UniProtKB - Q60823 (AKT2_MOUSE)
Protein
RAC-beta serine/threonine-protein kinase
Gene
Akt2
Organism
Mus musculus (Mouse)
Status
Functioni
AKT2 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI3P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
One of the few specific substrates of AKT2 identified so far 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. Phosphorylates CLK2 on 'Thr-343'.
Caution
In light of strong homologies in the primary amino acid sequence, the 3 AKT kinases were long surmised to play redundant and overlapping roles. More recent studies has brought into question the redundancy within AKT kinase isoforms and instead pointed to isoform specific functions in different cellular events and diseases. AKT1 is more specifically involved in cellular survival pathways, by inhibiting apoptotic processes; whereas AKT2 is more specific for the insulin receptor signaling pathway. Moreover, while AKT1 and AKT2 are often implicated in many aspects of cellular transformation, the 2 isoforms act in a complementary opposing manner. The role of AKT3 is less clear, though it appears to be predominantly expressed in brain.Curated
Catalytic activityi
Activity regulationi
Two specific sites, one in the kinase domain (Thr-309) and the other in the C-terminal regulatory region (Ser-474), need to be phosphorylated for its full activation.By similarity
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 181 | ATPPROSITE-ProRule annotation | 1 | |
Binding sitei | 181 | InhibitorBy similarity | 1 | |
Binding sitei | 200 | InhibitorBy similarity | 1 | |
Binding sitei | 232 | Inhibitor; via amide nitrogenBy similarity | 1 | |
Binding sitei | 236 | InhibitorBy similarity | 1 | |
Active sitei | 275 | Proton acceptorPROSITE-ProRule annotation | 1 | |
Binding sitei | 279 | Inhibitor; via carbonyl oxygenBy similarity | 1 | |
Metal bindingi | 280 | ManganeseBy similarity | 1 | |
Metal bindingi | 293 | ManganeseBy similarity | 1 | |
Binding sitei | 293 | InhibitorBy similarity | 1 | |
Binding sitei | 294 | Inhibitor; via amide nitrogenBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 158 – 166 | ATPPROSITE-ProRule annotation | 9 |
GO - Molecular functioni
- ATP binding Source: MGI
- metal ion binding Source: UniProtKB-KW
- protein kinase activity Source: MGI
- protein kinase C binding Source: MGI
- protein serine/threonine kinase activity Source: MGI
- protein serine kinase activity Source: UniProtKB-EC
- protein threonine kinase activity Source: UniProtKB-EC
GO - Biological processi
- activation of GTPase activity Source: MGI
- carbohydrate transport Source: UniProtKB-KW
- cellular response to high light intensity Source: MGI
- cellular response to insulin stimulus Source: UniProtKB
- cellular response to organic cyclic compound Source: MGI
- glucose metabolic process Source: MGI
- glycogen biosynthetic process Source: UniProtKB-KW
- insulin receptor signaling pathway Source: MGI
- intracellular protein transmembrane transport Source: UniProtKB
- intracellular signal transduction Source: GO_Central
- negative regulation of apoptotic process Source: MGI
- negative regulation of cysteine-type endopeptidase activity involved in apoptotic process Source: MGI
- negative regulation of long-chain fatty acid import across plasma membrane Source: MGI
- negative regulation of RNA splicing Source: MGI
- peptidyl-serine phosphorylation Source: GO_Central
- peripheral nervous system myelin maintenance Source: MGI
- positive regulation of cell migration Source: MGI
- positive regulation of cell motility Source: MGI
- positive regulation of cell population proliferation Source: MGI
- positive regulation of fatty acid beta-oxidation Source: MGI
- positive regulation of gene expression Source: MGI
- positive regulation of glucose import Source: MGI
- positive regulation of glucose metabolic process Source: MGI
- positive regulation of glycogen biosynthetic process Source: MGI
- positive regulation of mitochondrial membrane potential Source: MGI
- positive regulation of nitric oxide biosynthetic process Source: MGI
- positive regulation of peptidyl-serine phosphorylation Source: MGI
- positive regulation of positive chemotaxis Source: MGI
- positive regulation of protein phosphorylation Source: UniProtKB
- positive regulation of protein targeting to membrane Source: UniProtKB
- positive regulation of signal transduction Source: MGI
- positive regulation of sodium ion transport Source: MGI
- positive regulation of transcription by RNA polymerase II Source: MGI
- positive regulation of vesicle fusion Source: UniProtKB
- protein kinase B signaling Source: MGI
- protein localization to plasma membrane Source: MGI
- protein phosphorylation Source: MGI
- regulation of translation Source: UniProtKB-KW
- response to insulin Source: MGI
- retinal rod cell apoptotic process Source: MGI
Keywordsi
Molecular function | Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase |
Biological process | Apoptosis, Carbohydrate metabolism, Glucose metabolism, Glycogen biosynthesis, Glycogen metabolism, Sugar transport, Translation regulation, Transport |
Ligand | ATP-binding, Manganese, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 3474 |
Reactomei | R-MMU-1257604, PIP3 activates AKT signaling R-MMU-1358803, Downregulation of ERBB2:ERBB3 signaling R-MMU-165158, Activation of AKT2 R-MMU-165181, Inhibition of TSC complex formation by PKB R-MMU-198323, AKT phosphorylates targets in the cytosol R-MMU-198693, AKT phosphorylates targets in the nucleus R-MMU-199418, Negative regulation of the PI3K/AKT network R-MMU-211163, AKT-mediated inactivation of FOXO1A R-MMU-3769402, Deactivation of the beta-catenin transactivating complex R-MMU-389357, CD28 dependent PI3K/Akt signaling R-MMU-389513, CTLA4 inhibitory signaling R-MMU-392451, G beta:gamma signalling through PI3Kgamma R-MMU-5218920, VEGFR2 mediated vascular permeability R-MMU-5628897, TP53 Regulates Metabolic Genes R-MMU-6804757, Regulation of TP53 Degradation R-MMU-6804758, Regulation of TP53 Activity through Acetylation R-MMU-6804759, Regulation of TP53 Activity through Association with Co-factors R-MMU-69202, Cyclin E associated events during G1/S transition R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry R-MMU-8876198, RAB GEFs exchange GTP for GDP on RABs R-MMU-8948751, Regulation of PTEN stability and activity R-MMU-9607240, FLT3 Signaling R-MMU-9614399, Regulation of localization of FOXO transcription factors R-MMU-9634638, Estrogen-dependent nuclear events downstream of ESR-membrane signaling |
Names & Taxonomyi
Protein namesi | Recommended name: RAC-beta serine/threonine-protein kinase (EC:2.7.11.1)Alternative name(s): Protein kinase Akt-2 Protein kinase B beta Short name: PKB beta RAC-PK-beta |
Gene namesi | Name:Akt2 |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:104874, Akt2 |
Subcellular locationi
Nucleus
- Nucleus 1 Publication
Endosome
- Early endosome 1 Publication
Plasma membrane
- Cell membrane By similarity; Peripheral membrane protein By similarity
Cytoplasm and Cytosol
- Cytoplasm 1 Publication
Note: Localizes within both nucleus and cytoplasm of proliferative primary myoblasts and mostly within the nucleus of differentiated primary myoblasts. By virtue of the N-terminal PH domain, is recruited to sites of the plasma membrane containing increased PI(3,4,5)P3 or PI(3,4)P2, cell membrane targeting is also facilitared by interaction with CLIP3. Colocalizes with WDFY2 in early endosomes (PubMed:20189988).By similarity1 Publication
Cytosol
- cytosol Source: MGI
Endoplasmic reticulum
- sarcoplasmic reticulum Source: MGI
Endosome
- early endosome Source: UniProtKB-SubCell
Mitochondrion
- mitochondrion Source: MGI
Nucleus
- nucleoplasm Source: MGI
- nucleus Source: MGI
Plasma Membrane
- plasma membrane Source: UniProtKB
- ruffle membrane Source: UniProtKB
Other locations
- cell cortex Source: UniProtKB
- insulin-responsive compartment Source: MGI
- intracellular membrane-bounded organelle Source: MGI
- protein-containing complex Source: MGI
- vesicle Source: MGI
Keywords - Cellular componenti
Cell membrane, Cytoplasm, Endosome, Membrane, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000085609 | 1 – 481 | RAC-beta serine/threonine-protein kinaseAdd BLAST | 481 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 1 | N-acetylmethionineBy similarity | 1 | |
Modified residuei | 34 | PhosphoserineBy similarity | 1 | |
Disulfide bondi | 60 ↔ 77 | By similarity | ||
Modified residuei | 126 | PhosphoserineCombined sources | 1 | |
Glycosylationi | 128 | O-linked (GlcNAc) serineBy similarity | 1 | |
Glycosylationi | 131 | O-linked (GlcNAc) serineBy similarity | 1 | |
Disulfide bondi | 297 ↔ 311 | By similarity | ||
Glycosylationi | 306 | O-linked (GlcNAc) threonineBy similarity | 1 | |
Modified residuei | 309 | Phosphothreonine; by PDPK1By similarity | 1 | |
Glycosylationi | 313 | O-linked (GlcNAc) threonineBy similarity | 1 | |
Modified residuei | 447 | PhosphoserineBy similarity | 1 | |
Modified residuei | 451 | PhosphothreonineCombined sources | 1 | |
Modified residuei | 474 | PhosphoserineBy similarity | 1 | |
Modified residuei | 478 | PhosphoserineBy similarity | 1 |
Post-translational modificationi
Phosphorylation on Thr-309 and Ser-474 is required for full activity.By similarity
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity).By similarity
O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via disrupting the interaction between AKT and PDK1.By similarity
Keywords - PTMi
Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugationProteomic databases
EPDi | Q60823 |
jPOSTi | Q60823 |
MaxQBi | Q60823 |
PaxDbi | Q60823 |
PRIDEi | Q60823 |
ProteomicsDBi | 296016 |
PTM databases
GlyGeni | Q60823, 4 sites |
iPTMneti | Q60823 |
PhosphoSitePlusi | Q60823 |
Expressioni
Gene expression databases
Bgeei | ENSMUSG00000004056, Expressed in hindlimb stylopod muscle and 253 other tissues |
Genevisiblei | Q60823, MM |
Interactioni
Subunit structurei
Interacts (via PH domain) with MTCP1, TCL1A AND TCL1B.
Interacts with CLK2, PBH2 and TRAF6.
Interacts (when phosphorylated) with CLIP3, the interaction promotes cell membrane localization (By similarity).
Interacts with BTBD10 (PubMed:18160256).
Interacts with KCTD20 (PubMed:24156551).
Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529, PubMed:20189988).
By similarity4 PublicationsGO - Molecular functioni
- protein kinase C binding Source: MGI
Protein-protein interaction databases
BioGRIDi | 198057, 15 interactors |
IntActi | Q60823, 28 interactors |
STRINGi | 10090.ENSMUSP00000103981 |
Miscellaneous databases
RNActi | Q60823, protein |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 5 – 108 | PHPROSITE-ProRule annotationAdd BLAST | 104 | |
Domaini | 152 – 409 | Protein kinasePROSITE-ProRule annotationAdd BLAST | 258 | |
Domaini | 410 – 481 | AGC-kinase C-terminalPROSITE-ProRule annotationAdd BLAST | 72 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 230 – 232 | Inhibitor bindingBy similarity | 3 | |
Regioni | 277 – 279 | Inhibitor bindingBy similarity | 3 | |
Regioni | 292 – 293 | Inhibitor bindingBy similarity | 2 |
Domaini
Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PIK3CA) results in its targeting to the plasma membrane.By similarity
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG0690, Eukaryota |
GeneTreei | ENSGT00940000157189 |
HOGENOMi | CLU_000288_11_0_1 |
InParanoidi | Q60823 |
OMAi | ITPPDRC |
OrthoDBi | 614710at2759 |
PhylomeDBi | Q60823 |
TreeFami | TF102004 |
Family and domain databases
CDDi | cd01241, PH_PKB, 1 hit cd05595, STKc_PKB_beta, 1 hit |
Gene3Di | 2.30.29.30, 1 hit |
InterProi | View protein in InterPro IPR000961, AGC-kinase_C IPR034677, Akt2 IPR011009, Kinase-like_dom_sf IPR011993, PH-like_dom_sf IPR001849, PH_domain IPR039026, PH_PKB IPR017892, Pkinase_C IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00169, PH, 1 hit PF00069, Pkinase, 1 hit PF00433, Pkinase_C, 1 hit |
SMARTi | View protein in SMART SM00233, PH, 1 hit SM00133, S_TK_X, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS51285, AGC_KINASE_CTER, 1 hit PS50003, PH_DOMAIN, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 7 potential isoforms that are computationally mapped.Show allAlign All
Q60823-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP
60 70 80 90 100
PLNNFSVAEC QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM
110 120 130 140 150
RAIQMVANSL KQRGPGEDAM DYKCGSPSDS STSEMMEVAV NKARAKVTMN
160 170 180 190 200
DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE
210 220 230 240 250
SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTED
260 270 280 290 300
RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG
310 320 330 340 350
ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF
360 370 380 390 400
YNQDHERLFE LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA
410 420 430 440 450
KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI
460 470 480
TPPDRYDSLD PLELDQRTHF PQFSYSASIR E
Computationally mapped potential isoform sequencesi
There are 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF8WHG5 | F8WHG5_MOUSE | Non-specific serine/threonine prote... | Akt2 | 438 | Annotation score: | ||
D3Z3N2 | D3Z3N2_MOUSE | RAC-beta serine/threonine-protein k... | Akt2 | 229 | Annotation score: | ||
D3YXM7 | D3YXM7_MOUSE | RAC-beta serine/threonine-protein k... | Akt2 | 222 | Annotation score: | ||
D3Z490 | D3Z490_MOUSE | RAC-beta serine/threonine-protein k... | Akt2 | 98 | Annotation score: | ||
D3YZJ5 | D3YZJ5_MOUSE | RAC-beta serine/threonine-protein k... | Akt2 | 84 | Annotation score: | ||
D3Z5X2 | D3Z5X2_MOUSE | RAC-beta serine/threonine-protein k... | Akt2 | 63 | Annotation score: | ||
D3Z0M3 | D3Z0M3_MOUSE | RAC-beta serine/threonine-protein k... | Akt2 | 67 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U22445 mRNA Translation: AAA83557.1 BC026151 mRNA Translation: AAH26151.1 BC040377 mRNA Translation: AAH40377.1 |
CCDSi | CCDS21027.1 |
RefSeqi | NP_001103678.1, NM_001110208.2 NP_001318037.1, NM_001331108.1 NP_001318038.1, NM_001331109.1 NP_031460.1, NM_007434.4 XP_006539540.1, XM_006539477.1 XP_006539543.1, XM_006539480.1 XP_006539544.1, XM_006539481.3 |
Genome annotation databases
Ensembli | ENSMUST00000051356; ENSMUSP00000052103; ENSMUSG00000004056 ENSMUST00000108343; ENSMUSP00000103980; ENSMUSG00000004056 ENSMUST00000108344; ENSMUSP00000103981; ENSMUSG00000004056 ENSMUST00000167435; ENSMUSP00000132141; ENSMUSG00000004056 |
GeneIDi | 11652 |
KEGGi | mmu:11652 |
UCSCi | uc009fwr.2, mouse |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | U22445 mRNA Translation: AAA83557.1 BC026151 mRNA Translation: AAH26151.1 BC040377 mRNA Translation: AAH40377.1 |
CCDSi | CCDS21027.1 |
RefSeqi | NP_001103678.1, NM_001110208.2 NP_001318037.1, NM_001331108.1 NP_001318038.1, NM_001331109.1 NP_031460.1, NM_007434.4 XP_006539540.1, XM_006539477.1 XP_006539543.1, XM_006539480.1 XP_006539544.1, XM_006539481.3 |
3D structure databases
BMRBi | Q60823 |
SMRi | Q60823 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 198057, 15 interactors |
IntActi | Q60823, 28 interactors |
STRINGi | 10090.ENSMUSP00000103981 |
Chemistry databases
ChEMBLi | CHEMBL5382 |
PTM databases
GlyGeni | Q60823, 4 sites |
iPTMneti | Q60823 |
PhosphoSitePlusi | Q60823 |
Proteomic databases
EPDi | Q60823 |
jPOSTi | Q60823 |
MaxQBi | Q60823 |
PaxDbi | Q60823 |
PRIDEi | Q60823 |
ProteomicsDBi | 296016 |
Protocols and materials databases
Antibodypediai | 3775, 1598 antibodies |
Genome annotation databases
Organism-specific databases
CTDi | 208 |
MGIi | MGI:104874, Akt2 |
Phylogenomic databases
eggNOGi | KOG0690, Eukaryota |
GeneTreei | ENSGT00940000157189 |
HOGENOMi | CLU_000288_11_0_1 |
InParanoidi | Q60823 |
OMAi | ITPPDRC |
OrthoDBi | 614710at2759 |
PhylomeDBi | Q60823 |
TreeFami | TF102004 |
Enzyme and pathway databases
BRENDAi | 2.7.11.1, 3474 |
Reactomei | R-MMU-1257604, PIP3 activates AKT signaling R-MMU-1358803, Downregulation of ERBB2:ERBB3 signaling R-MMU-165158, Activation of AKT2 R-MMU-165181, Inhibition of TSC complex formation by PKB R-MMU-198323, AKT phosphorylates targets in the cytosol R-MMU-198693, AKT phosphorylates targets in the nucleus R-MMU-199418, Negative regulation of the PI3K/AKT network R-MMU-211163, AKT-mediated inactivation of FOXO1A R-MMU-3769402, Deactivation of the beta-catenin transactivating complex R-MMU-389357, CD28 dependent PI3K/Akt signaling R-MMU-389513, CTLA4 inhibitory signaling R-MMU-392451, G beta:gamma signalling through PI3Kgamma R-MMU-5218920, VEGFR2 mediated vascular permeability R-MMU-5628897, TP53 Regulates Metabolic Genes R-MMU-6804757, Regulation of TP53 Degradation R-MMU-6804758, Regulation of TP53 Activity through Acetylation R-MMU-6804759, Regulation of TP53 Activity through Association with Co-factors R-MMU-69202, Cyclin E associated events during G1/S transition R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry R-MMU-8876198, RAB GEFs exchange GTP for GDP on RABs R-MMU-8948751, Regulation of PTEN stability and activity R-MMU-9607240, FLT3 Signaling R-MMU-9614399, Regulation of localization of FOXO transcription factors R-MMU-9634638, Estrogen-dependent nuclear events downstream of ESR-membrane signaling |
Miscellaneous databases
BioGRID-ORCSi | 11652, 1 hit in 54 CRISPR screens |
ChiTaRSi | Akt2, mouse |
PROi | PR:Q60823 |
RNActi | Q60823, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000004056, Expressed in hindlimb stylopod muscle and 253 other tissues |
Genevisiblei | Q60823, MM |
Family and domain databases
CDDi | cd01241, PH_PKB, 1 hit cd05595, STKc_PKB_beta, 1 hit |
Gene3Di | 2.30.29.30, 1 hit |
InterProi | View protein in InterPro IPR000961, AGC-kinase_C IPR034677, Akt2 IPR011009, Kinase-like_dom_sf IPR011993, PH-like_dom_sf IPR001849, PH_domain IPR039026, PH_PKB IPR017892, Pkinase_C IPR000719, Prot_kinase_dom IPR017441, Protein_kinase_ATP_BS IPR008271, Ser/Thr_kinase_AS |
Pfami | View protein in Pfam PF00169, PH, 1 hit PF00069, Pkinase, 1 hit PF00433, Pkinase_C, 1 hit |
SMARTi | View protein in SMART SM00233, PH, 1 hit SM00133, S_TK_X, 1 hit SM00220, S_TKc, 1 hit |
SUPFAMi | SSF56112, SSF56112, 1 hit |
PROSITEi | View protein in PROSITE PS51285, AGC_KINASE_CTER, 1 hit PS50003, PH_DOMAIN, 1 hit PS00107, PROTEIN_KINASE_ATP, 1 hit PS50011, PROTEIN_KINASE_DOM, 1 hit PS00108, PROTEIN_KINASE_ST, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | AKT2_MOUSE | |
Accessioni | Q60823Primary (citable) accession number: Q60823 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | December 1, 2000 |
Last sequence update: | November 1, 1996 | |
Last modified: | April 7, 2021 | |
This is version 191 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- Human and mouse protein kinases
Human and mouse protein kinases: classification and index - MGD cross-references
Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot - SIMILARITY comments
Index of protein domains and families