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Forkhead box protein O3

 FOXO3_MOUSE             Reviewed;         672 AA.
Q9WVH4; D3Z6Y6; Q05CZ4;
25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
18-JUL-2018, entry version 162.
RecName: Full=Forkhead box protein O3 {ECO:0000305};
Name=Foxo3 {ECO:0000312|MGI:MGI:1890081};
Synonyms=Fkhr2 {ECO:0000303|PubMed:11353388},
Foxo3a {ECO:0000303|PubMed:11353388};
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=11353388; DOI=10.1007/s003350020002;
Biggs W.H. III, Cavenee W.K., Arden K.C.;
"Identification and characterization of members of the FKHR (FOX O)
subclass of winged-helix transcription factors in the mouse.";
Mamm. Genome 12:416-425(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Cerebellum;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-255.
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]
ACETYLATION, DEACETYLATION BY SIRT2, AND INTERACTION WITH SIRT2.
PubMed=17521387; DOI=10.1111/j.1474-9726.2007.00304.x;
Wang F., Nguyen M., Qin F.X., Tong Q.;
"SIRT2 deacetylates FOXO3a in response to oxidative stress and caloric
restriction.";
Aging Cell 6:505-514(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-293, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[8]
TISSUE SPECIFICITY.
PubMed=22510882; DOI=10.1038/emboj.2012.97;
Nakae J., Cao Y., Hakuno F., Takemori H., Kawano Y., Sekioka R.,
Abe T., Kiyonari H., Tanaka T., Sakai J., Takahashi S., Itoh H.;
"Novel repressor regulates insulin sensitivity through interaction
with Foxo1.";
EMBO J. 31:2275-2295(2012).
[9]
FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT,
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=23283301; DOI=10.1007/s00018-012-1244-6;
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D.,
Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C.,
Villani G., Puri P.L., Sartorelli V., Simone C.;
"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex
sensing glucose levels.";
Cell. Mol. Life Sci. 70:2015-2029(2013).
[10]
FUNCTION, INTERACTION WITH CALCINEURIN A; CAMK2A AND CAMK2B,
PHOSPHORYLATION AT SER-298, MUTAGENESIS OF SER-298, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=23805378; DOI=10.7554/eLife.00518;
Tao L., Xie Q., Ding Y.H., Li S.T., Peng S., Zhang Y.P., Tan D.,
Yuan Z., Dong M.Q.;
"CAMKII and Calcineurin regulate the lifespan of Caenorhabditis
elegans through the FOXO transcription factor DAF-16.";
Elife 2:E00518-E00518(2013).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-241, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
[12]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PROTEOLYTIC CLEAVAGE.
PubMed=29445193; DOI=10.1038/s41419-018-0336-0;
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G.,
Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A.,
Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T.,
Villani G., Moschetta A., Grossi V., Simone C.;
"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells
undergoing metabolic stress and chemotherapy.";
Cell Death Dis. 9:231-231(2018).
-!- FUNCTION: Transcriptional activator (PubMed:23805378). Triggers
apoptosis in the absence of survival factors, including neuronal
cell death upon oxidative stress (By similarity). Recognizes and
binds to the DNA sequence 5'-[AG]TAAA[TC]A-3' (By similarity).
Participates in post-transcriptional regulation of MYC: following
phosphorylation by MAPKAPK5, promotes induction of miR-34b and
miR-34c expression, 2 post-transcriptional regulators of MYC that
bind to the 3'UTR of MYC transcript and prevent its translation
(By similarity). In response to metabolic stress, translocates
into the mitochondria where it promotes mtDNA transcription
(PubMed:23283301). {ECO:0000250|UniProtKB:O43524,
ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23805378}.
-!- SUBUNIT: Upon metabolic stress, forms a complex composed of FOXO3,
SIRT3 and mitochondrial RNA polymerase POLRMT; the complex is
recruited to mtDNA in a SIRT3-dependent manner (PubMed:23283301).
Also forms a complex composed of FOXO3, SIRT3, TFAM and POLRMT (By
similarity). Interacts with SIRT2; the interaction occurs
independently of SIRT2 deacetylase activity (PubMed:17521387).
Interacts with YWHAB/14-3-3-beta and YWHAZ/14-3-3-zeta, which are
required for cytosolic sequestration. Upon oxidative stress,
interacts with STK4/MST1, which disrupts interaction with
YWHAB/14-3-3-beta and leads to nuclear translocation. Interacts
with PIM1. Interacts with DDIT3/CHOP. Interacts (deacetylated
form) with SKP2. Interacts with CHUK and IKBKB (By similarity).
Interacts with CAMK2A, CAMK2B and calcineurin A (PubMed:23805378).
{ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:17521387,
ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:23805378}.
-!- INTERACTION:
P0DJI6:Fcor; NbExp=2; IntAct=EBI-6127038, EBI-6126630;
Q8WTS6:SETD7 (xeno); NbExp=5; IntAct=EBI-6127038, EBI-1268586;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:23283301}. Nucleus
{ECO:0000269|PubMed:23283301}. Mitochondrion matrix
{ECO:0000269|PubMed:23283301, ECO:0000269|PubMed:29445193}.
Mitochondrion outer membrane {ECO:0000269|PubMed:29445193};
Peripheral membrane protein {ECO:0000269|PubMed:29445193};
Cytoplasmic side {ECO:0000269|PubMed:29445193}. Note=Retention in
the cytoplasm contributes to its inactivation (By similarity).
Translocates to the nucleus upon oxidative stress and in the
absence of survival factors (By similarity). Translocates in a
AMPK-dependent manner into the mitochondrion in response to
metabolic stress (PubMed:23283301, PubMed:29445193).
{ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:23283301,
ECO:0000269|PubMed:29445193}.
-!- TISSUE SPECIFICITY: Expressed in white and brown adipose tissues
(at protein level) (PubMed:22510882). Expressed in liver, kidney,
lung and colon (at protein level) (PubMed:29445193). Expressed in
skeletal muscles (at protein level) (PubMed:23283301).
{ECO:0000269|PubMed:22510882, ECO:0000269|PubMed:23283301,
ECO:0000269|PubMed:29445193}.
-!- PTM: Deacetylation by SIRT1 or SIRT2 stimulates interaction of
FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3
ubiquitination and proteasomal degradation (By similarity).
Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional
activity in response to oxidative stress (PubMed:17521387).
Deacetylated by SIRT3 (By similarity). Deacetylation by SIRT3
stimulates FOXO3-mediated mtDNA transcriptional activity in
response to metabolic stress (By similarity).
{ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:17521387}.
-!- PTM: In the presence of survival factors such as IGF-1,
phosphorylated on Thr-32 and Ser-252 by AKT1/PKB. This
phosphorylated form then interacts with 14-3-3 proteins and is
retained in the cytoplasm. Survival factor withdrawal induces
dephosphorylation and promotes translocation to the nucleus where
the dephosphorylated protein induces transcription of target genes
and triggers apoptosis. Although AKT1/PKB doesn't appear to
phosphorylate Ser-314 directly, it may activate other kinases that
trigger phosphorylation at this residue. Phosphorylated by
STK4/MST1 on Ser-208 upon oxidative stress, which leads to
dissociation from YWHAB/14-3-3-beta and nuclear translocation.
Phosphorylated by PIM1. Phosphorylation by AMPK leads to the
activation of transcriptional activity without affecting
subcellular localization. Phosphorylated by AMPK on Ser-30 in
response to metabolic stress which mediates FOXO3 mitochondrial
translocation (By similarity). Phosphorylation by MAPKAPK5
promotes nuclear localization and DNA-binding, leading to
induction of miR-34b and miR-34c expression, 2 post-
transcriptional regulators of MYC that bind to the 3'UTR of MYC
transcript and prevent its translation. Phosphorylated by
CHUK/IKKA and IKBKB/IKKB. TNF-induced inactivation of FOXO3
requires its phosphorylation at Ser-643 by IKBKB/IKKB which
promotes FOXO3 retention in the cytoplasm, polyubiquitination and
ubiquitin-mediated proteasomal degradation (By similarity). May be
dephosphorylated by calcineurin A on Ser-298 which abolishes FOXO3
transcriptional activity (PubMed:23805378).
{ECO:0000250|UniProtKB:O43524, ECO:0000269|PubMed:23805378}.
-!- PTM: Heavily methylated by SET9 which decreases stability, while
moderately increasing transcriptional activity. The main
methylation site is Lys-270. Methylation doesn't affect
subcellular location. {ECO:0000250|UniProtKB:O43524}.
-!- PTM: Polyubiquitinated. Ubiquitinated by a SCF complex containing
SKP2, leading to proteasomal degradation.
{ECO:0000250|UniProtKB:O43524}.
-!- PTM: The N-terminus is cleaved following import into the
mitochondrion. {ECO:0000269|PubMed:29445193}.
-!- SEQUENCE CAUTION:
Sequence=AAH19532.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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EMBL; AF114259; AAD42107.1; -; mRNA.
EMBL; AK047413; BAC33049.1; -; mRNA.
EMBL; AC116179; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC140402; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH466540; EDL04998.1; -; Genomic_DNA.
EMBL; BC019532; AAH19532.1; ALT_SEQ; mRNA.
CCDS; CCDS23810.1; -.
RefSeq; NP_062714.1; NM_019740.2.
RefSeq; XP_006512869.1; XM_006512806.1.
UniGene; Mm.338613; -.
UniGene; Mm.391700; -.
UniGene; Mm.417859; -.
UniGene; Mm.466459; -.
ProteinModelPortal; Q9WVH4; -.
SMR; Q9WVH4; -.
BioGrid; 208010; 5.
ComplexPortal; CPX-1144; FOXO3-MYC complex.
ComplexPortal; CPX-1148; Foxo3-Ywhaz complex.
IntAct; Q9WVH4; 3.
MINT; Q9WVH4; -.
STRING; 10090.ENSMUSP00000050683; -.
iPTMnet; Q9WVH4; -.
PhosphoSitePlus; Q9WVH4; -.
EPD; Q9WVH4; -.
MaxQB; Q9WVH4; -.
PaxDb; Q9WVH4; -.
PeptideAtlas; Q9WVH4; -.
PRIDE; Q9WVH4; -.
DNASU; 56484; -.
Ensembl; ENSMUST00000056974; ENSMUSP00000050683; ENSMUSG00000048756.
Ensembl; ENSMUST00000105502; ENSMUSP00000101141; ENSMUSG00000048756.
Ensembl; ENSMUST00000175881; ENSMUSP00000135380; ENSMUSG00000048756.
GeneID; 56484; -.
KEGG; mmu:56484; -.
UCSC; uc007eyl.1; mouse.
CTD; 2309; -.
MGI; MGI:1890081; Foxo3.
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00920000149005; -.
HOGENOM; HOG000169927; -.
HOVERGEN; HBG078744; -.
InParanoid; Q9WVH4; -.
KO; K09408; -.
OMA; PSVSKPC; -.
OrthoDB; EOG091G06K3; -.
PhylomeDB; Q9WVH4; -.
TreeFam; TF315583; -.
Reactome; R-MMU-1181150; Signaling by NODAL.
Reactome; R-MMU-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-MMU-5687128; MAPK6/MAPK4 signaling.
ChiTaRS; Foxo3; mouse.
PRO; PR:Q9WVH4; -.
Proteomes; UP000000589; Chromosome 10.
Bgee; ENSMUSG00000048756; -.
ExpressionAtlas; Q9WVH4; baseline and differential.
Genevisible; Q9WVH4; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
GO; GO:0005741; C:mitochondrial outer membrane; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; ISO:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; ISO:MGI.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:MGI.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:MGI.
GO; GO:0034246; F:mitochondrial sequence-specific DNA binding transcription factor activity; IMP:UniProtKB.
GO; GO:0019901; F:protein kinase binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:MGI.
GO; GO:0001221; F:transcription cofactor binding; ISO:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IDA:BHF-UCL.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IGI:MGI.
GO; GO:0007568; P:aging; ISO:MGI.
GO; GO:0001547; P:antral ovarian follicle growth; IMP:MGI.
GO; GO:0048854; P:brain morphogenesis; IGI:MGI.
GO; GO:1904646; P:cellular response to amyloid-beta; IEA:Ensembl.
GO; GO:0071386; P:cellular response to corticosterone stimulus; IEA:Ensembl.
GO; GO:0071333; P:cellular response to glucose stimulus; IEA:Ensembl.
GO; GO:0071456; P:cellular response to hypoxia; IEA:Ensembl.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0034599; P:cellular response to oxidative stress; IDA:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IDA:MGI.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IGI:MGI.
GO; GO:0042593; P:glucose homeostasis; IMP:MGI.
GO; GO:0001544; P:initiation of primordial ovarian follicle growth; IMP:MGI.
GO; GO:0006390; P:mitochondrial transcription; IMP:UniProtKB.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IGI:MGI.
GO; GO:0045665; P:negative regulation of neuron differentiation; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:MGI.
GO; GO:0097150; P:neuronal stem cell population maintenance; IGI:MGI.
GO; GO:0001556; P:oocyte maturation; IMP:MGI.
GO; GO:0001542; P:ovulation from ovarian follicle; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; ISO:MGI.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; ISO:MGI.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; ISO:MGI.
GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; ISO:MGI.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; ISO:MGI.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:2000177; P:regulation of neural precursor cell proliferation; IGI:MGI.
GO; GO:2000377; P:regulation of reactive oxygen species metabolic process; IGI:MGI.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:MGI.
GO; GO:0006417; P:regulation of translation; ISS:UniProtKB.
GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:1990785; P:response to water-immersion restraint stress; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; ISS:UniProtKB.
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;
Acetylation; Activator; Apoptosis; Complete proteome; Cytoplasm;
DNA-binding; Membrane; Methylation; Mitochondrion;
Mitochondrion outer membrane; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 672 Forkhead box protein O3.
/FTId=PRO_0000415334.
DNA_BIND 156 250 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
REGION 80 108 Required for mitochondrial import.
{ECO:0000250|UniProtKB:O43524}.
REGION 299 672 Mediates interaction with CHUK/IKKA and
IKBKB/IKKB.
{ECO:0000250|UniProtKB:O43524}.
MOTIF 241 258 Nuclear localization signal.
{ECO:0000250|UniProtKB:O43524}.
COMPBIAS 546 595 Ser-rich.
MOD_RES 30 30 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 32 32 Phosphothreonine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 46 46 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 148 148 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 178 178 Phosphothreonine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 208 208 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 214 214 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 229 229 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 241 241 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 252 252 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 261 261 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 270 270 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 279 279 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 283 283 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 289 289 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 293 293 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 298 298 Phosphoserine; by CaMK2A.
{ECO:0000269|PubMed:23805378}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 314 314 Phosphoserine; by SGK1.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 398 398 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 412 412 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 418 418 N6-methyllysine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 420 420 Phosphoserine.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 550 550 Phosphoserine; by MAPKAPK5.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 554 554 Phosphoserine; by AMPK and MAPKAPK5.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 587 587 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 625 625 Phosphoserine; by AMPK.
{ECO:0000250|UniProtKB:O43524}.
MOD_RES 643 643 Phosphoserine; by IKKB.
{ECO:0000250|UniProtKB:O43524}.
MUTAGEN 298 298 S->A: Abolishes phosphorylation by
CAMK2A. Loss of transcriptional activity.
{ECO:0000269|PubMed:23805378}.
SEQUENCE 672 AA; 71064 MW; EC218D9BA0C1DAC5 CRC64;
MAEAPASPVP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE TAADSMIPEE
DDDEDDEDGG GRASSAMVIG GGVSSTLGSG LLLEDSAMLL APGGQDLGSG PASAAGALSG
GTPTQLQPQQ PLPQPQPGAA GGSGQPRKCS SRRNAWGNLS YADLITRAIE SSPDKRLTLS
QIYEWMVRCV PYFKDKGDSN SSAGWKNSIR HNLSLHSRFM RVQNEGTGKS SWWIINPDGG
KSGKAPRRRA VSMDNSNKYT KSRGRAAKKK AALQAAPESA DDSPSQLSKW PGSPTSRSSD
ELDAWTDFRS RTNSNASTVS GRLSPILAST ELDDVQDDDG PLSPMLYSSS ASLSPSVSKP
CTVELPRLTD MAGTMNLNDG LAENLMDDLL DNIALPPSQP SPPGGLMQRG SSFPYTAKSS
GLGSPTGSFN STVFGPSSLN SLRQSPMQTI QENRPATFSS VSHYGNQTLQ DLLASDSLSH
SDVMMTQSDP LMSQASTAVS AQNARRNVML RNDPMMSFAA QPTQGSLVNQ NLLHHQHQTQ
GALGGSRALS NSVSNMGLSD SSSLGSAKHQ QQSPASQSMQ TLSDSLSGSS LYSASANLPV
MGHDKFPSDL DLDMFNGSLE CDMESIIRSE LMDADGLDFN FDSLISTQNV VGLNVGNFTG
AKQASSQSWV PG


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