Reviewed, UniProtKB/Swiss-Prot O16850 (FOXO_CAEEL)

Names and origin

Protein names

Recommended name:
    Forkhead box protein O
      Short name=FOXO
Alternative name(s):
    Abnormal dauer formation protein 16

Gene names

Name:	daf-16
ORF Names:	R13H8.1

Organism

Caenorhabditis elegans [Complete proteome]

Taxonomic identifier

6239 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Nematoda › Chromadorea › Rhabditida › Rhabditoidea › Rhabditidae › Peloderinae › Caenorhabditis

Protein attributes

Sequence length	568 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Forkhead-type transcription factor. Binds to the promoters of genes that contain the daf-16 binding element (DBE), TTGTTTAC, in their regulatory region. Functions in the Insulin/IGF-1-like signaling (IIS) mediated pathway which affects lipogenesis, lifespan, starvation survival, heat shock response, and dauer formation. Daf-16 transcriptional activity is negatively regulated by cytoplasmic sequestration. Inhibition is required for the carbon dioxide (CO2) avoidance response. 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. Has a protective role against muscle dystrophy. Involved in mediating protection against aberrant protein aggregation proteotoxicity. Influences transcription of genes that code for protein involved in immunity as part of a general stress response. Targets genes that inhibit and stimulate tumor growth. Thought to regulate ins-7 in FOXO-to-FOXO signaling, which coordinates daf-16 expression. Functions by indirect interaction with jnk-1 of the mitogen-activated protein kinase (MAPK) pathway.
Subunit structure	Interacts with rle-1.
Subcellular location	Isoform c: Nucleus. Cytoplasm. Note: Shuttles between cytoplasm and nucleus. Nuclear translocation is thought to be inhibited by phosphorylation by AKT proteins. Nucleocytoplasmic shuttling is induced by starvation, heat treatment, hypergravity, reactive oxygen species (generated by juglone) and the flavonoids kaempferol and fisetin.
Tissue specificity	Isoform b and isoform c are expressed in ectoderm, muscles, intestine and neurons. Isoform b is also expressed in the pharnyx.
Developmental stage	Expressed in embryos, larvae, dauer larvae and adults.
Post-translational modification	Phosphorylated by akt-1, akt-2 and sgk-1. Ubiquitinated. Ubiquitination by rle-1 leads to proteasome-mediated degradation.
Disruption phenotype	Increased carbonyl accumulation and increased sensitivity to starvation.
Sequence similarities	Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Growth regulation Stress response Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Phosphoprotein Ubl conjugation
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	regulation of transcription, DNA-dependent Inferred from electronic annotation. Source: InterPro
Cellular component	nucleus Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	protein binding Inferred from physical interaction. Source: IntAct sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro transcription factor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
sir-2.1	Q21921	1	EBI-324028,EBI-966082

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

Isoform f (identifier: O16850-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Note: No experimental confirmation available.

Isoform a (identifier: O16850-2)

Also known as: b;

The sequence of this isoform differs from the canonical sequence as follows:
     1-236: MQAWNCREVW...QVYEWMVQNV → MNDSIDDDFP...EIYQWFSDNI
     240-248: RDKGDSNSS → GERSSPEEA

Isoform c (identifier: O16850-3)

Also known as: a1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: MQAWNCREVW...LETVDSGRTS → MMEMLVDQGT...HEQIPEEDAD

Note: Shuttles between cytoplasm and nucleus. Nuclear translocation is thought to be inhibited by phosphorylation by AKT proteins. Nucleocytoplasmic shuttling is induced by starvation, heat treatment, hypergravity, reactive oxygen species (generated by juglone) and the flavonoids kaempferol and fisetin.

Isoform b (identifier: O16850-4)

Also known as: a2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-140: MQAWNCREVW...LETVDSGRTS → MMEMLVDQGT...HEQIPEEDAD
     179-181: DFR → E

Isoform d (identifier: O16850-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.

Isoform e (identifier: O16850-6)

The sequence of this isoform differs from the canonical sequence as follows:
     1-265: Missing.

Note: No experimental confirmation available. Derived from EST data.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 568	568	Forkhead box protein O		PRO_0000377712
Regions
	DNA binding	202 – 295	94	Fork-head
Natural variations
	Alternative sequence	1 – 265	265	Missing in isoform e.		VSP_053105
	Alternative sequence	1 – 236	236	MQAWN…MVQNV → MNDSIDDDFPPEPRGRCYTW PMQQYIYQESSATIPHHHLN QHNNPYHPMHPHHQLPHMQQ LPQPLLNLNMTTLTSSGSSV ASSIGGGAQCSPCASGSSTA ATNSSQQQQTVGQMLAASVP CSSSGMTLGMSLNLSQGGGP MPAKKKRCRKKPTDQLAQKK PNPWGEESYSDIIAKALESA PDGRLKLNEIYQWFSDNI in isoform a.		VSP_053106
	Alternative sequence	1 – 140	140	MQAWN…SGRTS → MMEMLVDQGTDASSSASTST SSVSRFGADTFMNTPDDVMM NDDMEPIPRDRCNTWPMRRP QLEPPLNSSPIIHEQIPEED AD in isoform b and isoform c.		VSP_053107
	Alternative sequence	1 – 81	81	Missing in isoform d.		VSP_053108
	Alternative sequence	179 – 181	3	DFR → E in isoform b.		VSP_053109
	Alternative sequence	240 – 248	9	RDKGDSNSS → GERSSPEEA in isoform a.		VSP_053110
Experimental info
	Mutagenesis	298	1	S → A: Prevents phosphorylation and results in strong nuclear localization.
	Mutagenesis	300	1	T → A: Prevents phosphorylation and results in strong nuclear localization.
	Mutagenesis	372	1	S → A: Prevents phosphorylation and results in strong nuclear localization.

Sequences

	Sequence		Length	Mass (Da)
	Isoform f [UniParc]. Last modified June 16, 2009. Version 2. Checksum: 8F7CA4295393BAF1	FASTA	568	63,164
	10 20 30 40 50 60 MQAWNCREVW RRIRKHLAHT SRTTVYSQFK FQIFEIFFQS FFPIFLHFAA KNSCFEPDFL 70 80 90 100 110 120 DSPLPSDITL HNLEPARPDS GMSFSTDFDD DFFNLDLHQQ ERSASFGGVT QYSQQFLREK 130 140 150 160 170 180 CSFSPYFHTS LETVDSGRTS LYGSNEQCGQ LGGASSNGST AMLHTPDGSN SHQTSFPSDF 190 200 210 220 230 240 RMSESPDDTV SGKKTTTRRN AWGNMSYAEL ITTAIMASPE KRLTLAQVYE WMVQNVPYFR 250 260 270 280 290 300 DKGDSNSSAG WKNSIRHNLS LHSRFMRIQN EGAGKSSWWV INPDAKPGRN PRRTRERSNT 310 320 330 340 350 360 IETTTKAQLE KSRRGAKKRI KERALMGSLH STLNGNSIAG SIQTISHDLY DDDSMQGAFD 370 380 390 400 410 420 NVPSSFRPRT QSNLSIPGSS SRVSPAIGSD IYDDLEFPSW VGESVPAIPS DIVDRTDQMR 430 440 450 460 470 480 IDATTHIGGV QIKQESKPIK TEPIAPPPSY HELNSVRGSC AQNPLLRNPI VPSTNFKPMP 490 500 510 520 530 540 LPGAYGNYQN GGITPINWLS TSNSSPLPGI QSCGIVAAQH TVASSSALPI DLENLTLPDQ 550 560 PLMDTMDVDA LIRHELSQAG GQHIHFDL
	Isoform a (b). Checksum: 8665FBDB428039D6	FASTA	530	57,899
	10 20 30 40 50 60 MNDSIDDDFP PEPRGRCYTW PMQQYIYQES SATIPHHHLN QHNNPYHPMH PHHQLPHMQQ 70 80 90 100 110 120 LPQPLLNLNM TTLTSSGSSV ASSIGGGAQC SPCASGSSTA ATNSSQQQQT VGQMLAASVP 130 140 150 160 170 180 CSSSGMTLGM SLNLSQGGGP MPAKKKRCRK KPTDQLAQKK PNPWGEESYS DIIAKALESA 190 200 210 220 230 240 PDGRLKLNEI YQWFSDNIPY FGERSSPEEA AGWKNSIRHN LSLHSRFMRI QNEGAGKSSW 250 260 270 280 290 300 WVINPDAKPG RNPRRTRERS NTIETTTKAQ LEKSRRGAKK RIKERALMGS LHSTLNGNSI 310 320 330 340 350 360 AGSIQTISHD LYDDDSMQGA FDNVPSSFRP RTQSNLSIPG SSSRVSPAIG SDIYDDLEFP 370 380 390 400 410 420 SWVGESVPAI PSDIVDRTDQ MRIDATTHIG GVQIKQESKP IKTEPIAPPP SYHELNSVRG 430 440 450 460 470 480 SCAQNPLLRN PIVPSTNFKP MPLPGAYGNY QNGGITPINW LSTSNSSPLP GIQSCGIVAA 490 500 510 520 530 QHTVASSSAL PIDLENLTLP DQPLMDTMDV DALIRHELSQ AGGQHIHFDL
	Isoform c (a1). Checksum: 52574F3F979B3583	FASTA	510	55,867
	10 20 30 40 50 60 MMEMLVDQGT DASSSASTST SSVSRFGADT FMNTPDDVMM NDDMEPIPRD RCNTWPMRRP 70 80 90 100 110 120 QLEPPLNSSP IIHEQIPEED ADLYGSNEQC GQLGGASSNG STAMLHTPDG SNSHQTSFPS 130 140 150 160 170 180 DFRMSESPDD TVSGKKTTTR RNAWGNMSYA ELITTAIMAS PEKRLTLAQV YEWMVQNVPY 190 200 210 220 230 240 FRDKGDSNSS AGWKNSIRHN LSLHSRFMRI QNEGAGKSSW WVINPDAKPG RNPRRTRERS 250 260 270 280 290 300 NTIETTTKAQ LEKSRRGAKK RIKERALMGS LHSTLNGNSI AGSIQTISHD LYDDDSMQGA 310 320 330 340 350 360 FDNVPSSFRP RTQSNLSIPG SSSRVSPAIG SDIYDDLEFP SWVGESVPAI PSDIVDRTDQ 370 380 390 400 410 420 MRIDATTHIG GVQIKQESKP IKTEPIAPPP SYHELNSVRG SCAQNPLLRN PIVPSTNFKP 430 440 450 460 470 480 MPLPGAYGNY QNGGITPINW LSTSNSSPLP GIQSCGIVAA QHTVASSSAL PIDLENLTLP 490 500 510 DQPLMDTMDV DALIRHELSQ AGGQHIHFDL
	Isoform b (a2). Checksum: 2C0CF97657CD6350	FASTA	508	55,578
	10 20 30 40 50 60 MMEMLVDQGT DASSSASTST SSVSRFGADT FMNTPDDVMM NDDMEPIPRD RCNTWPMRRP 70 80 90 100 110 120 QLEPPLNSSP IIHEQIPEED ADLYGSNEQC GQLGGASSNG STAMLHTPDG SNSHQTSFPS 130 140 150 160 170 180 EMSESPDDTV SGKKTTTRRN AWGNMSYAEL ITTAIMASPE KRLTLAQVYE WMVQNVPYFR 190 200 210 220 230 240 DKGDSNSSAG WKNSIRHNLS LHSRFMRIQN EGAGKSSWWV INPDAKPGRN PRRTRERSNT 250 260 270 280 290 300 IETTTKAQLE KSRRGAKKRI KERALMGSLH STLNGNSIAG SIQTISHDLY DDDSMQGAFD 310 320 330 340 350 360 NVPSSFRPRT QSNLSIPGSS SRVSPAIGSD IYDDLEFPSW VGESVPAIPS DIVDRTDQMR 370 380 390 400 410 420 IDATTHIGGV QIKQESKPIK TEPIAPPPSY HELNSVRGSC AQNPLLRNPI VPSTNFKPMP 430 440 450 460 470 480 LPGAYGNYQN GGITPINWLS TSNSSPLPGI QSCGIVAAQH TVASSSALPI DLENLTLPDQ 490 500 PLMDTMDVDA LIRHELSQAG GQHIHFDL
	Isoform d. Checksum: 6998CD8BF98A5747	FASTA	487	53,518
	10 20 30 40 50 60 MSFSTDFDDD FFNLDLHQQE RSASFGGVTQ YSQQFLREKC SFSPYFHTSL ETVDSGRTSL 70 80 90 100 110 120 YGSNEQCGQL GGASSNGSTA MLHTPDGSNS HQTSFPSDFR MSESPDDTVS GKKTTTRRNA 130 140 150 160 170 180 WGNMSYAELI TTAIMASPEK RLTLAQVYEW MVQNVPYFRD KGDSNSSAGW KNSIRHNLSL 190 200 210 220 230 240 HSRFMRIQNE GAGKSSWWVI NPDAKPGRNP RRTRERSNTI ETTTKAQLEK SRRGAKKRIK 250 260 270 280 290 300 ERALMGSLHS TLNGNSIAGS IQTISHDLYD DDSMQGAFDN VPSSFRPRTQ SNLSIPGSSS 310 320 330 340 350 360 RVSPAIGSDI YDDLEFPSWV GESVPAIPSD IVDRTDQMRI DATTHIGGVQ IKQESKPIKT 370 380 390 400 410 420 EPIAPPPSYH ELNSVRGSCA QNPLLRNPIV PSTNFKPMPL PGAYGNYQNG GITPINWLST 430 440 450 460 470 480 SNSSPLPGIQ SCGIVAAQHT VASSSALPID LENLTLPDQP LMDTMDVDAL IRHELSQAGG QHIHFDL
	Isoform e. Checksum: DD1DEB2F8E1BCCAD	FASTA	303	32,933
	10 20 30 40 50 60 MRIQNEGAGK SSWWVINPDA KPGRNPRRTR ERSNTIETTT KAQLEKSRRG AKKRIKERAL 70 80 90 100 110 120 MGSLHSTLNG NSIAGSIQTI SHDLYDDDSM QGAFDNVPSS FRPRTQSNLS IPGSSSRVSP 130 140 150 160 170 180 AIGSDIYDDL EFPSWVGESV PAIPSDIVDR TDQMRIDATT HIGGVQIKQE SKPIKTEPIA 190 200 210 220 230 240 PPPSYHELNS VRGSCAQNPL LRNPIVPSTN FKPMPLPGAY GNYQNGGITP INWLSTSNSS 250 260 270 280 290 300 PLPGIQSCGI VAAQHTVASS SALPIDLENL TLPDQPLMDT MDVDALIRHE LSQAGGQHIH FDL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The Fork head transcription factor DAF-16 transduces insulin-like metabolic and longevity signals in C. elegans." Ogg S., Paradis S., Gottlieb S., Patterson G.I., Lee L., Tissenbaum H.A., Ruvkun G. Nature 389:994-999(1997) [PubMed: 9353126] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Bristol N2.
[2]	"daf-16: An HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans." Lin K., Dorman J.B., Rodan A., Kenyon C. Science 278:1319-1322(1997) [PubMed: 9360933] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM C), FUNCTION. Strain: Bristol N2.
[3]	"Genome sequence of the nematode C. elegans: a platform for investigating biology." The C. elegans sequencing consortium Science 282:2012-2018(1998) [PubMed: 9851916] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], ALTERNATIVE SPLICING. Strain: Bristol N2.
[4]	"Identification of the differential distribution patterns of mRNAs and consensus binding sequences for mouse DAF-16 homologues." Furuyama T., Nakazawa T., Nakano I., Mori N. Biochem. J. 349:629-634(2000) [PubMed: 10880363] [Abstract] Cited for: FUNCTION.
[5]	"Regulation of C. elegans DAF-16 and its human ortholog FKHRL1 by the daf-2 insulin-like signaling pathway." Lee R.Y., Hench J., Ruvkun G. Curr. Biol. 11:1950-1957(2001) [PubMed: 11747821] [Abstract] Cited for: FUNCTION.
[6]	"daf-16 integrates developmental and environmental inputs to mediate aging in the nematode Caenorhabditis elegans." Henderson S.T., Johnson T.E. Curr. Biol. 11:1975-1980(2001) [PubMed: 11747825] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[7]	"Regulation of the Caenorhabditis elegans longevity protein DAF-16 by insulin/IGF-1 and germline signaling." Lin K., Hsin H., Libina N., Kenyon C. Nat. Genet. 28:139-145(2001) [PubMed: 11381260] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-298; THR-300 AND SER-372.
[8]	"Regulation of aging and age-related disease by DAF-16 and heat-shock factor." Hsu A.L., Murphy C.T., Kenyon C. Science 300:1142-1145(2003) [PubMed: 12750521] [Abstract] Cited for: FUNCTION.
[9]	"p38 MAPK regulates expression of immune response genes and contributes to longevity in C. elegans." Troemel E.R., Chu S.W., Reinke V., Lee S.S., Ausubel F.M., Kim D.H. PLoS Genet. 2:E183-E183(2006) [PubMed: 17096597] [Abstract] Cited for: FUNCTION.
[10]	"Opposing activities protect against age-onset proteotoxicity." Cohen E., Bieschke J., Perciavalle R.M., Kelly J.W., Dillin A. Science 313:1604-1610(2006) [PubMed: 16902091] [Abstract] Cited for: FUNCTION.
[11]	"Effects of the flavonoids kaempferol and fisetin on thermotolerance, oxidative stress and FoxO transcription factor DAF-16 in the model organism Caenorhabditis elegans." Kampkotter A., Gombitang Nkwonkam C., Zurawski R.F., Timpel C., Chovolou Y., Watjen W., Kahl R. Arch. Toxicol. 81:849-858(2007) [PubMed: 17551714] [Abstract] Cited for: SUBCELLULAR LOCATION.
[12]	"RLE-1, an E3 ubiquitin ligase, regulates C. elegans aging by catalyzing DAF-16 polyubiquitination." Li W., Gao B., Lee S.-M., Bennett K., Fang D. Dev. Cell 12:235-246(2007) [PubMed: 17276341] [Abstract] Cited for: INTERACTION WITH RLE-1, UBIQUITINATION.
[13]	"DAF-16/FOXO targets genes that regulate tumor growth in Caenorhabditis elegans." Pinkston-Gosse J., Kenyon C. Nat. Genet. 39:1403-1409(2007) [PubMed: 17934462] [Abstract] Cited for: FUNCTION.
[14]	"Tissue entrainment by feedback regulation of insulin gene expression in the endoderm of Caenorhabditis elegans." Murphy C.T., Lee S.J., Kenyon C. Proc. Natl. Acad. Sci. U.S.A. 104:19046-19050(2007) [PubMed: 18025456] [Abstract] Cited for: FUNCTION, DISRUPTION PHENOTYPE.
[15]	"Direct inhibition of the longevity-promoting factor SKN-1 by insulin-like signaling in C. elegans." Tullet J.M., Hertweck M., An J.H., Baker J., Hwang J.Y., Liu S., Oliveira R.P., Baumeister R., Blackwell T.K. Cell 132:1025-1038(2008) [PubMed: 18358814] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION.
[16]	"A 13C isotope labeling strategy reveals the influence of insulin signaling on lipogenesis in C. elegans." Perez C.L., Van Gilst M.R. Cell Metab. 8:266-274(2008) [PubMed: 18762027] [Abstract] Cited for: FUNCTION.
[17]	"DAF-16-dependent suppression of immunity during reproduction in Caenorhabditis elegans." Miyata S., Begun J., Troemel E.R., Ausubel F.M. Genetics 178:903-918(2008) [PubMed: 18245330] [Abstract] Cited for: FUNCTION.
[18]	"Sirtuin inhibition protects from the polyalanine muscular dystrophy protein PABPN1." Catoire H., Pasco M.Y., Abu-Baker A., Holbert S., Tourette C., Brais B., Rouleau G.A., Parker J.A., Neri C. Hum. Mol. Genet. 17:2108-2117(2008) [PubMed: 18397876] [Abstract] Cited for: FUNCTION.
[19]	"The MAP kinase JNK-1 of Caenorhabditis elegans: location, activation, and influences over temperature-dependent insulin-like signaling, stress responses, and fitness." Wolf M., Nunes F., Henkel A., Heinick A., Paul R.J. J. Cell. Physiol. 214:721-729(2008) [PubMed: 17894411] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
[20]	"A carbon dioxide avoidance behavior is integrated with responses to ambient oxygen and food in Caenorhabditis elegans." Bretscher A.J., Busch K.E., de Bono M. Proc. Natl. Acad. Sci. U.S.A. 105:8044-8049(2008) [PubMed: 18524954] [Abstract] Cited for: FUNCTION.
[21]	"Combined informatic and expression screen identifies the novel DAF-16 target HLH-13." Liachko N., Davidowitz R., Lee S.S. Dev. Biol. 327:97-105(2009) [PubMed: 19103192] [Abstract] Cited for: FUNCTION.
[22]	"Feeding a ROS-generator to Caenorhabditis elegans leads to increased expression of small heat shock protein HSP-16.2 and hormesis." Hartwig K., Heidler T., Moch J., Daniel H., Wenzel U. Genes Nutr. 4:59-67(2009) [PubMed: 19252938] [Abstract] Cited for: SUBCELLULAR LOCATION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF020342 mRNA. Translation: AAB84390.1. AF020343 mRNA. Translation: AAB84391.1. AF020344 mRNA. Translation: AAB84392.1. AF032112 mRNA. Translation: AAC47803.1. AF039717 Genomic DNA. Translation: AAK82917.1. AF039717 Genomic DNA. Translation: AAK82918.1. AF039717 Genomic DNA. Translation: AAK82919.1. AF039717 Genomic DNA. Translation: AAO21385.1. AF106585 Genomic DNA. No translation available.
PIR	T42234. T42255.
RefSeq	NP_001021593.1.
UniGene	Cel.18378
3D structure databases
HSSP	HSSP built from PDB template 1E17 based on UniProtKB P98177.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:25581N.
IntAct	O16850. 2 interactions.
Proteomic databases
PRIDE	O16850.
Genome annotation databases
Ensembl	R13H8.1. Caenorhabditis elegans. [Contig view]
GeneID	172981.
KEGG	cel:R13H8.1.
NMPDR	fig|6239.3.peg.2908.
Organism-specific databases
WormBase	WBGene00000912. daf-16.
WormPep	R13H8.1a. CE28771. [WorfDB] R13H8.1b. CE28772. [WorfDB] R13H8.1c. CE28773. [WorfDB] R13H8.1d. CE38722. [WorfDB] R13H8.1e. CE33160. [WorfDB] R13H8.1f. CE38723. [WorfDB]
Gene expression databases
ArrayExpress	O16850.
Family and domain databases
InterPro	IPR001766. TF_fork_head. IPR018122. TF_fork_head_CS. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
PANTHER	PTHR11829. Fork_box_protein. 1 hit.
Pfam	PF00250. Fork_head. 1 hit. [Graphical view]
PRINTS	PR00053. FORKHEAD.
ProDom	PD000425. TF_Fork_head. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00339. FH. 1 hit. [Graphical view]
PROSITE	PS00657. FORK_HEAD_1. False negative. PS00658. FORK_HEAD_2. 1 hit. PS50039. FORK_HEAD_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	877779.

Entry information

Entry name

FOXO_CAEEL

Accession

Primary (citable) accession number: O16850
Secondary accession number(s): O16849, O18676, Q86S42

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 16, 2009
Last sequence update:	June 16, 2009
Last modified:	July 7, 2009
This is version 66 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Caenorhabditis annotation project