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UniProtKB - P31751 (AKT2_HUMAN)

Entry version 212 (31 Jul 2019)
Sequence version 2 (01 Nov 1995)
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Protein

RAC-beta serine/threonine-protein kinase

Gene

AKT2

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

AKT2 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. 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 recently 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. Down-regulation by RNA interference reduces the expression of the phosphorylated form of BAD, resulting in the induction of caspase-dependent apoptosis. Phosphorylates CLK2 on 'Thr-343'.

Caution

In light of strong homologies in the primary amino acid sequence, the 3 AKT kinases were long surmised to play redundant and overlapping roles. More recent studies has brought into question the redundancy within AKT kinase isoforms and instead pointed to isoform specific functions in different cellular events and diseases. AKT1 is more specifically involved in cellular survival pathways, by inhibiting apoptotic processes; whereas AKT2 is more specific for the insulin receptor signaling pathway. Moreover, while AKT1 and AKT2 are often implicated in many aspects of cellular transformation, the 2 isoforms act in a complementary opposing manner. The role of AKT3 is less clear, though it appears to be predominantly expressed in brain.Curated

<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 <a href="http://www.uniprot.org/help/function_section">Function</a> 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-309) and the other in the C-terminal regulatory region (Ser-474), need to be phosphorylated for its full activation. Aminofurazans are potent AKT2 inhibitors.2 Publications

<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=358.4 µM for ATP (for purified and in vitro activated AKT2)1 Publication
  2. KM=3.4 µM for peptide substrate (for purified and in vitro activated AKT2)1 Publication
  3. KM=564 µM for ATP (for recombinant myristoylated AKT2 expressed and immunoprecipitated from Rat-1 cells)1 Publication
  4. KM=2.3 µM for peptide substrate (for recombinant myristoylated AKT2 expressed and immunoprecipitated from Rat-1 cells)1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei181ATPPROSITE-ProRule annotation1
    Binding sitei181Inhibitor1
    Binding sitei200Inhibitor1
    Binding sitei232Inhibitor; via amide nitrogen1
    Binding sitei236Inhibitor1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 sitei275Proton acceptorPROSITE-ProRule annotation1
    Binding sitei279Inhibitor; via carbonyl oxygen1
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi280Manganese1 Publication1
    Metal bindingi293Manganese1 Publication1
    Binding sitei293Inhibitor1
    Binding sitei294Inhibitor; via amide nitrogen1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> 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 bindingi158 – 166ATPPROSITE-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

    Complete GO annotation on QuickGO ...

    GO - Biological processi

    Complete GO annotation on QuickGO ...

    <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 functionDevelopmental protein, Kinase, Serine/threonine-protein kinase, Transferase
    Biological processApoptosis, Carbohydrate metabolism, Glucose metabolism, Glycogen biosynthesis, Glycogen metabolism, Sugar transport, Translation regulation, Transport
    LigandATP-binding, Manganese, Metal-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-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
    R-HSA-165158 Activation of AKT2
    R-HSA-165160 PDE3B signalling
    R-HSA-165181 Inhibition of TSC complex formation by PKB
    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-3769402 Deactivation of the beta-catenin transactivating complex
    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
    R-HSA-9614399 Regulation of localization of FOXO transcription factors
    R-HSA-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling

    SABIO-RK: Biochemical Reaction Kinetics Database

    More...    SABIO-RKi    		P31751

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

    More...    SignaLinki    		P31751

    SIGNOR Signaling Network Open Resource

    More...    SIGNORi    		P31751

    <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-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
    <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:AKT2
    <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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
    <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 19

    Organism-specific databases

    Human Gene Nomenclature Database

    More...    HGNCi    		HGNC:392 AKT2

    Online Mendelian Inheritance in Man (OMIM)

    More...    MIMi    		164731 gene

    neXtProt; the human protein knowledge platform

    More...    neXtProti    		NX_P31751

    <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 & Seán O’Donoghue; Source: COMPARTMENTS

    Keywords - Cellular componenti

    Cell membrane, Cytoplasm, Endosome, 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

    Defects in AKT2 are a cause of susceptibility to breast cancer (BC). AKT2 promotes metastasis of tumor cells without affecting the latency of tumor development. With AKT3, plays also a pivotal role in the biology of glioblastoma.
    Diabetes mellitus, non-insulin-dependent (NIDDM)2 Publications
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA multifactorial disorder of glucose homeostasis caused by a lack of sensitivity to the body's own insulin. Affected individuals usually have an obese body habitus and manifestations of a metabolic syndrome characterized by diabetes, insulin resistance, hypertension and hypertriglyceridemia. The disease results in long-term complications that affect the eyes, kidneys, nerves, and blood vessels.
    Related information in OMIM
    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_067310274R → H in NIDDM; associated with typical metabolic dyslipidemia with elevated fastin triglyceride, high VLDL triglyceride/cholesterol ratios, low HDL cholesterol levels and high small dense LDL levels; de novo lipogenesis and liver fat are also significantly elevated in this subject. 1 PublicationCorresponds to variant dbSNP:rs121434593EnsemblClinVar.1
    Hypoinsulinemic hypoglycemia with hemihypertrophy (HIHGHH)1 Publication
    The disease is caused by mutations affecting the gene represented in this entry.
    Disease descriptionA disorder characterized by hypoglycemia, low insulin levels, low serum levels of ketone bodies and branched-chain amino acids, left-sided hemihypertrophy, neonatal macrosomia, reduced consciousness and hypoglycemic seizures.
    Related information in OMIM
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06730917E → K in HIHGHH; exhibits plasma membrane localization in serum-starved cells and produced inappropriate tonic nuclear exclusion of FOXO1 in preadipocytes. 1 PublicationCorresponds to variant dbSNP:rs387906659EnsemblClinVar.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>Mutagenesisi309T → A: Impairs interaction with TTC3; when associated with A-474. 2 Publications1
    Mutagenesisi309T → E: Constitutively active; when associated with D-474. 2 Publications1
    Mutagenesisi474S → A: Impairs interaction with TTC3; when associated with A-309. 2 Publications1
    Mutagenesisi474S → D: Constitutively active; when associated with E-309. 2 Publications1

    Keywords - Diseasei

    Diabetes mellitus, Disease mutation, Proto-oncogene

    Organism-specific databases

    DisGeNET

    More...    DisGeNETi    		208

    MalaCards human disease database

    More...    MalaCardsi    		AKT2
    MIMi125853 phenotype
    240900 phenotype

    Open Targets

    More...    OpenTargetsi    		ENSG00000105221

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

    More...    Orphaneti    		79085 AKT2-related familial partial lipodystrophy
    293964 Hypoinsulinemic hypoglycemia and body hemihypertrophy

    The Pharmacogenetics and Pharmacogenomics Knowledge Base

    More...    PharmGKBi    		PA24685

    Chemistry databases

    ChEMBL database of bioactive drug-like small molecules

    More...    ChEMBLi    		CHEMBL2431

    Drug and drug target database

    More...    DrugBanki    		DB08073 (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
    DB07859 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE
    DB07947 ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE

    IUPHAR/BPS Guide to PHARMACOLOGY

    More...    GuidetoPHARMACOLOGYi    		1480

    Polymorphism and mutation databases

    BioMuta curated single-nucleotide variation and disease association database

    More...    BioMutai    		AKT2

    Domain mapping of disease mutations (DMDM)

    More...    DMDMi    		1170703

    <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 ‘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_00000856081 – 481RAC-beta serine/threonine-protein kinaseAdd BLAST481

    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 residuei1N-acetylmethionineCombined sources1
    Modified residuei34PhosphoserineCombined 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 bondi60 ↔ 77By similarity
    Modified residuei126PhosphoserineCombined sources1
    <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>Glycosylationi128O-linked (GlcNAc) serineBy similarity1
    Glycosylationi131O-linked (GlcNAc) serineBy similarity1
    Disulfide bondi297 ↔ 3111 Publication
    Glycosylationi306O-linked (GlcNAc) threonineBy similarity1
    Modified residuei309Phosphothreonine; by PDPK14 Publications1
    Glycosylationi313O-linked (GlcNAc) threonineBy similarity1
    Modified residuei447PhosphoserineCombined sources1
    Modified residuei451PhosphothreonineCombined sources1
    Modified residuei474PhosphoserineCombined sources2 Publications1
    Modified residuei478PhosphoserineCombined sources1

    <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-309 and Ser-474 is required for full activity.4 Publications
    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.2 Publications
    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

    The CPTAC Assay portal

    More...    CPTACi    		CPTAC-788
    CPTAC-789

    Encyclopedia of Proteome Dynamics

    More...    EPDi    		P31751

    jPOST - Japan Proteome Standard Repository/Database

    More...    jPOSTi    		P31751

    MaxQB - The MaxQuant DataBase

    More...    MaxQBi    		P31751

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

    More...    PaxDbi    		P31751

    PeptideAtlas

    More...    PeptideAtlasi    		P31751

    PRoteomics IDEntifications database

    More...    PRIDEi    		P31751

    ProteomicsDB human proteome resource

    More...    ProteomicsDBi    		54801 [P31751-1]
    58804

    PTM databases

    iPTMnet integrated resource for PTMs in systems biology context

    More...    iPTMneti    		P31751

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

    More...    PhosphoSitePlusi    		P31751

    <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

    Expressed in all cell types so far analyzed.

    Gene expression databases

    Bgee dataBase for Gene Expression Evolution

    More...    Bgeei    		ENSG00000105221 Expressed in 207 organ(s), highest expression level in right hemisphere of cerebellum

    ExpressionAtlas, Differential and Baseline Expression

    More...    ExpressionAtlasi    		P31751 baseline and differential

    Genevisible search portal to normalized and curated expression data from Genevestigator

    More...    Genevisiblei    		P31751 HS

    Organism-specific databases

    Human Protein Atlas

    More...    HPAi    		CAB004204
    HPA064521

    <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 with BTBD10 (By similarity).

    Interacts with KCTD20 (By similarity).

    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 (PubMed:19139280).

    Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529).

    By similarity7 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    		106711, 75 interactors

    CORUM comprehensive resource of mammalian protein complexes

    More...    CORUMi    		P31751

    Database of interacting proteins

    More...    DIPi    		DIP-32583N

    The Eukaryotic Linear Motif resource for Functional Sites in Proteins

    More...    ELMi    		P31751

    Protein interaction database and analysis system

    More...    IntActi    		P31751, 33 interactors

    Molecular INTeraction database

    More...    MINTi    		P31751

    STRING: functional protein association networks

    More...    STRINGi    		9606.ENSP00000375892

    Chemistry databases

    BindingDB database of measured binding affinities

    More...    BindingDBi    		P31751

    <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

    1481
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details

    3D structure databases

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

    More...    SMRi    		P31751

    Database of comparative protein structure models

    More...    ModBasei    		Search...

    Miscellaneous databases

    Relative evolutionary importance of amino acids within a protein sequence

    More...    EvolutionaryTracei    		P31751

    <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 – 108PHPROSITE-ProRule annotationAdd BLAST104
    Domaini152 – 409Protein kinasePROSITE-ProRule annotationAdd BLAST258
    Domaini410 – 481AGC-kinase C-terminalAdd BLAST72

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni230 – 232Inhibitor binding3
    Regioni277 – 279Inhibitor binding3
    Regioni292 – 293Inhibitor binding2

    <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 phosphatidylinositol 3,4,5-trisphosphate (PI(3,4,5)P3) following phosphatidylinositol 3-kinase alpha (PIK3CA) activity 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

    Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. RAC subfamily.Curated

    Phylogenomic databases

    evolutionary genealogy of genes: Non-supervised Orthologous Groups

    More...    eggNOGi    		KOG0598 Eukaryota
    ENOG410XNPH LUCA

    Ensembl GeneTree

    More...    GeneTreei    		ENSGT00940000157189

    The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

    More...    HOGENOMi    		HOG000233033

    InParanoid: Eukaryotic Ortholog Groups

    More...    InParanoidi    		P31751

    KEGG Orthology (KO)

    More...    KOi    		K04456

    Database of Orthologous Groups

    More...    OrthoDBi    		614710at2759

    Database for complete collections of gene phylogenies

    More...    PhylomeDBi    		P31751

    TreeFam database of animal gene trees

    More...    TreeFami    		TF102004

    Family and domain databases

    Conserved Domains Database

    More...    CDDi    		cd01241 PH_PKB, 1 hit
    cd05595 STKc_PKB_beta, 1 hit

    Database of protein disorder

    More...    DisProti    		DP00304

    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
    IPR034677 Akt2
    IPR011009 Kinase-like_dom_sf
    IPR011993 PH-like_dom_sf
    IPR001849 PH_domain
    IPR039026 PH_PKB
    IPR017892 Pkinase_C
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    IPR008271 Ser/Thr_kinase_AS

    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>. The information is filed in different subsections. The current subsections and their content are listed below:<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.

    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 22 potential isoforms that are computationally mapped.Show allAlign All

    Isoform 1 (identifier: P31751-1) [UniParc]FASTAAdd to basket

    This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
    MNEVSVIKEG WLHKRGEYIK TWRPRYFLLK SDGSFIGYKE RPEAPDQTLP 
            60         70         80         90        100
    PLNNFSVAEC QLMKTERPRP NTFVIRCLQW TTVIERTFHV DSPDEREEWM 
           110        120        130        140        150
    RAIQMVANSL KQRAPGEDPM DYKCGSPSDS STTEEMEVAV SKARAKVTMN 
           160        170        180        190        200
    DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE 
           210        220        230        240        250
    SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTEE 
           260        270        280        290        300
    RARFYGAEIV SALEYLHSRD VVYRDIKLEN LMLDKDGHIK ITDFGLCKEG 
           310        320        330        340        350
    ISDGATMKTF CGTPEYLAPE VLEDNDYGRA VDWWGLGVVM YEMMCGRLPF 
           360        370        380        390        400
    YNQDHERLFE LILMEEIRFP RTLSPEAKSL LAGLLKKDPK QRLGGGPSDA 
           410        420        430        440        450
    KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI 
           460        470        480 
    TPPDRYDSLG LLELDQRTHF PQFSYSASIR E
    Length:481
    Mass (Da):55,769
    Last modified:November 1, 1995 - v2
    <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:iB18C87A7246BFB24
    GO
    Isoform 2 (identifier: P31751-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         278-320: Missing.

    Note: No experimental confirmation available.
    Show »
    Length:438
    Mass (Da):51,083
    Checksum:iEEAF3B6E42F6A5C1
    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 are 22 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
    EntryEntry nameProtein names
    		Gene namesLengthAnnotation
    M0R0P9M0R0P9_HUMAN
    Non-specific serine/threonine prote...
    AKT2
    		450Annotation score:

    Annotation score:3 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>
    C9JHS6C9JHS6_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		184Annotation score:

    Annotation score:2 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>
    J3QLS6J3QLS6_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		157Annotation score:

    Annotation score:2 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>
    M0QZK3M0QZK3_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		151Annotation score:

    Annotation score:2 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>
    J3QKW1J3QKW1_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		292Annotation 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>
    M0R283M0R283_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		117Annotation 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>
    M0R275M0R275_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		129Annotation 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>
    J3QL45J3QL45_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		106Annotation 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>
    J3KT31J3KT31_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		69Annotation 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>
    A8MX96A8MX96_HUMAN
    RAC-beta serine/threonine-protein k...
    AKT2
    		133Annotation 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>
    There are more potential isoformsShow all

    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 conflicti478 – 481SIRE → FREEKDLLMSLFVSLILFSD FSSLKSHSFSSNFILLSFSS LKK in AAA36585 (PubMed:1801921).Curated4

    Natural variant

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Natural variantiVAR_06730917E → K in HIHGHH; exhibits plasma membrane localization in serum-starved cells and produced inappropriate tonic nuclear exclusion of FOXO1 in preadipocytes. 1 PublicationCorresponds to variant dbSNP:rs387906659EnsemblClinVar.1
    Natural variantiVAR_040356188I → V1 PublicationCorresponds to variant dbSNP:rs55859611Ensembl.1
    Natural variantiVAR_040357208R → K1 PublicationCorresponds to variant dbSNP:rs35817154Ensembl.1
    Natural variantiVAR_067310274R → H in NIDDM; associated with typical metabolic dyslipidemia with elevated fastin triglyceride, high VLDL triglyceride/cholesterol ratios, low HDL cholesterol levels and high small dense LDL levels; de novo lipogenesis and liver fat are also significantly elevated in this subject. 1 PublicationCorresponds to variant dbSNP:rs121434593EnsemblClinVar.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.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_056930278 – 320Missing in isoform 2. 1 PublicationAdd BLAST43

    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
    		M77198 mRNA Translation: AAA36585.1
    M95936 mRNA Translation: AAA58364.1
    AK314619 mRNA Translation: BAG37185.1
    AC118344 Genomic DNA No translation available.
    BC032709 mRNA Translation: AAH32709.1
    BC120995 mRNA Translation: AAI20996.1
    BC120994 mRNA Translation: AAI20995.1
    AY708392 Genomic DNA Translation: AAT97984.1

    The Consensus CDS (CCDS) project

    More...    CCDSi    		CCDS12552.1 [P31751-1]
    CCDS82350.1 [P31751-2]

    Protein sequence database of the Protein Information Resource

    More...    PIRi    		A46288

    NCBI Reference Sequences

    More...    RefSeqi    		NP_001317440.1, NM_001330511.1 [P31751-2]
    NP_001617.1, NM_001626.5 [P31751-1]
    XP_011524916.1, XM_011526614.1 [P31751-1]
    XP_011524917.1, XM_011526615.1 [P31751-1]
    XP_011524918.1, XM_011526616.1 [P31751-1]
    XP_011524920.1, XM_011526618.1 [P31751-1]
    XP_011524921.1, XM_011526619.1 [P31751-1]
    XP_011524922.1, XM_011526620.1 [P31751-1]
    XP_016881959.1, XM_017026470.1 [P31751-1]

    Genome annotation databases

    Ensembl eukaryotic genome annotation project

    More...    Ensembli    		ENST00000311278; ENSP00000309428; ENSG00000105221 [P31751-2]
    ENST00000392038; ENSP00000375892; ENSG00000105221 [P31751-1]
    ENST00000424901; ENSP00000399532; ENSG00000105221 [P31751-2]

    Database of genes from NCBI RefSeq genomes

    More...    GeneIDi    		208

    KEGG: Kyoto Encyclopedia of Genes and Genomes

    More...    KEGGi    		hsa:208

    UCSC genome browser

    More...    UCSCi    		uc002onf.3 human [P31751-1]

    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
    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    		M77198 mRNA Translation: AAA36585.1
    M95936 mRNA Translation: AAA58364.1
    AK314619 mRNA Translation: BAG37185.1
    AC118344 Genomic DNA No translation available.
    BC032709 mRNA Translation: AAH32709.1
    BC120995 mRNA Translation: AAI20996.1
    BC120994 mRNA Translation: AAI20995.1
    AY708392 Genomic DNA Translation: AAT97984.1
    CCDSiCCDS12552.1 [P31751-1]
    CCDS82350.1 [P31751-2]
    PIRiA46288
    RefSeqiNP_001317440.1, NM_001330511.1 [P31751-2]
    NP_001617.1, NM_001626.5 [P31751-1]
    XP_011524916.1, XM_011526614.1 [P31751-1]
    XP_011524917.1, XM_011526615.1 [P31751-1]
    XP_011524918.1, XM_011526616.1 [P31751-1]
    XP_011524920.1, XM_011526618.1 [P31751-1]
    XP_011524921.1, XM_011526619.1 [P31751-1]
    XP_011524922.1, XM_011526620.1 [P31751-1]
    XP_016881959.1, XM_017026470.1 [P31751-1]

    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
    1GZKX-ray2.30A146-460[»]
    1GZNX-ray2.50A146-480[»]
    1GZOX-ray2.75A146-460[»]
    1MRVX-ray2.80A143-481[»]
    1MRYX-ray2.80A143-481[»]
    1O6KX-ray1.70A146-481[»]
    1O6LX-ray1.60A146-467[»]
    1P6SNMR-A1-111[»]
    2JDOX-ray1.80A146-467[»]
    2JDRX-ray2.30A146-467[»]
    2UW9X-ray2.10A146-467[»]
    2X39X-ray1.93A146-467[»]
    2XH5X-ray2.72A146-479[»]
    3D0EX-ray2.00A/B146-480[»]
    3E87X-ray2.30A/B146-480[»]
    3E88X-ray2.50A/B146-480[»]
    3E8DX-ray2.70A/B146-480[»]
    SMRiP31751
    ModBaseiSearch...

    Protein-protein interaction databases

    BioGridi106711, 75 interactors
    CORUMiP31751
    DIPiDIP-32583N
    ELMiP31751
    IntActiP31751, 33 interactors
    MINTiP31751
    STRINGi9606.ENSP00000375892

    Chemistry databases

    BindingDBiP31751
    ChEMBLiCHEMBL2431
    DrugBankiDB08073 (2S)-1-(1H-INDOL-3-YL)-3-{[5-(3-METHYL-1H-INDAZOL-5-YL)PYRIDIN-3-YL]OXY}PROPAN-2-AMINE
    DB07859 4-(4-CHLOROPHENYL)-4-[4-(1H-PYRAZOL-4-YL)PHENYL]PIPERIDINE
    DB07947 ISOQUINOLINE-5-SULFONIC ACID (2-(2-(4-CHLOROBENZYLOXY)ETHYLAMINO)ETHYL)AMIDE
    GuidetoPHARMACOLOGYi1480

    PTM databases

    iPTMnetiP31751
    PhosphoSitePlusiP31751

    Polymorphism and mutation databases

    BioMutaiAKT2
    DMDMi1170703

    Proteomic databases

    CPTACiCPTAC-788
    CPTAC-789
    EPDiP31751
    jPOSTiP31751
    MaxQBiP31751
    PaxDbiP31751
    PeptideAtlasiP31751
    PRIDEiP31751
    ProteomicsDBi54801 [P31751-1]
    58804

    Protocols and materials databases

    The DNASU plasmid repository

    More...    DNASUi    		208
    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000311278; ENSP00000309428; ENSG00000105221 [P31751-2]
    ENST00000392038; ENSP00000375892; ENSG00000105221 [P31751-1]
    ENST00000424901; ENSP00000399532; ENSG00000105221 [P31751-2]
    GeneIDi208
    KEGGihsa:208
    UCSCiuc002onf.3 human [P31751-1]

    Organism-specific databases

    Comparative Toxicogenomics Database

    More...    CTDi    		208
    DisGeNETi208

    GeneCards: human genes, protein and diseases

    More...    GeneCardsi    		AKT2
    HGNCiHGNC:392 AKT2
    HPAiCAB004204
    HPA064521
    MalaCardsiAKT2
    MIMi125853 phenotype
    164731 gene
    240900 phenotype
    neXtProtiNX_P31751
    OpenTargetsiENSG00000105221
    Orphaneti79085 AKT2-related familial partial lipodystrophy
    293964 Hypoinsulinemic hypoglycemia and body hemihypertrophy
    PharmGKBiPA24685

    GenAtlas: human gene database

    More...    GenAtlasi    		Search...

    Phylogenomic databases

    eggNOGiKOG0598 Eukaryota
    ENOG410XNPH LUCA
    GeneTreeiENSGT00940000157189
    HOGENOMiHOG000233033
    InParanoidiP31751
    KOiK04456
    OrthoDBi614710at2759
    PhylomeDBiP31751
    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-1445148 Translocation of SLC2A4 (GLUT4) to the plasma membrane
    R-HSA-165158 Activation of AKT2
    R-HSA-165160 PDE3B signalling
    R-HSA-165181 Inhibition of TSC complex formation by PKB
    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-3769402 Deactivation of the beta-catenin transactivating complex
    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
    R-HSA-9614399 Regulation of localization of FOXO transcription factors
    R-HSA-9634638 Estrogen-dependent nuclear events downstream of ESR-membrane signaling
    SABIO-RKiP31751
    SignaLinkiP31751
    SIGNORiP31751

    Miscellaneous databases

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

    More...    ChiTaRSi    		AKT2 human
    EvolutionaryTraceiP31751

    The Gene Wiki collection of pages on human genes and proteins

    More...    GeneWikii    		AKT2

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

    More...    GenomeRNAii    		208

    Protein Ontology

    More...    PROi    		PR:P31751

    The Stanford Online Universal Resource for Clones and ESTs

    More...    SOURCEi    		Search...

    Gene expression databases

    BgeeiENSG00000105221 Expressed in 207 organ(s), highest expression level in right hemisphere of cerebellum
    ExpressionAtlasiP31751 baseline and differential
    GenevisibleiP31751 HS

    Family and domain databases

    CDDicd01241 PH_PKB, 1 hit
    cd05595 STKc_PKB_beta, 1 hit
    DisProtiDP00304
    Gene3Di2.30.29.30, 1 hit
    InterProiView protein in InterPro
    IPR000961 AGC-kinase_C
    IPR034677 Akt2
    IPR011009 Kinase-like_dom_sf
    IPR011993 PH-like_dom_sf
    IPR001849 PH_domain
    IPR039026 PH_PKB
    IPR017892 Pkinase_C
    IPR000719 Prot_kinase_dom
    IPR017441 Protein_kinase_ATP_BS
    IPR008271 Ser/Thr_kinase_AS
    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...

    MobiDB: a database of protein disorder and mobility annotations

    More...    MobiDBi    		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 nameiAKT2_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: P31751
    Secondary accession number(s): B2RBD8
    , Q05BV0, Q0VAN0, Q0VAN1, Q68GC0
    <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: July 1, 1993
    Last sequence update: November 1, 1995
    Last modified: July 31, 2019
    This is version 212 of the entry and version 2 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families
    3. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    UniProt is an ELIXIR core data resource
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