Q9WUA6
Gene name |
Akt3 |
Protein name |
RAC-gamma serine/threonine-protein kinase |
Names |
Protein kinase Akt-3, Protein kinase B gamma, PKB gamma, RAC-PK-gamma |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:23797 |
EC number |
2.7.11.1: Protein-serine/threonine kinases |
Protein Class |
|
Descriptions
(Annotation based on sequence homology with P31749)
The protein kinase Akt is one of the primary effectors of growth factor signaling in the cell. Akt responds specifically to the lipid second messengers phosphatidylinositol-3,4,5-trisphosphate [PI(3,4,5)P3] and phosphatidylinositol-3,4-bisphosphate [PI(3,4)P2] via its autoinhibitory domain (PH domain). Recruitment of Akt to PI(3,4,5)P3 in the plasma membrane promotes its phosphorylation by phosphoinositide-dependent kinase 1 (PDK1) in its activation loop (T308). Phosphorylation of S473 within AGC kinase C-terminal domain activates Akt through the formation of an electrostatic interaction with a conserved basic residue (R144) in the PH-kinase domain linker, thereby relieving PH domain- mediated autoinhibition.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
288-311 (Activation loop from InterPro)
Target domain |
132-479 (Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma, also called Akt3) |
Relief mechanism |
|
Assay |
|
Autoinhibited structure
Activated structure
1 structures for Q9WUA6
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9WUA6-F1 | Predicted | AlphaFoldDB |
24 variants for Q9WUA6
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388521282 | 8 | K>N | No | EVA | |
| rs3388520897 | 8 | K>R | No | EVA | |
| rs3388519264 | 9 | E>D | No | EVA | |
| rs3388518176 | 9 | E>D | No | EVA | |
| rs3388519302 | 11 | W>* | No | EVA | |
| rs3388518757 | 21 | N>I | No | EVA | |
| rs3388514994 | 98 | W>* | No | EVA | |
| rs3388519573 | 118 | N>I | No | EVA | |
| rs3388520531 | 176 | M>I | No | EVA | |
| rs3388520156 | 178 | I>N | No | EVA | |
| rs3388520006 | 186 | A>P | No | EVA | |
| rs3388520962 | 191 | A>P | No | EVA | |
| rs3388519981 | 320 | D>E | No | EVA | |
| rs3388520900 | 326 | A>V | No | EVA | |
| rs3388514539 | 353 | K>E | No | EVA | |
| rs3388518791 | 358 | I>L | No | EVA | |
| rs247597104 | 367 | R>G | No | EVA | |
| rs3388520912 | 381 | L>W | No | EVA | |
| rs3388517017 | 406 | S>F | No | EVA | |
| rs1131706834 | 446 | I>L | No | EVA | |
| rs1134633760 | 447 | T>A | No | EVA | |
| rs1134272733 | 449 | P>A | No | EVA | |
| rs3410965115 | 462 | N>S | No | EVA | |
| rs3388519932 | 475 | A>V | No | EVA |
No associated diseases with Q9WUA6
8 regional properties for Q9WUA6
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Protein kinase domain | 148 - 405 | IPR000719 |
| domain | AGC-kinase, C-terminal | 406 - 479 | IPR000961 |
| domain | Pleckstrin homology domain | 5 - 109 | IPR001849 |
| active_site | Serine/threonine-protein kinase, active site | 267 - 279 | IPR008271 |
| binding_site | Protein kinase, ATP binding site | 154 - 187 | IPR017441 |
| domain | Protein kinase, C-terminal | 426 - 473 | IPR017892 |
| domain | Protein kinase B gamma, catalytic domain | 132 - 479 | IPR034675 |
| domain | Protein Kinase B, pleckstrin homology domain | 4 - 110 | IPR039026 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.11.1 | Protein-serine/threonine kinases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| nucleus | A membrane-bounded organelle of eukaryotic cells in which chromosomes are housed and replicated. In most cells, the nucleus contains all of the cell's chromosomes except the organellar chromosomes, and is the site of RNA synthesis and processing. In some species, or in specialized cell types, RNA metabolism or DNA replication may be absent. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| protein kinase activity | Catalysis of the phosphorylation of an amino acid residue in a protein, usually according to the reaction: a protein + ATP = a phosphoprotein + ADP. |
| protein kinase C binding | Binding to protein kinase C. |
| protein serine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate. |
| protein serine/threonine kinase activity | Catalysis of the reactions: ATP + protein serine = ADP + protein serine phosphate, and ATP + protein threonine = ADP + protein threonine phosphate. |
19 GO annotations of biological process
| Name | Definition |
|---|---|
| brain morphogenesis | The process in which the anatomical structures of the brain are generated and organized. The brain is one of the two components of the central nervous system and is the center of thought and emotion. It is responsible for the coordination and control of bodily activities and the interpretation of information from the senses (sight, hearing, smell, etc.). |
| cellular response to insulin stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of an insulin stimulus. Insulin is a polypeptide hormone produced by the islets of Langerhans of the pancreas in mammals, and by the homologous organs of other organisms. |
| homeostasis of number of cells within a tissue | Any biological process involved in the maintenance of the steady-state number of cells within a population of cells in a tissue. |
| intracellular signal transduction | The process in which a signal is passed on to downstream components within the cell, which become activated themselves to further propagate the signal and finally trigger a change in the function or state of the cell. |
| mitochondrial genome maintenance | The maintenance of the structure and integrity of the mitochondrial genome; includes replication and segregation of the mitochondrial chromosome. |
| negative regulation of cellular senescence | Any process that stops, prevents or reduces the frequency, rate or extent of cellular senescence. |
| peptidyl-serine phosphorylation | The phosphorylation of peptidyl-serine to form peptidyl-O-phospho-L-serine. |
| peptidyl-threonine phosphorylation | The phosphorylation of peptidyl-threonine to form peptidyl-O-phospho-L-threonine. |
| positive regulation of angiogenesis | Any process that activates or increases angiogenesis. |
| positive regulation of artery morphogenesis | Any process that activates or increases the frequency, rate or extent of artery morphogenesis. |
| positive regulation of blood vessel endothelial cell migration | Any process that activates or increases the frequency, rate or extent of the migration of the endothelial cells of blood vessels. |
| positive regulation of cell migration involved in sprouting angiogenesis | Any process that increases the frequency, rate or extent of cell migration involved in sprouting angiogenesis. Cell migration involved in sprouting angiogenesis is the orderly movement of endothelial cells into the extracellular matrix in order to form new blood vessels contributing to the process of sprouting angiogenesis. |
| positive regulation of cell size | Any process that increases cell size. |
| positive regulation of endothelial cell proliferation | Any process that activates or increases the rate or extent of endothelial cell proliferation. |
| positive regulation of sodium ion transport | Any process that increases the frequency, rate or extent of the directed movement of sodium ions (Na+) into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. |
| positive regulation of TOR signaling | Any process that activates or increases the frequency, rate or extent of TOR signaling. |
| positive regulation of vascular endothelial cell proliferation | Any process that activates or increases the frequency, rate or extent of vascular endothelial cell proliferation. |
| protein phosphorylation | The process of introducing a phosphate group on to a protein. |
| signal transduction | The cellular process in which a signal is conveyed to trigger a change in the activity or state of a cell. Signal transduction begins with reception of a signal (e.g. a ligand binding to a receptor or receptor activation by a stimulus such as light), or for signal transduction in the absence of ligand, signal-withdrawal or the activity of a constitutively active receptor. Signal transduction ends with regulation of a downstream cellular process, e.g. regulation of transcription or regulation of a metabolic process. Signal transduction covers signaling from receptors located on the surface of the cell and signaling via molecules located within the cell. For signaling between cells, signal transduction is restricted to events at and within the receiving cell. |
29 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q01314 | AKT1 | RAC-alpha serine/threonine-protein kinase | Bos taurus (Bovine) | SS |
| Q8INB9 | Akt | RAC serine/threonine-protein kinase | Drosophila melanogaster (Fruit fly) | SS |
| P31751 | AKT2 | RAC-beta serine/threonine-protein kinase | Homo sapiens (Human) | EV SS |
| P31749 | AKT1 | RAC-alpha serine/threonine-protein kinase | Homo sapiens (Human) | EV |
| Q9Y243 | AKT3 | RAC-gamma serine/threonine-protein kinase | Homo sapiens (Human) | SS |
| Q9Z2A0 | Pdpk1 | 3-phosphoinositide-dependent protein kinase 1 | Mus musculus (Mouse) | SS |
| Q02956 | Prkcz | Protein kinase C zeta type | Mus musculus (Mouse) | SS |
| Q62074 | Prkci | Protein kinase C iota type | Mus musculus (Mouse) | SS |
| P70268 | Pkn1 | Serine/threonine-protein kinase N1 | Mus musculus (Mouse) | SS |
| Q8K045 | Pkn3 | Serine/threonine-protein kinase N3 | Mus musculus (Mouse) | SS |
| Q8BWW9 | Pkn2 | Serine/threonine-protein kinase N2 | Mus musculus (Mouse) | SS |
| P23298 | Prkch | Protein kinase C eta type | Mus musculus (Mouse) | PR |
| P16054 | Prkce | Protein kinase C epsilon type | Mus musculus (Mouse) | PR |
| Q02111 | Prkcq | Protein kinase C theta type | Mus musculus (Mouse) | PR |
| P28867 | Prkcd | Protein kinase C delta type | Mus musculus (Mouse) | PR |
| P20444 | Prkca | Protein kinase C alpha type | Mus musculus (Mouse) | SS |
| P63318 | Prkcg | Protein kinase C gamma type | Mus musculus (Mouse) | SS |
| P68404 | Prkcb | Protein kinase C beta type | Mus musculus (Mouse) | SS |
| Q60823 | Akt2 | RAC-beta serine/threonine-protein kinase | Mus musculus (Mouse) | PR |
| P31750 | Akt1 | RAC-alpha serine/threonine-protein kinase | Mus musculus (Mouse) | PR |
| Q9ERE3 | Sgk3 | Serine/threonine-protein kinase Sgk3 | Mus musculus (Mouse) | PR |
| Q8QZV4 | Stk32c | Serine/threonine-protein kinase 32C | Mus musculus (Mouse) | PR |
| Q91VJ4 | Stk38 | Serine/threonine-protein kinase 38 | Mus musculus (Mouse) | SS |
| Q7TSE6 | Stk38l | Serine/threonine-protein kinase 38-like | Mus musculus (Mouse) | SS |
| P47197 | Akt2 | RAC-beta serine/threonine-protein kinase | Rattus norvegicus (Rat) | SS |
| P47196 | Akt1 | RAC-alpha serine/threonine-protein kinase | Rattus norvegicus (Rat) | PR |
| Q63484 | Akt3 | RAC-gamma serine/threonine-protein kinase | Rattus norvegicus (Rat) | PR |
| Q9XTG7 | akt-2 | Serine/threonine-protein kinase akt-2 | Caenorhabditis elegans | SS |
| Q17941 | akt-1 | Serine/threonine-protein kinase akt-1 | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSDVTIVKEG | WVQKRGEYIK | NWRPRYFLLK | TDGSFIGYKE | KPQDVDLPYP | LNNFSVAKCQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LMKTERPKPN | TFIIRCLQWT | TVIERTFHVD | TPEEREEWTE | AIQAVADRLQ | RQEEERMNCS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PTSQIDNIGE | EEMDASTTHH | KRKTMNDFDY | LKLLGKGTFG | KVILVREKAS | GKYYAMKILK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEVIIAKDEV | AHTLTESRVL | KNTRHPFLTS | LKYSFQTKDR | LCFVMEYVNG | GELFFHLSRE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RVFSEDRTRF | YGAEIVSALD | YLHSGKIVYR | DLKLENLMLD | KDGHIKITDF | GLCKEGITDA |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ATMKTFCGTP | EYLAPEVLED | NDYGRAVDWW | GLGVVMYEMM | CGRLPFYNQD | HEKLFELILM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| EDIKFPRTLS | SDAKSLLSGL | LIKDPNKRLG | GGPDDAKEIM | RHSFFSGVNW | QDVYDKKLVP |
| 430 | 440 | 450 | 460 | 470 | |
| PFKPQVTSET | DTRYFDEEFT | AQTITITPPE | KYDDDGMDGM | DNERRPHFPQ | FSYSASGRE |