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Protein

Forkhead box protein O1

Gene

FOXO1

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

Transcription factor that is the main target of insulin signaling and regulates metabolic homeostasis in response to oxidative stress. Binds to the insulin response element (IRE) with consensus sequence 5'-TT[G/A]TTTTG-3' and the related Daf-16 family binding element (DBE) with consensus sequence 5'-TT[G/A]TTTAC-3'. Activity suppressed by insulin. Main regulator of redox balance and osteoblast numbers and controls bone mass. Orchestrates the endocrine function of the skeleton in regulating glucose metabolism. Acts synergistically with ATF4 to suppress osteocalcin/BGLAP activity, increasing glucose levels and triggering glucose intolerance and insulin insensitivity. Also suppresses the transcriptional activity of RUNX2, an upstream activator of osteocalcin/BGLAP. In hepatocytes, promotes gluconeogenesis by acting together with PPARGC1A and CEBPA to activate the expression of genes such as IGFBP1, G6PC and PCK1. Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death. Mediates insulin action on adipose tissue. Regulates the expression of adipogenic genes such as PPARG during preadipocyte differentiation and, adipocyte size and adipose tissue-specific gene expression in response to excessive calorie intake. Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells. Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner. Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (By similarity).By similarity8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei158DNA-binding1
Sitei165DNA-binding1
Sitei225DNA-binding1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi159 – 235Fork-headPROSITE-ProRule annotationAdd BLAST77

<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 functionActivator, DNA-binding
Biological processApoptosis, Autophagy, Differentiation, Transcription, Transcription regulation

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-198693 AKT phosphorylates targets in the nucleus
R-HSA-210745 Regulation of gene expression in beta cells
R-HSA-211163 AKT-mediated inactivation of FOXO1A
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling

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

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SignaLinki
Q12778

SIGNOR Signaling Network Open Resource

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SIGNORi
Q12778

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Forkhead box protein O1
Alternative name(s):
Forkhead box protein O1A
Forkhead in rhabdomyosarcoma
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FOXO1
Synonyms:FKHR, FOXO1A
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 13

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000150907.6

Human Gene Nomenclature Database

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HGNCi
HGNC:3819 FOXO1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
136533 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q12778

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

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

Keywords - Cellular componenti

Cytoplasm, 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

Rhabdomyosarcoma 2 (RMS2)
The gene represented in this entry may be involved in disease pathogenesis. Chromosomal aberrations involving FOXO1 are found in rhabdomyosarcoma. Translocation (2;13)(q35;q14) with PAX3 and translocation t(1;13)(p36;q14) with PAX7. The resulting protein is a transcriptional activator.
Disease descriptionA form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchymal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas.
See also OMIM:268220

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi24T → A: Abolishes PKB/AKT1-mediated phosphorylation but does not prevent phosphorylation of Ser-256 or Ser-319. Also inhibits binding of 14-3-3 proteins. Nuclear in unstimulated cells, and little export to cytoplasm on IGF1 stimulation. Inhibits the PKB/AKT1-mediated activity towards other substrates but does not block the IGF1-activated 'T-308' of phosphorylation of PKB/AKT1; when associated with A-256 and A-319. Targeted to the nucleus and enhances transactivation; when associated with A-319. 2 Publications1
Mutagenesisi212S → A: Abolishes STK4/MST1-mediated phosphorylation. 1 Publication1
Mutagenesisi245K → A: Disrupts DNA-binding; when associated with A-248. 1
Mutagenesisi248K → A: Disrupts DNA-binding; when associated with A-245. 1
Mutagenesisi249S → A: Impaired phosphorylation by CDK1. 2 Publications1
Mutagenesisi249S → E: No effect on DNA-binding. 2 Publications1
Mutagenesisi251 – 253RRR → SAS: No targeting to the nucleus and disruption of DNA-binding. 3
Mutagenesisi256S → A: Completely abolishes PKB/AKT1-mediated phosphorylation at all three sites, and inhibits binding of 14-3-3 proteins. Inhibits the PKB/AKT1-mediated activity towards other substrates but does not block the IGF1-activated 'T-308' of phosphorylation of PKB/AKT1; when associated with or without A-24 and A-319. Nuclear in unstimulated cells, and little export to cytoplasm on IGF1 stimulation. Abolishes the ability of IGF1 to suppress transactivation. Prevents T-24 and S-319 phosphorylation. Enhances transactivation; when associated with A-24 and A-319. 3 Publications1
Mutagenesisi256S → D: Reduces DNA binding, promotes nuclear exclusion and partially promotes T-24 and S-319 phosphorylation. Reduces DNA binding, does not promote nuclear exclusion but reduces transactivation; when associated with A-24 and A-319. 3 Publications1
Mutagenesisi262K → R: Inhibits interaction with ATG7 and FOXO1-acetylation-induced autophagic cell death; when associated with R-265 and R-274. 1
Mutagenesisi265K → R: Inhibits interaction with ATG7 and FOXO1-acetylation-induced autophagic cell death; when associated with R-262 and R-274. 1
Mutagenesisi274K → R: Inhibits interaction with ATG7 and FOXO1-acetylation-induced autophagic cell death; when associated with R-262 and R-265. 1
Mutagenesisi319S → A: Abolishes PKB/AKT1-mediated phosphorylation but does not prevent phosphorylation of Ser-24 or Ser-256. Inhibits the PKB/AKT1-mediated activity towards other substrates but does not block the IGF1-activated 'T-308' of phosphorylation of PKB/AKT1; when associated with A-24 and A-256. Targeted to the nucleus and enhances transactivation; when associated with A-24. 2 Publications1
Mutagenesisi329S → A: Targeted to the nucleus and enhances transactivation. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNET

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DisGeNETi
2308

MalaCards human disease database

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MalaCardsi
FOXO1
MIMi268220 phenotype

Open Targets

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OpenTargetsi
ENSG00000150907

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

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Orphaneti
99756 Alveolar rhabdomyosarcoma

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28237

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL5294

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FOXO1

Domain mapping of disease mutations (DMDM)

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DMDMi
116241368

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000918721 – 655Forkhead box protein O1Add BLAST655

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 residuei24Phosphothreonine; by PKB/AKT1 or PKB/AKT2 and SGK13 Publications1
Modified residuei212Phosphoserine; by STK4/MST13 Publications1
Modified residuei218Phosphoserine; by STK4/MST11 Publication1
Modified residuei234Phosphoserine; by STK4/MST11 Publication1
Modified residuei235Phosphoserine; by STK4/MST11 Publication1
Modified residuei245N6-acetyllysineBy similarity1
Modified residuei248N6-acetyllysineBy similarity1
Modified residuei249Phosphoserine; by CDK11 Publication1
Modified residuei251Omega-N-methylarginine; by PRMT1By similarity1
Modified residuei253Omega-N-methylarginine; by PRMT1By similarity1
Modified residuei256Phosphoserine; by PKB/AKT1 and SGK14 Publications1
Modified residuei262N6-acetyllysine1 Publication1
Modified residuei265N6-acetyllysine1 Publication1
Modified residuei274N6-acetyllysine1 Publication1
Modified residuei287PhosphoserineCombined sources1
Modified residuei298PhosphoserineBy similarity1
Modified residuei319Phosphoserine; by PKB/AKT13 Publications1
Modified residuei322Phosphoserine; by CK1 and SGK11 Publication1
Modified residuei325Phosphoserine; by CK11 Publication1
Modified residuei329Phosphoserine; by DYRK1A2 Publications1
Modified residuei333PhosphothreonineBy similarity1

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

Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-256 and Ser-322 by PKB/AKT1 promotes nuclear export and inactivation of transactivational activity. Phosphorylation on Thr-24 is required for binding 14-3-3 proteins. Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CDK1, leading to nuclear exclusion and loss of function. Stress signals, such as response to oxygen or nitric oxide, attenuate the PKB/AKT1-mediated phosphorylation leading to nuclear retention. Phosphorylation of Ser-329 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-256 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity). Phosphorylation of Ser-249 by CDK1 disrupts binding of 14-3-3 proteins leading to nuclear accumulation and has no effect on DNA-binding nor transcriptional activity. Phosphorylation by STK4/MST1 on Ser-212, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export.By similarity9 Publications
Acetylated. Acetylation at Lys-262, Lys-265 and Lys-274 are necessary for autophagic cell death induction. Deacetylated by SIRT2 in response to oxidative stress or serum deprivation, thereby negatively regulating FOXO1-mediated autophagic cell death.1 Publication
Ubiquitinated by SRT2. Ubiquitination leads to proteasomal degradation.1 Publication
Methylation inhibits AKT1-mediated phosphorylation at Ser-256 and is increased by oxidative stress.By similarity
Once in the nucleus, acetylated by CREBBP/EP300. Acetylation diminishes the interaction with target DNA and attenuates the transcriptional activity. It increases the phosphorylation at Ser-256. Deacetylation by SIRT1 results in reactivation of the transcriptional activity. Oxidative stress by hydrogen peroxide treatment appears to promote deacetylation and uncoupling of insulin-induced phosphorylation. By contrast, resveratrol acts independently of acetylation.4 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q12778

MaxQB - The MaxQuant DataBase

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MaxQBi
Q12778

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

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PaxDbi
Q12778

PeptideAtlas

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PeptideAtlasi
Q12778

PRoteomics IDEntifications database

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PRIDEi
Q12778

ProteomicsDB human proteome resource

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ProteomicsDBi
58922

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q12778

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

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PhosphoSitePlusi
Q12778

<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

Ubiquitous.1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is regulated by KRIT1. Levels of expression also regulated by FOXC1 which binds to a conserved element in the FOXO1 promoter.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000150907 Expressed in 244 organ(s), highest expression level in female gonad

CleanEx database of gene expression profiles

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CleanExi
HS_FOXO1

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q12778 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB022326
HPA001252

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

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

Interacts with LRPPRC. Interacts with RUNX2; the interaction inhibits RUNX2 transcriptional activity and mediates the IGF1/insulin-dependent BGLAP expression in osteoblasts Interacts with PPP2R1A; the interaction regulates the dephosphorylation of FOXO1 at Thr-24 and Ser-256 leading to its nuclear import. Interacts (acetylated form) with PPARG. Interacts with XBP1 isoform 2; this interaction is direct and leads to FOXO1 ubiquitination and degradation via the proteasome pathway (By similarity). Interacts with NLK. Interacts with SIRT1; the interaction results in the deacetylation of FOXO1 leading to activation of FOXO1-mediated transcription of genes involved in DNA repair and stress resistance. Binds to CDK1. Interacts with the 14-3-3 proteins, YWHAG and YWHAZ; the interactions require insulin-stimulated phosphorylation on Thr-24, promote nuclear exit and loss of transcriptional activity. Interacts with SKP2; the interaction ubiquitinates FOXO1 leading to its proteosomal degradation. The interaction requires the presence of KRIT1. Interacts (via the C-terminal half) with ATF4 (via its DNA-binding domain); the interaction occurs in osteoblasts, regulates glucose homeostasis via suppression of beta-cell proliferation and subsequent decrease in insulin production. Interacts with PRMT1; the interaction methylates FOXO1, prevents PKB/AKT1 phosphorylation and retains FOXO1 in the nucleus. Interacts with EP300 and CREBBP; the interactions acetylate FOXO1. Interacts with SIRT2; the interaction is disrupted in response to oxidative stress or serum deprivation, leading to increased level of acetylated FOXO1, which promotes stress-induced autophagy by stimulating E1-like activating enzyme ATG7. Interacts (acetylated form) with ATG7; the interaction is increased in response to oxidative stress or serum deprivation and promotes the autophagic process leading to cell death. Interacts (via the Fork-head domain) with CEBPA; the interaction increases when FOXO1 is deacetylated. Interacts with WDFY2. Forms a complex with WDFY2 and AKT1 (By similarity).By similarity7 Publications

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

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108597, 62 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q12778

Database of interacting proteins

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DIPi
DIP-35654N

Protein interaction database and analysis system

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IntActi
Q12778, 31 interactors

Molecular INTeraction database

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MINTi
Q12778

STRING: functional protein association networks

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STRINGi
9606.ENSP00000368880

Chemistry databases

BindingDB database of measured binding affinities

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BindingDBi
Q12778

<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

1655
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q12778

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

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SMRi
Q12778

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q12778

<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

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>Regioni211 – 218DNA-binding8
Regioni234 – 237DNA-binding4
Regioni283 – 563Sufficient for interaction with NLKBy similarityAdd BLAST281
Regioni363 – 459Required for interaction with RUNX2By similarityAdd BLAST97

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi251 – 253Nuclear localization signal3
Motifi462 – 466Required for interaction with SIRT1By similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi91 – 102Poly-AlaAdd BLAST12
Compositional biasi120 – 130Poly-ProAdd BLAST11
Compositional biasi152 – 155Poly-Ser4

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2294 Eukaryota
COG5025 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161558

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000251635

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG057789

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q12778

KEGG Orthology (KO)

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KOi
K07201

Identification of Orthologs from Complete Genome Data

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OMAi
KWPGSPN

Database of Orthologous Groups

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OrthoDBi
EOG091G06K3

Database for complete collections of gene phylogenies

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PhylomeDBi
Q12778

TreeFam database of animal gene trees

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TreeFami
TF315583

Family and domain databases

Conserved Domains Database

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CDDi
cd00059 FH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001766 Fork_head_dom
IPR032067 FOXO-TAD
IPR032068 FOXO_KIX-bd
IPR030456 TF_fork_head_CS_2
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf

Pfam protein domain database

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Pfami
View protein in Pfam
PF00250 Forkhead, 1 hit
PF16676 FOXO-TAD, 1 hit
PF16675 FOXO_KIX_bdg, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00053 FORKHEAD

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00339 FH, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF46785 SSF46785, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit

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

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

Q12778-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEAPQVVEI DPDFEPLPRP RSCTWPLPRP EFSQSNSATS SPAPSGSAAA
60 70 80 90 100
NPDAAAGLPS ASAAAVSADF MSNLSLLEES EDFPQAPGSV AAAVAAAAAA
110 120 130 140 150
AATGGLCGDF QGPEAGCLHP APPQPPPPGP LSQHPPVPPA AAGPLAGQPR
160 170 180 190 200
KSSSSRRNAW GNLSYADLIT KAIESSAEKR LTLSQIYEWM VKSVPYFKDK
210 220 230 240 250
GDSNSSAGWK NSIRHNLSLH SKFIRVQNEG TGKSSWWMLN PEGGKSGKSP
260 270 280 290 300
RRRAASMDNN SKFAKSRSRA AKKKASLQSG QEGAGDSPGS QFSKWPASPG
310 320 330 340 350
SHSNDDFDNW STFRPRTSSN ASTISGRLSP IMTEQDDLGE GDVHSMVYPP
360 370 380 390 400
SAAKMASTLP SLSEISNPEN MENLLDNLNL LSSPTSLTVS TQSSPGTMMQ
410 420 430 440 450
QTPCYSFAPP NTSLNSPSPN YQKYTYGQSS MSPLPQMPIQ TLQDNKSSYG
460 470 480 490 500
GMSQYNCAPG LLKELLTSDS PPHNDIMTPV DPGVAQPNSR VLGQNVMMGP
510 520 530 540 550
NSVMSTYGSQ ASHNKMMNPS SHTHPGHAQQ TSAVNGRPLP HTVSTMPHTS
560 570 580 590 600
GMNRLTQVKT PVQVPLPHPM QMSALGGYSS VSSCNGYGRM GLLHQEKLPS
610 620 630 640 650
DLDGMFIERL DCDMESIIRN DLMDGDTLDF NFDNVLPNQS FPHSVKTTTH

SWVSG
Length:655
Mass (Da):69,662
Last modified:October 17, 2006 - 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:i6DEF6C994BDFDBAB
GO

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 conflicti131L → V in AAA03629 (PubMed:8275086).Curated1
Sequence conflicti343V → M in AAH70065 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
U02310 mRNA Translation: AAA03629.1
AF032885 mRNA Translation: AAC39591.1
BT007455 mRNA Translation: AAP36123.1
AL355132 Genomic DNA No translation available.
AL133318 Genomic DNA No translation available.
BC021981 mRNA Translation: AAH21981.1
BC070065 mRNA Translation: AAH70065.3

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9371.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S40521

NCBI Reference Sequences

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RefSeqi
NP_002006.2, NM_002015.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.370666

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000379561; ENSP00000368880; ENSG00000150907

Database of genes from NCBI RefSeq genomes

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GeneIDi
2308

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2308

UCSC genome browser

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UCSCi
uc001uxl.5 human

Keywords - Coding sequence diversityi

Chromosomal rearrangement

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

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U02310 mRNA Translation: AAA03629.1
AF032885 mRNA Translation: AAC39591.1
BT007455 mRNA Translation: AAP36123.1
AL355132 Genomic DNA No translation available.
AL133318 Genomic DNA No translation available.
BC021981 mRNA Translation: AAH21981.1
BC070065 mRNA Translation: AAH70065.3
CCDSiCCDS9371.1
PIRiS40521
RefSeqiNP_002006.2, NM_002015.3
UniGeneiHs.370666

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3CO6X-ray2.10C151-249[»]
3CO7X-ray2.91C/F151-266[»]
3COAX-ray2.20C/F151-266[»]
4LG0X-ray2.19A143-270[»]
5DUIX-ray2.31A/B151-259[»]
ProteinModelPortaliQ12778
SMRiQ12778
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108597, 62 interactors
CORUMiQ12778
DIPiDIP-35654N
IntActiQ12778, 31 interactors
MINTiQ12778
STRINGi9606.ENSP00000368880

Chemistry databases

BindingDBiQ12778
ChEMBLiCHEMBL5294

PTM databases

iPTMnetiQ12778
PhosphoSitePlusiQ12778

Polymorphism and mutation databases

BioMutaiFOXO1
DMDMi116241368

Proteomic databases

EPDiQ12778
MaxQBiQ12778
PaxDbiQ12778
PeptideAtlasiQ12778
PRIDEiQ12778
ProteomicsDBi58922

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
2308
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000379561; ENSP00000368880; ENSG00000150907
GeneIDi2308
KEGGihsa:2308
UCSCiuc001uxl.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2308
DisGeNETi2308
EuPathDBiHostDB:ENSG00000150907.6

GeneCards: human genes, protein and diseases

More...
GeneCardsi
FOXO1
HGNCiHGNC:3819 FOXO1
HPAiCAB022326
HPA001252
MalaCardsiFOXO1
MIMi136533 gene
268220 phenotype
neXtProtiNX_Q12778
OpenTargetsiENSG00000150907
Orphaneti99756 Alveolar rhabdomyosarcoma
PharmGKBiPA28237

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2294 Eukaryota
COG5025 LUCA
GeneTreeiENSGT00940000161558
HOGENOMiHOG000251635
HOVERGENiHBG057789
InParanoidiQ12778
KOiK07201
OMAiKWPGSPN
OrthoDBiEOG091G06K3
PhylomeDBiQ12778
TreeFamiTF315583

Enzyme and pathway databases

ReactomeiR-HSA-198693 AKT phosphorylates targets in the nucleus
R-HSA-210745 Regulation of gene expression in beta cells
R-HSA-211163 AKT-mediated inactivation of FOXO1A
R-HSA-5674400 Constitutive Signaling by AKT1 E17K in Cancer
R-HSA-5687128 MAPK6/MAPK4 signaling
R-HSA-6785807 Interleukin-4 and Interleukin-13 signaling
SignaLinkiQ12778
SIGNORiQ12778

Miscellaneous databases

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

More...
ChiTaRSi
FOXO1 human
EvolutionaryTraceiQ12778

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
FOXO1

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

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GenomeRNAii
2308

Protein Ontology

More...
PROi
PR:Q12778

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000150907 Expressed in 244 organ(s), highest expression level in female gonad
CleanExiHS_FOXO1
GenevisibleiQ12778 HS

Family and domain databases

CDDicd00059 FH, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR001766 Fork_head_dom
IPR032067 FOXO-TAD
IPR032068 FOXO_KIX-bd
IPR030456 TF_fork_head_CS_2
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00250 Forkhead, 1 hit
PF16676 FOXO-TAD, 1 hit
PF16675 FOXO_KIX_bdg, 1 hit
PRINTSiPR00053 FORKHEAD
SMARTiView protein in SMART
SM00339 FH, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOXO1_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: Q12778
Secondary accession number(s): O43523, Q5VYC7, Q6NSK6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: December 5, 2018
This is version 200 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Human chromosome 13
    Human chromosome 13: entries, gene names and cross-references to MIM
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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