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Forkhead box protein O (FOXO) (Abnormal dauer formation protein 16)

 FOXO_CAEEL              Reviewed;         541 AA.
O16850; F3NWW7; F3NWX0; G4RQR7; G4S686; G4SKG3; G4SKH0; O16849;
O18676; Q86S42;
16-JUN-2009, integrated into UniProtKB/Swiss-Prot.
25-JAN-2012, sequence version 3.
13-FEB-2019, entry version 161.
RecName: Full=Forkhead box protein O {ECO:0000305};
Short=FOXO {ECO:0000303|PubMed:12750521};
AltName: Full=Abnormal dauer formation protein 16 {ECO:0000312|WormBase:R13H8.1h};
Name=daf-16 {ECO:0000312|WormBase:R13H8.1h};
ORFNames=R13H8.1 {ECO:0000312|WormBase:R13H8.1h};
Caenorhabditis elegans.
Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
Caenorhabditis.
NCBI_TaxID=6239;
[1] {ECO:0000305, ECO:0000312|EMBL:AAB84390.1}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY,
AND DEVELOPMENTAL STAGE.
STRAIN=Bristol N2 {ECO:0000312|EMBL:AAB84392.1};
PubMed=9353126; DOI=10.1038/40194;
Ogg S., Paradis S., Gottlieb S., Patterson G.I., Lee L.,
Tissenbaum H.A., Ruvkun G.;
"The Fork head transcription factor DAF-16 transduces insulin-like
metabolic and longevity signals in C. elegans.";
Nature 389:994-999(1997).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION, AND DISRUPTION
PHENOTYPE.
STRAIN=Bristol N2;
PubMed=9360933; DOI=10.1126/science.278.5341.1319;
Lin K., Dorman J.B., Rodan A., Kenyon C.;
"daf-16: An HNF-3/forkhead family member that can function to double
the life-span of Caenorhabditis elegans.";
Science 278:1319-1322(1997).
[3] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE
SPLICING.
STRAIN=Bristol N2;
PubMed=9851916; DOI=10.1126/science.282.5396.2012;
The C. elegans sequencing consortium;
"Genome sequence of the nematode C. elegans: a platform for
investigating biology.";
Science 282:2012-2018(1998).
[4]
FUNCTION.
PubMed=8247153; DOI=10.1038/366461a0;
Kenyon C., Chang J., Gensch E., Rudner A., Tabtiang R.;
"A C. elegans mutant that lives twice as long as wild type.";
Nature 366:461-464(1993).
[5] {ECO:0000305}
FUNCTION.
PubMed=10880363; DOI=10.1042/0264-6021:3490629;
Furuyama T., Nakazawa T., Nakano I., Mori N.;
"Identification of the differential distribution patterns of mRNAs and
consensus binding sequences for mouse DAF-16 homologues.";
Biochem. J. 349:629-634(2000).
[6] {ECO:0000305}
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=11747821; DOI=10.1016/S0960-9822(01)00595-4;
Lee R.Y., Hench J., Ruvkun G.;
"Regulation of C. elegans DAF-16 and its human ortholog FKHRL1 by the
daf-2 insulin-like signaling pathway.";
Curr. Biol. 11:1950-1957(2001).
[7] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11747825; DOI=10.1016/S0960-9822(01)00594-2;
Henderson S.T., Johnson T.E.;
"daf-16 integrates developmental and environmental inputs to mediate
aging in the nematode Caenorhabditis elegans.";
Curr. Biol. 11:1975-1980(2001).
[8] {ECO:0000305}
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF SER-271; THR-273
AND SER-345.
PubMed=11381260; DOI=10.1038/88850;
Lin K., Hsin H., Libina N., Kenyon C.;
"Regulation of the Caenorhabditis elegans longevity protein DAF-16 by
insulin/IGF-1 and germline signaling.";
Nat. Genet. 28:139-145(2001).
[9]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=14622602; DOI=10.1016/S0092-8674(03)00889-4;
Libina N., Berman J.R., Kenyon C.;
"Tissue-specific activities of C. elegans DAF-16 in the regulation of
lifespan.";
Cell 115:489-502(2003).
[10] {ECO:0000305}
FUNCTION.
PubMed=12750521; DOI=10.1126/science.1083701;
Hsu A.L., Murphy C.T., Kenyon C.;
"Regulation of aging and age-related disease by DAF-16 and heat-shock
factor.";
Science 300:1142-1145(2003).
[11]
SUBCELLULAR LOCATION.
PubMed=15888317; DOI=10.1016/j.mad.2004.11.012;
Kondo M., Yanase S., Ishii T., Hartman P.S., Matsumoto K., Ishii N.;
"The p38 signal transduction pathway participates in the oxidative
stress-mediated translocation of DAF-16 to Caenorhabditis elegans
nuclei.";
Mech. Ageing Dev. 126:642-647(2005).
[12]
INTERACTION WITH JNK-1, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=15767565; DOI=10.1073/pnas.0500749102;
Oh S.W., Mukhopadhyay A., Svrzikapa N., Jiang F., Davis R.J.,
Tissenbaum H.A.;
"JNK regulates lifespan in Caenorhabditis elegans by modulating
nuclear translocation of forkhead transcription factor/DAF-16.";
Proc. Natl. Acad. Sci. U.S.A. 102:4494-4499(2005).
[13]
INTERACTION WITH FTT-2.
PubMed=16777605; DOI=10.1016/j.cell.2006.04.036;
Berdichevsky A., Viswanathan M., Horvitz H.R., Guarente L.;
"C. elegans SIR-2.1 interacts with 14-3-3 proteins to activate DAF-16
and extend life span.";
Cell 125:1165-1177(2006).
[14]
FUNCTION.
PubMed=17096597; DOI=10.1371/journal.pgen.0020183;
Troemel E.R., Chu S.W., Reinke V., Lee S.S., Ausubel F.M., Kim D.H.;
"p38 MAPK regulates expression of immune response genes and
contributes to longevity in C. elegans.";
PLoS Genet. 2:E183-E183(2006).
[15]
FUNCTION.
PubMed=16902091; DOI=10.1126/science.1124646;
Cohen E., Bieschke J., Perciavalle R.M., Kelly J.W., Dillin A.;
"Opposing activities protect against age-onset proteotoxicity.";
Science 313:1604-1610(2006).
[16]
SUBCELLULAR LOCATION.
PubMed=17551714; DOI=10.1007/s00204-007-0215-4;
Kampkotter A., Gombitang Nkwonkam C., Zurawski R.F., Timpel C.,
Chovolou Y., Watjen W., Kahl R.;
"Effects of the flavonoids kaempferol and fisetin on thermotolerance,
oxidative stress and FoxO transcription factor DAF-16 in the model
organism Caenorhabditis elegans.";
Arch. Toxicol. 81:849-858(2007).
[17]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17900900; DOI=10.1016/j.cub.2007.08.047;
Greer E.L., Dowlatshahi D., Banko M.R., Villen J., Hoang K.,
Blanchard D., Gygi S.P., Brunet A.;
"An AMPK-FOXO pathway mediates longevity induced by a novel method of
dietary restriction in C. elegans.";
Curr. Biol. 17:1646-1656(2007).
[18]
INTERACTION WITH RLE-1, AND UBIQUITINATION.
PubMed=17276341; DOI=10.1016/j.devcel.2006.12.002;
Li W., Gao B., Lee S.-M., Bennett K., Fang D.;
"RLE-1, an E3 ubiquitin ligase, regulates C. elegans aging by
catalyzing DAF-16 polyubiquitination.";
Dev. Cell 12:235-246(2007).
[19]
FUNCTION.
PubMed=17934462; DOI=10.1038/ng.2007.1;
Pinkston-Gosse J., Kenyon C.;
"DAF-16/FOXO targets genes that regulate tumor growth in
Caenorhabditis elegans.";
Nat. Genet. 39:1403-1409(2007).
[20]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=18025456; DOI=10.1073/pnas.0709613104;
Murphy C.T., Lee S.J., Kenyon C.;
"Tissue entrainment by feedback regulation of insulin gene expression
in the endoderm of Caenorhabditis elegans.";
Proc. Natl. Acad. Sci. U.S.A. 104:19046-19050(2007).
[21]
FUNCTION, AND PHOSPHORYLATION BY AKT-1; AKT-2 AND SGK-1.
PubMed=18358814; DOI=10.1016/j.cell.2008.01.030;
Tullet J.M., Hertweck M., An J.H., Baker J., Hwang J.Y., Liu S.,
Oliveira R.P., Baumeister R., Blackwell T.K.;
"Direct inhibition of the longevity-promoting factor SKN-1 by insulin-
like signaling in C. elegans.";
Cell 132:1025-1038(2008).
[22]
FUNCTION.
PubMed=18762027; DOI=10.1016/j.cmet.2008.08.007;
Perez C.L., Van Gilst M.R.;
"A 13C isotope labeling strategy reveals the influence of insulin
signaling on lipogenesis in C. elegans.";
Cell Metab. 8:266-274(2008).
[23]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18832074; DOI=10.1101/gad.478408;
Neumann-Haefelin E., Qi W., Finkbeiner E., Walz G., Baumeister R.,
Hertweck M.;
"SHC-1/p52Shc targets the insulin/IGF-1 and JNK signaling pathways to
modulate life span and stress response in C. elegans.";
Genes Dev. 22:2721-2735(2008).
[24]
FUNCTION.
PubMed=18245330; DOI=10.1534/genetics.107.083923;
Miyata S., Begun J., Troemel E.R., Ausubel F.M.;
"DAF-16-dependent suppression of immunity during reproduction in
Caenorhabditis elegans.";
Genetics 178:903-918(2008).
[25]
FUNCTION.
PubMed=18397876; DOI=10.1093/hmg/ddn109;
Catoire H., Pasco M.Y., Abu-Baker A., Holbert S., Tourette C.,
Brais B., Rouleau G.A., Parker J.A., Neri C.;
"Sirtuin inhibition protects from the polyalanine muscular dystrophy
protein PABPN1.";
Hum. Mol. Genet. 17:2108-2117(2008).
[26]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17894411; DOI=10.1002/jcp.21269;
Wolf M., Nunes F., Henkel A., Heinick A., Paul R.J.;
"The MAP kinase JNK-1 of Caenorhabditis elegans: location, activation,
and influences over temperature-dependent insulin-like signaling,
stress responses, and fitness.";
J. Cell. Physiol. 214:721-729(2008).
[27]
FUNCTION.
PubMed=18524954; DOI=10.1073/pnas.0707607105;
Bretscher A.J., Busch K.E., de Bono M.;
"A carbon dioxide avoidance behavior is integrated with responses to
ambient oxygen and food in Caenorhabditis elegans.";
Proc. Natl. Acad. Sci. U.S.A. 105:8044-8049(2008).
[28]
FUNCTION.
PubMed=19489741; DOI=10.1111/j.1474-9726.2009.00495.x;
Hahm J.H., Kim S., Paik Y.K.;
"Endogenous cGMP regulates adult longevity via the insulin signaling
pathway in Caenorhabditis elegans.";
Aging Cell 8:473-483(2009).
[29]
FUNCTION.
PubMed=19103192; DOI=10.1016/j.ydbio.2008.11.019;
Liachko N., Davidowitz R., Lee S.S.;
"Combined informatic and expression screen identifies the novel DAF-16
target HLH-13.";
Dev. Biol. 327:97-105(2009).
[30]
SUBCELLULAR LOCATION.
PubMed=19252938; DOI=10.1007/s12263-009-0113-x;
Hartwig K., Heidler T., Moch J., Daniel H., Wenzel U.;
"Feeding a ROS-generator to Caenorhabditis elegans leads to increased
expression of small heat shock protein HSP-16.2 and hormesis.";
Genes Nutr. 4:59-67(2009).
[31]
FUNCTION, INTERACTION WITH FTT-2 AND PRMT-1, SUBCELLULAR LOCATION,
PHOSPHORYLATION BY AKT, PHOSPHORYLATION AT THR-273, AND MUTAGENESIS OF
ARG-266; ARG-268; ARG-270; SER-271 AND THR-273.
PubMed=21531333; DOI=10.1016/j.cmet.2011.03.017;
Takahashi Y., Daitoku H., Hirota K., Tamiya H., Yokoyama A., Kako K.,
Nagashima Y., Nakamura A., Shimada T., Watanabe S., Yamagata K.,
Yasuda K., Ishii N., Fukamizu A.;
"Asymmetric arginine dimethylation determines life span in C. elegans
by regulating forkhead transcription factor DAF-16.";
Cell Metab. 13:505-516(2011).
[32]
FUNCTION.
PubMed=22081913; DOI=10.1111/j.1474-9726.2011.00768.x;
McCormick M., Chen K., Ramaswamy P., Kenyon C.;
"New genes that extend Caenorhabditis elegans' lifespan in response to
reproductive signals.";
Aging Cell 11:192-202(2012).
[33]
SUBCELLULAR LOCATION.
PubMed=22875284; DOI=10.1007/s00128-012-0760-2;
Wang Y., Jian F., Wu J., Wang S.;
"Stress-response protein expression and DAF-16 translocation were
induced in tributyltin-exposed Caenorhabditis elegans.";
Bull. Environ. Contam. Toxicol. 89:704-711(2012).
[34]
SUBCELLULAR LOCATION.
PubMed=23000058; DOI=10.1016/j.freeradbiomed.2012.08.594;
Shukla V., Yadav D., Phulara S.C., Gupta M.M., Saikia S.K., Pandey R.;
"Longevity-promoting effects of 4-hydroxy-E-globularinin in
Caenorhabditis elegans.";
Free Radic. Biol. Med. 53:1848-1856(2012).
[35]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=22922647; DOI=10.1038/nature11315;
Vilchez D., Morantte I., Liu Z., Douglas P.M., Merkwirth C.,
Rodrigues A.P., Manning G., Dillin A.;
"RPN-6 determines C. elegans longevity under proteotoxic stress
conditions.";
Nature 489:263-268(2012).
[36]
INDUCTION BY QUINIC ACID.
PubMed=22950425; DOI=10.1089/rej.2012.1342;
Zhang L., Zhang J., Zhao B., Zhao-Wilson X.;
"Quinic acid could be a potential rejuvenating natural compound by
improving survival of Caenorhabditis elegans under deleterious
conditions.";
Rejuvenation Res. 15:573-583(2012).
[37]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=23770237; DOI=10.1016/j.celrep.2013.05.012;
Matilainen O., Arpalahti L., Rantanen V., Hautaniemi S.,
Holmberg C.I.;
"Insulin/IGF-1 signaling regulates proteasome activity through the
deubiquitinating enzyme UBH-4.";
Cell Rep. 3:1980-1995(2013).
[38]
INTERACTION WITH UNC-43 AND TAX-6, SUBCELLULAR LOCATION,
PHOSPHORYLATION AT SER-319, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
SER-319.
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).
[39]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=24146615; DOI=10.1371/journal.ppat.1003660;
Zou C.G., Tu Q., Niu J., Ji X.L., Zhang K.Q.;
"The DAF-16/FOXO transcription factor functions as a regulator of
epidermal innate immunity.";
PLoS Pathog. 9:E1003660-E1003660(2013).
[40]
FUNCTION.
PubMed=25448701;
Safra M., Fickentscher R., Levi-Ferber M., Danino Y.M.,
Haviv-Chesner A., Hansen M., Juven-Gershon T., Weiss M.,
Henis-Korenblit S.;
"The FOXO transcription factor DAF-16 bypasses ire-1 requirement to
promote endoplasmic reticulum hoymeostasis.";
Cell Metab. 20:870-881(2014).
[41]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=24957743; DOI=10.1007/s12263-014-0414-6;
Fischer M., Fitzenberger E., Kull R., Boll M., Wenzel U.;
"The zinc matrix metalloproteinase ZMP-2 increases survival of
Caenorhabditis elegans through interference with lipoprotein
absorption.";
Genes Nutr. 9:414-414(2014).
[42]
FUNCTION.
PubMed=25383666; DOI=10.1038/nsmb.2915;
Nakagawa A., Sullivan K.D., Xue D.;
"Caspase-activated phosphoinositide binding by CNT-1 promotes
apoptosis by inhibiting the AKT pathway.";
Nat. Struct. Mol. Biol. 21:1082-1090(2014).
[43]
FUNCTION.
PubMed=24516399; DOI=10.1371/journal.pgen.1004109;
Tullet J.M., Araiz C., Sanders M.J., Au C., Benedetto A.,
Papatheodorou I., Clark E., Schmeisser K., Jones D., Schuster E.F.,
Thornton J.M., Gems D.;
"DAF-16/FoxO directly regulates an atypical AMP-activated protein
kinase gamma isoform to mediate the effects of insulin/IGF-1 signaling
on aging in Caenorhabditis elegans.";
PLoS Genet. 10:E1004109-E1004109(2014).
[44]
FUNCTION.
PubMed=25330323; DOI=10.1371/journal.pgen.1004703;
Warnhoff K., Murphy J.T., Kumar S., Schneider D.L., Peterson M.,
Hsu S., Guthrie J., Robertson J.D., Kornfeld K.;
"The DAF-16 FOXO transcription factor regulates natc-1 to modulate
stress resistance in Caenorhabditis elegans, linking insulin/IGF-1
signaling to protein N-terminal acetylation.";
PLoS Genet. 10:E1004703-E1004703(2014).
[45]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=25357003; DOI=10.1371/journal.pgen.1004707;
Gruner M., Nelson D., Winbush A., Hintz R., Ryu L., Chung S.H.,
Kim K., Gabel C.V., van der Linden A.M.;
"Feeding state, insulin and NPR-1 modulate Chemoreceptor gene
expression via integration of sensory and circuit inputs.";
PLoS Genet. 10:E1004707-E1004707(2014).
-!- FUNCTION: Forkhead-type transcription factor (PubMed:9360933).
Binds to the promoters of genes that contain the daf-16 binding
element (DBE), TTGTTTAC, in their regulatory region
(PubMed:10880363, PubMed:23770237). Functions in the Insulin/IGF-
1-like signaling (IIS) mediated pathway which affects lipogenesis,
lifespan, starvation survival, heat shock and oxidative stress
responses, and dauer formation (PubMed:9360933, PubMed:8247153,
PubMed:11747821, PubMed:11747825, PubMed:11381260,
PubMed:14622602, PubMed:12750521, PubMed:17900900,
PubMed:18358814, PubMed:18762027, PubMed:18832074,
PubMed:19103192, PubMed:21531333, PubMed:22081913). Longevity
signaling predominantly arises from expression in the intestine
(PubMed:14622602). Daf-16 transcriptional activity is negatively
regulated by cytoplasmic sequestration by association with ftt-2
(PubMed:11381260, PubMed:21531333). Inhibition is required for the
carbon dioxide (CO2) avoidance response (PubMed:18524954). Upon
loss of inhibition, daf-16 translocates to the nucleus to regulate
genes that result in delayed reproduction and growth while
increasing stress resistance starvation tolerance and longevity
(PubMed:11747825, PubMed:21531333). Association with arginine
methyltransferase prmt-1 prevents phosphorylation and allows for
translocation to the nucleus and the subsequent transcription of
longevity-related genes (PubMed:21531333). Modulation of its
activity by cGMP levels in sensory neurons regulates lifespan
(PubMed:19489741). Has a protective role against muscle dystrophy
(PubMed:18397876). Involved in mediating protection against
aberrant protein aggregation proteotoxicity (PubMed:16902091).
Influences transcription of genes that code for proteins involved
in immunity as part of a general stress response (PubMed:17096597,
PubMed:18245330). Targets genes that inhibit and stimulate tumor
growth (PubMed:17934462). Targets kinases, phosphatases and
transcription factors that are primarily involved in signaling and
gene regulation (PubMed:24516399). Thought to regulate ins-7 in
FOXO-to-FOXO signaling, which coordinates daf-16 expression
(PubMed:18025456). Activity is positively regulated by shc-1-
mediated inhibition of daf-2 and activation of JNK pathway
(PubMed:18832074). Functions by indirect interaction with jnk-1 of
the mitogen-activated protein kinase (MAPK) pathway
(PubMed:17894411). Involved in increased proteasome activity by
activating expression of rpn-6.1 in response to proteotoxic
stress, leading to enhanced assembly of the 26S proteasome,
followed by higher proteasome activity (PubMed:22922647). Also
regulates proteasome activity in the intestine by preventing
expression of deubiquitinase ubh-4 (PubMed:23770237). Represses
transcription of natc-1 (PubMed:25330323). Involved in regulation
of srh-234 expression (PubMed:25357003). Binds to the promoter of
the AMPK-gamma regulatory subunit, aakg-4, and activates its
transcription (PubMed:24516399). Also activates transcription of
AMPK-gamma regulatory subunit, aakg-1 (PubMed:24516399). Maintains
endoplasmic reticulum (ER) function by inducing protein
degradation and elimination to remove misfolded secretory proteins
from the ER independently of the ire-1/xbp-1 unfolded protein
response pathway (PubMed:25448701). Regulates epidermal innate
immunity to nematophagous fungal infection and physical wounding
which trigger bli-3 induced ROS release, leading to daf-16
activation independently of daf-2 signaling (PubMed:24146615). May
negatively regulate resistance to stress caused by oxidized
cholesterol adducts by preventing the activation of daf-9 and
nuclear hormone receptor daf-12, two members of the steroid
signaling pathway (PubMed:24957743). Promotes apoptosis during
embryonic development (PubMed:25383666).
{ECO:0000269|PubMed:10880363, ECO:0000269|PubMed:11381260,
ECO:0000269|PubMed:11747821, ECO:0000269|PubMed:11747825,
ECO:0000269|PubMed:12750521, ECO:0000269|PubMed:14622602,
ECO:0000269|PubMed:16902091, ECO:0000269|PubMed:17096597,
ECO:0000269|PubMed:17894411, ECO:0000269|PubMed:17900900,
ECO:0000269|PubMed:17934462, ECO:0000269|PubMed:18025456,
ECO:0000269|PubMed:18245330, ECO:0000269|PubMed:18358814,
ECO:0000269|PubMed:18397876, ECO:0000269|PubMed:18524954,
ECO:0000269|PubMed:18762027, ECO:0000269|PubMed:18832074,
ECO:0000269|PubMed:19103192, ECO:0000269|PubMed:19489741,
ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:22081913,
ECO:0000269|PubMed:22922647, ECO:0000269|PubMed:23770237,
ECO:0000269|PubMed:24146615, ECO:0000269|PubMed:24516399,
ECO:0000269|PubMed:24957743, ECO:0000269|PubMed:25330323,
ECO:0000269|PubMed:25357003, ECO:0000269|PubMed:25383666,
ECO:0000269|PubMed:25448701, ECO:0000269|PubMed:8247153,
ECO:0000269|PubMed:9360933}.
-!- SUBUNIT: Interacts with rle-1 (PubMed:17276341). Interacts with
unc-43 and tax-6 (PubMed:23805378). Interacts with jnk-1
(PubMed:15767565). Interacts with ftt-2 (PubMed:16777605,
PubMed:21531333). Interacts with prmt-1 (PubMed:21531333).
{ECO:0000269|PubMed:15767565, ECO:0000269|PubMed:17276341,
ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:23805378}.
-!- INTERACTION:
Q17941:akt-1; NbExp=3; IntAct=EBI-324028, EBI-1770718;
Q9XTG7:akt-2; NbExp=3; IntAct=EBI-324028, EBI-320656;
Q2PJ68:sgk-1; NbExp=3; IntAct=EBI-324028, EBI-1770776;
Q21921:sir-2.1; NbExp=2; IntAct=EBI-324028, EBI-966082;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11381260,
ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:15767565,
ECO:0000269|PubMed:15888317, ECO:0000269|PubMed:17551714,
ECO:0000269|PubMed:17894411, ECO:0000269|PubMed:18832074,
ECO:0000269|PubMed:19252938, ECO:0000269|PubMed:21531333,
ECO:0000269|PubMed:23805378, ECO:0000269|PubMed:24146615}.
Cytoplasm {ECO:0000269|PubMed:11381260,
ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:15767565,
ECO:0000269|PubMed:15888317, ECO:0000269|PubMed:17551714,
ECO:0000269|PubMed:17894411, ECO:0000269|PubMed:18832074,
ECO:0000269|PubMed:19252938, ECO:0000269|PubMed:21531333,
ECO:0000269|PubMed:23805378, ECO:0000269|PubMed:24146615}.
Note=Shuttles between cytoplasm and nucleus (PubMed:11381260,
PubMed:17894411). Nuclear translocation is inhibited by
phosphorylation by AKT proteins (PubMed:11381260, PubMed:11747825,
PubMed:21531333). Association with ftt-2 sequesters daf-16 in the
cytoplasm (PubMed:21531333). Association with prmt-1 allows for
translocation to the nucleus (PubMed:21531333). Nuclear
translocation is promoted by phosphorylation by unc-43 and
inhibited by dephosphorylation by tax-6 (PubMed:23805378). Nuclear
translocation is promoted by jnk-1 upon heat stress and by sek-1
upon oxidative stress (PubMed:15888317, PubMed:15767565).
Nucleocytoplasmic shuttling is induced by starvation, heat
treatment, hypergravity, reactive oxygen species (generated by
juglone), exposure to tributyltin or 4-hydroxy-E-globularinin (4-
HEG) and the flavonoids kaempferol and fisetin (PubMed:11381260,
PubMed:17551714, PubMed:18832074, PubMed:19252938,
PubMed:21531333, PubMed:23805378). Nuclear localization induced by
nematophagous fungal infection (PubMed:24146615).
{ECO:0000269|PubMed:11381260, ECO:0000269|PubMed:11747825,
ECO:0000269|PubMed:15767565, ECO:0000269|PubMed:15888317,
ECO:0000269|PubMed:17551714, ECO:0000269|PubMed:17894411,
ECO:0000269|PubMed:18832074, ECO:0000269|PubMed:19252938,
ECO:0000269|PubMed:21531333, ECO:0000269|PubMed:24146615}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=8;
Name=h {ECO:0000312|WormBase:R13H8.1h};
IsoId=O16850-8; Sequence=Displayed;
Note=No experimental confirmation available. {ECO:0000305};
Name=a {ECO:0000312|WormBase:R13H8.1h}; Synonyms=b
{ECO:0000303|PubMed:9353126};
IsoId=O16850-2; Sequence=VSP_053106;
Name=b {ECO:0000312|WormBase:R13H8.1h}; Synonyms=a2
{ECO:0000303|PubMed:9353126};
IsoId=O16850-4; Sequence=VSP_053107, VSP_053109;
Name=c {ECO:0000312|WormBase:R13H8.1h}; Synonyms=a1
{ECO:0000303|PubMed:9353126};
IsoId=O16850-3; Sequence=VSP_053107;
Name=d {ECO:0000312|WormBase:R13H8.1h};
IsoId=O16850-5; Sequence=VSP_053108;
Note=No experimental confirmation available. {ECO:0000305};
Name=e {ECO:0000312|WormBase:R13H8.1h};
IsoId=O16850-6; Sequence=VSP_053105;
Note=No experimental confirmation available. Derived from EST
data. {ECO:0000305};
Name=f {ECO:0000312|WormBase:R13H8.1h};
IsoId=O16850-1; Sequence=VSP_042148;
Note=No experimental confirmation available. {ECO:0000305};
Name=g {ECO:0000312|WormBase:R13H8.1h};
IsoId=O16850-7; Sequence=VSP_042147, VSP_042149;
Note=No experimental confirmation available. {ECO:0000305};
-!- TISSUE SPECIFICITY: Isoform b and isoform c are expressed in
ectoderm, muscles, intestine and neurons (PubMed:9353126,
PubMed:11747825, PubMed:14622602, PubMed:17894411). Isoform b is
also expressed in the pharynx (PubMed:11747821). The intestine
appears to be the primary site of longevity function
(PubMed:14622602). {ECO:0000269|PubMed:11747821,
ECO:0000269|PubMed:11747825, ECO:0000269|PubMed:14622602,
ECO:0000269|PubMed:17894411, ECO:0000269|PubMed:9353126}.
-!- DEVELOPMENTAL STAGE: Expressed in embryos, larvae, dauer larvae
and adults. {ECO:0000269|PubMed:9353126}.
-!- INDUCTION: Induced by quinic acid. {ECO:0000269|PubMed:22950425}.
-!- PTM: Phosphorylated by akt-1 and/or akt-2 (PubMed:18358814,
PubMed:21531333). Phosphorylated by sgk-1 (PubMed:18358814).
Phosphorylated by unc-43 (PubMed:23805378). Phosphorylated by jnk-
1 (PubMed:15767565). Dephosphorylated by tax-6 in vitro
(PubMed:23805378). {ECO:0000269|PubMed:15767565,
ECO:0000269|PubMed:18358814, ECO:0000269|PubMed:21531333,
ECO:0000269|PubMed:23805378}.
-!- PTM: Ubiquitinated. Ubiquitination by rle-1 leads to proteasome-
mediated degradation. {ECO:0000269|PubMed:17276341}.
-!- PTM: Methylation by prmt-1 prevents phosphorylation and promotes
translocation to the nucleus to allow for daf-16-dependent
transcription. {ECO:0000269|PubMed:21531333}.
-!- DISRUPTION PHENOTYPE: Dauer defective phenotype in larvae and a
reduced stress phenotype in adults (PubMed:9360933). Increased
carbonyl accumulation and increased sensitivity to starvation
(PubMed:18025456). Increased expression of the srh-234
chemoreceptor during starvation (PubMed:25357003). Increased
sensitivity to physical injury and more susceptible to death by
nematophagous fungal infection (PubMed:24146615). Increased
lifespan (PubMed:23805378). Causes a delay in apoptosis during
embryonic development (PubMed:25383666). RNAi-mediated knock-down
reduces expression of daf-16 target genes and genes up-regulated
in response to nematophagous fungal infection such as sod-3
(PubMed:24146615). RNAi-mediated knockdown causes reduced ability
of dietary restriction to extend lifespan (PubMed:17900900).
Simultaneous RNAi-mediated knockdown of metalloproteinase zmp-2
restores normal survival upon heat stress and prevents increased
susceptibility to heat stress in a daf-9 or daf-12 mutant
background (PubMed:24957743). RNAi-mediated knockdown in a daf-2
(e1370) mutant background restores expression of deubiquitinase
ubh-4 in the intestine (PubMed:23770237).
{ECO:0000269|PubMed:17900900, ECO:0000269|PubMed:18025456,
ECO:0000269|PubMed:23770237, ECO:0000269|PubMed:23805378,
ECO:0000269|PubMed:24146615, ECO:0000269|PubMed:24957743,
ECO:0000269|PubMed:25357003, ECO:0000269|PubMed:25383666,
ECO:0000269|PubMed:9360933}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AF020342; AAB84390.1; -; mRNA.
EMBL; AF020343; AAB84391.1; -; mRNA.
EMBL; AF020344; AAB84392.1; -; mRNA.
EMBL; AF032112; AAC47803.1; -; mRNA.
EMBL; FO081472; CCD71850.1; -; Genomic_DNA.
EMBL; FO081472; CCD71851.1; -; Genomic_DNA.
EMBL; FO081472; CCD71852.1; -; Genomic_DNA.
EMBL; FO081472; CCD71853.1; -; Genomic_DNA.
EMBL; FO081472; CCD71854.1; -; Genomic_DNA.
EMBL; FO081472; CCD71855.1; -; Genomic_DNA.
EMBL; FO080113; CCD71855.1; JOINED; Genomic_DNA.
EMBL; FO081472; CCD71856.1; -; Genomic_DNA.
EMBL; FO080113; CCD71856.1; JOINED; Genomic_DNA.
EMBL; FO081472; CCD71857.1; -; Genomic_DNA.
EMBL; FO080113; CCD71857.1; JOINED; Genomic_DNA.
PIR; T42234; T42234.
PIR; T42255; T42255.
RefSeq; NP_001021593.1; NM_001026422.4. [O16850-2]
RefSeq; NP_001021594.1; NM_001026423.4. [O16850-4]
RefSeq; NP_001021595.1; NM_001026424.4. [O16850-3]
RefSeq; NP_001021596.1; NM_001026425.3. [O16850-5]
RefSeq; NP_001021597.1; NM_001026426.2. [O16850-6]
RefSeq; NP_001021598.2; NM_001026427.4. [O16850-1]
RefSeq; NP_001251490.1; NM_001264561.1. [O16850-8]
RefSeq; NP_001251492.1; NM_001264563.1. [O16850-7]
UniGene; Cel.18378; -.
ProteinModelPortal; O16850; -.
SMR; O16850; -.
BioGrid; 38392; 5.
ComplexPortal; CPX-3882; daf-16-ftt-2 complex.
ComplexPortal; CPX-3883; daf-16-sir-2.1 complex.
ComplexPortal; CPX-3884; daf-16-par-5 complex.
DIP; DIP-25581N; -.
IntAct; O16850; 23.
STRING; 6239.R13H8.1h; -.
iPTMnet; O16850; -.
PaxDb; O16850; -.
PeptideAtlas; O16850; -.
PRIDE; O16850; -.
EnsemblMetazoa; R13H8.1a; R13H8.1a; WBGene00000912. [O16850-2]
EnsemblMetazoa; R13H8.1b.1; R13H8.1b.1; WBGene00000912. [O16850-4]
EnsemblMetazoa; R13H8.1b.2; R13H8.1b.2; WBGene00000912. [O16850-4]
EnsemblMetazoa; R13H8.1c.1; R13H8.1c.1; WBGene00000912. [O16850-3]
EnsemblMetazoa; R13H8.1c.2; R13H8.1c.2; WBGene00000912. [O16850-3]
EnsemblMetazoa; R13H8.1d; R13H8.1d; WBGene00000912. [O16850-5]
EnsemblMetazoa; R13H8.1e; R13H8.1e; WBGene00000912. [O16850-6]
EnsemblMetazoa; R13H8.1f; R13H8.1f; WBGene00000912. [O16850-1]
EnsemblMetazoa; R13H8.1g; R13H8.1g; WBGene00000912. [O16850-7]
EnsemblMetazoa; R13H8.1h; R13H8.1h; WBGene00000912. [O16850-8]
GeneID; 172981; -.
KEGG; cel:CELE_R13H8.1; -.
UCSC; R13H8.1c; c. elegans.
CTD; 172981; -.
WormBase; R13H8.1a; CE28771; WBGene00000912; daf-16. [O16850-2]
WormBase; R13H8.1b; CE28772; WBGene00000912; daf-16. [O16850-4]
WormBase; R13H8.1c; CE28773; WBGene00000912; daf-16. [O16850-3]
WormBase; R13H8.1d; CE38722; WBGene00000912; daf-16. [O16850-5]
WormBase; R13H8.1e; CE33160; WBGene00000912; daf-16. [O16850-6]
WormBase; R13H8.1f; CE44821; WBGene00000912; daf-16. [O16850-1]
WormBase; R13H8.1g; CE44935; WBGene00000912; daf-16. [O16850-7]
WormBase; R13H8.1h; CE45185; WBGene00000912; daf-16. [O16850-8]
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00940000170843; -.
HOGENOM; HOG000019698; -.
InParanoid; O16850; -.
KO; K09408; -.
OMA; SASSGNC; -.
OrthoDB; 753070at2759; -.
Reactome; R-CEL-198693; AKT phosphorylates targets in the nucleus.
Reactome; R-CEL-211163; AKT-mediated inactivation of FOXO1A.
Reactome; R-CEL-5687128; MAPK6/MAPK4 signaling.
Reactome; R-CEL-5689880; Ub-specific processing proteases.
Reactome; R-CEL-9614399; Regulation of localization of FOXO transcription factors.
Reactome; R-CEL-9615017; FOXO-mediated transcription of oxidative stress, metabolic and neuronal genes.
Reactome; R-CEL-9617629; Regulation of FOXO transcriptional activity by acetylation.
SignaLink; O16850; -.
PRO; PR:O16850; -.
Proteomes; UP000001940; Chromosome I.
Bgee; WBGene00000912; Expressed in 6 organ(s), highest expression level in adult organism.
ExpressionAtlas; O16850; baseline and differential.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0071889; F:14-3-3 protein binding; IPI:UniProtKB.
GO; GO:0033613; F:activating transcription factor binding; IPI:UniProtKB.
GO; GO:0008013; F:beta-catenin binding; IPI:ParkinsonsUK-UCL.
GO; GO:0017151; F:DEAD/H-box RNA helicase binding; IPI:WormBase.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
GO; GO:0019899; F:enzyme binding; IPI:WormBase.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:WormBase.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:WormBase.
GO; GO:0008134; F:transcription factor binding; IBA:GO_Central.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:UniProtKB.
GO; GO:1990381; F:ubiquitin-specific protease binding; IPI:WormBase.
GO; GO:0007568; P:aging; IDA:UniProtKB.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0034605; P:cellular response to heat; IDA:UniProtKB.
GO; GO:0034599; P:cellular response to oxidative stress; IGI:ParkinsonsUK-UCL.
GO; GO:0040024; P:dauer larval development; IGI:WormBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:WormBase.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:UniProtKB.
GO; GO:0008340; P:determination of adult lifespan; IDA:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; IBA:GO_Central.
GO; GO:0010286; P:heat acclimation; IGI:UniProtKB.
GO; GO:0045087; P:innate immune response; IMP:WormBase.
GO; GO:0008286; P:insulin receptor signaling pathway; IDA:WormBase.
GO; GO:0060537; P:muscle tissue development; IMP:UniProtKB.
GO; GO:0040015; P:negative regulation of multicellular organism growth; IMP:WormBase.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0002119; P:nematode larval development; IMP:UniProtKB.
GO; GO:0002821; P:positive regulation of adaptive immune response; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0061066; P:positive regulation of dauer larval development; IMP:WormBase.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:1900075; P:positive regulation of neuromuscular synaptic transmission; IGI:UniProtKB.
GO; GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IMP:UniProtKB.
GO; GO:0045887; P:positive regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:WormBase.
GO; GO:0010564; P:regulation of cell cycle process; IEP:UniProtKB.
GO; GO:1905909; P:regulation of dauer entry; IGI:UniProtKB.
GO; GO:0061065; P:regulation of dauer larval development; IGI:UniProtKB.
GO; GO:0043620; P:regulation of DNA-templated transcription in response to stress; IMP:UniProtKB.
GO; GO:0010468; P:regulation of gene expression; IGI:UniProtKB.
GO; GO:0046890; P:regulation of lipid biosynthetic process; IMP:UniProtKB.
GO; GO:0010883; P:regulation of lipid storage; IGI:UniProtKB.
GO; GO:0008582; P:regulation of synaptic growth at neuromuscular junction; IGI:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0006979; P:response to oxidative stress; IGI:UniProtKB.
GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
GO; GO:0009411; P:response to UV; IDA:UniProtKB.
GO; GO:0007614; P:short-term memory; IGI:WormBase.
CDD; cd00059; FH; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR001766; Fork_head_dom.
InterPro; IPR030456; TF_fork_head_CS_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00250; Forkhead; 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;
Alternative splicing; Complete proteome; Cytoplasm;
Developmental protein; DNA-binding; Growth regulation; Immunity;
Innate immunity; Nucleus; Phosphoprotein; Reference proteome;
Repressor; Stress response; Transcription; Transcription regulation;
Ubl conjugation.
CHAIN 1 541 Forkhead box protein O. {ECO:0000305}.
/FTId=PRO_0000414886.
DNA_BIND 175 268 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
MOD_RES 273 273 Phosphothreonine.
{ECO:0000269|PubMed:21531333}.
MOD_RES 319 319 Phosphoserine; by CaMK2.
{ECO:0000269|PubMed:23805378}.
VAR_SEQ 1 238 Missing (in isoform e). {ECO:0000305}.
/FTId=VSP_053105.
VAR_SEQ 1 221 MQLEQKSSLHCSKCRNFLQKFSQDMQAWNCRELDSPLPSDI
TLHNLEPARPDSGMSFSTDFDDDFFNLDLHQQERSASFGGV
TQYSQQFLREKCSFSPYFHTSLETVDSGRTSLYGSNEQCGQ
LGGASSNGSTAMLHTPDGSNSHQTSFPSDFRMSESPDDTVS
GKKTTTRRNAWGNMSYAELITTAIMASPEKRLTLAQVYEWM
VQNVPYFRDKGDSNSS -> MNDSIDDDFPPEPRGRCYTWP
MQQYIYQESSATIPHHHLNQHNNPYHPMHPHHQLPHMQQLP
QPLLNLNMTTLTSSGSSVASSIGGGAQCSPCASGSSTAATN
SSQQQQTVGQMLAASVPCSSSGMTLGMSLNLSQGGGPMPAK
KKRCRKKPTDQLAQKKPNPWGEESYSDIIAKALESAPDGRL
KLNEIYQWFSDNIPYFGERSSPEEA (in isoform a).
{ECO:0000303|PubMed:9353126}.
/FTId=VSP_053106.
VAR_SEQ 1 217 Missing (in isoform g). {ECO:0000305}.
/FTId=VSP_042147.
VAR_SEQ 1 113 MQLEQKSSLHCSKCRNFLQKFSQDMQAWNCRELDSPLPSDI
TLHNLEPARPDSGMSFSTDFDDDFFNLDLHQQERSASFGGV
TQYSQQFLREKCSFSPYFHTSLETVDSGRTS -> MMEMLV
DQGTDASSSASTSTSSVSRFGADTFMNTPDDVMMNDDMEPI
PRDRCNTWPMRRPQLEPPLNSSPIIHEQIPEEDAD (in
isoform b and isoform c).
{ECO:0000303|PubMed:9353126,
ECO:0000303|PubMed:9360933}.
/FTId=VSP_053107.
VAR_SEQ 1 54 Missing (in isoform d). {ECO:0000305}.
/FTId=VSP_053108.
VAR_SEQ 1 24 Missing (in isoform f). {ECO:0000305}.
/FTId=VSP_042148.
VAR_SEQ 152 154 DFR -> E (in isoform b).
{ECO:0000303|PubMed:9353126}.
/FTId=VSP_053109.
VAR_SEQ 218 225 SNSSAGWK -> MREMSTKN (in isoform g).
{ECO:0000305}.
/FTId=VSP_042149.
MUTAGEN 266 266 R->K: Decreases methylation by prmt-1;
when associated with K-268 and K-270.
{ECO:0000269|PubMed:21531333}.
MUTAGEN 268 268 R->K: Decreases methylation by prmt-1;
when associated with K-266 and K-270.
Prevents phosphorylation by akt 1 and/or
2; when associated with K-270.
{ECO:0000269|PubMed:21531333}.
MUTAGEN 270 270 R->K: Decreases methylation by prmt-1;
when associated with K-266 and K-268.
Prevents phosphorylation by akt 1 and/or
2; when associated with K-268.
{ECO:0000269|PubMed:21531333}.
MUTAGEN 271 271 S->A: Prevents phosphorylation and
results in strong nuclear localization.
Reduces phosphorylation; when associated
with A-273. {ECO:0000269|PubMed:11381260,
ECO:0000269|PubMed:21531333}.
MUTAGEN 273 273 T->A: Prevents phosphorylation and
results in strong nuclear localization.
{ECO:0000269|PubMed:11381260}.
MUTAGEN 273 273 T->A: Reduces phosphorylation in normal
and starved conditions. Reduces
phosphorylation; when associated with A-
271. {ECO:0000269|PubMed:21531333}.
MUTAGEN 319 319 S->A: Prevents phosphorylation and
results in cytoplasmic localization in
unc-43 n498 gain-of-function or tax-6
mutant backgrounds.
{ECO:0000269|PubMed:23805378}.
MUTAGEN 319 319 S->D: Phosphomimetic mutant which causes
constitutive nuclear localization.
{ECO:0000269|PubMed:23805378}.
MUTAGEN 345 345 S->A: Prevents phosphorylation and
results in strong nuclear localization.
{ECO:0000269|PubMed:11381260}.
SEQUENCE 541 AA; 59732 MW; 8A36A86311A32CBB CRC64;
MQLEQKSSLH CSKCRNFLQK FSQDMQAWNC RELDSPLPSD ITLHNLEPAR PDSGMSFSTD
FDDDFFNLDL HQQERSASFG GVTQYSQQFL REKCSFSPYF HTSLETVDSG RTSLYGSNEQ
CGQLGGASSN GSTAMLHTPD GSNSHQTSFP SDFRMSESPD DTVSGKKTTT RRNAWGNMSY
AELITTAIMA SPEKRLTLAQ VYEWMVQNVP YFRDKGDSNS SAGWKNSIRH NLSLHSRFMR
IQNEGAGKSS WWVINPDAKP GRNPRRTRER SNTIETTTKA QLEKSRRGAK KRIKERALMG
SLHSTLNGNS IAGSIQTISH DLYDDDSMQG AFDNVPSSFR PRTQSNLSIP GSSSRVSPAI
GSDIYDDLEF PSWVGESVPA IPSDIVDRTD QMRIDATTHI GGVQIKQESK PIKTEPIAPP
PSYHELNSVR GSCAQNPLLR NPIVPSTNFK PMPLPGAYGN YQNGGITPIN WLSTSNSSPL
PGIQSCGIVA AQHTVASSSA LPIDLENLTL PDQPLMDTMD VDALIRHELS QAGGQHIHFD
L


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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
18-003-42177 Forkhead box protein L1 - Forkhead-related protein FKHL11; Forkhead-related transcription factor 7; FREAC-7 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
18-003-42178 Forkhead box protein E3 - Forkhead-related protein FKHL12; Forkhead-related transcription factor 8; FREAC-8 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
E0762h ELISA AF6q21 protein,FKHRL1,Forkhead box protein O3,Forkhead in rhabdomyosarcoma-like 1,FOXO3,FOXO3A,Homo sapiens,Human 96T
E0762h ELISA kit AF6q21 protein,FKHRL1,Forkhead box protein O3,Forkhead in rhabdomyosarcoma-like 1,FOXO3,FOXO3A,Homo sapiens,Human 96T
U0762h CLIA AF6q21 protein,FKHRL1,Forkhead box protein O3,Forkhead in rhabdomyosarcoma-like 1,FOXO3,FOXO3A,Homo sapiens,Human 96T
18-003-43387 Forkhead box protein Q1 - Hepatocyte nuclear factor 3 forkhead homolog 1; HNF-3_forkhead-like protein 1; HFH-1 Polyclonal 0.1 mg Protein A
18-003-43151 Forkhead box protein D1 - Forkhead-related protein FKHL8; Forkhead-related transcription factor 4; FREAC-4; Brain factor 2; HFH-BF-2 Polyclonal 0.05 mg Aff Pur


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