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Forkhead box protein O1 (Forkhead box protein O1A) (Forkhead in rhabdomyosarcoma)

 FOXO1_HUMAN             Reviewed;         655 AA.
Q12778; O43523; Q5VYC7; Q6NSK6;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
25-OCT-2017, entry version 188.
RecName: Full=Forkhead box protein O1;
AltName: Full=Forkhead box protein O1A;
AltName: Full=Forkhead in rhabdomyosarcoma;
Name=FOXO1; Synonyms=FKHR, FOXO1A;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND CHROMOSOMAL TRANSLOCATION WITH PAX3.
PubMed=8275086; DOI=10.1038/ng1193-230;
Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S.,
Rauscher F.J. III, Emanuel B.S., Rovera G., Barr F.G.;
"Fusion of a fork head domain gene to PAX3 in the solid tumour
alveolar rhabdomyosarcoma.";
Nat. Genet. 5:230-235(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
TISSUE=Rhabdomyosarcoma;
PubMed=9479491; DOI=10.1006/geno.1997.5122;
Anderson M.J., Viars C.S., Czekay S., Cavenee W.K., Arden K.C.;
"Cloning and characterization of three human forkhead genes that
comprise an FKHR-like gene subfamily.";
Genomics 47:187-199(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057823; DOI=10.1038/nature02379;
Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L.,
Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E.,
Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E.,
Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T.,
Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R.,
Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S.,
Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P.,
Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M.,
Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J.,
Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E.,
Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L.,
Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J.,
Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S.,
Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J.,
Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M.,
King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A.,
Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S.,
Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S.,
Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S.,
Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A.,
Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L.,
Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M.,
Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T.;
"The DNA sequence and analysis of human chromosome 13.";
Nature 428:522-528(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lymph, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
CHROMOSOMAL TRANSLOCATION WITH PAX7.
PubMed=8187070;
Davis R.J., D'Cruz C.M., Lovell M.A., Biegel J.A., Barr F.G.;
"Fusion of PAX7 to FKHR by the variant t(1;13)(p36;q14) translocation
in alveolar rhabdomyosarcoma.";
Cancer Res. 54:2869-2872(1994).
[7]
PHOSPHORYLATION AT THR-24; SER-256 AND SER-319.
PubMed=10358075; DOI=10.1074/jbc.274.24.17179;
Rena G., Guo S., Cichy S.C., Unterman T.G., Cohen P.;
"Phosphorylation of the transcription factor forkhead family member
FKHR by protein kinase B.";
J. Biol. Chem. 274:17179-17183(1999).
[8]
DNA-BINDING, PHOSPHORYLATION AT SER-256, AND FUNCTION.
PubMed=10358076; DOI=10.1074/jbc.274.24.17184;
Guo S., Rena G., Cichy S., He X., Cohen P., Unterman T.;
"Phosphorylation of serine 256 by protein kinase B disrupts
transactivation by FKHR and mediates effects of insulin on insulin-
like growth factor-binding protein-1 promoter activity through a
conserved insulin response sequence.";
J. Biol. Chem. 274:17184-17192(1999).
[9]
SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-329, AND MUTAGENESIS OF
SER-329.
PubMed=11311120;
Woods Y.L., Rena G., Morrice N., Barthel A., Becker W., Guo S.,
Unterman T.G., Cohen P.;
"The kinase DYRK1A phosphorylates the transcription factor FKHR at
Ser329 in vitro, a novel in vivo phosphorylation site.";
Biochem. J. 355:597-607(2001).
[10]
INTERACTION WITH YWHAG AND YWHAZ, PHOSPHORYLATION AT THR-24; SER-256
AND SER-319, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-24; SER-256
AND SER-319.
PubMed=11237865; DOI=10.1042/0264-6021:3540605;
Rena G., Prescott A.R., Guo S., Cohen P., Unterman T.G.;
"Roles of the forkhead in rhabdomyosarcoma (FKHR) phosphorylation
sites in regulating 14-3-3 binding, transactivation and nuclear
targetting.";
Biochem. J. 354:605-612(2001).
[11]
PHOSPHORYLATION AT THR-24; SER-256; SER-319; SER-322; SER-325 AND
SER-329.
PubMed=11980723; DOI=10.1093/emboj/21.9.2263;
Rena G., Woods Y.L., Prescott A.R., Peggie M., Unterman T.G.,
Williams M.R., Cohen P.;
"Two novel phosphorylation sites on FKHR that are critical for its
nuclear exclusion.";
EMBO J. 21:2263-2271(2002).
[12]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF THR-24; SER-256 AND
SER-319.
PubMed=12228231; DOI=10.1074/jbc.M208063200;
Zhang X., Gan L., Pan H., Guo S., He X., Olson S.T., Mesecar A.,
Adam S., Unterman T.G.;
"Phosphorylation of serine 256 suppresses transactivation by FKHR
(FOXO1) by multiple mechanisms. Direct and indirect effects on
nuclear/cytoplasmic shuttling and DNA binding.";
J. Biol. Chem. 277:45276-45284(2002).
[13]
INTERACTION WITH CREBBP AND SIRT1, ACETYLATION, DEACETYLATION, AND
FUNCTION.
PubMed=15220471; DOI=10.1073/pnas.0400593101;
Daitoku H., Hatta M., Matsuzaki H., Aratani S., Ohshima T.,
Miyagishi M., Nakajima T., Fukamizu A.;
"Silent information regulator 2 potentiates Foxo1-mediated
transcription through its deacetylase activity.";
Proc. Natl. Acad. Sci. U.S.A. 101:10042-10047(2004).
[14]
INTERACTION WITH EP300, ACETYLATION, SUBCELLULAR LOCATION,
PHOSPHORYLATION, AND FUNCTION.
PubMed=15890677; DOI=10.1210/me.2004-0292;
Perrot V., Rechler M.M.;
"The coactivator p300 directly acetylates the forkhead transcription
factor Foxo1 and stimulates Foxo1-induced transcription.";
Mol. Endocrinol. 19:2283-2298(2005).
[15]
INTERACTION WITH SKP2, UBIQUITINATION, AND MUTAGENESIS OF SER-256.
PubMed=15668399; DOI=10.1073/pnas.0406789102;
Huang H., Regan K.M., Wang F., Wang D., Smith D.I., van Deursen J.M.,
Tindall D.J.;
"Skp2 inhibits FOXO1 in tumor suppression through ubiquitin-mediated
degradation.";
Proc. Natl. Acad. Sci. U.S.A. 102:1649-1654(2005).
[16]
INTERACTION WITH PRMT1.
PubMed=18951090; DOI=10.1016/j.molcel.2008.09.013;
Yamagata K., Daitoku H., Takahashi Y., Namiki K., Hisatake K.,
Kako K., Mukai H., Kasuya Y., Fukamizu A.;
"Arginine methylation of FOXO transcription factors inhibits their
phosphorylation by Akt.";
Mol. Cell 32:221-231(2008).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[18]
FUNCTION, PHOSPHORYLATION AT SER-249 BY CDK1, INTERACTION WITH CDK1
AND 14-3-3 PROTEINS, AND MUTAGENESIS OF SER-249.
PubMed=18356527; DOI=10.1126/science.1152337;
Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y.,
Schaefer E.M., Bonni A.;
"Activation of FOXO1 by Cdk1 in cycling cells and postmitotic
neurons.";
Science 319:1665-1668(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
PHOSPHORYLATION AT SER-212, SUBCELLULAR LOCATION, FUNCTION, AND
MUTAGENESIS OF SER-212.
PubMed=19221179; DOI=10.1074/jbc.M900461200;
Yuan Z., Lehtinen M.K., Merlo P., Villen J., Gygi S., Bonni A.;
"Regulation of neuronal cell death by MST1-FOXO1 signaling.";
J. Biol. Chem. 284:11285-11292(2009).
[21]
ACETYLATION AT LYS-262; LYS-265 AND LYS-274, DEACETYLATION BY SIRT2,
FUNCTION IN AUTOPHAGY, AND INTERACTION WITH SIRT2 AND ATG7.
PubMed=20543840; DOI=10.1038/ncb2069;
Zhao Y., Yang J., Liao W., Liu X., Zhang H., Wang S., Wang D.,
Feng J., Yu L., Zhu W.G.;
"Cytosolic FoxO1 is essential for the induction of autophagy and
tumour suppressor activity.";
Nat. Cell Biol. 12:665-675(2010).
[22]
INDUCTION.
PubMed=20668652; DOI=10.1371/journal.pone.0011786;
Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P.,
Retta S.F.;
"KRIT1 regulates the homeostasis of intracellular reactive oxygen
species.";
PLoS ONE 5:E11786-E11786(2010).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[24]
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION AT SER-212.
PubMed=21245099; DOI=10.1158/0008-5472.CAN-10-2203;
Valis K., Prochazka L., Boura E., Chladova J., Obsil T., Rohlena J.,
Truksa J., Dong L.F., Ralph S.J., Neuzil J.;
"Hippo/Mst1 stimulates transcription of the proapoptotic mediator NOXA
in a FoxO1-dependent manner.";
Cancer Res. 71:946-954(2011).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[27]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 151-266, DNA-BINDING,
PHOSPHORYLATION AT SER-212; SER-218; SER-234 AND SER-235, ACETYLATION,
IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF SER-249.
PubMed=18786403; DOI=10.1016/j.str.2008.06.013;
Brent M.M., Anand R., Marmorstein R.;
"Structural basis for DNA recognition by FoxO1 and its regulation by
posttranslational modification.";
Structure 16:1407-1416(2008).
-!- FUNCTION: 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. Mediates the function of MLIP in
cardiomyocytes hypertrophy and cardiac remodeling (By similarity).
{ECO:0000250|UniProtKB:G3V7R4, ECO:0000250|UniProtKB:Q9R1E0,
ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:12228231,
ECO:0000269|PubMed:15220471, ECO:0000269|PubMed:15890677,
ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:19221179,
ECO:0000269|PubMed:20543840, ECO:0000269|PubMed:21245099}.
-!- SUBUNIT: 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). {ECO:0000250|UniProtKB:Q9R1E0,
ECO:0000269|PubMed:11237865, ECO:0000269|PubMed:15220471,
ECO:0000269|PubMed:15668399, ECO:0000269|PubMed:15890677,
ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:18951090,
ECO:0000269|PubMed:20543840}.
-!- INTERACTION:
P31749:AKT1; NbExp=2; IntAct=EBI-1108782, EBI-296087;
P14635:CCNB1; NbExp=2; IntAct=EBI-1108782, EBI-495332;
P06493:CDK1; NbExp=5; IntAct=EBI-1108782, EBI-444308;
Q92793:CREBBP; NbExp=3; IntAct=EBI-1108782, EBI-81215;
P03372:ESR1; NbExp=2; IntAct=EBI-1108782, EBI-78473;
Q14192:FHL2; NbExp=8; IntAct=EBI-1108782, EBI-701903;
Q01105:SET; NbExp=5; IntAct=EBI-1108782, EBI-1053182;
Q96EB6:SIRT1; NbExp=4; IntAct=EBI-1108782, EBI-1802965;
Q923E4:Sirt1 (xeno); NbExp=2; IntAct=EBI-1108782, EBI-1802585;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9R1E0}.
Nucleus {ECO:0000250|UniProtKB:Q9R1E0}. 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. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9479491}.
-!- INDUCTION: Expression is regulated by KRIT1. Levels of expression
also regulated by FOXC1 which binds to a conserved element in the
FOXO1 promoter. {ECO:0000269|PubMed:20668652}.
-!- PTM: 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.
{ECO:0000250, ECO:0000269|PubMed:10358075,
ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:11311120, ECO:0000269|PubMed:11980723,
ECO:0000269|PubMed:18356527, ECO:0000269|PubMed:18786403,
ECO:0000269|PubMed:19221179, ECO:0000269|PubMed:21245099}.
-!- PTM: 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. {ECO:0000269|PubMed:20543840}.
-!- PTM: Ubiquitinated by SRT2. Ubiquitination leads to proteasomal
degradation. {ECO:0000269|PubMed:15668399}.
-!- PTM: Methylation inhibits AKT1-mediated phosphorylation at Ser-256
and is increased by oxidative stress. {ECO:0000250}.
-!- PTM: 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. {ECO:0000269|PubMed:10358075,
ECO:0000269|PubMed:10358076, ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:11980723}.
-!- DISEASE: Rhabdomyosarcoma 2 (RMS2) [MIM:268220]: A 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. Note=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.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FOXO1ID83ch13q14.html";
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EMBL; U02310; AAA03629.1; -; mRNA.
EMBL; AF032885; AAC39591.1; -; mRNA.
EMBL; BT007455; AAP36123.1; -; mRNA.
EMBL; AL355132; CAH70978.1; -; Genomic_DNA.
EMBL; AL133318; CAH70978.1; JOINED; Genomic_DNA.
EMBL; AL133318; CAI16970.1; -; Genomic_DNA.
EMBL; AL355132; CAI16970.1; JOINED; Genomic_DNA.
EMBL; BC021981; AAH21981.1; -; mRNA.
EMBL; BC070065; AAH70065.3; -; mRNA.
CCDS; CCDS9371.1; -.
PIR; S40521; S40521.
RefSeq; NP_002006.2; NM_002015.3.
UniGene; Hs.370666; -.
PDB; 3CO6; X-ray; 2.10 A; C=151-249.
PDB; 3CO7; X-ray; 2.91 A; C/F=151-266.
PDB; 3COA; X-ray; 2.20 A; C/F=151-266.
PDB; 4LG0; X-ray; 2.19 A; A=143-270.
PDB; 5DUI; X-ray; 2.31 A; A/B=151-259.
PDBsum; 3CO6; -.
PDBsum; 3CO7; -.
PDBsum; 3COA; -.
PDBsum; 4LG0; -.
PDBsum; 5DUI; -.
ProteinModelPortal; Q12778; -.
SMR; Q12778; -.
BioGrid; 108597; 58.
CORUM; Q12778; -.
DIP; DIP-35654N; -.
IntAct; Q12778; 31.
STRING; 9606.ENSP00000368880; -.
BindingDB; Q12778; -.
ChEMBL; CHEMBL5294; -.
iPTMnet; Q12778; -.
PhosphoSitePlus; Q12778; -.
BioMuta; FOXO1; -.
DMDM; 116241368; -.
EPD; Q12778; -.
MaxQB; Q12778; -.
PaxDb; Q12778; -.
PeptideAtlas; Q12778; -.
PRIDE; Q12778; -.
DNASU; 2308; -.
Ensembl; ENST00000379561; ENSP00000368880; ENSG00000150907.
GeneID; 2308; -.
KEGG; hsa:2308; -.
UCSC; uc001uxl.5; human.
CTD; 2308; -.
DisGeNET; 2308; -.
EuPathDB; HostDB:ENSG00000150907.6; -.
GeneCards; FOXO1; -.
HGNC; HGNC:3819; FOXO1.
HPA; CAB022326; -.
HPA; HPA001252; -.
MalaCards; FOXO1; -.
MIM; 136533; gene.
MIM; 268220; phenotype.
neXtProt; NX_Q12778; -.
OpenTargets; ENSG00000150907; -.
Orphanet; 99756; Alveolar rhabdomyosarcoma.
PharmGKB; PA28237; -.
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00790000123003; -.
HOGENOM; HOG000251635; -.
HOVERGEN; HBG057789; -.
InParanoid; Q12778; -.
KO; K07201; -.
OMA; KWPGSPN; -.
OrthoDB; EOG091G06K3; -.
PhylomeDB; Q12778; -.
TreeFam; TF315583; -.
Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-HSA-210745; Regulation of gene expression in beta cells.
Reactome; R-HSA-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
Reactome; R-HSA-6785807; Interleukin-4 and 13 signaling.
SignaLink; Q12778; -.
SIGNOR; Q12778; -.
ChiTaRS; FOXO1; human.
EvolutionaryTrace; Q12778; -.
GeneWiki; FOXO1; -.
GenomeRNAi; 2308; -.
PRO; PR:Q12778; -.
Proteomes; UP000005640; Chromosome 13.
Bgee; ENSG00000150907; -.
CleanEx; HS_FOXO1; -.
Genevisible; Q12778; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISS:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IDA:ParkinsonsUK-UCL.
GO; GO:0003682; F:chromatin binding; ISS:UniProtKB.
GO; GO:0051721; F:protein phosphatase 2A binding; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001223; F:transcription coactivator binding; IEA:Ensembl.
GO; GO:0000989; F:transcription factor activity, transcription factor binding; IEA:Ensembl.
GO; GO:0001078; F:transcriptional repressor activity, RNA polymerase II core promoter proximal region sequence-specific binding; IEA:Ensembl.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
GO; GO:0001568; P:blood vessel development; IEA:Ensembl.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0001678; P:cellular glucose homeostasis; ISS:UniProtKB.
GO; GO:0070417; P:cellular response to cold; ISS:UniProtKB.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
GO; GO:0070301; P:cellular response to hydrogen peroxide; IEA:Ensembl.
GO; GO:0071455; P:cellular response to hyperoxia; IDA:UniProtKB.
GO; GO:0032869; P:cellular response to insulin stimulus; ISS:UniProtKB.
GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; ISS:UniProtKB.
GO; GO:0009267; P:cellular response to starvation; IDA:UniProtKB.
GO; GO:0070166; P:enamel mineralization; IEA:Ensembl.
GO; GO:0031018; P:endocrine pancreas development; TAS:Reactome.
GO; GO:0045444; P:fat cell differentiation; ISS:UniProtKB.
GO; GO:0008286; P:insulin receptor signaling pathway; ISS:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:1903243; P:negative regulation of cardiac muscle hypertrophy in response to stress; ISS:UniProtKB.
GO; GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
GO; GO:0032873; P:negative regulation of stress-activated MAPK cascade; IDA:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISS:UniProtKB.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0010508; P:positive regulation of autophagy; IMP:UniProtKB.
GO; GO:0045722; P:positive regulation of gluconeogenesis; IEA:Ensembl.
GO; GO:0045732; P:positive regulation of protein catabolic process; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006473; P:protein acetylation; ISS:UniProtKB.
GO; GO:2000505; P:regulation of energy homeostasis; ISS:UniProtKB.
GO; GO:0035947; P:regulation of gluconeogenesis by regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IEA:Ensembl.
GO; GO:1902617; P:response to fluoride; IEA:Ensembl.
GO; GO:0001659; P:temperature homeostasis; ISS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00059; FH; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR001766; Fork_head_dom.
InterPro; IPR032067; FOXO-TAD.
InterPro; IPR032068; FOXO_KIX-bd.
InterPro; IPR030456; TF_fork_head_CS_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00250; Forkhead; 1.
Pfam; PF16676; FOXO-TAD; 1.
Pfam; PF16675; FOXO_KIX_bdg; 1.
PRINTS; PR00053; FORKHEAD.
SMART; SM00339; FH; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00658; FORK_HEAD_2; 1.
PROSITE; PS50039; FORK_HEAD_3; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Apoptosis; Autophagy;
Chromosomal rearrangement; Complete proteome; Cytoplasm;
Differentiation; DNA-binding; Methylation; Nucleus; Phosphoprotein;
Proto-oncogene; Reference proteome; Transcription;
Transcription regulation; Ubl conjugation.
CHAIN 1 655 Forkhead box protein O1.
/FTId=PRO_0000091872.
DNA_BIND 159 235 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
REGION 211 218 DNA-binding.
REGION 234 237 DNA-binding.
REGION 283 563 Sufficient for interaction with NLK.
{ECO:0000250}.
REGION 363 459 Required for interaction with RUNX2.
{ECO:0000250}.
MOTIF 251 253 Nuclear localization signal.
MOTIF 462 466 Required for interaction with SIRT1.
{ECO:0000250}.
COMPBIAS 91 102 Poly-Ala.
COMPBIAS 120 130 Poly-Pro.
COMPBIAS 152 155 Poly-Ser.
SITE 158 158 DNA-binding.
SITE 165 165 DNA-binding.
SITE 225 225 DNA-binding.
MOD_RES 24 24 Phosphothreonine; by PKB/AKT1 or PKB/AKT2
and SGK1. {ECO:0000269|PubMed:10358075,
ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:11980723}.
MOD_RES 212 212 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:18786403,
ECO:0000269|PubMed:19221179,
ECO:0000269|PubMed:21245099}.
MOD_RES 218 218 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:18786403}.
MOD_RES 234 234 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:18786403}.
MOD_RES 235 235 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:18786403}.
MOD_RES 245 245 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9R1E0}.
MOD_RES 248 248 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9R1E0}.
MOD_RES 249 249 Phosphoserine; by CDK1.
{ECO:0000269|PubMed:18356527}.
MOD_RES 251 251 Omega-N-methylarginine; by PRMT1.
{ECO:0000250|UniProtKB:Q9R1E0}.
MOD_RES 253 253 Omega-N-methylarginine; by PRMT1.
{ECO:0000250|UniProtKB:Q9R1E0}.
MOD_RES 256 256 Phosphoserine; by PKB/AKT1 and SGK1.
{ECO:0000269|PubMed:10358075,
ECO:0000269|PubMed:10358076,
ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:11980723}.
MOD_RES 262 262 N6-acetyllysine.
{ECO:0000269|PubMed:20543840}.
MOD_RES 265 265 N6-acetyllysine.
{ECO:0000269|PubMed:20543840}.
MOD_RES 274 274 N6-acetyllysine.
{ECO:0000269|PubMed:20543840}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000250|UniProtKB:Q9R1E0}.
MOD_RES 319 319 Phosphoserine; by PKB/AKT1.
{ECO:0000269|PubMed:10358075,
ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:11980723}.
MOD_RES 322 322 Phosphoserine; by CK1 and SGK1.
{ECO:0000269|PubMed:11980723}.
MOD_RES 325 325 Phosphoserine; by CK1.
{ECO:0000269|PubMed:11980723}.
MOD_RES 329 329 Phosphoserine; by DYRK1A.
{ECO:0000269|PubMed:11311120,
ECO:0000269|PubMed:11980723}.
MOD_RES 333 333 Phosphothreonine.
{ECO:0000250|UniProtKB:Q9R1E0}.
MUTAGEN 24 24 T->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. {ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:12228231}.
MUTAGEN 212 212 S->A: Abolishes STK4/MST1-mediated
phosphorylation.
{ECO:0000269|PubMed:19221179}.
MUTAGEN 245 245 K->A: Disrupts DNA-binding; when
associated with A-248.
MUTAGEN 248 248 K->A: Disrupts DNA-binding; when
associated with A-245.
MUTAGEN 249 249 S->A: Impaired phosphorylation by CDK1.
{ECO:0000269|PubMed:18356527,
ECO:0000269|PubMed:18786403}.
MUTAGEN 249 249 S->E: No effect on DNA-binding.
{ECO:0000269|PubMed:18356527,
ECO:0000269|PubMed:18786403}.
MUTAGEN 251 253 RRR->SAS: No targeting to the nucleus and
disruption of DNA-binding.
MUTAGEN 256 256 S->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.
{ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:12228231,
ECO:0000269|PubMed:15668399}.
MUTAGEN 256 256 S->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.
{ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:12228231,
ECO:0000269|PubMed:15668399}.
MUTAGEN 262 262 K->R: Inhibits interaction with ATG7 and
FOXO1-acetylation-induced autophagic cell
death; when associated with R-265 and R-
274.
MUTAGEN 265 265 K->R: Inhibits interaction with ATG7 and
FOXO1-acetylation-induced autophagic cell
death; when associated with R-262 and R-
274.
MUTAGEN 274 274 K->R: Inhibits interaction with ATG7 and
FOXO1-acetylation-induced autophagic cell
death; when associated with R-262 and R-
265.
MUTAGEN 319 319 S->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. {ECO:0000269|PubMed:11237865,
ECO:0000269|PubMed:12228231}.
MUTAGEN 329 329 S->A: Targeted to the nucleus and
enhances transactivation.
{ECO:0000269|PubMed:11311120}.
CONFLICT 131 131 L -> V (in Ref. 1; AAA03629).
{ECO:0000305}.
CONFLICT 343 343 V -> M (in Ref. 5; AAH70065).
{ECO:0000305}.
STRAND 156 158 {ECO:0000244|PDB:3CO6}.
HELIX 165 175 {ECO:0000244|PDB:3CO6}.
STRAND 176 181 {ECO:0000244|PDB:5DUI}.
HELIX 183 193 {ECO:0000244|PDB:3CO6}.
HELIX 195 197 {ECO:0000244|PDB:3CO6}.
HELIX 203 219 {ECO:0000244|PDB:3CO6}.
STRAND 223 226 {ECO:0000244|PDB:3CO6}.
TURN 230 232 {ECO:0000244|PDB:3CO6}.
STRAND 236 239 {ECO:0000244|PDB:3CO6}.
SEQUENCE 655 AA; 69662 MW; 6DEF6C994BDFDBAB CRC64;
MAEAPQVVEI DPDFEPLPRP RSCTWPLPRP EFSQSNSATS SPAPSGSAAA NPDAAAGLPS
ASAAAVSADF MSNLSLLEES EDFPQAPGSV AAAVAAAAAA AATGGLCGDF QGPEAGCLHP
APPQPPPPGP LSQHPPVPPA AAGPLAGQPR KSSSSRRNAW GNLSYADLIT KAIESSAEKR
LTLSQIYEWM VKSVPYFKDK GDSNSSAGWK NSIRHNLSLH SKFIRVQNEG TGKSSWWMLN
PEGGKSGKSP RRRAASMDNN SKFAKSRSRA AKKKASLQSG QEGAGDSPGS QFSKWPASPG
SHSNDDFDNW STFRPRTSSN ASTISGRLSP IMTEQDDLGE GDVHSMVYPP SAAKMASTLP
SLSEISNPEN MENLLDNLNL LSSPTSLTVS TQSSPGTMMQ QTPCYSFAPP NTSLNSPSPN
YQKYTYGQSS MSPLPQMPIQ TLQDNKSSYG GMSQYNCAPG LLKELLTSDS PPHNDIMTPV
DPGVAQPNSR VLGQNVMMGP NSVMSTYGSQ ASHNKMMNPS SHTHPGHAQQ TSAVNGRPLP
HTVSTMPHTS GMNRLTQVKT PVQVPLPHPM QMSALGGYSS VSSCNGYGRM GLLHQEKLPS
DLDGMFIERL DCDMESIIRN DLMDGDTLDF NFDNVLPNQS FPHSVKTTTH SWVSG


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