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Q60823

- AKT2_MOUSE

UniProt

Q60823 - AKT2_MOUSE

Protein

RAC-beta serine/threonine-protein kinase

Gene

Akt2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 132 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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'.

    Catalytic activityi

    ATP + a protein = ADP + a phosphoprotein.

    Enzyme 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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei181 – 1811ATPPROSITE-ProRule annotation
    Binding sitei181 – 1811InhibitorBy similarity
    Binding sitei200 – 2001InhibitorBy similarity
    Binding sitei232 – 2321Inhibitor; via amide nitrogenBy similarity
    Binding sitei236 – 2361InhibitorBy similarity
    Active sitei275 – 2751Proton acceptorPROSITE-ProRule annotation
    Binding sitei279 – 2791Inhibitor; via carbonyl oxygenBy similarity
    Binding sitei280 – 2801ManganeseBy similarity
    Binding sitei293 – 2931InhibitorBy similarity
    Binding sitei293 – 2931ManganeseBy similarity
    Binding sitei294 – 2941Inhibitor; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi158 – 1669ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. protein binding Source: UniProtKB
    3. protein kinase activity Source: MGI
    4. protein serine/threonine kinase activity Source: MGI

    GO - Biological processi

    1. activation of Ral GTPase activity Source: MGI
    2. apoptotic process Source: UniProtKB-KW
    3. carbohydrate transport Source: UniProtKB-KW
    4. cellular response to insulin stimulus Source: UniProtKB
    5. glucose metabolic process Source: UniProtKB-KW
    6. glycogen biosynthetic process Source: UniProtKB-KW
    7. insulin receptor signaling pathway Source: MGI
    8. intracellular protein transmembrane transport Source: UniProtKB
    9. negative regulation of plasma membrane long-chain fatty acid transport Source: Ensembl
    10. peripheral nervous system myelin maintenance Source: MGI
    11. positive regulation of cell motility Source: Ensembl
    12. positive regulation of fatty acid beta-oxidation Source: Ensembl
    13. positive regulation of glucose import in response to insulin stimulus Source: MGI
    14. positive regulation of glycogen biosynthetic process Source: Ensembl
    15. positive regulation of protein phosphorylation Source: UniProtKB
    16. positive regulation of protein targeting to membrane Source: UniProtKB
    17. positive regulation of vesicle fusion Source: UniProtKB
    18. protein localization to plasma membrane Source: MGI
    19. protein phosphorylation Source: MGI
    20. regulation of translation Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein, Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Biological processi

    Apoptosis, Carbohydrate metabolism, Glucose metabolism, Glycogen biosynthesis, Glycogen metabolism, Sugar transport, Translation regulation, Transport

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 3474.
    ReactomeiREACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 7

    Organism-specific databases

    MGIiMGI:104874. Akt2.

    Subcellular locationi

    Cytoplasm By similarity. Nucleus By similarity. Cell membrane By similarity; Peripheral membrane protein By similarity
    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.By similarity

    GO - Cellular componenti

    1. cell cortex Source: UniProtKB
    2. nucleus Source: UniProtKB-SubCell
    3. plasma membrane Source: UniProtKB
    4. ruffle membrane Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Membrane, Nucleus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 481481RAC-beta serine/threonine-protein kinasePRO_0000085609Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionineBy similarity
    Disulfide bondi60 ↔ 77By similarity
    Modified residuei126 – 1261PhosphoserineBy similarity
    Glycosylationi128 – 1281O-linked (GlcNAc)By similarity
    Glycosylationi131 – 1311O-linked (GlcNAc)By similarity
    Disulfide bondi297 ↔ 311By similarity
    Glycosylationi306 – 3061O-linked (GlcNAc)By similarity
    Modified residuei309 – 3091Phosphothreonine; by PDPK1By similarity
    Glycosylationi313 – 3131O-linked (GlcNAc)By similarity
    Modified residuei447 – 4471PhosphoserineBy similarity
    Modified residuei451 – 4511PhosphothreonineBy similarity
    Modified residuei474 – 4741PhosphoserineBy similarity
    Modified residuei478 – 4781PhosphoserineBy similarity

    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 conjugation

    Proteomic databases

    MaxQBiQ60823.
    PaxDbiQ60823.
    PRIDEiQ60823.

    PTM databases

    PhosphoSiteiQ60823.

    Expressioni

    Gene expression databases

    ArrayExpressiQ60823.
    BgeeiQ60823.
    CleanExiMM_AKT2.
    GenevestigatoriQ60823.

    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.By similarity

    Protein-protein interaction databases

    BioGridi198057. 2 interactions.
    IntActiQ60823. 6 interactions.
    MINTiMINT-1770302.

    Structurei

    3D structure databases

    ProteinModelPortaliQ60823.
    SMRiQ60823. Positions 1-480.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 108104PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini152 – 409258Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini410 – 48172AGC-kinase C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni230 – 2323Inhibitor bindingBy similarity
    Regioni277 – 2793Inhibitor bindingBy similarity
    Regioni292 – 2932Inhibitor bindingBy similarity

    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

    Contains 1 AGC-kinase C-terminal domain.Curated
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiCOG0515.
    GeneTreeiENSGT00740000114960.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ60823.
    KOiK04456.
    OMAiATGMYYA.
    OrthoDBiEOG7Q5HCW.
    PhylomeDBiQ60823.
    TreeFamiTF102004.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view]
    PfamiPF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view]
    SMARTiSM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS51285. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Q60823-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP    50
    PLNNFSVAEC QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM 100
    RAIQMVANSL KQRGPGEDAM DYKCGSPSDS STSEMMEVAV NKARAKVTMN 150
    DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE 200
    SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTED 250
    RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG 300
    ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF 350
    YNQDHERLFE LILMEEIRFP RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA 400
    KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI 450
    TPPDRYDSLD PLELDQRTHF PQFSYSASIR E 481
    Length:481
    Mass (Da):55,742
    Last modified:November 1, 1996 - v1
    Checksum:i4AB4A9C4FB9CFA7D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U22445 mRNA. Translation: AAA83557.1.
    BC026151 mRNA. Translation: AAH26151.1.
    BC040377 mRNA. Translation: AAH40377.1.
    CCDSiCCDS21027.1.
    RefSeqiNP_001103678.1. NM_001110208.1.
    NP_031460.1. NM_007434.3.
    XP_006539540.1. XM_006539477.1.
    XP_006539541.1. XM_006539478.1.
    XP_006539542.1. XM_006539479.1.
    XP_006539543.1. XM_006539480.1.
    XP_006539544.1. XM_006539481.1.
    UniGeneiMm.177194.

    Genome annotation databases

    EnsembliENSMUST00000051356; ENSMUSP00000052103; ENSMUSG00000004056.
    ENSMUST00000108343; ENSMUSP00000103980; ENSMUSG00000004056.
    ENSMUST00000108344; ENSMUSP00000103981; ENSMUSG00000004056.
    ENSMUST00000167435; ENSMUSP00000132141; ENSMUSG00000004056.
    GeneIDi11652.
    KEGGimmu:11652.
    UCSCiuc009fwr.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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_001110208.1.
    NP_031460.1. NM_007434.3.
    XP_006539540.1. XM_006539477.1.
    XP_006539541.1. XM_006539478.1.
    XP_006539542.1. XM_006539479.1.
    XP_006539543.1. XM_006539480.1.
    XP_006539544.1. XM_006539481.1.
    UniGenei Mm.177194.

    3D structure databases

    ProteinModelPortali Q60823.
    SMRi Q60823. Positions 1-480.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 198057. 2 interactions.
    IntActi Q60823. 6 interactions.
    MINTi MINT-1770302.

    Chemistry

    ChEMBLi CHEMBL5382.

    PTM databases

    PhosphoSitei Q60823.

    Proteomic databases

    MaxQBi Q60823.
    PaxDbi Q60823.
    PRIDEi Q60823.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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.

    Organism-specific databases

    CTDi 208.
    MGIi MGI:104874. Akt2.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00740000114960.
    HOGENOMi HOG000233033.
    HOVERGENi HBG108317.
    InParanoidi Q60823.
    KOi K04456.
    OMAi ATGMYYA.
    OrthoDBi EOG7Q5HCW.
    PhylomeDBi Q60823.
    TreeFami TF102004.

    Enzyme and pathway databases

    BRENDAi 2.7.11.1. 3474.
    Reactomei REACT_199054. Translocation of GLUT4 to the plasma membrane.
    REACT_219771. deactivation of the beta-catenin transactivating complex.

    Miscellaneous databases

    NextBioi 279261.
    PROi Q60823.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q60823.
    Bgeei Q60823.
    CleanExi MM_AKT2.
    Genevestigatori Q60823.

    Family and domain databases

    Gene3Di 2.30.29.30. 1 hit.
    InterProi IPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    IPR002290. Ser/Thr_dual-sp_kinase_dom.
    IPR008271. Ser/Thr_kinase_AS.
    [Graphical view ]
    Pfami PF00169. PH. 1 hit.
    PF00069. Pkinase. 1 hit.
    PF00433. Pkinase_C. 1 hit.
    [Graphical view ]
    SMARTi SM00233. PH. 1 hit.
    SM00133. S_TK_X. 1 hit.
    SM00220. S_TKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, chromosomal localization and expression analysis of the mouse Akt2 oncogene."
      Altomare D.A., Guo K., Cheng J.Q., Sonoda G., Walsh K., Testa J.R.
      Oncogene 11:1055-1060(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6 X CBA.
      Tissue: Thymus.
    2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Retina and Salivary gland.
    3. "Akt2-mediated phosphorylation of Pitx2 controls Ccnd1 mRNA decay during muscle cell differentiation."
      Gherzi R., Trabucchi M., Ponassi M., Gallouzi I.E., Rosenfeld M.G., Briata P.
      Cell Death Differ. 17:975-983(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF PTIX2.
    4. "C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
      Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
      Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PHOSPHORYLATION OF C2CD5.
    5. Cited for: REVIEW ON FUNCTION.
    6. "Akt1 and Akt2: differentiating the aktion."
      Heron-Milhavet L., Khouya N., Fernandez A., Lamb N.J.
      Histol. Histopathol. 26:651-662(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW ON FUNCTION.

    Entry informationi

    Entry nameiAKT2_MOUSE
    AccessioniPrimary (citable) accession number: Q60823
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1996
    Last modified: October 1, 2014
    This is version 132 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3