Structure
atLeast majority ProS Experiment
:order disorder conflict PDB cluster ProS Pfam Domain SEG
481
order/disorder by at least rule
disorder by at least rule
order/disorder by majority rule
Region 1p6s A 1-111 order
Region 1p6s A 1-1 high_rmsd
Region 1p6s A 44-48 high_rmsd
Region 1p6s A 79-84 high_rmsd
Region 1gzk A 146-188 order
Region 1gzk A 189-197 disorder
Region 1gzk A 198-296 order
Region 1gzk A 297-312 disorder
Region 1gzk A 313-441 order
Region 1gzk A 442-460 disorder
Region 1gzn A 146-188 order
Region 1gzn A 189-197 disorder
Region 1gzn A 198-296 order
Region 1gzn A 297-312 disorder
Region 1gzn A 313-441 order
Region 1gzn A 442-480 disorder
Region 1gzo A 146-188 order
Region 1gzo A 189-197 disorder
Region 1gzo A 198-296 order
Region 1gzo A 297-312 disorder
Region 1gzo A 313-441 order
Region 1gzo A 442-460 disorder
Region 1mrv A 143-146 disorder
Region 1mrv A 147-188 order
Region 1mrv A 189-202 disorder
Region 1mrv A 203-294 order
Region 1mrv A 295-313 disorder
Region 1mrv A 314-440 order
Region 1mrv A 441-481 disorder
Region 1mry A 143-145 disorder
Region 1mry A 146-189 order
Region 1mry A 190-201 disorder
Region 1mry A 202-297 order
Region 1mry A 298-310 disorder
Region 1mry A 311-440 order
Region 1mry A 441-481 disorder
Region 3d0e B 146-454 order
Region 3d0e B 455-465 disorder
Region 3d0e B 466-480 order
Region 3d0e A 146-454 order
Region 3d0e A 455-465 disorder
Region 3d0e A 466-480 order
Seq 146-481 Hetero dimer : IID00052 Complex
Region 3e87 A 146-453 order
Region 3e87 A 454-465 disorder
Region 3e87 A 466-480 order
Region 3e87 B 146-453 order
Region 3e87 B 454-465 disorder
Region 3e87 B 466-480 order
Region 3e88 A 146-451 order
Region 3e88 A 452-465 disorder
Region 3e88 A 466-480 order
Region 3e88 B 146-451 order
Region 3e88 B 452-465 disorder
Region 3e88 B 466-480 order
Region 3e8d A 146-448 order
Region 3e8d A 449-467 disorder
Region 3e8d A 468-480 order
Region 3e8d B 146-448 order
Region 3e8d B 449-465 disorder
Region 3e8d B 466-480 order
Region 2jdo A 146-449 order
Region 2jdo A 450-467 disorder
Region 2jdr A 146-449 order
Region 2jdr A 450-467 disorder
Region 1o6k A 146-449 order
Region 1o6k A 450-465 disorder
Region 1o6k A 466-479 order
Region 1o6k A 480-481 disorder
Region 1o6l A 146-449 order
Region 1o6l A 450-467 disorder
Region 2uw9 A 146-449 order
Region 2uw9 A 450-467 disorder
Region 2x39 A 146-449 order
Region 2xh5 A 146-449 order
Region 2xh5 A 450-467 disorder
Seq ProS verified 189-197,297-312 Hetero dimer : IID00052 Complex
Region 3e87 A 146-453 order
Region 3e87 B 146-453 order
Region 2uw9 A 146-449 order
Region 1o6l A 146-449 order
Region 2jdo A 146-449 order
Region 1o6k A 146-449 order
Region 3e8d A 146-448 order
Region 3e8d B 146-448 order
Region 3e88 A 146-451 order
Region 3e88 B 146-451 order
Region 2jdr A 146-449 order
Region 2xh5 A 146-449 order
Region 2x39 A 146-449 order
Region 1gzn A 189-197 disorder
Region 1gzn A 297-312 disorder
309-309 Phosphothreonine; by PDPK1
Prediction
Disorder 1-1,110-146,456-460
Order 2-109,147-455,466-481
Disorder 1-3,16-20,44-52,78-84,114-145,324-325,447-469,478-481
Order 4-15,21-43,53-77,85-113,146-323,326-446,470-477
Function
Function in SwissProt
One of the few specific substrates of AKT2 identified recently is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.
Biological Process
Diagram with PDB data
AKT2/GSK3B Structure of activated form of PKB kinase domain S474D with GSK3 peptide and AMP-PNP
See also
Diagram with PDB data
CREB1/CRBBP/KMT2A Allosteric communication in the KIX
domain proceeds through dynamic re-packing of the hydrophobic core