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Entry version 191 (07 Apr 2021)
Sequence version 1 (01 Nov 1996)
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Protein

RAC-beta serine/threonine-protein kinase

Gene

Akt2

Organism
Mus musculus (Mouse)
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 kinases, and which regulate many processes including metabolism, proliferation, cell survival, growth and angiogenesis. This is mediated through serine and/or threonine phosphorylation of a range of downstream substrates. Over 100 substrate candidates have been reported so far, but for most of them, no isoform specificity has been reported. AKT is responsible of the regulation of glucose uptake by mediating insulin-induced translocation of the SLC2A4/GLUT4 glucose transporter to the cell surface. Phosphorylation of PTPN1 at 'Ser-50' negatively modulates its phosphatase activity preventing dephosphorylation of the insulin receptor and the attenuation of insulin signaling. Phosphorylation of TBC1D4 triggers the binding of this effector to inhibitory 14-3-3 proteins, which is required for insulin-stimulated glucose transport. AKT regulates also the storage of glucose in the form of glycogen by phosphorylating GSK3A at 'Ser-21' and GSK3B at 'Ser-9', resulting in inhibition of its kinase activity. Phosphorylation of GSK3 isoforms by AKT is also thought to be one mechanism by which cell proliferation is driven. AKT regulates also cell survival via the phosphorylation of MAP3K5 (apoptosis signal-related kinase). Phosphorylation of 'Ser-83' decreases MAP3K5 kinase activity stimulated by oxidative stress and thereby prevents apoptosis. AKT mediates insulin-stimulated protein synthesis by phosphorylating TSC2 at 'Ser-939' and 'Thr-1462', thereby activating mTORC1 signaling and leading to both phosphorylation of 4E-BP1 and in activation of RPS6KB1. AKT is involved in the phosphorylation of members of the FOXO factors (Forkhead family of transcription factors), leading to binding of 14-3-3 proteins and cytoplasmic localization. In particular, FOXO1 is phosphorylated at 'Thr-24', 'Ser-256' and 'Ser-319'. FOXO3 and FOXO4 are phosphorylated on equivalent sites. AKT has an important role in the regulation of NF-kappa-B-dependent gene transcription and positively regulates the activity of CREB1 (cyclic AMP (cAMP)-response element binding protein). The phosphorylation of CREB1 induces the binding of accessory proteins that are necessary for the transcription of pro-survival genes such as BCL2 and MCL1. AKT phosphorylates 'Ser-454' on ATP citrate lyase (ACLY), thereby potentially regulating ACLY activity and fatty acid synthesis. Activates the 3B isoform of cyclic nucleotide phosphodiesterase (PDE3B) via phosphorylation of 'Ser-273', resulting in reduced cyclic AMP levels and inhibition of lipolysis. Phosphorylates PIKFYVE on 'Ser-318', which results in increased PI3P-5 activity. The Rho GTPase-activating protein DLC1 is another substrate and its phosphorylation is implicated in the regulation cell proliferation and cell growth. AKT plays a role as key modulator of the AKT-mTOR signaling pathway controlling the tempo of the process of newborn neurons integration during adult neurogenesis, including correct neuron positioning, dendritic development and synapse formation. Signals downstream of phosphatidylinositol 3-kinase (PI3K) to mediate the effects of various growth factors such as platelet-derived growth factor (PDGF), epidermal growth factor (EGF), insulin and insulin-like growth factor I (IGF-I). AKT mediates the antiapoptotic effects of IGF-I. Essential for the SPATA13-mediated regulation of cell migration and adhesion assembly and disassembly. May be involved in the regulation of the placental development.
One of the few specific substrates of AKT2 identified so far is PITX2. Phosphorylation of PITX2 impairs its association with the CCND1 mRNA-stabilizing complex thus shortening the half-life of CCND1. AKT2 seems also to be the principal isoform responsible of the regulation of glucose uptake. Phosphorylates C2CD5 on 'Ser-197' during insulin-stimulated adipocytes. AKT2 is also specifically involved in skeletal muscle differentiation, one of its substrates in this process being ANKRD2. Phosphorylates CLK2 on 'Thr-343'.

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.By similarity

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 sitei181InhibitorBy similarity1
Binding sitei200InhibitorBy similarity1
Binding sitei232Inhibitor; via amide nitrogenBy similarity1
Binding sitei236InhibitorBy similarity1
<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
Binding sitei279Inhibitor; via carbonyl oxygenBy similarity1
<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 bindingi280ManganeseBy similarity1
Metal bindingi293ManganeseBy similarity1
Binding sitei293InhibitorBy similarity1
Binding sitei294Inhibitor; via amide nitrogenBy similarity1

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

More...
BRENDAi
2.7.11.1, 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-1257604, PIP3 activates AKT signaling
R-MMU-1358803, Downregulation of ERBB2:ERBB3 signaling
R-MMU-165158, Activation of AKT2
R-MMU-165181, Inhibition of TSC complex formation by PKB
R-MMU-198323, AKT phosphorylates targets in the cytosol
R-MMU-198693, AKT phosphorylates targets in the nucleus
R-MMU-199418, Negative regulation of the PI3K/AKT network
R-MMU-211163, AKT-mediated inactivation of FOXO1A
R-MMU-3769402, Deactivation of the beta-catenin transactivating complex
R-MMU-389357, CD28 dependent PI3K/Akt signaling
R-MMU-389513, CTLA4 inhibitory signaling
R-MMU-392451, G beta:gamma signalling through PI3Kgamma
R-MMU-5218920, VEGFR2 mediated vascular permeability
R-MMU-5628897, TP53 Regulates Metabolic Genes
R-MMU-6804757, Regulation of TP53 Degradation
R-MMU-6804758, Regulation of TP53 Activity through Acetylation
R-MMU-6804759, Regulation of TP53 Activity through Association with Co-factors
R-MMU-69202, Cyclin E associated events during G1/S transition
R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry
R-MMU-8876198, RAB GEFs exchange GTP for GDP on RABs
R-MMU-8948751, Regulation of PTEN stability and activity
R-MMU-9607240, FLT3 Signaling
R-MMU-9614399, Regulation of localization of FOXO transcription factors
R-MMU-9634638, Estrogen-dependent nuclear events downstream of ESR-membrane signaling

<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 7

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:104874, Akt2

<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

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL5382

<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_00000856091 – 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-acetylmethionineBy similarity1
Modified residuei34PhosphoserineBy similarity1
<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 ↔ 311By similarity
Glycosylationi306O-linked (GlcNAc) threonineBy similarity1
Modified residuei309Phosphothreonine; by PDPK1By similarity1
Glycosylationi313O-linked (GlcNAc) threonineBy similarity1
Modified residuei447PhosphoserineBy similarity1
Modified residuei451PhosphothreonineCombined sources1
Modified residuei474PhosphoserineBy similarity1
Modified residuei478PhosphoserineBy similarity1

<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.By similarity
Ubiquitinated; undergoes both 'Lys-48'- and 'Lys-63'-linked polyubiquitination. TRAF6-induced 'Lys-63'-linked AKT2 ubiquitination. When fully phosphorylated and translocated into the nucleus, undergoes 'Lys-48'-polyubiquitination catalyzed by TTC3, leading to its degradation by the proteasome (By similarity).By similarity
O-GlcNAcylation at Thr-306 and Thr-313 inhibits activating phosphorylation at Thr-309 via disrupting the interaction between AKT and PDK1.By similarity

Keywords - PTMi

Acetylation, Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q60823

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q60823

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q60823

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

More...
PaxDbi
Q60823

PRoteomics IDEntifications database

More...
PRIDEi
Q60823

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
296016

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

More...
GlyGeni
Q60823, 4 sites

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q60823

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

More...
PhosphoSitePlusi
Q60823

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000004056, Expressed in hindlimb stylopod muscle and 253 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q60823, MM

<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 (via PH domain) with MTCP1, TCL1A AND TCL1B.

Interacts with CLK2, PBH2 and TRAF6.

Interacts (when phosphorylated) with CLIP3, the interaction promotes cell membrane localization (By similarity).

Interacts with BTBD10 (PubMed:18160256).

Interacts with KCTD20 (PubMed:24156551).

Interacts with WDFY2 (via WD repeats 1-3) (PubMed:16792529, PubMed:20189988).

By similarity4 Publications

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
198057, 15 interactors

Protein interaction database and analysis system

More...
IntActi
Q60823, 28 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000103981

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q60823, 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

3D structure databases

Biological Magnetic Resonance Data Bank

More...
BMRBi
Q60823

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

More...
SMRi
Q60823

Database of comparative protein structure models

More...
ModBasei
Search...

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

Domains and Repeats

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

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 bindingBy similarity3
Regioni277 – 279Inhibitor bindingBy similarity3
Regioni292 – 293Inhibitor bindingBy similarity2

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

Binding of the PH domain to the phosphatidylinositol 3-kinase alpha (PIK3CA) results in its targeting to the plasma membrane.By similarity

<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

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_000288_11_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q60823

Identification of Orthologs from Complete Genome Data

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OMAi
ITPPDRC

Database of Orthologous Groups

More...
OrthoDBi
614710at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q60823

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

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

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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>Sequence (1+)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 has 1 described isoform and 7 potential isoforms that are computationally mapped.Show allAlign All

Q60823-1 [UniParc]FASTAAdd to basket
« 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 KQRGPGEDAM DYKCGSPSDS STSEMMEVAV NKARAKVTMN
160 170 180 190 200
DFDYLKLLGK GTFGKVILVR EKATGRYYAM KILRKEVIIA KDEVAHTVTE
210 220 230 240 250
SRVLQNTRHP FLTALKYAFQ THDRLCFVME YANGGELFFH LSRERVFTED
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 RTLGPEAKSL LAGLLKKDPK QRLGGGPSDA
410 420 430 440 450
KEVMEHRFFL SINWQDVVQK KLLPPFKPQV TSEVDTRYFD DEFTAQSITI
460 470 480
TPPDRYDSLD PLELDQRTHF PQFSYSASIR E
Length:481
Mass (Da):55,742
Last modified:November 1, 1996 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4AB4A9C4FB9CFA7D
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 7 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F8WHG5F8WHG5_MOUSE
Non-specific serine/threonine prote...
Akt2
438Annotation 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>
D3Z3N2D3Z3N2_MOUSE
RAC-beta serine/threonine-protein k...
Akt2
229Annotation 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>
D3YXM7D3YXM7_MOUSE
RAC-beta serine/threonine-protein k...
Akt2
222Annotation 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>
D3Z490D3Z490_MOUSE
RAC-beta serine/threonine-protein k...
Akt2
98Annotation 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>
D3YZJ5D3YZJ5_MOUSE
RAC-beta serine/threonine-protein k...
Akt2
84Annotation 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>
D3Z5X2D3Z5X2_MOUSE
RAC-beta serine/threonine-protein k...
Akt2
63Annotation 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>
D3Z0M3D3Z0M3_MOUSE
RAC-beta serine/threonine-protein k...
Akt2
67Annotation 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>

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
U22445 mRNA Translation: AAA83557.1
BC026151 mRNA Translation: AAH26151.1
BC040377 mRNA Translation: AAH40377.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS21027.1

NCBI Reference Sequences

More...
RefSeqi
NP_001103678.1, NM_001110208.2
NP_001318037.1, NM_001331108.1
NP_001318038.1, NM_001331109.1
NP_031460.1, NM_007434.4
XP_006539540.1, XM_006539477.1
XP_006539543.1, XM_006539480.1
XP_006539544.1, XM_006539481.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000051356; ENSMUSP00000052103; ENSMUSG00000004056
ENSMUST00000108343; ENSMUSP00000103980; ENSMUSG00000004056
ENSMUST00000108344; ENSMUSP00000103981; ENSMUSG00000004056
ENSMUST00000167435; ENSMUSP00000132141; ENSMUSG00000004056

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
11652

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:11652

UCSC genome browser

More...
UCSCi
uc009fwr.2, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U22445 mRNA Translation: AAA83557.1
BC026151 mRNA Translation: AAH26151.1
BC040377 mRNA Translation: AAH40377.1
CCDSiCCDS21027.1
RefSeqiNP_001103678.1, NM_001110208.2
NP_001318037.1, NM_001331108.1
NP_001318038.1, NM_001331109.1
NP_031460.1, NM_007434.4
XP_006539540.1, XM_006539477.1
XP_006539543.1, XM_006539480.1
XP_006539544.1, XM_006539481.3

3D structure databases

BMRBiQ60823
SMRiQ60823
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi198057, 15 interactors
IntActiQ60823, 28 interactors
STRINGi10090.ENSMUSP00000103981

Chemistry databases

ChEMBLiCHEMBL5382

PTM databases

GlyGeniQ60823, 4 sites
iPTMnetiQ60823
PhosphoSitePlusiQ60823

Proteomic databases

EPDiQ60823
jPOSTiQ60823
MaxQBiQ60823
PaxDbiQ60823
PRIDEiQ60823
ProteomicsDBi296016

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
3775, 1598 antibodies

Genome annotation databases

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

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
208
MGIiMGI:104874, Akt2

Phylogenomic databases

eggNOGiKOG0690, Eukaryota
GeneTreeiENSGT00940000157189
HOGENOMiCLU_000288_11_0_1
InParanoidiQ60823
OMAiITPPDRC
OrthoDBi614710at2759
PhylomeDBiQ60823
TreeFamiTF102004

Enzyme and pathway databases

BRENDAi2.7.11.1, 3474
ReactomeiR-MMU-1257604, PIP3 activates AKT signaling
R-MMU-1358803, Downregulation of ERBB2:ERBB3 signaling
R-MMU-165158, Activation of AKT2
R-MMU-165181, Inhibition of TSC complex formation by PKB
R-MMU-198323, AKT phosphorylates targets in the cytosol
R-MMU-198693, AKT phosphorylates targets in the nucleus
R-MMU-199418, Negative regulation of the PI3K/AKT network
R-MMU-211163, AKT-mediated inactivation of FOXO1A
R-MMU-3769402, Deactivation of the beta-catenin transactivating complex
R-MMU-389357, CD28 dependent PI3K/Akt signaling
R-MMU-389513, CTLA4 inhibitory signaling
R-MMU-392451, G beta:gamma signalling through PI3Kgamma
R-MMU-5218920, VEGFR2 mediated vascular permeability
R-MMU-5628897, TP53 Regulates Metabolic Genes
R-MMU-6804757, Regulation of TP53 Degradation
R-MMU-6804758, Regulation of TP53 Activity through Acetylation
R-MMU-6804759, Regulation of TP53 Activity through Association with Co-factors
R-MMU-69202, Cyclin E associated events during G1/S transition
R-MMU-69656, Cyclin A:Cdk2-associated events at S phase entry
R-MMU-8876198, RAB GEFs exchange GTP for GDP on RABs
R-MMU-8948751, Regulation of PTEN stability and activity
R-MMU-9607240, FLT3 Signaling
R-MMU-9614399, Regulation of localization of FOXO transcription factors
R-MMU-9634638, Estrogen-dependent nuclear events downstream of ESR-membrane signaling

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...
BioGRID-ORCSi
11652, 1 hit in 54 CRISPR screens

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

More...
ChiTaRSi
Akt2, mouse

Protein Ontology

More...
PROi
PR:Q60823
RNActiQ60823, protein

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000004056, Expressed in hindlimb stylopod muscle and 253 other tissues
GenevisibleiQ60823, MM

Family and domain databases

CDDicd01241, PH_PKB, 1 hit
cd05595, STKc_PKB_beta, 1 hit
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_MOUSE
<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: Q60823
<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: December 1, 2000
Last sequence update: November 1, 1996
Last modified: April 7, 2021
This is version 191 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<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

Reference proteome

Documents

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