1 
TSC2_HUMAN TSC2 1457 1465 SPSGLRPRGYTISDSAPSRR TP 1 Homo sapiens (Human)
1 
Please cite: The Eukaryotic Linear Motif Resource ELM: 10 Years and Counting (PMID:24214962)

ELM data can be downloaded & distributed for non-commercial use according to the ELM Software License Agreement
feedback@elm.eu.org