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Protein

RAC-gamma serine/threonine-protein kinase

Gene

AKT3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

AKT3 is one of 3 closely related serine/threonine-protein kinases (AKT1, AKT2 and AKT3) called the AKT kinase, 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. AKT3 is the least studied AKT isoform. It plays an important role in brain development and is crucial for the viability of malignant glioma cells. AKT3 isoform may also be the key molecule in up-regulation and down-regulation of MMP13 via IL13. Required for the coordination of mitochondrial biogenesis with growth factor-induced increases in cellular energy demands. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis.2 Publications

Catalytic activityi

ATP + a protein = ADP + a phosphoprotein.

Enzyme regulationi

Two specific sites, one in the kinase domain (Thr-305) and the other in the C-terminal regulatory region (Ser-472), need to be phosphorylated for its full activation (By similarity). IGF-1 leads to the activation of AKT3, which may play a role in regulating cell survival.By similarity

Kineticsi

  1. KM=87.9 µM for ATP (for purified and in vitro activated AKT3)1 Publication
  2. KM=12.4 µM for peptide substrate (for purified and in vitro activated AKT3)1 Publication
  3. KM=118.7 µM for ATP (for recombinant myristoylated AKT3 expressed and immunoprecipitated from Rat-1 cells)1 Publication
  4. KM=2.3 µM for peptide substrate (for recombinant myristoylated AKT3 expressed and immunoprecipitated from Rat-1 cells)1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei177 – 1771ATPPROSITE-ProRule annotation
    Active sitei271 – 2711Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi154 – 1629ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    • ATP binding Source: UniProtKB
    • protein kinase activity Source: ProtInc
    • protein serine/threonine kinase activity Source: UniProtKB

    GO - Biological processi

    • intracellular signal transduction Source: GO_Central
    • mitochondrial genome maintenance Source: UniProtKB
    • peptidyl-serine phosphorylation Source: GO_Central
    • protein phosphorylation Source: ProtInc
    • signal transduction Source: UniProtKB
    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Serine/threonine-protein kinase, Transferase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
    R-HSA-114604. GPVI-mediated activation cascade.
    R-HSA-1257604. PIP3 activates AKT signaling.
    R-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
    R-HSA-198323. AKT phosphorylates targets in the cytosol.
    R-HSA-198693. AKT phosphorylates targets in the nucleus.
    R-HSA-199418. Negative regulation of the PI3K/AKT network.
    R-HSA-211163. AKT-mediated inactivation of FOXO1A.
    R-HSA-389357. CD28 dependent PI3K/Akt signaling.
    R-HSA-389513. CTLA4 inhibitory signaling.
    R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
    R-HSA-5218920. VEGFR2 mediated vascular permeability.
    R-HSA-5628897. TP53 Regulates Metabolic Genes.
    R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
    R-HSA-6804757. Regulation of TP53 Degradation.
    R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
    R-HSA-6804759. Regulation of TP53 Activity through Association with Co-factors.
    SABIO-RKQ9Y243.
    SignaLinkiQ9Y243.
    SIGNORiQ9Y243.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    RAC-gamma serine/threonine-protein kinase (EC:2.7.11.1)
    Alternative name(s):
    Protein kinase Akt-3
    Protein kinase B gamma
    Short name:
    PKB gamma
    RAC-PK-gamma
    STK-2
    Gene namesi
    Name:AKT3
    Synonyms:PKBG
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    Proteomesi
    • UP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:393. AKT3.

    Subcellular locationi

    GO - Cellular componenti

    Complete GO annotation...

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    AKT3 is a key modulator of several tumors like melanoma, glioma and ovarian cancer. Active AKT3 increases progressively during melanoma tumor progression with highest levels present in advanced-stage metastatic melanomas. Promotes melanoma tumorigenesis by decreasing apoptosis. Plays a key role in the genesis of ovarian cancers through modulation of G2/M phase transition. With AKT2, plays a pivotal role in the biology of glioblastoma.

    Megalencephaly-polymicrogyria-polydactyly-hydrocephalus syndrome 2 (MPPH2)4 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA syndrome characterized by megalencephaly, hydrocephalus, and polymicrogyria; polydactyly may also be seen. There is considerable phenotypic similarity between this disorder and the megalencephaly-capillary malformation syndrome.
    See also OMIM:615937
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171E → K in MPPH2 and melanoma; results in activation of AKT. 3 Publications
    Corresponds to variant rs397514606 [ dbSNP | Ensembl ].
    VAR_065830
    Natural varianti229 – 2291N → S in MPPH2. 2 Publications
    Corresponds to variant rs397514605 [ dbSNP | Ensembl ].
    VAR_069260
    Natural varianti465 – 4651R → W in MPPH2; disease phenotype overlaps with megalencephaly-capillary malformation syndrome. 1 Publication
    Corresponds to variant rs587776935 [ dbSNP | Ensembl ].
    VAR_069261

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi305 – 3051T → A: No activation after pervanadate treatment. 1 Publication
    Mutagenesisi305 – 3051T → D: 2-fold increase of phosphorylation steady state level, no activation after pervanadate treatment. 1 Publication
    Mutagenesisi447 – 4471T → A: No effect. 1 Publication
    Mutagenesisi447 – 4471T → D: No effect. 1 Publication
    Mutagenesisi472 – 4721S → A: 67% decrease of activity after pervanadate treatment. 1 Publication
    Mutagenesisi472 – 4721S → D: 1.4-fold increase of phosphorylation steady state level, 50% decrease of activity after pervanadate treatment. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MalaCardsiAKT3.
    MIMi615937. phenotype.
    Orphaneti99802. Hemimegalencephaly.
    83473. Megalencephaly - polymicrogyria - postaxial polydactyly - hydrocephalus.
    PharmGKBiPA24686.

    Chemistry

    ChEMBLiCHEMBL2111353.
    GuidetoPHARMACOLOGYi2286.

    Polymorphism and mutation databases

    BioMutaiAKT3.
    DMDMi12643943.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methionineiRemovedCombined sources
    Chaini2 – 479478RAC-gamma serine/threonine-protein kinasePRO_0000085611Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineCombined sources
    Disulfide bondi59 ↔ 76By similarity
    Disulfide bondi293 ↔ 307By similarity
    Glycosylationi302 – 3021O-linked (GlcNAc)By similarity
    Modified residuei305 – 3051Phosphothreonine; by PDPK11 Publication
    Glycosylationi309 – 3091O-linked (GlcNAc)By similarity
    Modified residuei447 – 4471PhosphothreonineCombined sources
    Modified residuei472 – 4721Phosphoserine; by PKC/PRKCZ1 Publication

    Post-translational modificationi

    Phosphorylation on Thr-305 and Ser-472 is required for full activity.By similarity
    Ubiquitinated. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome.3 Publications
    O-GlcNAcylation at Thr-302 and Thr-309 inhibits activating phosphorylation at Thr-305 via disrupting the interaction between AKT and PDK1.By similarity

    Keywords - PTMi

    Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9Y243.
    PaxDbiQ9Y243.
    PeptideAtlasiQ9Y243.
    PRIDEiQ9Y243.

    PTM databases

    iPTMnetiQ9Y243.
    PhosphoSiteiQ9Y243.

    Expressioni

    Tissue specificityi

    In adult tissues, it is highly expressed in brain, lung and kidney, but weakly in heart, testis and liver. In fetal tissues, it is highly expressed in heart, liver and brain and not at all in kidney.

    Gene expression databases

    BgeeiENSG00000117020.
    CleanExiHS_AKT3.
    ExpressionAtlasiQ9Y243. baseline and differential.
    GenevisibleiQ9Y243. HS.

    Organism-specific databases

    HPAiCAB013090.
    HPA026441.

    Interactioni

    Subunit structurei

    Interacts (via PH domain) with TCL1A; this enhances AKT3 phosphorylation and activation. Interacts with TRAF6. Interacts with KCTD20 (By similarity). Interacts with BTBD10 (By similarity).By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CASP3P425742EBI-296115,EBI-524064
    CDC37Q165432EBI-296115,EBI-295634

    Protein-protein interaction databases

    BioGridi115318. 26 interactions.
    DIPiDIP-32584N.
    IntActiQ9Y243. 7 interactions.
    MINTiMINT-222821.
    STRINGi9606.ENSP00000263826.

    Chemistry

    BindingDBiQ9Y243.

    Structurei

    Secondary structure

    1
    479
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi6 – 1510Combined sources
    Beta strandi17 – 3014Combined sources
    Beta strandi33 – 419Combined sources
    Helixi44 – 463Combined sources
    Beta strandi51 – 555Combined sources
    Beta strandi60 – 645Combined sources
    Beta strandi66 – 683Combined sources
    Beta strandi71 – 755Combined sources
    Turni80 – 823Combined sources
    Beta strandi84 – 885Combined sources
    Helixi92 – 11322Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X18X-ray1.46A/B/C/D/E/F/G/H1-118[»]
    ProteinModelPortaliQ9Y243.
    SMRiQ9Y243. Positions 3-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini5 – 107103PHPROSITE-ProRule annotationAdd
    BLAST
    Domaini148 – 405258Protein kinasePROSITE-ProRule annotationAdd
    BLAST
    Domaini406 – 47974AGC-kinase C-terminalAdd
    BLAST

    Domaini

    Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PI3K) results in its targeting to the plasma membrane.

    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

    eggNOGiKOG0598. Eukaryota.
    ENOG410XNPH. LUCA.
    GeneTreeiENSGT00820000126961.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9Y243.
    KOiK04456.
    OMAiREYIKNW.
    OrthoDBiEOG091G06FF.
    PhylomeDBiQ9Y243.
    TreeFamiTF102004.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR011993. PH_dom-like.
    IPR001849. PH_domain.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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]
    SUPFAMiSSF50729. SSF50729. 1 hit.
    SSF56112. 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]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: Q9Y243-1) [UniParc]FASTAAdd to basket
    Also known as: PKB gamma

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

            10         20         30         40         50
    MSDVTIVKEG WVQKRGEYIK NWRPRYFLLK TDGSFIGYKE KPQDVDLPYP
    60 70 80 90 100
    LNNFSVAKCQ LMKTERPKPN TFIIRCLQWT TVIERTFHVD TPEEREEWTE
    110 120 130 140 150
    AIQAVADRLQ RQEEERMNCS PTSQIDNIGE EEMDASTTHH KRKTMNDFDY
    160 170 180 190 200
    LKLLGKGTFG KVILVREKAS GKYYAMKILK KEVIIAKDEV AHTLTESRVL
    210 220 230 240 250
    KNTRHPFLTS LKYSFQTKDR LCFVMEYVNG GELFFHLSRE RVFSEDRTRF
    260 270 280 290 300
    YGAEIVSALD YLHSGKIVYR DLKLENLMLD KDGHIKITDF GLCKEGITDA
    310 320 330 340 350
    ATMKTFCGTP EYLAPEVLED NDYGRAVDWW GLGVVMYEMM CGRLPFYNQD
    360 370 380 390 400
    HEKLFELILM EDIKFPRTLS SDAKSLLSGL LIKDPNKRLG GGPDDAKEIM
    410 420 430 440 450
    RHSFFSGVNW QDVYDKKLVP PFKPQVTSET DTRYFDEEFT AQTITITPPE
    460 470
    KYDEDGMDCM DNERRPHFPQ FSYSASGRE
    Length:479
    Mass (Da):55,775
    Last modified:November 1, 1999 - v1
    Checksum:iF08BDDE6502E78FB
    GO
    Isoform 2 (identifier: Q9Y243-2) [UniParc]FASTAAdd to basket
    Also known as: PKB gamma 1

    The sequence of this isoform differs from the canonical sequence as follows:
         452-479: YDEDGMDCMDNERRPHFPQFSYSASGRE → CQQSDCGMLGNWKK

    Show »
    Length:465
    Mass (Da):54,032
    Checksum:i592EF88B6937D1E0
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti279 – 2791L → R in AAI21155 (PubMed:15489334).Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti17 – 171E → K in MPPH2 and melanoma; results in activation of AKT. 3 Publications
    Corresponds to variant rs397514606 [ dbSNP | Ensembl ].
    VAR_065830
    Natural varianti171 – 1711G → R in a glioblastoma multiforme sample; somatic mutation. 1 Publication
    VAR_040358
    Natural varianti229 – 2291N → S in MPPH2. 2 Publications
    Corresponds to variant rs397514605 [ dbSNP | Ensembl ].
    VAR_069260
    Natural varianti465 – 4651R → W in MPPH2; disease phenotype overlaps with megalencephaly-capillary malformation syndrome. 1 Publication
    Corresponds to variant rs587776935 [ dbSNP | Ensembl ].
    VAR_069261

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei452 – 47928YDEDG…ASGRE → CQQSDCGMLGNWKK in isoform 2. 3 PublicationsVSP_004947Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF124141 mRNA. Translation: AAD29089.1.
    AF135794 mRNA. Translation: AAD24196.1.
    AF085234 mRNA. Translation: AAL40392.1.
    AJ245709 mRNA. Translation: CAB53537.1.
    AL117525 mRNA. Translation: CAB55977.1. Different termination.
    AY005799 mRNA. Translation: AAF91073.1.
    AL591721
    , AC096539, AL592151, AL662889 Genomic DNA. Translation: CAH71866.1.
    AL591721
    , AC096539, AL592151, AL662889 Genomic DNA. Translation: CAH71867.1.
    AL592151
    , AC096539, AL591721, AL662889 Genomic DNA. Translation: CAH72891.1.
    AL592151
    , AC096539, AL591721, AL662889 Genomic DNA. Translation: CAH72892.1.
    AL662889
    , AC096539, AL591721, AL592151 Genomic DNA. Translation: CAH73072.1.
    AL662889
    , AC096539, AL591721, AL592151 Genomic DNA. Translation: CAH73073.1.
    CH471148 Genomic DNA. Translation: EAW77093.1.
    CH471148 Genomic DNA. Translation: EAW77094.1.
    BC121154 mRNA. Translation: AAI21155.1.
    CCDSiCCDS31076.1. [Q9Y243-2]
    CCDS31077.1. [Q9Y243-1]
    PIRiA59380.
    T17287.
    RefSeqiNP_001193658.1. NM_001206729.1. [Q9Y243-2]
    NP_005456.1. NM_005465.4. [Q9Y243-1]
    NP_859029.1. NM_181690.2. [Q9Y243-2]
    XP_005273051.1. XM_005272994.4. [Q9Y243-1]
    XP_005273052.1. XM_005272995.2. [Q9Y243-1]
    UniGeneiHs.498292.

    Genome annotation databases

    EnsembliENST00000263826; ENSP00000263826; ENSG00000117020. [Q9Y243-1]
    ENST00000336199; ENSP00000336943; ENSG00000117020. [Q9Y243-2]
    ENST00000366539; ENSP00000355497; ENSG00000117020. [Q9Y243-1]
    ENST00000366540; ENSP00000355498; ENSG00000117020. [Q9Y243-2]
    ENST00000613395; ENSP00000479922; ENSG00000275199. [Q9Y243-2]
    ENST00000619536; ENSP00000483054; ENSG00000275199. [Q9Y243-2]
    ENST00000621586; ENSP00000479081; ENSG00000275199. [Q9Y243-1]
    GeneIDi10000.
    KEGGihsa:10000.
    UCSCiuc001hzz.2. human. [Q9Y243-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AF124141 mRNA. Translation: AAD29089.1.
    AF135794 mRNA. Translation: AAD24196.1.
    AF085234 mRNA. Translation: AAL40392.1.
    AJ245709 mRNA. Translation: CAB53537.1.
    AL117525 mRNA. Translation: CAB55977.1. Different termination.
    AY005799 mRNA. Translation: AAF91073.1.
    AL591721
    , AC096539, AL592151, AL662889 Genomic DNA. Translation: CAH71866.1.
    AL591721
    , AC096539, AL592151, AL662889 Genomic DNA. Translation: CAH71867.1.
    AL592151
    , AC096539, AL591721, AL662889 Genomic DNA. Translation: CAH72891.1.
    AL592151
    , AC096539, AL591721, AL662889 Genomic DNA. Translation: CAH72892.1.
    AL662889
    , AC096539, AL591721, AL592151 Genomic DNA. Translation: CAH73072.1.
    AL662889
    , AC096539, AL591721, AL592151 Genomic DNA. Translation: CAH73073.1.
    CH471148 Genomic DNA. Translation: EAW77093.1.
    CH471148 Genomic DNA. Translation: EAW77094.1.
    BC121154 mRNA. Translation: AAI21155.1.
    CCDSiCCDS31076.1. [Q9Y243-2]
    CCDS31077.1. [Q9Y243-1]
    PIRiA59380.
    T17287.
    RefSeqiNP_001193658.1. NM_001206729.1. [Q9Y243-2]
    NP_005456.1. NM_005465.4. [Q9Y243-1]
    NP_859029.1. NM_181690.2. [Q9Y243-2]
    XP_005273051.1. XM_005272994.4. [Q9Y243-1]
    XP_005273052.1. XM_005272995.2. [Q9Y243-1]
    UniGeneiHs.498292.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X18X-ray1.46A/B/C/D/E/F/G/H1-118[»]
    ProteinModelPortaliQ9Y243.
    SMRiQ9Y243. Positions 3-476.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi115318. 26 interactions.
    DIPiDIP-32584N.
    IntActiQ9Y243. 7 interactions.
    MINTiMINT-222821.
    STRINGi9606.ENSP00000263826.

    Chemistry

    BindingDBiQ9Y243.
    ChEMBLiCHEMBL2111353.
    GuidetoPHARMACOLOGYi2286.

    PTM databases

    iPTMnetiQ9Y243.
    PhosphoSiteiQ9Y243.

    Polymorphism and mutation databases

    BioMutaiAKT3.
    DMDMi12643943.

    Proteomic databases

    MaxQBiQ9Y243.
    PaxDbiQ9Y243.
    PeptideAtlasiQ9Y243.
    PRIDEiQ9Y243.

    Protocols and materials databases

    DNASUi10000.
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000263826; ENSP00000263826; ENSG00000117020. [Q9Y243-1]
    ENST00000336199; ENSP00000336943; ENSG00000117020. [Q9Y243-2]
    ENST00000366539; ENSP00000355497; ENSG00000117020. [Q9Y243-1]
    ENST00000366540; ENSP00000355498; ENSG00000117020. [Q9Y243-2]
    ENST00000613395; ENSP00000479922; ENSG00000275199. [Q9Y243-2]
    ENST00000619536; ENSP00000483054; ENSG00000275199. [Q9Y243-2]
    ENST00000621586; ENSP00000479081; ENSG00000275199. [Q9Y243-1]
    GeneIDi10000.
    KEGGihsa:10000.
    UCSCiuc001hzz.2. human. [Q9Y243-1]

    Organism-specific databases

    CTDi10000.
    GeneCardsiAKT3.
    HGNCiHGNC:393. AKT3.
    HPAiCAB013090.
    HPA026441.
    MalaCardsiAKT3.
    MIMi611223. gene.
    615937. phenotype.
    neXtProtiNX_Q9Y243.
    Orphaneti99802. Hemimegalencephaly.
    83473. Megalencephaly - polymicrogyria - postaxial polydactyly - hydrocephalus.
    PharmGKBiPA24686.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiKOG0598. Eukaryota.
    ENOG410XNPH. LUCA.
    GeneTreeiENSGT00820000126961.
    HOGENOMiHOG000233033.
    HOVERGENiHBG108317.
    InParanoidiQ9Y243.
    KOiK04456.
    OMAiREYIKNW.
    OrthoDBiEOG091G06FF.
    PhylomeDBiQ9Y243.
    TreeFamiTF102004.

    Enzyme and pathway databases

    BRENDAi2.7.11.1. 2681.
    ReactomeiR-HSA-111447. Activation of BAD and translocation to mitochondria.
    R-HSA-114604. GPVI-mediated activation cascade.
    R-HSA-1257604. PIP3 activates AKT signaling.
    R-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
    R-HSA-198323. AKT phosphorylates targets in the cytosol.
    R-HSA-198693. AKT phosphorylates targets in the nucleus.
    R-HSA-199418. Negative regulation of the PI3K/AKT network.
    R-HSA-211163. AKT-mediated inactivation of FOXO1A.
    R-HSA-389357. CD28 dependent PI3K/Akt signaling.
    R-HSA-389513. CTLA4 inhibitory signaling.
    R-HSA-392451. G beta:gamma signalling through PI3Kgamma.
    R-HSA-5218920. VEGFR2 mediated vascular permeability.
    R-HSA-5628897. TP53 Regulates Metabolic Genes.
    R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
    R-HSA-6804757. Regulation of TP53 Degradation.
    R-HSA-6804758. Regulation of TP53 Activity through Acetylation.
    R-HSA-6804759. Regulation of TP53 Activity through Association with Co-factors.
    SABIO-RKQ9Y243.
    SignaLinkiQ9Y243.
    SIGNORiQ9Y243.

    Miscellaneous databases

    ChiTaRSiAKT3. human.
    GeneWikiiAKT3.
    GenomeRNAii10000.
    PROiQ9Y243.
    SOURCEiSearch...

    Gene expression databases

    BgeeiENSG00000117020.
    CleanExiHS_AKT3.
    ExpressionAtlasiQ9Y243. baseline and differential.
    GenevisibleiQ9Y243. HS.

    Family and domain databases

    Gene3Di2.30.29.30. 1 hit.
    InterProiIPR000961. AGC-kinase_C.
    IPR011009. Kinase-like_dom.
    IPR011993. PH_dom-like.
    IPR001849. PH_domain.
    IPR017892. Pkinase_C.
    IPR000719. Prot_kinase_dom.
    IPR017441. Protein_kinase_ATP_BS.
    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]
    SUPFAMiSSF50729. SSF50729. 1 hit.
    SSF56112. 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]
    ProtoNetiSearch...

    Entry informationi

    Entry nameiAKT3_HUMAN
    AccessioniPrimary (citable) accession number: Q9Y243
    Secondary accession number(s): Q0VAA6
    , Q5VTI1, Q5VTI2, Q96QV3, Q9UFP5
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: September 7, 2016
    This is version 177 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    7. SIMILARITY comments
      Index of protein domains and families

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.