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Protein

Forkhead box protein O1

Gene

Foxo1

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

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 similarity15 Publications

Miscellaneous

In an animal model of diabetes mellitus type 2 (db/db mice), beta-cell islets exhibit increased levels of PPP2R1A leading to increased dephosphorylation at Thr-24 and Ser-253 and nuclear retention of FOXO1.

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>Sitei155DNA-bindingBy similarity1
Sitei162DNA-bindingBy similarity1
Sitei222DNA-bindingBy similarity1

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 bindingi156 – 232Fork-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

More...
Reactomei
R-MMU-198693 AKT phosphorylates targets in the nucleus
R-MMU-211163 AKT-mediated inactivation of FOXO1A
R-MMU-5687128 MAPK6/MAPK4 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_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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<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
  • UP000000589 <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 3

Organism-specific databases

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

More...
MGIi
MGI:1890077 Foxo1

<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 describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Null mice die around embryonic day 11 and exhibit abnormal angiogenesis. Defects are observed in branchial arches and there is remarkably impaired vascular development of embryos and yolk sacs. Exogeneous VEGF on FOX1-deficient endothelial cells show markedly different morphological response. Active osteocalcin/BGLAP as well as serum insulin and beta-cell and gonadal fat levels were increased, but there is no change in total fat content, lean mass, and body weight. Effect on RUNX2 activity was inhibited. FOXO1 and ATF4 double happlo-insufficient mice exhibit also an increase in insulin levels and beta cell proliferation, but there is an increase in insulin sensitivity demonstrated by an increase in expression of insulin-sensitizing hormone adiponectin. Gonadal fat levels and adipocyte numbers were decreased. Osteocalcin/BGLAP levels were unchanged.2 Publications

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: Decreases insulin-induced phosphorylation by approximately 30%. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-253; A-316; A-462 and A-463. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with Q-219; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with R-219; R-242; R-245; R-259; R-262; R-271 and R-291. 3 Publications1
Mutagenesisi29R → K: Little change in levels of methylation; when associated with K-147; K-154; K-311 and K-313. 1 Publication1
Mutagenesisi147R → K: Little change in levels of methylation; when associated with K-29; K-154; K-311 and K-313. 1 Publication1
Mutagenesisi154R → K: Little change in levels of methylation; when associated with K-29; K-147; K-311 and K-313. 1 Publication1
Mutagenesisi206W → G: Loss of interaction with CEBPA. 1 Publication1
Mutagenesisi212H → P: Loss of interaction with CEBPA. 1 Publication1
Mutagenesisi219K → Q: Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-242; Q-245; Q-259; Q-262; Q-271 and Q-291. 1 Publication1
Mutagenesisi219K → R: Translocates to the cytoplasm after insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-242; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-242; R-245; R-259; R-262; R-271 and R-291. 1 Publication1
Mutagenesisi242K → Q or A: Mimics acetylation. Cytoplasmic location in absence or presence of insulin. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-245 or Q-245 and either A-262 or Q-262. either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-245; Q-259; Q-262; Q-271 and Q-291. 5 Publications1
Mutagenesisi242K → R: Reduced acetylation and transcriptional activity increased by about 1.5 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-245 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-245; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-245; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-245; R-259; R-262; R-271 and R-291. 5 Publications1
Mutagenesisi245K → Q or A: Mimics acetylation. Decreased DNA-binding by about half. Enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-262 or Q-262. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-259; Q-262; Q-271 and Q-291. 5 Publications1
Mutagenesisi245K → R: Reduced acetylation and transcriptional activity increased by about 1.5-fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-262. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-259; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-259; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-259; R-262; R-271 and R-291. 5 Publications1
Mutagenesisi248R → K: Some decrease in levels of methylation. Greatly decreased methylation levels; when associated with K-250. 1 Publication1
Mutagenesisi249R → K: No change in methylation levels. 1
Mutagenesisi250R → K: Some decrease in levels of methylation. Greatly decreased methylation levels; when associated with K-248. 1 Publication1
Mutagenesisi253S → A: Abolishes insulin-induced phosphorylation when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-316; A-462 and A-463. 4 Publications1
Mutagenesisi259K → Q: Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-262; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-262; Q-271 and Q-291. 2 Publications1
Mutagenesisi259K → R: Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-262; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-262; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-262; R-271 and R-291. 2 Publications1
Mutagenesisi262K → Q or A: Mimics acetylation. Decreased DNA-binding by about half and enhanced phosphorylation by PKB/AKT1, no effect on interaction with CEBPA; when associated with either A-242 or Q-242 and either A-245 or Q-245. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-271 and Q-291. 5 Publications1
Mutagenesisi262K → R: Significant reduction in acetylation and transcriptional activity increased by about 2.0 fold. Completely abolishes acetylation, increases interaction with CEBPA and transcriptional activity increased by about 3-fold; when associated with R-242 and R-245. Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-271 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-271 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-271 and R-291. 5 Publications1
Mutagenesisi271K → Q: Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24; Q-219; Q-242; Q-245; Q-259; Q-262 and Q-291. 2 Publications1
Mutagenesisi271K → R: Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-291. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-291. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-291. 2 Publications1
Mutagenesisi284S → A: Decreases phosphorylation by NLK; when associated with A-295; A-326; A-380; A-391; A-399; A-413 and A-415. 1 Publication1
Mutagenesisi291K → Q: Mimics acetylation. Cytoplasmic location in absence or presence of insulin, no change on the inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271. Increased insulin-induced phosphorylation at Ser-253 and binding of 14-3-3 proteins; when associated with A-24: Q-219; Q-242; Q-245; Q-259; Q-262 and Q-271. 2 Publications1
Mutagenesisi291K → R: Transcriptional activity not inhibited by FCOR; when associated with R-242; R-245; R-259; R-262 and R-271. Predominantly nuclear and translocates to the cytoplasm on insulin-stimulation. No inhibitory effect of oxidative stress on insulin-induced phosphorylations, but no inhibition of these phosphorylations by resveratrol; when associated with R-219; R-242; R-245; R-259; R-262 and R-271. Increased binding of 14-3-3 proteins even with decreased insulin-induced phosphorylation at Ser-253; when associated with A-24; R-219; R-242; R-245; R-259; R-262 and R-271. 2 Publications1
Mutagenesisi295S → A: Decreases phosphorylation by NLK; when associated with A-284; A-326; A-380; A-391; A-399; A-413 and A-415. 1 Publication1
Mutagenesisi311R → K: Little change in levels of methylation; when associated with K-29; K-147; K-154 and K-313. 1 Publication1
Mutagenesisi313R → K: Little change in levels of methylation; when associated with K-29; K-147; K-154 and K-311. 1 Publication1
Mutagenesisi316S → A: Decreases insulin-induced phosphorylation by approximately 30%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-462 and A-463. 2 Publications1
Mutagenesisi326S → A: Decreases phosphorylation by NLK; when associated with A-284; A-295; A-380; A-391; A-399; A-413 and A-415. 1 Publication1
Mutagenesisi380S → A: Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-391; A-399; A-413 and A-415. 1 Publication1
Mutagenesisi391S → A: Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-399; A-413 and A-415. 1 Publication1
Mutagenesisi399T → A: Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-391; A-413 and A-415. 1 Publication1
Mutagenesisi413S → A: Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-391; A-399 and A-415. 1 Publication1
Mutagenesisi415S → A: Decreases phosphorylation by NLK; when associated with A-284; A-295; A-326; A-380; A-391; A-399 and A-413. 1 Publication1
Mutagenesisi462L → A: Decreased transcriptional activity by about 2-fold in the absence of serum; when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-316 and A-463. 1 Publication1
Mutagenesisi463L → A: Decreased transcriptional activity by about 2-fold in the absence of serum; when associated with A-463. Nuclear location but transcriptional activity decreased by about 50%. Abolishes the SIRT1 deacetylase binding and increases acetylation; when associated with A-24; A-253; A-316 and A-462. 1 Publication1

<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_00000918731 – 652Forkhead box protein O1Add BLAST652

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 residuei209Phosphoserine; by STK4/MST1By similarity1
Modified residuei215PhosphoserineBy similarity1
Modified residuei231PhosphoserineBy similarity1
Modified residuei232PhosphoserineBy similarity1
Modified residuei242N6-acetyllysine3 Publications1
Modified residuei245N6-acetyllysine3 Publications1
Modified residuei246Phosphoserine; by CDK1By similarity1
Modified residuei248Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei250Omega-N-methylarginine; by PRMT11 Publication1
Modified residuei253Phosphoserine; by PKB/AKT1 and SGK15 Publications1
Modified residuei259N6-acetyllysineBy similarity1
Modified residuei262N6-acetyllysine3 Publications1
Modified residuei271N6-acetyllysineBy similarity1
Modified residuei284PhosphoserineCombined sources1
Modified residuei295PhosphoserineCombined sources1
Modified residuei316Phosphoserine; by PKB/AKT1 or PKB/AKT21 Publication1
Modified residuei319Phosphoserine; by CK1 and SGK11 Publication1
Modified residuei322Phosphoserine; by CK1By similarity1
Modified residuei326PhosphoserineCombined sources1
Modified residuei330PhosphothreonineCombined sources1

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

Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-253 and Ser-319 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-253 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-316, permitting phosphorylation of Ser-319 and Ser-322, 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-326 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-253 by PP2A in beta-cells under oxidative stress leading to nuclear retention (By similarity). Phosphorylation of Ser-246 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-209, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export.By similarity4 Publications
Ubiquitinated by SRT2. Ubiquitination leads to proteasomal degradation (By similarity).By similarity
Methylation inhibits PKB/AKT1-mediated phosphorylation at Ser-253, promoting nuclear retention and increasing the transcriptional activity and cell death. Methylation increased by oxidative stress.5 Publications
Acetylation at Lys-259 and Lys-271 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 (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-253, and is required for the transcriptional inhibition by FCOR. Deacetylation by SIRT1 results in reactivation of the transcriptional activity (PubMed:17090532). Acetylation of FOXO1 diminishes its binding to PPARG in adipocytes. Deacetylated by SIRT2; deacetylation of FOXO1 directly increases its repressive binding to PPARG and inhibits adipocyte differentiation. Oxidative stress by hydrogen peroxide treatment appears to promote deacetylation and uncoupling of insulin-induced phosphorylation. By contrast, resveratrol acts independently of acetylation.By similarity9 Publications

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
Q9R1E0

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9R1E0

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

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PaxDbi
Q9R1E0

PeptideAtlas

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PeptideAtlasi
Q9R1E0

PRoteomics IDEntifications database

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PRIDEi
Q9R1E0

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9R1E0

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

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PhosphoSitePlusi
Q9R1E0

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9R1E0

<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 liver, white and brown adipose tissues (at protein level).2 Publications

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

In liver, barely expressed at E14.5, expression dramatically increases at E18.5. Abundantly expressed in neonate liver but levels strongly decrease in adult liver (at protein level).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 (PubMed:20668652). Transiently up-regulated during adipogenesis (at protein level) (PubMed:18388859).2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000044167 Expressed in 287 organ(s), highest expression level in female gonad

CleanEx database of gene expression profiles

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CleanExi
MM_FOXO1

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9R1E0 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_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 EP300 and CREBBP; the interactions acetylate FOXO1. 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. Interacts with PMRT1; methylates FOXO1, prevents PKB/AKT1 phosphorylation and retains FOXO1 in the nucleus (By similarity). Interacts (via an N-terminal domain) with FCOR; the interaction is direct, occurs in a forskolin-independent manner and prevents SIRT1 binding to FOXO1. 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 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-253 leading to its nuclear import. Binds to CDK1. Interacts with LRPPRC. Interacts with RUNX2; the interaction inhibits RUNX2 transcriptional activity and mediates the IGF1/insulin-dependent BGLAP expression in osteoblasts. 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. The interaction requires the presence of KRIT1 and is inhibited by FCOR. 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 (acetylated form) with PPARG (PubMed:12754525, PubMed:15220471, PubMed:16917544, PubMed:17050673, PubMed:17681146, PubMed:19037106, PubMed:20061393, PubMed:20668652, PubMed:21471200, PubMed:22298775, PubMed:22417654, PubMed:22510882). Interacts with XBP1 isoform 2; this interaction is direct and leads to FOXO1 ubiquitination and degradation via the proteasome pathway (PubMed:21317886). Interacts (via the Fork-head domain) with CEBPA; the interaction increases when FOXO1 is deacetylated (PubMed:17090532, PubMed:17627282). Interacts with WDFY2 (PubMed:18388859). Forms a complex with WDFY2 and AKT1 (PubMed:18388859).By similarity16 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
207997, 10 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9R1E0

Protein interaction database and analysis system

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IntActi
Q9R1E0, 16 interactors

Molecular INTeraction database

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MINTi
Q9R1E0

STRING: functional protein association networks

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STRINGi
10090.ENSMUSP00000055308

<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

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q9R1E0

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

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SMRi
Q9R1E0

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...

<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>Regioni208 – 215DNA-bindingBy similarity8
Regioni231 – 234DNA-bindingBy similarity4
Regioni280 – 562Sufficient for interaction with NLK1 PublicationAdd BLAST283
Regioni360 – 456Required for interaction with RUNX21 PublicationAdd 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>Motifi248 – 250Nuclear localization signalBy similarity3
Motifi459 – 463Required for interaction with SIRT15

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 biasi89 – 96Poly-Ala8
Compositional biasi135 – 139Poly-Ala5
Compositional biasi149 – 152Poly-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
Q9R1E0

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

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

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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

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SUPFAMi
SSF46785 SSF46785, 1 hit

PROSITE; a protein domain and family database

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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.

Q9R1E0-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEAPQVVET DPDFEPLPRQ RSCTWPLPRP EFNQSNSTTS SPAPSGGAAA
60 70 80 90 100
NPDAAASLAS ASAVSTDFMS NLSLLEESED FARAPGCVAV AAAAAASRGL
110 120 130 140 150
CGDFQGPEAG CVHPAPPQPP PTGPLSQPPP VPPSAAAAAG PLAGQPRKTS
160 170 180 190 200
SSRRNAWGNL SYADLITKAI ESSAEKRLTL SQIYEWMVKS VPYFKDKGDS
210 220 230 240 250
NSSAGWKNSI RHNLSLHSKF IRVQNEGTGK SSWWMLNPEG GKSGKSPRRR
260 270 280 290 300
AASMDNNSKF AKSRGRAAKK KASLQSGQEG PGDSPGSQFS KWPASPGSHS
310 320 330 340 350
NDDFDNWSTF RPRTSSNAST ISGRLSPIMT EQDDLGDGDV HSLVYPPSAA
360 370 380 390 400
KMASTLPSLS EISNPENMEN LLDNLNLLSS PTSLTVSTQS SPGSMMQQTP
410 420 430 440 450
CYSFAPPNTS LNSPSPNYSK YTYGQSSMSP LPQMPMQTLQ DSKSSYGGLN
460 470 480 490 500
QYNCAPGLLK ELLTSDSPPH NDIMSPVDPG VAQPNSRVLG QNVMMGPNSV
510 520 530 540 550
MPAYGSQASH NKMMNPSSHT HPGHAQQTAS VNGRTLPHVV NTMPHTSAMN
560 570 580 590 600
RLTPVKTPLQ VPLSHPMQMS ALGSYSSVSS CNGYGRMGVL HQEKLPSDLD
610 620 630 640 650
GMFIERLDCD MESIIRNDLM DGDTLDFNFD NVLPNQSFPH SVKTTTHSWV

SG
Length:652
Mass (Da):69,518
Last modified:July 27, 2011 - 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:i3FF58636EA85205F
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 conflicti619L → P in AAD40636 (PubMed:10347145).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

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DDBJi
Links Updated
AF126056 mRNA Translation: AAD40636.1
AJ252157 mRNA Translation: CAB86873.1
AK137629 mRNA Translation: BAE23437.1
AK154041 mRNA Translation: BAE32333.1
CH466530 Genomic DNA Translation: EDL35224.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS17343.1

NCBI Reference Sequences

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RefSeqi
NP_062713.2, NM_019739.3

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Mm.29891

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000053764; ENSMUSP00000055308; ENSMUSG00000044167

Database of genes from NCBI RefSeq genomes

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GeneIDi
56458

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:56458

UCSC genome browser

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UCSCi
uc008pei.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
AF126056 mRNA Translation: AAD40636.1
AJ252157 mRNA Translation: CAB86873.1
AK137629 mRNA Translation: BAE23437.1
AK154041 mRNA Translation: BAE32333.1
CH466530 Genomic DNA Translation: EDL35224.1
CCDSiCCDS17343.1
RefSeqiNP_062713.2, NM_019739.3
UniGeneiMm.29891

3D structure databases

ProteinModelPortaliQ9R1E0
SMRiQ9R1E0
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207997, 10 interactors
CORUMiQ9R1E0
IntActiQ9R1E0, 16 interactors
MINTiQ9R1E0
STRINGi10090.ENSMUSP00000055308

PTM databases

iPTMnetiQ9R1E0
PhosphoSitePlusiQ9R1E0
SwissPalmiQ9R1E0

Proteomic databases

EPDiQ9R1E0
MaxQBiQ9R1E0
PaxDbiQ9R1E0
PeptideAtlasiQ9R1E0
PRIDEiQ9R1E0

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
56458
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000053764; ENSMUSP00000055308; ENSMUSG00000044167
GeneIDi56458
KEGGimmu:56458
UCSCiuc008pei.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2308
MGIiMGI:1890077 Foxo1

Phylogenomic databases

eggNOGiKOG2294 Eukaryota
COG5025 LUCA
GeneTreeiENSGT00940000161558
HOGENOMiHOG000251635
HOVERGENiHBG057789
InParanoidiQ9R1E0
KOiK07201
OMAiKWPGSPN
OrthoDBiEOG091G06K3
TreeFamiTF315583

Enzyme and pathway databases

ReactomeiR-MMU-198693 AKT phosphorylates targets in the nucleus
R-MMU-211163 AKT-mediated inactivation of FOXO1A
R-MMU-5687128 MAPK6/MAPK4 signaling

Miscellaneous databases

Protein Ontology

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PROi
PR:Q9R1E0

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000044167 Expressed in 287 organ(s), highest expression level in female gonad
CleanExiMM_FOXO1
GenevisibleiQ9R1E0 MM

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

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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_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: Q9R1E0
Secondary accession number(s): Q9JJW4
<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: May 30, 2000
Last sequence update: July 27, 2011
Last modified: December 5, 2018
This is version 172 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

<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

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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