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Entry version 226 (23 Feb 2022)
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'.

Miscellaneous

4-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol corresponds to compound 32.1 Publication

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%5Fsection">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%5Fsection">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%5Fsection">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 sitei2004-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol; inhibitorCombined sources1 Publication1
Binding sitei2324-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol; inhibitor; via amide nitrogenCombined sources1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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
Binding sitei2824-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol; inhibitorCombined sources1 Publication1
Metal bindingi293Manganese1 Publication1
Binding sitei2934-[2-(4-amino-2,5-dihydro-1,2,5-oxadiazol-3-yl)-6-{[(1S)-3-amino-1-phenylpropyl]oxy}-1-ethyl-1H-imidazo[4,5-c]pyridin-4-yl]-2-methylbut-3-yn-2-ol; inhibitorCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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

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 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

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BRENDAi
2.7.11.1, 2681

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P31751

Reactome - a knowledgebase of biological pathways and processes

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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-9607240, FLT3 Signaling
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

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SABIO-RKi
P31751

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

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SignaLinki
P31751

SIGNOR Signaling Network Open Resource

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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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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%5Fmanual">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

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HGNCi
HGNC:392, AKT2

Online Mendelian Inheritance in Man (OMIM)

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MIMi
164731, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P31751

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000105221

<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

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 variants 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 variants 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%5Fand%5Fbiotech%5Fsection">'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 variant, Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
208

MalaCards human disease database

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MalaCardsi
AKT2
MIMi125853, phenotype
240900, phenotype

Open Targets

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OpenTargetsi
ENSG00000105221

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

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

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA24685

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P31751, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL2431

Drug and drug target database

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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
DB07812, N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide

DrugCentral

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DrugCentrali
P31751

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1480

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
AKT2

Domain mapping of disease mutations (DMDM)

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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 or proteolytic cleavage.<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%5Fprocessing%5Fsection">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%5Fprocessing%5Fsection">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

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CPTACi
CPTAC-788
CPTAC-789

Encyclopedia of Proteome Dynamics

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EPDi
P31751

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P31751

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P31751

MaxQB - The MaxQuant DataBase

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MaxQBi
P31751

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

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PaxDbi
P31751

PeptideAtlas

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PeptideAtlasi
P31751

PRoteomics IDEntifications database

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PRIDEi
P31751

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
54801 [P31751-1]
58804

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
P31751, 5 sites, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P31751

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

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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

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Bgeei
ENSG00000105221, Expressed in right hemisphere of cerebellum and 222 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P31751, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P31751, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000105221, Low tissue specificity

<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%5Fsection">'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%5Fsection">'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%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
106711, 96 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, 45 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

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
P31751, protein

<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

Biological Magnetic Resonance Data Bank

More...
BMRBi
P31751

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

More...
SMRi
P31751

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
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%5Fand%5Fdomains%5Fsection">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-terminalPROSITE-ProRule annotationAdd BLAST72

<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

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0690, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000157189

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P31751

Database of Orthologous Groups

More...
OrthoDBi
442523at2759

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

Intrinsically Disordered proteins with Extensive Annotations and Literature

More...
IDEALi
IID00037

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%5Flength">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 23 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 <p><strong>What is the canonical sequence?</strong><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.

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 23 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
396Annotation 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>
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>
E7EVP8E7EVP8_HUMAN
RAC-beta serine/threonine-protein k...
AKT2
134Annotation 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>
J3KRI8J3KRI8_HUMAN
RAC-beta serine/threonine-protein k...
AKT2
130Annotation 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>
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
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

Matched Annotation from NCBI and EMBL-EBI (MANE) - Phase one

More...
MANE-Selecti
ENST00000392038.7; ENSP00000375892.2; NM_001626.6; NP_001617.1

UCSC genome browser

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

Keywords - Coding sequence diversityi

Alternative splicing

<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%5Freferences%5Fsection">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[»]
BMRBiP31751
SMRiP31751
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi106711, 96 interactors
CORUMiP31751
DIPiDIP-32583N
ELMiP31751
IntActiP31751, 45 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
DB07812, N-[(1S)-2-amino-1-phenylethyl]-5-(1H-pyrrolo[2,3-b]pyridin-4-yl)thiophene-2-carboxamide
DrugCentraliP31751
GuidetoPHARMACOLOGYi1480

PTM databases

GlyGeniP31751, 5 sites, 1 O-linked glycan (1 site)
iPTMnetiP31751
PhosphoSitePlusiP31751

Genetic variation databases

BioMutaiAKT2
DMDMi1170703

Proteomic databases

CPTACiCPTAC-788
CPTAC-789
EPDiP31751
jPOSTiP31751
MassIVEiP31751
MaxQBiP31751
PaxDbiP31751
PeptideAtlasiP31751
PRIDEiP31751
ProteomicsDBi54801 [P31751-1]
58804

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3775, 1619 antibodies from 50 providers

The CPTC Antibody Portal

More...
CPTCi
P31751, 6 antibodies

The DNASU plasmid repository

More...
DNASUi
208

Genome annotation databases

EnsembliENST00000311278; ENSP00000309428; ENSG00000105221 [P31751-2]
ENST00000392038; ENSP00000375892; ENSG00000105221
ENST00000424901; ENSP00000399532; ENSG00000105221 [P31751-2]
GeneIDi208
KEGGihsa:208
MANE-SelectiENST00000392038.7; ENSP00000375892.2; NM_001626.6; NP_001617.1
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
HPAiENSG00000105221, Low tissue specificity
MalaCardsiAKT2
MIMi125853, phenotype
164731, gene
240900, phenotype
neXtProtiNX_P31751
OpenTargetsiENSG00000105221
Orphaneti79085, AKT2-related familial partial lipodystrophy
293964, Hypoinsulinemic hypoglycemia and body hemihypertrophy
PharmGKBiPA24685
VEuPathDBiHostDB:ENSG00000105221

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0690, Eukaryota
GeneTreeiENSGT00940000157189
InParanoidiP31751
OrthoDBi442523at2759
PhylomeDBiP31751
TreeFamiTF102004

Enzyme and pathway databases

BRENDAi2.7.11.1, 2681
PathwayCommonsiP31751
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-9607240, FLT3 Signaling
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

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
208, 30 hits in 1080 CRISPR screens

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

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ChiTaRSi
AKT2, human
EvolutionaryTraceiP31751

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
AKT2

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

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GenomeRNAii
208
PharosiP31751, Tchem

Protein Ontology

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PROi
PR:P31751
RNActiP31751, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
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Gene expression databases

BgeeiENSG00000105221, Expressed in right hemisphere of cerebellum and 222 other tissues
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
IDEALiIID00037
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

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<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%5Fand%5Fisoforms">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: February 23, 2022
This is version 226 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, Reference proteome

Documents

  1. UniProtKB entry view manual
    User manual for the UniProtKB entry view
  2. Human and mouse protein kinases
    Human and mouse protein kinases: classification and index
  3. Human chromosome 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  4. Human entries with genetic variants
    List of human entries with genetic variants
  5. Human variants curated from literature reports
    Index of human variants curated from literature reports
  6. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  7. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  8. SIMILARITY comments
    Index of protein domains and families
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