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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-Experimental evidence at protein leveli

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 SKT4/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.By similarity8 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei158DNA-binding1
Sitei165DNA-binding1
Sitei225DNA-binding1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi159 – 235Fork-headPROSITE-ProRule annotationAdd BLAST77

GO - Molecular functioni

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • autophagy Source: UniProtKB-KW
  • blood vessel development Source: Ensembl
  • cellular glucose homeostasis Source: UniProtKB
  • cellular response to cold Source: UniProtKB
  • cellular response to dexamethasone stimulus Source: Ensembl
  • cellular response to DNA damage stimulus Source: UniProtKB
  • cellular response to hydrogen peroxide Source: Ensembl
  • cellular response to hyperoxia Source: UniProtKB
  • cellular response to insulin stimulus Source: UniProtKB
  • cellular response to nitric oxide Source: UniProtKB
  • cellular response to oxidative stress Source: UniProtKB
  • cellular response to starvation Source: UniProtKB
  • enamel mineralization Source: Ensembl
  • endocrine pancreas development Source: Reactome
  • fat cell differentiation Source: UniProtKB
  • insulin receptor signaling pathway Source: UniProtKB
  • negative regulation of apoptotic process Source: UniProtKB
  • negative regulation of canonical Wnt signaling pathway Source: Ensembl
  • negative regulation of fat cell differentiation Source: UniProtKB
  • negative regulation of stress-activated MAPK cascade Source: BHF-UCL
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • neuronal stem cell population maintenance Source: Ensembl
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of autophagy Source: UniProtKB
  • positive regulation of gluconeogenesis Source: Ensembl
  • positive regulation of protein catabolic process Source: UniProtKB
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  • protein acetylation Source: UniProtKB
  • regulation of energy homeostasis Source: UniProtKB
  • regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • regulation of neural precursor cell proliferation Source: Ensembl
  • regulation of reactive oxygen species metabolic process Source: Ensembl
  • response to fluoride Source: Ensembl
  • temperature homeostasis Source: UniProtKB
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Autophagy, Differentiation, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000150907-MONOMER.
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.
SignaLinkiQ12778.
SIGNORiQ12778.

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein O1
Alternative name(s):
Forkhead box protein O1A
Forkhead in rhabdomyosarcoma
Gene namesi
Name:FOXO1
Synonyms:FKHR, FOXO1A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 13

Organism-specific databases

HGNCiHGNC:3819. FOXO1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity

  • Note: Shuttles between the cytoplasm and nucleus. Largely nuclear in unstimulated cells. In osteoblasts, colocalizes with ATF4 and RUNX2 in the nucleus (By similarity). Insulin-induced phosphorylation at Ser-256 by PKB/AKT1 leads, via stimulation of Thr-24 phosphorylation, to binding of 14-3-3 proteins and nuclear export to the cytoplasm where it is degraded by the ubiquitin-proteosomal pathway. Phosphorylation at Ser-249 by CDK1 disrupts binding of 14-3-3 proteins and promotes nuclear accumulation. Phosphorylation by NLK results in nuclear export. Translocates to the nucleus upon oxidative stress-induced phosphorylation at Ser-212 by STK4/MST1. SGK1-mediated phosphorylation also results in nuclear translocation. Retained in the nucleus under stress stimuli including oxidative stress, nutrient deprivation or nitric oxide. Retained in the nucleus on methylation.By similarity

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: UniProtKB
  • mitochondrion Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

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
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

DisGeNETi2308.
MalaCardsiFOXO1.
MIMi268220. phenotype.
OpenTargetsiENSG00000150907.
Orphaneti99756. Alveolar rhabdomyosarcoma.
PharmGKBiPA28237.

Chemistry databases

ChEMBLiCHEMBL5294.

Polymorphism and mutation databases

BioMutaiFOXO1.
DMDMi116241368.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000918721 – 655Forkhead box protein O1Add BLAST655

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

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

EPDiQ12778.
MaxQBiQ12778.
PaxDbiQ12778.
PeptideAtlasiQ12778.
PRIDEiQ12778.

PTM databases

iPTMnetiQ12778.
PhosphoSitePlusiQ12778.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

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

BgeeiENSG00000150907.
CleanExiHS_FOXO1.
GenevisibleiQ12778. HS.

Organism-specific databases

HPAiCAB022326.
HPA001252.

Interactioni

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

Binary interactionsi

WithEntry#Exp.IntActNotes
CCNB1P146352EBI-1108782,EBI-495332
CDK1P064935EBI-1108782,EBI-444308
CREBBPQ927933EBI-1108782,EBI-81215
ESR1P033722EBI-1108782,EBI-78473
FHL2Q141928EBI-1108782,EBI-701903
SETQ011055EBI-1108782,EBI-1053182
SIRT1Q96EB63EBI-1108782,EBI-1802965
Sirt1Q923E42EBI-1108782,EBI-1802585From a different organism.

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • protein phosphatase 2A binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108597. 55 interactors.
DIPiDIP-35654N.
IntActiQ12778. 30 interactors.
STRINGi9606.ENSP00000368880.

Chemistry databases

BindingDBiQ12778.

Structurei

Secondary structure

1655
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi156 – 158Combined sources3
Helixi165 – 175Combined sources11
Beta strandi176 – 181Combined sources6
Helixi183 – 193Combined sources11
Helixi195 – 197Combined sources3
Helixi203 – 219Combined sources17
Beta strandi223 – 226Combined sources4
Turni230 – 232Combined sources3
Beta strandi236 – 239Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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...

Miscellaneous databases

EvolutionaryTraceiQ12778.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Motifi251 – 253Nuclear localization signal3
Motifi462 – 466Required for interaction with SIRT1By similarity5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi91 – 102Poly-AlaAdd BLAST12
Compositional biasi120 – 130Poly-ProAdd BLAST11
Compositional biasi152 – 155Poly-Ser4

Sequence similaritiesi

Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2294. Eukaryota.
COG5025. LUCA.
GeneTreeiENSGT00790000123003.
HOGENOMiHOG000251635.
HOVERGENiHBG057789.
InParanoidiQ12778.
KOiK07201.
OMAiKWPGSPN.
OrthoDBiEOG091G06K3.
PhylomeDBiQ12778.
TreeFamiTF315583.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. Fork_head_dom.
IPR032067. FOXO-TAD.
IPR032068. FOXO_KIX-bd.
IPR030456. TF_fork_head_CS_2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Forkhead. 1 hit.
PF16676. FOXO-TAD. 1 hit.
PF16675. FOXO_KIX_bdg. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

Sequencei

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
Checksum:i6DEF6C994BDFDBAB
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti131L → V in AAA03629 (PubMed:8275086).Curated1
Sequence conflicti343V → M in AAH70065 (PubMed:15489334).Curated1

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, AL133318 Genomic DNA. Translation: CAH70978.1.
AL133318, AL355132 Genomic DNA. Translation: CAI16970.1.
BC021981 mRNA. Translation: AAH21981.1.
BC070065 mRNA. Translation: AAH70065.3.
CCDSiCCDS9371.1.
PIRiS40521.
RefSeqiNP_002006.2. NM_002015.3.
UniGeneiHs.370666.

Genome annotation databases

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

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

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, AL133318 Genomic DNA. Translation: CAH70978.1.
AL133318, AL355132 Genomic DNA. Translation: CAI16970.1.
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:
PDBei
RCSB PDBi
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. 55 interactors.
DIPiDIP-35654N.
IntActiQ12778. 30 interactors.
STRINGi9606.ENSP00000368880.

Chemistry databases

BindingDBiQ12778.
ChEMBLiCHEMBL5294.

PTM databases

iPTMnetiQ12778.
PhosphoSitePlusiQ12778.

Polymorphism and mutation databases

BioMutaiFOXO1.
DMDMi116241368.

Proteomic databases

EPDiQ12778.
MaxQBiQ12778.
PaxDbiQ12778.
PeptideAtlasiQ12778.
PRIDEiQ12778.

Protocols and materials databases

DNASUi2308.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi2308.
DisGeNETi2308.
GeneCardsiFOXO1.
HGNCiHGNC:3819. FOXO1.
HPAiCAB022326.
HPA001252.
MalaCardsiFOXO1.
MIMi136533. gene.
268220. phenotype.
neXtProtiNX_Q12778.
OpenTargetsiENSG00000150907.
Orphaneti99756. Alveolar rhabdomyosarcoma.
PharmGKBiPA28237.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2294. Eukaryota.
COG5025. LUCA.
GeneTreeiENSGT00790000123003.
HOGENOMiHOG000251635.
HOVERGENiHBG057789.
InParanoidiQ12778.
KOiK07201.
OMAiKWPGSPN.
OrthoDBiEOG091G06K3.
PhylomeDBiQ12778.
TreeFamiTF315583.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000150907-MONOMER.
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.
SignaLinkiQ12778.
SIGNORiQ12778.

Miscellaneous databases

ChiTaRSiFOXO1. human.
EvolutionaryTraceiQ12778.
GeneWikiiFOXO1.
GenomeRNAii2308.
PROiQ12778.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000150907.
CleanExiHS_FOXO1.
GenevisibleiQ12778. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. Fork_head_dom.
IPR032067. FOXO-TAD.
IPR032068. FOXO_KIX-bd.
IPR030456. TF_fork_head_CS_2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Forkhead. 1 hit.
PF16676. FOXO-TAD. 1 hit.
PF16675. FOXO_KIX_bdg. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFOXO1_HUMAN
AccessioniPrimary (citable) accession number: Q12778
Secondary accession number(s): O43523, Q5VYC7, Q6NSK6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: October 17, 2006
Last modified: November 30, 2016
This is version 180 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.