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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

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

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei177ATPPROSITE-ProRule annotation1
    <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei271Proton acceptorPROSITE-ProRule annotation1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi154 – 162ATPPROSITE-ProRule annotation9

    <p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

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

    GO - Biological processi

    <p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

    Molecular functionKinase, Serine/threonine-protein kinase, Transferase
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDA Comprehensive Enzyme Information System

    More...
    BRENDAi
    2.7.11.1 2681

    Reactome - a knowledgebase of biological pathways and processes

    More...
    Reactomei
    R-HSA-111447 Activation of BAD and translocation to mitochondria
    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
    R-HSA-69202 Cyclin E associated events during G1/S transition
    R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
    R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs
    R-HSA-8941332 RUNX2 regulates genes involved in cell migration
    R-HSA-8948751 Regulation of PTEN stability and activity

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...
    SABIO-RKi
    Q9Y243

    SignaLink: a signaling pathway resource with multi-layered regulatory networks

    More...
    SignaLinki
    Q9Y243

    SIGNOR Signaling Network Open Resource

    More...
    SIGNORi
    Q9Y243

    <p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
    Name:AKT3
    Synonyms:PKBG
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
    • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

    Organism-specific databases

    Eukaryotic Pathogen Database Resources

    More...
    EuPathDBi
    HostDB:ENSG00000117020.16

    Human Gene Nomenclature Database

    More...
    HGNCi
    HGNC:393 AKT3

    Online Mendelian Inheritance in Man (OMIM)

    More...
    MIMi
    611223 gene

    neXtProt; the human protein knowledge platform

    More...
    neXtProti
    NX_Q9Y243

    <p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

    Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    <p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

    <p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06583017E → K in MPPH2 and melanoma; results in activation of AKT. 3 PublicationsCorresponds to variant dbSNP:rs397514606EnsemblClinVar.1
    Natural variantiVAR_069260229N → S in MPPH2. 2 PublicationsCorresponds to variant dbSNP:rs397514605EnsemblClinVar.1
    Natural variantiVAR_069261465R → W in MPPH2; disease phenotype overlaps with megalencephaly-capillary malformation syndrome. 1 PublicationCorresponds to variant dbSNP:rs587776935EnsemblClinVar.1

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi305T → A: No activation after pervanadate treatment. 1 Publication1
    Mutagenesisi305T → D: 2-fold increase of phosphorylation steady state level, no activation after pervanadate treatment. 1 Publication1
    Mutagenesisi447T → A: No effect. 1 Publication1
    Mutagenesisi447T → D: No effect. 1 Publication1
    Mutagenesisi472S → A: 67% decrease of activity after pervanadate treatment. 1 Publication1
    Mutagenesisi472S → D: 1.4-fold increase of phosphorylation steady state level, 50% decrease of activity after pervanadate treatment. 1 Publication1

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    DisGeNET

    More...
    DisGeNETi
    10000

    GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

    More...
    GeneReviewsi
    AKT3

    MalaCards human disease database

    More...
    MalaCardsi
    AKT3
    MIMi615937 phenotype

    Open Targets

    More...
    OpenTargetsi
    ENSG00000117020

    Orphanet; a database dedicated to information on rare diseases and orphan drugs

    More...
    Orphaneti
    99802 Hemimegalencephaly
    83473 Megalencephaly-polymicrogyria-postaxial polydactyly-hydrocephalus syndrome

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...
    PharmGKBi
    PA24686

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...
    ChEMBLi
    CHEMBL4816

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...
    GuidetoPHARMACOLOGYi
    2286

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...
    BioMutai
    AKT3

    Domain mapping of disease mutations (DMDM)

    More...
    DMDMi
    12643943

    <p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedCombined sources
    <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000856112 – 479RAC-gamma serine/threonine-protein kinaseAdd BLAST478

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylserineCombined sources1
    <p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi59 ↔ 76By similarity
    Disulfide bondi293 ↔ 307By similarity
    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi302O-linked (GlcNAc) threonineBy similarity1
    Modified residuei305Phosphothreonine; by PDPK11 Publication1
    Glycosylationi309O-linked (GlcNAc) threonineBy similarity1
    Modified residuei447PhosphothreonineCombined sources1
    Modified residuei472Phosphoserine; by PKC/PRKCZ1 Publication1

    <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

    Encyclopedia of Proteome Dynamics

    More...
    EPDi
    Q9Y243

    jPOST - Japan Proteome Standard Repository/Database

    More...
    jPOSTi
    Q9Y243

    PaxDb, a database of protein abundance averages across all three domains of life

    More...
    PaxDbi
    Q9Y243

    PeptideAtlas

    More...
    PeptideAtlasi
    Q9Y243

    PRoteomics IDEntifications database

    More...
    PRIDEi
    Q9Y243

    ProteomicsDB human proteome resource

    More...
    ProteomicsDBi
    85641
    85642 [Q9Y243-2]

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...
    iPTMneti
    Q9Y243

    Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

    More...
    PhosphoSitePlusi
    Q9Y243

    <p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

    <p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

    Bgee dataBase for Gene Expression Evolution

    More...
    Bgeei
    ENSG00000117020 Expressed in 236 organ(s), highest expression level in neocortex

    CleanEx database of gene expression profiles

    More...
    CleanExi
    HS_AKT3

    ExpressionAtlas, Differential and Baseline Expression

    More...
    ExpressionAtlasi
    Q9Y243 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...
    Genevisiblei
    Q9Y243 HS

    Organism-specific databases

    Human Protein Atlas

    More...
    HPAi
    CAB013090
    HPA026441

    <p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

    <p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

    <p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

    Protein-protein interaction databases

    The Biological General Repository for Interaction Datasets (BioGrid)

    More...
    BioGridi
    115318, 30 interactors

    Database of interacting proteins

    More...
    DIPi
    DIP-32584N

    Protein interaction database and analysis system

    More...
    IntActi
    Q9Y243, 8 interactors

    Molecular INTeraction database

    More...
    MINTi
    Q9Y243

    STRING: functional protein association networks

    More...
    STRINGi
    9606.ENSP00000263826

    Chemistry databases

    BindingDB database of measured binding affinities

    More...
    BindingDBi
    Q9Y243

    <p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

    Secondary structure

    1479
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

    Select the link destinations:

    Protein Data Bank Europe

    More...
    PDBei

    Protein Data Bank RCSB

    More...
    RCSB PDBi

    Protein Data Bank Japan

    More...
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2X18X-ray1.46A/B/C/D/E/F/G/H1-118[»]

    Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

    More...
    ProteinModelPortali
    Q9Y243

    SWISS-MODEL Repository - a database of annotated 3D protein structure models

    More...
    SMRi
    Q9Y243

    Database of comparative protein structure models

    More...
    ModBasei
    Search...

    MobiDB: a database of protein disorder and mobility annotations

    More...
    MobiDBi
    Search...

    <p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini5 – 107PHPROSITE-ProRule annotationAdd BLAST103
    Domaini148 – 405Protein kinasePROSITE-ProRule annotationAdd BLAST258
    Domaini406 – 479AGC-kinase C-terminalAdd BLAST74

    <p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

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

    <p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...
    eggNOGi
    KOG0598 Eukaryota
    ENOG410XNPH LUCA

    Ensembl GeneTree

    More...
    GeneTreei
    ENSGT00940000157060

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...
    HOGENOMi
    HOG000233033

    The HOVERGEN Database of Homologous Vertebrate Genes

    More...
    HOVERGENi
    HBG108317

    InParanoid: Eukaryotic Ortholog Groups

    More...
    InParanoidi
    Q9Y243

    KEGG Orthology (KO)

    More...
    KOi
    K04456

    Identification of Orthologs from Complete Genome Data

    More...
    OMAi
    RGCQIMS

    Database of Orthologous Groups

    More...
    OrthoDBi
    787710at2759

    Database for complete collections of gene phylogenies

    More...
    PhylomeDBi
    Q9Y243

    TreeFam database of animal gene trees

    More...
    TreeFami
    TF102004

    Family and domain databases

    Conserved Domains Database

    More...
    CDDi
    cd01241 PH_PKB, 1 hit
    cd05593 STKc_PKB_gamma, 1 hit

    Gene3D Structural and Functional Annotation of Protein Families

    More...
    Gene3Di
    2.30.29.30, 1 hit

    Integrated resource of protein families, domains and functional sites

    More...
    InterProi
    View protein in InterPro
    IPR000961 AGC-kinase_C
    IPR034675 Akt3
    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
    IPR039029 RAC_gamma-like
    IPR008271 Ser/Thr_kinase_AS

    The PANTHER Classification System

    More...
    PANTHERi
    PTHR24356:SF190 PTHR24356:SF190, 1 hit

    Pfam protein domain database

    More...
    Pfami
    View protein in Pfam
    PF00169 PH, 1 hit
    PF00069 Pkinase, 1 hit
    PF00433 Pkinase_C, 1 hit

    Simple Modular Architecture Research Tool; a protein domain database

    More...
    SMARTi
    View protein in SMART
    SM00233 PH, 1 hit
    SM00133 S_TK_X, 1 hit
    SM00220 S_TKc, 1 hit

    Superfamily database of structural and functional annotation

    More...
    SUPFAMi
    SSF56112 SSF56112, 1 hit

    PROSITE; a protein domain and family database

    More...
    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

    <p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2+)i

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

    <p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

    This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

    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
    <p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

    <p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

    There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    Gene namesLengthAnnotation
    F8VS91F8VS91_HUMAN
    RAC-gamma serine/threonine-protein ...
    AKT3
    139Annotation score:

    Annotation score:1 out of 5

    <p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

    Experimental Info

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti279L → R in AAI21155 (PubMed:15489334).Curated1

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06583017E → K in MPPH2 and melanoma; results in activation of AKT. 3 PublicationsCorresponds to variant dbSNP:rs397514606EnsemblClinVar.1
    Natural variantiVAR_040358171G → R in a glioblastoma multiforme sample; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs1402272180Ensembl.1
    Natural variantiVAR_069260229N → S in MPPH2. 2 PublicationsCorresponds to variant dbSNP:rs397514605EnsemblClinVar.1
    Natural variantiVAR_069261465R → W in MPPH2; disease phenotype overlaps with megalencephaly-capillary malformation syndrome. 1 PublicationCorresponds to variant dbSNP:rs587776935EnsemblClinVar.1

    Alternative sequence

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_004947452 – 479YDEDG…ASGRE → CQQSDCGMLGNWKK in isoform 2. 3 PublicationsAdd BLAST28

    Sequence databases

    Select the link destinations:

    EMBL nucleotide sequence database

    More...
    EMBLi

    GenBank nucleotide sequence database

    More...
    GenBanki

    DNA Data Bank of Japan; a nucleotide sequence database

    More...
    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
    AC096539 Genomic DNA No translation available.
    AL591721 Genomic DNA No translation available.
    AL592151 Genomic DNA No translation available.
    AL662889 Genomic DNA No translation available.
    CH471148 Genomic DNA Translation: EAW77093.1
    CH471148 Genomic DNA Translation: EAW77094.1
    BC121154 mRNA Translation: AAI21155.1

    The Consensus CDS (CCDS) project

    More...
    CCDSi
    CCDS31076.1 [Q9Y243-2]
    CCDS31077.1 [Q9Y243-1]

    Protein sequence database of the Protein Information Resource

    More...
    PIRi
    A59380
    T17287

    NCBI Reference Sequences

    More...
    RefSeqi
    NP_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
    XP_005273052.1, XM_005272995.2 [Q9Y243-1]

    UniGene gene-oriented nucleotide sequence clusters

    More...
    UniGenei
    Hs.498292

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...
    Ensembli
    ENST00000263826; 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]

    Database of genes from NCBI RefSeq genomes

    More...
    GeneIDi
    10000

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...
    KEGGi
    hsa:10000

    UCSC genome browser

    More...
    UCSCi
    uc001hzz.2 human [Q9Y243-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    <p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

    <p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

    <p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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
    AC096539 Genomic DNA No translation available.
    AL591721 Genomic DNA No translation available.
    AL592151 Genomic DNA No translation available.
    AL662889 Genomic DNA No translation available.
    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
    XP_005273052.1, XM_005272995.2 [Q9Y243-1]
    UniGeneiHs.498292

    3D structure databases

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

    Protein-protein interaction databases

    BioGridi115318, 30 interactors
    DIPiDIP-32584N
    IntActiQ9Y243, 8 interactors
    MINTiQ9Y243
    STRINGi9606.ENSP00000263826

    Chemistry databases

    BindingDBiQ9Y243
    ChEMBLiCHEMBL4816
    GuidetoPHARMACOLOGYi2286

    PTM databases

    iPTMnetiQ9Y243
    PhosphoSitePlusiQ9Y243

    Polymorphism and mutation databases

    BioMutaiAKT3
    DMDMi12643943

    Proteomic databases

    EPDiQ9Y243
    jPOSTiQ9Y243
    PaxDbiQ9Y243
    PeptideAtlasiQ9Y243
    PRIDEiQ9Y243
    ProteomicsDBi85641
    85642 [Q9Y243-2]

    Protocols and materials databases

    The DNASU plasmid repository

    More...
    DNASUi
    10000
    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

    Comparative Toxicogenomics Database

    More...
    CTDi
    10000
    DisGeNETi10000
    EuPathDBiHostDB:ENSG00000117020.16

    GeneCards: human genes, protein and diseases

    More...
    GeneCardsi
    AKT3
    GeneReviewsiAKT3
    HGNCiHGNC:393 AKT3
    HPAiCAB013090
    HPA026441
    MalaCardsiAKT3
    MIMi611223 gene
    615937 phenotype
    neXtProtiNX_Q9Y243
    OpenTargetsiENSG00000117020
    Orphaneti99802 Hemimegalencephaly
    83473 Megalencephaly-polymicrogyria-postaxial polydactyly-hydrocephalus syndrome
    PharmGKBiPA24686

    GenAtlas: human gene database

    More...
    GenAtlasi
    Search...

    Phylogenomic databases

    eggNOGiKOG0598 Eukaryota
    ENOG410XNPH LUCA
    GeneTreeiENSGT00940000157060
    HOGENOMiHOG000233033
    HOVERGENiHBG108317
    InParanoidiQ9Y243
    KOiK04456
    OMAiRGCQIMS
    OrthoDBi787710at2759
    PhylomeDBiQ9Y243
    TreeFamiTF102004

    Enzyme and pathway databases

    BRENDAi2.7.11.1 2681
    ReactomeiR-HSA-111447 Activation of BAD and translocation to mitochondria
    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
    R-HSA-69202 Cyclin E associated events during G1/S transition
    R-HSA-69656 Cyclin A:Cdk2-associated events at S phase entry
    R-HSA-8876198 RAB GEFs exchange GTP for GDP on RABs
    R-HSA-8941332 RUNX2 regulates genes involved in cell migration
    R-HSA-8948751 Regulation of PTEN stability and activity
    SABIO-RKiQ9Y243
    SignaLinkiQ9Y243
    SIGNORiQ9Y243

    Miscellaneous databases

    ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

    More...
    ChiTaRSi
    AKT3 human

    The Gene Wiki collection of pages on human genes and proteins

    More...
    GeneWikii
    AKT3

    Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

    More...
    GenomeRNAii
    10000

    Protein Ontology

    More...
    PROi
    PR:Q9Y243

    The Stanford Online Universal Resource for Clones and ESTs

    More...
    SOURCEi
    Search...

    Gene expression databases

    BgeeiENSG00000117020 Expressed in 236 organ(s), highest expression level in neocortex
    CleanExiHS_AKT3
    ExpressionAtlasiQ9Y243 baseline and differential
    GenevisibleiQ9Y243 HS

    Family and domain databases

    CDDicd01241 PH_PKB, 1 hit
    cd05593 STKc_PKB_gamma, 1 hit
    Gene3Di2.30.29.30, 1 hit
    InterProiView protein in InterPro
    IPR000961 AGC-kinase_C
    IPR034675 Akt3
    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
    IPR039029 RAC_gamma-like
    IPR008271 Ser/Thr_kinase_AS
    PANTHERiPTHR24356:SF190 PTHR24356:SF190, 1 hit
    PfamiView protein in Pfam
    PF00169 PH, 1 hit
    PF00069 Pkinase, 1 hit
    PF00433 Pkinase_C, 1 hit
    SMARTiView protein in SMART
    SM00233 PH, 1 hit
    SM00133 S_TK_X, 1 hit
    SM00220 S_TKc, 1 hit
    SUPFAMiSSF56112 SSF56112, 1 hit
    PROSITEiView 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

    ProtoNet; Automatic hierarchical classification of proteins

    More...
    ProtoNeti
    Search...

    <p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

    <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAKT3_HUMAN
    <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9Y243
    Secondary accession number(s): Q0VAA6
    , Q5VTI1, Q5VTI2, Q96QV3, Q9UFP5
    <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: November 1, 1999
    Last modified: January 16, 2019
    This is version 199 of the entry and version 1 of the sequence. See complete history.
    <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

    <p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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