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Forkhead box protein O3 (AF6q21 protein) (Forkhead in rhabdomyosarcoma-like 1)

 FOXO3_HUMAN             Reviewed;         673 AA.
O43524; B4DVZ6; E1P5E6; O15171; Q5T2I7; Q9BZ04;
30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
01-JUN-1998, sequence version 1.
25-OCT-2017, entry version 192.
RecName: Full=Forkhead box protein O3 {ECO:0000305};
AltName: Full=AF6q21 protein {ECO:0000303|PubMed:9345057};
AltName: Full=Forkhead in rhabdomyosarcoma-like 1 {ECO:0000303|PubMed:9479491};
Name=FOXO3 {ECO:0000312|HGNC:HGNC:3821};
Synonyms=FKHRL1 {ECO:0000303|PubMed:9479491},
FOXO3A {ECO:0000303|PubMed:11154281};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), 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).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Stomach;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle, 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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-383 (ISOFORM 1), AND
INVOLVEMENT IN SECONDARY ACUTE LEUKEMIAS.
PubMed=9345057;
Hillion J., Le Coniat M., Jonveaux P., Berger R., Bernard O.A.;
"AF6q21, a novel partner of the MLL gene in t(6;11)(q21;q23), defines
a forkhead transcriptional factor subfamily.";
Blood 90:3714-3719(1997).
[7]
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-32; SER-253 AND
SER-315, AND MUTAGENESIS OF THR-32; SER-253 AND SER-315.
PubMed=10102273; DOI=10.1016/S0092-8674(00)80595-4;
Brunet A., Bonni A., Zigmond M.J., Lin M.Z., Juo P., Hu L.S.,
Anderson M.J., Arden K.C., Blenis J., Greenberg M.E.;
"Akt promotes cell survival by phosphorylating and inhibiting a
Forkhead transcription factor.";
Cell 96:857-868(1999).
[8]
PHOSPHORYLATION AT SER-315.
PubMed=11154281; DOI=10.1128/MCB.21.3.952-965.2001;
Brunet A., Park J., Tran H., Hu L.S., Hemmings B.A., Greenberg M.E.;
"Protein kinase SGK mediates survival signals by phosphorylating the
forkhead transcription factor FKHRL1 (FOXO3a).";
Mol. Cell. Biol. 21:952-965(2001).
[9]
INTERACTION WITH CHUK AND IKBKB, REGION, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT SER-644, AND MUTAGENESIS OF SER-644.
PubMed=15084260; DOI=10.1016/S0092-8674(04)00302-2;
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y.,
Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.;
"IkappaB kinase promotes tumorigenesis through inhibition of forkhead
FOXO3a.";
Cell 117:225-237(2004).
[10]
FUNCTION, PHOSPHORYLATION AT SER-209, INTERACTION WITH STK4/MST1 AND
YWHAB, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-209.
PubMed=16751106; DOI=10.1016/j.cell.2006.03.046;
Lehtinen M.K., Yuan Z., Boag P.R., Yang Y., Villen J., Becker E.B.E.,
DiBacco S., de la Iglesia N., Gygi S.P., Blackwell T.K., Bonni A.;
"A conserved MST-FOXO signaling pathway mediates oxidative-stress
responses and extends life span.";
Cell 125:987-1001(2006).
[11]
PHOSPHORYLATION AT THR-179; SER-399; SER-413; SER-555; SER-588 AND
SER-626, MUTAGENESIS OF THR-179; SER-399; SER-413; SER-555; SER-588
AND SER-626, AND SUBCELLULAR LOCATION.
PubMed=17711846; DOI=10.1074/jbc.M705325200;
Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P.,
Gygi S.P., Brunet A.;
"The energy sensor AMP-activated protein kinase directly regulates the
mammalian FOXO3 transcription factor.";
J. Biol. Chem. 282:30107-30119(2007).
[12]
INTERACTION WITH PIM1, AND PHOSPHORYLATION.
PubMed=18593906; DOI=10.1158/0008-5472.CAN-08-0634;
Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.;
"Pim kinases promote cell cycle progression by phosphorylating and
down-regulating p27Kip1 at the transcriptional and posttranscriptional
levels.";
Cancer Res. 68:5076-5085(2008).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-284, 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).
[15]
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).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[18]
FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, AND PHOSPHORYLATION AT
SER-215; SER-253; SER-551 AND SER-555.
PubMed=21329882; DOI=10.1016/j.molcel.2011.01.023;
Kress T.R., Cannell I.G., Brenkman A.B., Samans B., Gaestel M.,
Roepman P., Burgering B.M., Bushell M., Rosenwald A., Eilers M.;
"The MK5/PRAK kinase and Myc form a negative feedback loop that is
disrupted during colorectal tumorigenesis.";
Mol. Cell 41:445-457(2011).
[19]
METHYLATION AT LYS-46; LYS-149; LYS-230; LYS-262; LYS-271; LYS-290 AND
LYS-419, AND MUTAGENESIS OF LYS-269; LYS-270 AND LYS-271.
PubMed=22820736;
Calnan D.R., Webb A.E., White J.L., Stowe T.R., Goswami T., Shi X.,
Espejo A., Bedford M.T., Gozani O., Gygi S.P., Brunet A.;
"Methylation by Set9 modulates FoxO3 stability and transcriptional
activity.";
Aging (Albany NY) 4:462-479(2012).
[20]
INTERACTION WITH IKBKB, AND SUBCELLULAR LOCATION.
PubMed=22313691; DOI=10.1016/j.cellsig.2012.01.012;
Tezil T., Bodur C., Kutuk O., Basaga H.;
"IKK-beta mediates chemoresistance by sequestering FOXO3; a critical
factor for cell survival and death.";
Cell. Signal. 24:1361-1368(2012).
[21]
ACETYLATION, DEACETYLATION BY SIRT2, INTERACTION WITH SKP2,
UBIQUITINATION BY SKP2, AND MUTAGENESIS OF LYS-242; LYS-259; LYS-290
AND LYS-569.
PubMed=21841822; DOI=10.1038/onc.2011.347;
Wang F., Chan C.H., Chen K., Guan X., Lin H.K., Tong Q.;
"Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3
ubiquitination and degradation.";
Oncogene 31:1546-1557(2012).
[22]
INTERACTION WITH DDIT3, AND SUBCELLULAR LOCATION.
PubMed=22761832; DOI=10.1371/journal.pone.0039586;
Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.;
"CHOP potentially co-operates with FOXO3a in neuronal cells to
regulate PUMA and BIM expression in response to ER stress.";
PLoS ONE 7:E39586-E39586(2012).
[23]
PHOSPHORYLATION AT SER-299, 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-284; SER-299;
SER-311; SER-413 AND SER-551, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
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).
[25]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 158-253 IN COMPLEX WITH DNA,
MUTAGENESIS OF LYS-242 AND LYS-245, AND NUCLEAR LOCALIZATION SIGNAL.
PubMed=17940099; DOI=10.1093/nar/gkm703;
Tsai K.-L., Sun Y.-J., Huang C.-Y., Yang J.-Y., Hung M.-C.,
Hsiao C.-D.;
"Crystal structure of the human FOXO3a-DBD/DNA complex suggests the
effects of post-translational modification.";
Nucleic Acids Res. 35:6984-6994(2007).
-!- FUNCTION: Transcriptional activator which triggers apoptosis in
the absence of survival factors, including neuronal cell death
upon oxidative stress. Recognizes and binds to the DNA sequence
5'-[AG]TAAA[TC]A-3'. 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.
{ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:16751106,
ECO:0000269|PubMed:21329882}.
-!- SUBUNIT: Interacts with SIRT2; the interaction occurs
independently of SIRT2 deacetylase activity (By similarity).
Interacts with YWHAB/14-3-3-beta and YWHAZ/14-3-3-zeta, which are
required for cytosolic sequestration (PubMed:16751106). Upon
oxidative stress, interacts with STK4/MST1, which disrupts
interaction with YWHAB/14-3-3-beta and leads to nuclear
translocation (PubMed:16751106). Interacts with PIM1
(PubMed:18593906). Interacts with DDIT3/CHOP (PubMed:22761832).
Interacts (deacetylated form) with SKP2 (PubMed:21841822).
Interacts with CHUK and IKBKB (PubMed:15084260, PubMed:22313691).
Interacts with CAMK2A, CAMK2B and calcineurin A (By similarity).
{ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:18593906,
ECO:0000269|PubMed:21841822, ECO:0000269|PubMed:22313691,
ECO:0000269|PubMed:22761832}.
-!- INTERACTION:
P31749:AKT1; NbExp=3; IntAct=EBI-1644164, EBI-296087;
Q92974:ARHGEF2; NbExp=2; IntAct=EBI-1644164, EBI-302405;
P30260:CDC27; NbExp=2; IntAct=EBI-1644164, EBI-994813;
Q92793:CREBBP; NbExp=3; IntAct=EBI-1644164, EBI-81215;
Q60987:Foxg1 (xeno); NbExp=5; IntAct=EBI-1644164, EBI-11166131;
P85037:FOXK1; NbExp=2; IntAct=EBI-1644164, EBI-2509974;
Q08050:FOXM1; NbExp=2; IntAct=EBI-1644164, EBI-866480;
P51610:HCFC1; NbExp=2; IntAct=EBI-1644164, EBI-396176;
P01106:MYC; NbExp=3; IntAct=EBI-1644164, EBI-447544;
P11309:PIM1; NbExp=2; IntAct=EBI-1644164, EBI-696621;
Q96T60:PNKP; NbExp=2; IntAct=EBI-1644164, EBI-1045072;
P06400:RB1; NbExp=2; IntAct=EBI-1644164, EBI-491274;
P28749:RBL1; NbExp=3; IntAct=EBI-1644164, EBI-971402;
Q96EB6:SIRT1; NbExp=5; IntAct=EBI-1644164, EBI-1802965;
P84022:SMAD3; NbExp=5; IntAct=EBI-1644164, EBI-347161;
Q13485:SMAD4; NbExp=9; IntAct=EBI-1644164, EBI-347263;
O75529:TAF5L; NbExp=2; IntAct=EBI-1644164, EBI-1785876;
P04637:TP53; NbExp=2; IntAct=EBI-1644164, EBI-366083;
P63104:YWHAZ; NbExp=2; IntAct=EBI-1644164, EBI-347088;
P63101:Ywhaz (xeno); NbExp=2; IntAct=EBI-1644164, EBI-354751;
-!- SUBCELLULAR LOCATION: Cytoplasm, cytosol
{ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846,
ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:22313691,
ECO:0000269|PubMed:22761832}. Nucleus
{ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846,
ECO:0000269|PubMed:21329882, ECO:0000269|PubMed:22313691,
ECO:0000269|PubMed:22761832}. Note=Retention in the cytoplasm
contributes to its inactivation. Translocates to the nucleus upon
oxidative stress and in the absence of survival factors.
{ECO:0000269|PubMed:10102273, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:16751106}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O43524-1; Sequence=Displayed;
Name=2;
IsoId=O43524-2; Sequence=VSP_056225;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:9479491}.
-!- PTM: In the presence of survival factors such as IGF-1,
phosphorylated on Thr-32 and Ser-253 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-315 directly, it may activate other kinases that
trigger phosphorylation at this residue. Phosphorylated by
STK4/MST1 on Ser-209 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. 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 (PubMed:10102273, PubMed:11154281, PubMed:16751106,
PubMed:17711846, PubMed:18593906, PubMed:21329882). Phosphorylated
by CHUK/IKKA and IKBKB/IKKB. TNF-induced inactivation of FOXO3
requires its phosphorylation at Ser-644 by IKBKB/IKKB which
promotes FOXO3 retention in the cytoplasm, polyubiquitination and
ubiquitin-mediated proteasomal degradation (PubMed:15084260). May
be dephosphorylated by calcineurin A on Ser-299 which abolishes
FOXO3 transcriptional activity (By similarity).
{ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:10102273,
ECO:0000269|PubMed:11154281, ECO:0000269|PubMed:15084260,
ECO:0000269|PubMed:16751106, ECO:0000269|PubMed:17711846,
ECO:0000269|PubMed:18593906, ECO:0000269|PubMed:21329882}.
-!- PTM: Deacetylation by SIRT1 or SIRT2 stimulates interaction of
FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3
ubiquitination and proteasomal degradation (PubMed:21841822).
Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional
activity in response to oxidative stress (By similarity).
{ECO:0000250|UniProtKB:Q9WVH4, ECO:0000269|PubMed:21841822}.
-!- PTM: Heavily methylated by SET9 which decreases stability, while
moderately increasing transcriptional activity. The main
methylation site is Lys-271. Methylation doesn't affect
subcellular location. {ECO:0000269|PubMed:22820736}.
-!- PTM: Polyubiquitinated. Ubiquitinated by a SCF complex containing
SKP2, leading to proteasomal degradation.
{ECO:0000269|PubMed:21841822}.
-!- DISEASE: Note=A chromosomal aberration involving FOXO3 is found in
secondary acute leukemias. Translocation t(6;11)(q21;q23) with
KMT2A/MLL1.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/AF6q21ID125.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF032886; AAC39592.1; -; mRNA.
EMBL; AK301304; BAG62858.1; -; mRNA.
EMBL; AL096818; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AL391646; CAI16405.1; -; Genomic_DNA.
EMBL; AL365509; CAI16405.1; JOINED; Genomic_DNA.
EMBL; AL365509; CAI16295.1; -; Genomic_DNA.
EMBL; AL391646; CAI16295.1; JOINED; Genomic_DNA.
EMBL; CH471051; EAW48373.1; -; Genomic_DNA.
EMBL; CH471051; EAW48374.1; -; Genomic_DNA.
EMBL; BC020227; AAH20227.1; -; mRNA.
EMBL; BC021224; AAH21224.1; -; mRNA.
EMBL; BC068552; AAH68552.1; -; mRNA.
EMBL; AJ001589; CAA04860.1; -; mRNA.
EMBL; AJ001590; CAA04861.1; -; Genomic_DNA.
CCDS; CCDS5068.1; -. [O43524-1]
RefSeq; NP_001446.1; NM_001455.3. [O43524-1]
RefSeq; NP_963853.1; NM_201559.2. [O43524-1]
RefSeq; XP_005266925.1; XM_005266868.3. [O43524-2]
RefSeq; XP_011533930.1; XM_011535628.2. [O43524-2]
RefSeq; XP_011533931.1; XM_011535629.2. [O43524-2]
RefSeq; XP_016866075.1; XM_017010586.1. [O43524-2]
UniGene; Hs.220950; -.
PDB; 2K86; NMR; -; A=151-251.
PDB; 2LQH; NMR; -; B=461-635.
PDB; 2LQI; NMR; -; B=461-635.
PDB; 2UZK; X-ray; 2.70 A; A/C=158-253.
PDBsum; 2K86; -.
PDBsum; 2LQH; -.
PDBsum; 2LQI; -.
PDBsum; 2UZK; -.
ProteinModelPortal; O43524; -.
SMR; O43524; -.
BioGrid; 108598; 65.
CORUM; O43524; -.
DIP; DIP-29723N; -.
IntAct; O43524; 43.
MINT; MINT-89098; -.
STRING; 9606.ENSP00000339527; -.
BindingDB; O43524; -.
ChEMBL; CHEMBL5778; -.
iPTMnet; O43524; -.
PhosphoSitePlus; O43524; -.
BioMuta; FOXO3; -.
EPD; O43524; -.
MaxQB; O43524; -.
PaxDb; O43524; -.
PeptideAtlas; O43524; -.
PRIDE; O43524; -.
DNASU; 2309; -.
Ensembl; ENST00000343882; ENSP00000339527; ENSG00000118689. [O43524-1]
Ensembl; ENST00000406360; ENSP00000385824; ENSG00000118689. [O43524-1]
Ensembl; ENST00000540898; ENSP00000446316; ENSG00000118689. [O43524-2]
GeneID; 2309; -.
KEGG; hsa:2309; -.
UCSC; uc003psk.3; human. [O43524-1]
CTD; 2309; -.
DisGeNET; 2309; -.
EuPathDB; HostDB:ENSG00000118689.14; -.
GeneCards; FOXO3; -.
HGNC; HGNC:3821; FOXO3.
HPA; CAB004074; -.
HPA; HPA063104; -.
MIM; 602681; gene.
neXtProt; NX_O43524; -.
OpenTargets; ENSG00000118689; -.
PharmGKB; PA28239; -.
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00790000123003; -.
HOGENOM; HOG000251635; -.
HOVERGEN; HBG057789; -.
InParanoid; O43524; -.
KO; K09408; -.
OMA; PSVSKPC; -.
OrthoDB; EOG091G06K3; -.
PhylomeDB; O43524; -.
TreeFam; TF315583; -.
Reactome; R-HSA-1181150; Signaling by NODAL.
Reactome; R-HSA-198693; AKT phosphorylates targets in the nucleus.
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.
Reactome; R-HSA-8862803; Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
Reactome; R-HSA-8952158; RUNX3 regulates BCL2L11 (BIM) transcription.
SignaLink; O43524; -.
SIGNOR; O43524; -.
ChiTaRS; FOXO3; human.
EvolutionaryTrace; O43524; -.
GeneWiki; FOXO3; -.
GenomeRNAi; 2309; -.
PRO; PR:O43524; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000118689; -.
CleanEx; HS_FOXO3; -.
Genevisible; O43524; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:FlyBase.
GO; GO:0016020; C:membrane; IEA:Ensembl.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:ParkinsonsUK-UCL.
GO; GO:0031490; F:chromatin DNA binding; ISS:UniProtKB.
GO; GO:0001047; F:core promoter binding; ISS:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0001221; F:transcription cofactor binding; IEA:Ensembl.
GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IDA:MGI.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding; IEA:Ensembl.
GO; GO:0001227; F:transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding; IDA:BHF-UCL.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0001547; P:antral ovarian follicle growth; IEA:Ensembl.
GO; GO:0048854; P:brain morphogenesis; IEA:Ensembl.
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; ISS:UniProtKB.
GO; GO:0030330; P:DNA damage response, signal transduction by p53 class mediator; IEA:Ensembl.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0001544; P:initiation of primordial ovarian follicle growth; IEA:Ensembl.
GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
GO; GO:0045665; P:negative regulation of neuron differentiation; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0097150; P:neuronal stem cell population maintenance; IEA:Ensembl.
GO; GO:0001556; P:oocyte maturation; IEA:Ensembl.
GO; GO:0001542; P:ovulation from ovarian follicle; IEA:Ensembl.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:BHF-UCL.
GO; GO:2000353; P:positive regulation of endothelial cell apoptotic process; IEA:Ensembl.
GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IDA:MGI.
GO; GO:1901300; P:positive regulation of hydrogen peroxide-mediated programmed cell death; IEA:Ensembl.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IMP:UniProtKB.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; IEA:Ensembl.
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:2000177; P:regulation of neural precursor cell proliferation; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0006417; P:regulation of translation; IDA:UniProtKB.
GO; GO:0071548; P:response to dexamethasone; IEA:Ensembl.
GO; GO:0042493; P:response to drug; 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; IMP: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;
3D-structure; Acetylation; Activator; Alternative splicing; Apoptosis;
Chromosomal rearrangement; Complete proteome; Cytoplasm; DNA-binding;
Methylation; Nucleus; Phosphoprotein; Proto-oncogene;
Reference proteome; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 673 Forkhead box protein O3.
/FTId=PRO_0000091874.
DNA_BIND 157 251 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
REGION 300 673 Mediates interaction with CHUK/IKKA and
IKBKB/IKKB.
{ECO:0000269|PubMed:15084260}.
MOTIF 242 259 Nuclear localization signal.
{ECO:0000269|PubMed:17940099}.
MOD_RES 32 32 Phosphothreonine; by PKB/AKT1.
{ECO:0000269|PubMed:10102273}.
MOD_RES 46 46 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 149 149 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 179 179 Phosphothreonine; by AMPK.
{ECO:0000269|PubMed:17711846}.
MOD_RES 209 209 Phosphoserine; by STK4/MST1.
{ECO:0000269|PubMed:16751106}.
MOD_RES 215 215 Phosphoserine; by MAPKAPK5.
{ECO:0000269|PubMed:21329882}.
MOD_RES 230 230 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 242 242 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9WVH4}.
MOD_RES 253 253 Phosphoserine; by PKB/AKT1 and MAPKAPK5.
{ECO:0000269|PubMed:10102273,
ECO:0000269|PubMed:21329882}.
MOD_RES 262 262 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 271 271 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 280 280 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 284 284 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 290 290 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 294 294 Phosphoserine.
{ECO:0000250|UniProtKB:Q9WVH4}.
MOD_RES 299 299 Phosphoserine; by CaMK2A.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:23805378}.
MOD_RES 311 311 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 315 315 Phosphoserine; by SGK1.
{ECO:0000269|PubMed:10102273,
ECO:0000269|PubMed:11154281}.
MOD_RES 399 399 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:17711846}.
MOD_RES 413 413 Phosphoserine; by AMPK.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:17711846}.
MOD_RES 419 419 N6-methyllysine.
{ECO:0000269|PubMed:22820736}.
MOD_RES 421 421 Phosphoserine.
{ECO:0000244|PubMed:18220336}.
MOD_RES 551 551 Phosphoserine; by MAPKAPK5.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:21329882}.
MOD_RES 555 555 Phosphoserine; by AMPK and MAPKAPK5.
{ECO:0000269|PubMed:17711846,
ECO:0000269|PubMed:21329882}.
MOD_RES 588 588 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:17711846}.
MOD_RES 626 626 Phosphoserine; by AMPK.
{ECO:0000269|PubMed:17711846}.
MOD_RES 644 644 Phosphoserine; by IKKB.
{ECO:0000269|PubMed:15084260}.
VAR_SEQ 1 220 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056225.
MUTAGEN 32 32 T->A: Abolishes YWHAZ-binding; when
associated with A-253. Exclusively
nuclear, induces transcription and
promotes apoptosis; when associated with
A-253 and A-315.
{ECO:0000269|PubMed:10102273}.
MUTAGEN 179 179 T->A: Decreased phosphorylation by AMPK
and impaired ability to transactivate a
reporter gene; when associated with A-
399; A-413; A-555; A-588 and A-626.
{ECO:0000269|PubMed:17711846}.
MUTAGEN 209 209 S->A: Impairs nuclear translocation upon
oxidative stress.
{ECO:0000269|PubMed:16751106}.
MUTAGEN 242 242 K->A: Slightly decreases DNA affinity.
{ECO:0000269|PubMed:17940099,
ECO:0000269|PubMed:21841822}.
MUTAGEN 242 242 K->R: Reduces acetylation, increases
interaction with SKP2 and inhibits FOXO3
ubiquitination and degradation; when
associated with R-259; R-290 and R-569.
{ECO:0000269|PubMed:17940099,
ECO:0000269|PubMed:21841822}.
MUTAGEN 245 245 K->A: Decreases DNA affinity.
{ECO:0000269|PubMed:17940099}.
MUTAGEN 253 253 S->A: Abolishes YWHAZ-binding; when
associated with A-32. Exclusively
nuclear, induces transcription and
promotes apoptosis; when associated with
A-32 and A-315.
{ECO:0000269|PubMed:10102273}.
MUTAGEN 259 259 K->R: Reduces acetylation, increases
interaction with SKP2 and inhibits FOXO3
ubiquitination and degradation; when
associated with R-242; R-290 and R-569.
{ECO:0000269|PubMed:21841822}.
MUTAGEN 269 269 K->R: Methylation levels similar to wild-
type; when associated with ARG-270.
{ECO:0000269|PubMed:22820736}.
MUTAGEN 270 270 K->R: Methylation levels similar to wild-
type; when associated with ARG-269.
{ECO:0000269|PubMed:22820736}.
MUTAGEN 271 271 K->R: Methylation levels strongly
reduced. {ECO:0000269|PubMed:22820736}.
MUTAGEN 290 290 K->R: Reduces acetylation, increases
interaction with SKP2 and inhibits FOXO3
ubiquitination and degradation; when
associated with R-242; R-259 and R-569.
{ECO:0000269|PubMed:21841822}.
MUTAGEN 315 315 S->A: No effect on YWHAZ-binding.
Promotes nuclear translocation.
Exclusively nuclear, induces
transcription and promotes apoptosis;
when associated with A-32 and A-253.
{ECO:0000269|PubMed:10102273}.
MUTAGEN 399 399 S->A: Decreased phosphorylation by AMPK
and impaired ability to transactivate a
reporter gene; when associated with A-
179; A-413; A-555; A-588 and A-626.
{ECO:0000269|PubMed:17711846}.
MUTAGEN 413 413 S->A: Decreased phosphorylation by AMPK
and impaired ability to transactivate a
reporter gene; when associated with A-
179; A-399; A-555; A-588 and A-626.
{ECO:0000269|PubMed:17711846}.
MUTAGEN 555 555 S->A: Decreased phosphorylation by AMPK
and impaired ability to transactivate a
reporter gene; when associated with A-
179; A-399; A-413; A-588 and A-626.
{ECO:0000269|PubMed:17711846}.
MUTAGEN 569 569 K->R: Reduces acetylation, increases
interaction with SKP2 and inhibits FOXO3
ubiquitination and degradation; when
associated with R-242; R-259 and R-290.
{ECO:0000269|PubMed:21841822}.
MUTAGEN 588 588 S->A: Decreased phosphorylation by AMPK
and impaired ability to transactivate a
reporter gene; when associated with A-
179; A-399; A-413; A-555 and A-626.
{ECO:0000269|PubMed:17711846}.
MUTAGEN 626 626 S->A: Decreased phosphorylation by AMPK
and impaired ability to transactivate a
reporter gene; when associated with A-
179; A-399; A-413; A-555 and A-588.
{ECO:0000269|PubMed:17711846}.
MUTAGEN 644 644 S->A: Loss of phosphorylation by IKKB.
{ECO:0000269|PubMed:15084260}.
CONFLICT 156 163 AWGNLSYA -> WGKPVYS (in Ref. 6;
CAA04860). {ECO:0000305}.
CONFLICT 238 246 PDGGKSGKA -> LMGEERKT (in Ref. 6;
CAA04860). {ECO:0000305}.
CONFLICT 253 253 S -> T (in Ref. 6; CAA04860).
{ECO:0000305}.
CONFLICT 271 271 Missing (in Ref. 6; CAA04860).
{ECO:0000305}.
CONFLICT 292 330 PGSPTSRSSDELDAWTDFRSRTNSNASTVSGRLSPIMAS
-> AWQPHVNAAVMSWMRGRTSVHAPILTPAQSVAACRPSW
QV (in Ref. 6; CAA04860). {ECO:0000305}.
CONFLICT 345 361 PMLYSSSASLSPSVSKP -> AHALQHVSQPVTFSKQA
(in Ref. 6; CAA04860). {ECO:0000305}.
CONFLICT 367 367 P -> R (in Ref. 6; CAA04860).
{ECO:0000305}.
CONFLICT 371 371 D -> E (in Ref. 6; CAA04860).
{ECO:0000305}.
CONFLICT 382 383 LT -> AD (in Ref. 6; CAA04860).
{ECO:0000305}.
TURN 156 158 {ECO:0000244|PDB:2K86}.
HELIX 162 169 {ECO:0000244|PDB:2UZK}.
STRAND 172 176 {ECO:0000244|PDB:2UZK}.
HELIX 180 189 {ECO:0000244|PDB:2UZK}.
STRAND 198 200 {ECO:0000244|PDB:2UZK}.
HELIX 206 216 {ECO:0000244|PDB:2UZK}.
STRAND 217 229 {ECO:0000244|PDB:2UZK}.
STRAND 233 236 {ECO:0000244|PDB:2UZK}.
STRAND 238 240 {ECO:0000244|PDB:2K86}.
STRAND 463 465 {ECO:0000244|PDB:2LQH}.
HELIX 468 477 {ECO:0000244|PDB:2LQH}.
TURN 478 480 {ECO:0000244|PDB:2LQH}.
HELIX 621 623 {ECO:0000244|PDB:2LQI}.
HELIX 624 633 {ECO:0000244|PDB:2LQH}.
SEQUENCE 673 AA; 71277 MW; E5B4E830665A9982 CRC64;
MAEAPASPAP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE TAADSMIPEE
EDDEDDEDGG GRAGSAMAIG GGGGSGTLGS GLLLEDSARV LAPGGQDPGS GPATAAGGLS
GGTQALLQPQ QPLPPPQPGA AGGSGQPRKC SSRRNAWGNL SYADLITRAI ESSPDKRLTL
SQIYEWMVRC VPYFKDKGDS NSSAGWKNSI RHNLSLHSRF MRVQNEGTGK SSWWIINPDG
GKSGKAPRRR AVSMDNSNKY TKSRGRAAKK KAALQTAPES ADDSPSQLSK WPGSPTSRSS
DELDAWTDFR SRTNSNASTV SGRLSPIMAS TELDEVQDDD APLSPMLYSS SASLSPSVSK
PCTVELPRLT DMAGTMNLND GLTENLMDDL LDNITLPPSQ PSPTGGLMQR SSSFPYTTKG
SGLGSPTSSF NSTVFGPSSL NSLRQSPMQT IQENKPATFS SMSHYGNQTL QDLLTSDSLS
HSDVMMTQSD PLMSQASTAV SAQNSRRNVM LRNDPMMSFA AQPNQGSLVN QNLLHHQHQT
QGALGGSRAL SNSVSNMGLS ESSSLGSAKH QQQSPVSQSM QTLSDSLSGS SLYSTSANLP
VMGHEKFPSD LDLDMFNGSL ECDMESIIRS ELMDADGLDF NFDSLISTQN VVGLNVGNFT
GAKQASSQSW VPG


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18-003-43334 Forkhead box protein J1 - Forkhead-related protein FKHL13; Hepatocyte nuclear factor 3 forkhead homolog 4; HFH-4 Polyclonal 0.05 mg Aff Pur
18-003-42083 Forkhead box protein F2 - Forkhead-related protein FKHL6; Forkhead-related transcription factor 2; FREAC-2; Forkhead-related activator 2 Polyclonal 0.1 mg Protein A
18-003-42082 Forkhead box protein F1 - Forkhead-related protein FKHL5; Forkhead-related transcription factor 1; FREAC-1; Forkhead-related activator 1 Polyclonal 0.1 mg Protein A
18-003-42174 Forkhead box protein F1 - Forkhead-related protein FKHL5; Forkhead-related transcription factor 1; FREAC-1; Forkhead-related activator 1 Polyclonal 0.1 mg Protein A
18-003-43076 Forkhead box protein I1 - Forkhead-related protein FKHL10; Forkhead-related transcription factor 6; FREAC-6; Hepatocyte nuclear factor 3 forkhead homolog 3; HNF-3_fork-head homolog 3; HFH-3 Polyclonal 0.05 mg Aff Pur
18-003-42175 Forkhead box protein C1 - Forkhead-related protein FKHL7; Forkhead-related transcription factor 3; FREAC-3 Polyclonal 0.1 mg Protein A
18-003-43801 Forkhead box protein D2 - Forkhead-related protein FKHL17; Forkhead-related transcription factor 9; FREAC-9 Polyclonal 0.1 mg Protein A
18-003-42177 Forkhead box protein L1 - Forkhead-related protein FKHL11; Forkhead-related transcription factor 7; FREAC-7 Polyclonal 0.1 mg Protein A
18-003-42178 Forkhead box protein E3 - Forkhead-related protein FKHL12; Forkhead-related transcription factor 8; FREAC-8 Polyclonal 0.05 mg Aff Pur
18-003-42180 Forkhead box protein C2 - Forkhead-related protein FKHL14; Mesenchyme fork head protein 1; MFH-1 protein; Transcription factor FKH-14 Polyclonal 0.1 mg Protein A


 

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