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Entry version 77 (07 Oct 2020)
Sequence version 1 (16 Nov 2011)
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Protein

Forkhead box protein O1

Gene

Foxo1

Organism
Rattus norvegicus (Rat)
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. Also acts as a key regulator of chondrogenic commitment of skeletal progenitor cells in response to lipid availability: when lipids levels are low, translocates to the nucleus and promotes expression of SOX9, which induces chondrogenic commitment and suppresses fatty acid oxidation. 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 (By similarity). Important regulator of cell death acting downstream of CDK1, PKB/AKT1 and STK4/MST1. Promotes neural cell death (By similarity). 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 (By similarity). Regulates the transcriptional activity of GADD45A and repair of nitric oxide-damaged DNA in beta-cells (By similarity). Required for the autophagic cell death induction in response to starvation or oxidative stress in a transcription-independent manner (By similarity). Mediates the function of MLIP in cardiomyocytes hypertrophy and cardiac remodeling (PubMed:26436652). Regulates endothelial cell (EC) viability and apoptosis in a PPIA/CYPA-dependent manner via transcription of CCL2 and BCL2L11 which are involved in EC chemotaxis and apoptosis (By similarity).By similarity1 Publication

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>Sitei152DNA bindingBy similarity1
Sitei159DNA bindingBy similarity1
Sitei219DNA bindingBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> 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 bindingi154 – 248Fork-headPROSITE-ProRule annotationAdd BLAST95

<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-RNO-198693, AKT phosphorylates targets in the nucleus
R-RNO-211163, AKT-mediated inactivation of FOXO1A
R-RNO-5687128, MAPK6/MAPK4 signaling
R-RNO-9614399, Regulation of localization of FOXO transcription factors
R-RNO-9617629, Regulation of FOXO transcriptional activity by acetylation
R-RNO-9617828, FOXO-mediated transcription of cell cycle genes

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
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%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Foxo1
Synonyms:Foxo1a
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 2
  • UP000234681 Componentsi: Chromosome 2, Unassembled WGS sequence

Organism-specific databases

Rat genome database

More...
RGDi
620283, 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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004192451 – 649Forkhead box protein O1Add BLAST649

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 SGK1By similarity1
Modified residuei206Phosphoserine; by STK4/MST1By similarity1
Modified residuei212PhosphoserineBy similarity1
Modified residuei228PhosphoserineBy similarity1
Modified residuei229PhosphoserineBy similarity1
Modified residuei239N6-acetyllysineBy similarity1
Modified residuei242N6-acetyllysineBy similarity1
Modified residuei243Phosphoserine; by CDK1By similarity1
Modified residuei245Omega-N-methylarginine; by PRMT1By similarity1
Modified residuei247Omega-N-methylarginine; by PRMT1By similarity1
Modified residuei250Phosphoserine; by PKB/AKT1 and SGK1By similarity1
Modified residuei256N6-acetyllysineBy similarity1
Modified residuei259N6-acetyllysineBy similarity1
Modified residuei268N6-acetyllysineBy similarity1
Modified residuei281PhosphoserineCombined sources1
Modified residuei292PhosphoserineBy similarity1
Modified residuei313Phosphoserine; by PKB/AKT1By similarity1
Modified residuei316Phosphoserine; by CK1 and SGK1By similarity1
Modified residuei319Phosphoserine; by CK1By similarity1
Modified residuei323PhosphoserineCombined sources1
Modified residuei327PhosphothreonineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylation by NLK promotes nuclear export and inhibits the transcriptional activity. In response to growth factors, phosphorylation on Thr-24, Ser-250 and Ser-313 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-250 decreases DNA-binding activity and promotes the phosphorylation of Thr-24 and Ser-313, permitting phosphorylation of Ser-316 and Ser-319, 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-323 is independent of IGF1 and leads to reduced function. Dephosphorylated on Thr-24 and Ser-250 by PP2A in beta-cells under oxidative stress leading to nuclear retention. Phosphorylation of Ser-243 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-206, upon oxidative stress, inhibits binding to 14-3-3 proteins and nuclear export (By similarity). PPIA/CYPA promotes its dephosphorylation on Ser-250 (By similarity).By similarity
Ubiquitinated by SKP2. Ubiquitination leads to proteasomal degradation (By similarity).By similarity
Methylation inhibits AKT1-mediated phosphorylation at Ser-250 and is increased by oxidative stress.By similarity
Acetylation at Lys-256 and Lys-268 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. 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-250. 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 (By similarity).By similarity

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
G3V7R4

PRoteomics IDEntifications database

More...
PRIDEi
G3V7R4

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
G3V7R4

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

More...
PhosphoSitePlusi
G3V7R4

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000013397, Expressed in female gonad and 21 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
G3V7R4, RN

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

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with 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-250 leading to its nuclear import.

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 (acetylated form) with PPARG.

Interacts with XBP1; this interaction is direct and leads to FOXO1 ubiquitination and degradation via the proteasome pathway (By similarity).

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).

Interacts with CRY1 (By similarity).

Interacts with PPIA/CYPA; the interaction promotes FOXO1 dephosphorylation, nuclear accumulation and transcriptional activity (By similarity).

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
249982, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000018244

<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

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

More...
SMRi
G3V7R4

Database of comparative protein structure models

More...
ModBasei
Search...

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

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>Regioni205 – 212DNA bindingBy similarity8
Regioni228 – 231DNA bindingBy similarity4
Regioni277 – 557Sufficient for interaction with NLKBy similarityAdd BLAST281
Regioni357 – 453Required 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>Motifi245 – 247Nuclear localization signalBy similarity3
Motifi456 – 460Required 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 biasi89 – 96Poly-Ala8
Compositional biasi116 – 143Pro-richAdd BLAST28

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG2294, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000161558

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_023456_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
G3V7R4

KEGG Orthology (KO)

More...
KOi
K07201

Identification of Orthologs from Complete Genome Data

More...
OMAi
YSKWPGS

Database of Orthologous Groups

More...
OrthoDBi
1160384at2759

TreeFam database of animal gene trees

More...
TreeFami
TF315583

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00059, FH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...
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

More...
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%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

G3V7R4-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAEAPQVVET DPDFEPLPRQ RSCTWPLPRP EFNQSNSTTS SPAPSGSTAA
60 70 80 90 100
NPDATASLAS ASAVSTDFMS NLSLLEESED FARAPGCVAV AAAAAASRGL
110 120 130 140 150
CGDFQGPEAG CVHSAPPQPP PTGPLSQPPP VPPAAAGPLA GQPRKTSSSR
160 170 180 190 200
RNAWGNLSYA DLITKAIESS AEKRLTLSQI YEWMVKSVPY FKDKGDSNSS
210 220 230 240 250
AGWKNSIRHN LSLHSKFIRV QNEGTGKSSW WMLNPEGGKS GKSPRRRAAS
260 270 280 290 300
MDNNSKFAKS RGRAAKKKAS LQSGQEGPGD SPGSQFSKWP ASPGSHSNDD
310 320 330 340 350
FDNWSTFRPR TSSNASTISG RLSPIMTEQD DLGDGDVHSL VYPPSAAKMA
360 370 380 390 400
STLPSLSEIS NPENMENLLD NLNLLSSPTS LTVSTQSSPG SMMQQTPCYS
410 420 430 440 450
FAPPNTSLNS PSPNYAKYTY GQSSMSPVPQ MPMQTLQDSK SSYGGLNQYN
460 470 480 490 500
CAPGLLKELL TSDSPPHNDI MSPVDPGVAQ PNSRVLGQNV LMGPNSVMPA
510 520 530 540 550
YGSQAPHNKM MNPSSHTHPG HAQQTSSVNG RALPHVVNTM PHTSAMNRLT
560 570 580 590 600
PVKTPLQVPL SHPMQMSALG NYSSVSSCNG YGRMGVLHQE KLPSDLDGMF
610 620 630 640
IERLDCDMES IIRNDLMDGD TLDFNFDNVL PNQSFPHSVK TTTHSWVSG
Length:649
Mass (Da):69,344
Last modified:November 16, 2011 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i6232AA82C12F5AEA
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
CH474003 Genomic DNA Translation: EDM14970.1

NCBI Reference Sequences

More...
RefSeqi
NP_001178775.1, NM_001191846.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000018244; ENSRNOP00000018244; ENSRNOG00000013397

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
84482

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:84482

<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
CH474003 Genomic DNA Translation: EDM14970.1
RefSeqiNP_001178775.1, NM_001191846.2

3D structure databases

SMRiG3V7R4
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi249982, 3 interactors
STRINGi10116.ENSRNOP00000018244

PTM databases

iPTMnetiG3V7R4
PhosphoSitePlusiG3V7R4

Proteomic databases

PaxDbiG3V7R4
PRIDEiG3V7R4

Genome annotation databases

EnsembliENSRNOT00000018244; ENSRNOP00000018244; ENSRNOG00000013397
GeneIDi84482
KEGGirno:84482

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
2308
RGDi620283, Foxo1

Phylogenomic databases

eggNOGiKOG2294, Eukaryota
GeneTreeiENSGT00940000161558
HOGENOMiCLU_023456_1_1_1
InParanoidiG3V7R4
KOiK07201
OMAiYSKWPGS
OrthoDBi1160384at2759
TreeFamiTF315583

Enzyme and pathway databases

ReactomeiR-RNO-198693, AKT phosphorylates targets in the nucleus
R-RNO-211163, AKT-mediated inactivation of FOXO1A
R-RNO-5687128, MAPK6/MAPK4 signaling
R-RNO-9614399, Regulation of localization of FOXO transcription factors
R-RNO-9617629, Regulation of FOXO transcriptional activity by acetylation
R-RNO-9617828, FOXO-mediated transcription of cell cycle genes

Miscellaneous databases

Protein Ontology

More...
PROi
PR:G3V7R4

Gene expression databases

BgeeiENSRNOG00000013397, Expressed in female gonad and 21 other tissues
GenevisibleiG3V7R4, RN

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
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MobiDB: a database of protein disorder and mobility annotations

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

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOXO1_RAT
<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: G3V7R4
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 3, 2012
Last sequence update: November 16, 2011
Last modified: October 7, 2020
This is version 77 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

Reference proteome
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