Q12778 (FOXO1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Forkhead box protein O1

Alternative name(s):
Forkhead box protein O1A
Forkhead in rhabdomyosarcoma

Gene names

Name:	FOXO1
Synonyms:	FKHR, FOXO1A

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	655 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Transcription factor which acts as a regulator of cell responses to oxidative stress. In the presence of KIRT1, mediates down-regulation of cyclin D1 and up-regulation of CDKN1B levels which are required for cell transition from proliferative growth to quiescence By similarity. Triggers death of postmitotic neurons when phosphorylated by CDK1. Activates transcription of PMAIP1. Ref.9 Ref.12 Ref.15
Subunit structure	Interacts with LRPPRC By similarity. Interacts with SIRT1 and this interaction requires the presence of KRIT1 By similarity. Interacts with NLK By similarity. Binds to CDK1 and 14-3-3 proteins. Ref.12
Subcellular location	Cytoplasm. Nucleus. Note: Shuttles between cytoplasm and nucleus. Translocates to the nucleus upon oxidative stress induced phosphorylation at Ser-212 by STK4/MST1. Translocates to the nucleus upon phosphorylation of Thr-24, Ser-256 and Ser-322 by SGK1 By similarity. Ref.7 Ref.9 Ref.15
Tissue specificity	Ubiquitous. Ref.2
Induction	Expression is regulated by KRIT1. Ref.14
Post-translational modification	Phosphorylated by AKT1; insulin-induced By similarity. Phosphorylated by NLK, which inhibits transcriptional activity and promotes nuclear export By similarity. IGF1 rapidly induces phosphorylation of Ser-256, Thr-24, and Ser-319. Phosphorylation of Ser-256 decreases DNA-binding activity and promotes the phosphorylation of Thr-24, and Ser-319, permitting phosphorylation of Ser-322 and Ser-325, probably by CK1, leading to nuclear exclusion and loss of function. Phosphorylation of Ser-329 is independent of IGF1 and leads to reduced function. Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylation of Ser-249 by CDK1 disrupts 14-3-3 proteins binding and thereby promotes FOXO1 nuclear accumulation and subsequent transcription activation and cell death. Phosphorylated by STK4/MST1 on Ser-212 upon oxidative stress. Phosphorylated on Thr-24, Ser-256 and Ser-322 by SGK1 resulting in its translocation from the nucleus to the cytoplasm By similarity. Ref.6 Ref.7 Ref.8 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15
Involvement in disease	Defects in FOXO1 are a cause of rhabdomyosarcoma type 2 (RMS2) [MIM:268220]. It is a form of rhabdomyosarcoma, a highly malignant tumor of striated muscle derived from primitive mesenchimal cells and exhibiting differentiation along rhabdomyoblastic lines. Rhabdomyosarcoma is one of the most frequently occurring soft tissue sarcomas and the most common in children. It occurs in four forms: alveolar, pleomorphic, embryonal and botryoidal rhabdomyosarcomas. Note=Chromosomal aberrations involving FOXO1 are found in rhabdomyosarcoma. Translocation (2;13)(q35;q14) with PAX3; translocation t(1;13)(p36;q14) with PAX7. The resulting protein is a transcriptional activator.
Sequence similarities	Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Chromosomal rearrangement
Disease	Proto-oncogene
Ligand	DNA-binding
Molecular function	Activator
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Uncategorized	promoter binding Inferred from Biological aspect of Ancestor. Source: RefGenome specific RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome specific transcriptional repressor activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Biological process	anti-apoptosis Inferred from direct assay. Source: UniProtKB blood vessel development Inferred from Biological aspect of Ancestor. Source: RefGenome embryo development Inferred from Biological aspect of Ancestor. Source: RefGenome endocrine pancreas development Traceable author statement. Source: Reactome fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome insulin receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of stress-activated MAPK cascade Inferred from direct assay. Source: BHF-UCL nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome pattern specification process Inferred from Biological aspect of Ancestor. Source: RefGenome phosphatidylinositol-mediated signaling Traceable author statement. Source: Reactome positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay Ref.9. Source: UniProtKB regulation of cell proliferation Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome response to DNA damage stimulus Inferred from Biological aspect of Ancestor. Source: RefGenome tissue development Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytosol Traceable author statement. Source: Reactome transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	DNA binding, bending Inferred from Biological aspect of Ancestor. Source: RefGenome double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein kinase binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from direct assay Ref.9. Source: UniProtKB sequence-specific distal enhancer binding RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription factor binding Inferred from Biological aspect of Ancestor. Source: RefGenome
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDK1	P06493	5	EBI-1108782,EBI-444308
ESR1	P03372	2	EBI-1108782,EBI-78473
FHL2	Q14192	8	EBI-1108782,EBI-701903
SIRT1	Q96EB6	2	EBI-1108782,EBI-1802965

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 655

655

Forkhead box protein O1

PRO_0000091872

Regions

DNA binding

159 – 235

77

Fork-head

Compositional bias

91 – 102

12

Poly-Ala

Compositional bias

120 – 130

11

Poly-Pro

Compositional bias

152 – 155

4

Poly-Ser

Amino acid modifications

Modified residue

24

1

Phosphothreonine; by PKB/AKT1 or PKB/AKT2 and SGK1 Ref.6 Ref.8

Modified residue

212

1

Phosphoserine; by STK4/MST1 Ref.15

Modified residue

249

1

Phosphoserine; by CDK1 Ref.12

Modified residue

256

1

Phosphoserine; by PKB/AKT1 and SGK1 Ref.6 Ref.8

Modified residue

287

1

Phosphoserine Ref.11 Ref.13

Modified residue

319

1

Phosphoserine; by PKB/AKT1 Ref.6 Ref.8

Modified residue

322

1

Phosphoserine; by CK1 and SGK1 Ref.8

Modified residue

325

1

Phosphoserine; by CK1 Ref.8

Modified residue

329

1

Phosphoserine; by DYRK1A Ref.7 Ref.8

Modified residue

467

1

Phosphothreonine By similarity

Modified residue

468

1

Phosphoserine By similarity

Modified residue

505

1

Phosphoserine Ref.10

Modified residue

509

1

Phosphoserine Ref.10

Experimental info

Mutagenesis

24

1

T → A: Nuclear targeting and enhanced transactivation; when associated with A-319. Ref.9

Mutagenesis

245

1

K → A: Disrupts DNA binding; when associated with A-248.

Mutagenesis

248

1

K → A: Disrupts DNA binding; when associated with A-245.

Mutagenesis

249

1

S → A: Impaired phosphorylation by CDK1. Ref.12

Mutagenesis

251 – 253

3

RRR → SAS: Disrupts DNA binding.

Mutagenesis

256

1

S → A: Nuclear targeting. Abolishes the ability of IGF1 to suppress transactivation. Prevents T-24 and S-319 phosphorylation. Enhances transactivation; when associated with A-24 and A-319. Ref.9

Mutagenesis

256

1

S → D: Reduces DNA binding, promotes nuclear exclusion and partially promotes T-24 and S-319 phosphorylation. Reduces DNA binding, does not promote nuclear exclusion but reduces transactivation; when associated with A-24 and A-319. Ref.9

Mutagenesis

319

1

S → A: Nuclear targeting and enhanced transactivation; when associated with A-24. Ref.9

Mutagenesis

329

1

S → A: Nuclear targeting and enhanced transactivation. Ref.7

Sequence conflict

131

1

L → V in AAA03629. Ref.1

Sequence conflict

343

1

V → M in AAH70065. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

655

Helix Strand Turn

Details...

Beta strand

156 – 158

3

Helix

165 – 175

11

Helix

183 – 193

11

Helix

195 – 197

3

Helix

203 – 206

4

Helix

210 – 219

10

Beta strand

223 – 226

4

Beta strand

236 – 239

4

Sequences

	Sequence		Length	Mass (Da)
	Q12778 [UniParc]. Last modified October 17, 2006. Version 2. Checksum: 6DEF6C994BDFDBAB	FASTA	655	69,662
	10 20 30 40 50 60 MAEAPQVVEI DPDFEPLPRP RSCTWPLPRP EFSQSNSATS SPAPSGSAAA NPDAAAGLPS 70 80 90 100 110 120 ASAAAVSADF MSNLSLLEES EDFPQAPGSV AAAVAAAAAA AATGGLCGDF QGPEAGCLHP 130 140 150 160 170 180 APPQPPPPGP LSQHPPVPPA AAGPLAGQPR KSSSSRRNAW GNLSYADLIT KAIESSAEKR 190 200 210 220 230 240 LTLSQIYEWM VKSVPYFKDK GDSNSSAGWK NSIRHNLSLH SKFIRVQNEG TGKSSWWMLN 250 260 270 280 290 300 PEGGKSGKSP RRRAASMDNN SKFAKSRSRA AKKKASLQSG QEGAGDSPGS QFSKWPASPG 310 320 330 340 350 360 SHSNDDFDNW STFRPRTSSN ASTISGRLSP IMTEQDDLGE GDVHSMVYPP SAAKMASTLP 370 380 390 400 410 420 SLSEISNPEN MENLLDNLNL LSSPTSLTVS TQSSPGTMMQ QTPCYSFAPP NTSLNSPSPN 430 440 450 460 470 480 YQKYTYGQSS MSPLPQMPIQ TLQDNKSSYG GMSQYNCAPG LLKELLTSDS PPHNDIMTPV 490 500 510 520 530 540 DPGVAQPNSR VLGQNVMMGP NSVMSTYGSQ ASHNKMMNPS SHTHPGHAQQ TSAVNGRPLP 550 560 570 580 590 600 HTVSTMPHTS GMNRLTQVKT PVQVPLPHPM QMSALGGYSS VSSCNGYGRM GLLHQEKLPS 610 620 630 640 650 DLDGMFIERL DCDMESIIRN DLMDGDTLDF NFDNVLPNQS FPHSVKTTTH SWVSG

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Fusion of a fork head domain gene to PAX3 in the solid tumour alveolar rhabdomyosarcoma." Galili N., Davis R.J., Fredericks W.J., Mukhopadhyay S., Rauscher F.J. III, Emanuel B.S., Rovera G., Barr F.G. Nat. Genet. 5:230-235(1993) [PubMed: 8275086] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], CHROMOSOMAL TRANSLOCATION WITH PAX3.
[2]	"Cloning and characterization of three human forkhead genes that comprise an FKHR-like gene subfamily." Anderson M.J., Viars C.S., Czekay S., Cavenee W.K., Arden K.C. Genomics 47:187-199(1998) [PubMed: 9479491] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. Tissue: Rhabdomyosarcoma.
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"The DNA sequence and analysis of human chromosome 13." Dunham A., Matthews L.H., Burton J., Ashurst J.L., Howe K.L., Ashcroft K.J., Beare D.M., Burford D.C., Hunt S.E., Griffiths-Jones S., Jones M.C., Keenan S.J., Oliver K., Scott C.E., Ainscough R., Almeida J.P., Ambrose K.D., Andrews D.T. , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Bannerjee R., Barlow K.F., Bates K., Beasley H., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burrill W., Carder C., Carter N.P., Chapman J.C., Clamp M.E., Clark S.Y., Clarke G., Clee C.M., Clegg S.C., Cobley V., Collins J.E., Corby N., Coville G.J., Deloukas P., Dhami P., Dunham I., Dunn M., Earthrowl M.E., Ellington A.G., Faulkner L., Frankish A.G., Frankland J., French L., Garner P., Garnett J., Gilbert J.G.R., Gilson C.J., Ghori J., Grafham D.V., Gribble S.M., Griffiths C., Hall R.E., Hammond S., Harley J.L., Hart E.A., Heath P.D., Howden P.J., Huckle E.J., Hunt P.J., Hunt A.R., Johnson C., Johnson D., Kay M., Kimberley A.M., King A., Laird G.K., Langford C.J., Lawlor S., Leongamornlert D.A., Lloyd D.M., Lloyd C., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., McLaren S.J., McMurray A., Milne S., Moore M.J.F., Nickerson T., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K.M., Rice C.M., Searle S., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Steward C.A., Sycamore N., Tester J., Thomas D.W., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Wilming L., Wray P.W., Wright M.W., Young L., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Beck S., Bentley D.R., Rogers J., Ross M.T. Nature 428:522-528(2004) [PubMed: 15057823] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lymph and Placenta.
[6]	"Phosphorylation of the transcription factor forkhead family member FKHR by protein kinase B." Rena G., Guo S., Cichy S.C., Unterman T.G., Cohen P. J. Biol. Chem. 274:17179-17183(1999) [PubMed: 10358075] [Abstract] Cited for: PHOSPHORYLATION AT THR-24; SER-256 AND SER-319.
[7]	"The kinase DYRK1A phosphorylates the transcription factor FKHR at Ser329 in vitro, a novel in vivo phosphorylation site." Woods Y.L., Rena G., Morrice N., Barthel A., Becker W., Guo S., Unterman T.G., Cohen P. Biochem. J. 355:597-607(2001) [PubMed: 11311120] [Abstract] Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-329, MUTAGENESIS OF SER-329.
[8]	"Two novel phosphorylation sites on FKHR that are critical for its nuclear exclusion." Rena G., Woods Y.L., Prescott A.R., Peggie M., Unterman T.G., Williams M.R., Cohen P. EMBO J. 21:2263-2271(2002) [PubMed: 11980723] [Abstract] Cited for: PHOSPHORYLATION AT THR-24; SER-256; SER-319; SER-322; SER-325 AND SER-329.
[9]	"Phosphorylation of serine 256 suppresses transactivation by FKHR (FOXO1) by multiple mechanisms. Direct and indirect effects on nuclear/cytoplasmic shuttling and DNA binding." Zhang X., Gan L., Pan H., Guo S., He X., Olson S.T., Mesecar A., Adam S., Unterman T.G. J. Biol. Chem. 277:45276-45284(2002) [PubMed: 12228231] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-24; SER-256 AND SER-319.
[10]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-505 AND SER-509, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[11]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"Activation of FOXO1 by Cdk1 in cycling cells and postmitotic neurons." Yuan Z., Becker E.B.E., Merlo P., Yamada T., DiBacco S., Konishi Y., Schaefer E.M., Bonni A. Science 319:1665-1668(2008) [PubMed: 18356527] [Abstract] Cited for: FUNCTION, PHOSPHORYLATION AT SER-249 BY CDK1, INTERACTION WITH CDK1 AND 14-3-3 PROTEINS, MUTAGENESIS OF SER-249.
[13]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[14]	"KRIT1 regulates the homeostasis of intracellular reactive oxygen species." Goitre L., Balzac F., Degani S., Degan P., Marchi S., Pinton P., Retta S.F. PLoS ONE 5:E11786-E11786(2010) [PubMed: 20668652] [Abstract] Cited for: INDUCTION.
[15]	"Hippo/Mst1 stimulates transcription of the proapoptotic mediator NOXA in a FoxO1-dependent manner." Valis K., Prochazka L., Boura E., Chladova J., Obsil T., Rohlena J., Truksa J., Dong L.F., Ralph S.J., Neuzil J. Cancer Res. 71:946-954(2011) [PubMed: 21245099] [Abstract] Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-212.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U02310 mRNA. Translation: AAA03629.1.
AF032885 mRNA. Translation: AAC39591.1.
BT007455 mRNA. Translation: AAP36123.1.
AL355132, AL133318 Genomic DNA. Translation: CAH70978.1.
AL133318, AL355132 Genomic DNA. Translation: CAI16970.1.
BC021981 mRNA. Translation: AAH21981.1.
BC070065 mRNA. Translation: AAH70065.3.

IPI

IPI00289866.

PIR

S40521.

RefSeq

NP_002006.2. NM_002015.3.

UniGene

Hs.370666.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3CO6	X-ray	2.10	C	151-249	[»]
3CO7	X-ray	2.91	C/F	151-266	[»]
3COA	X-ray	2.20	C/F	151-266	[»]

ProteinModelPortal

Q12778.

SMR

Q12778. Positions 154-244.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-35654N.

IntAct

Q12778. 6 interactions.

STRING

Q12778.

PTM databases

PhosphoSite

Q12778.

Polymorphism databases

DMDM

116241368.

Proteomic databases

PRIDE

Q12778.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000379561; ENSP00000368880; ENSG00000150907.

GeneID

2308.

KEGG

hsa:2308.

UCSC

uc001uxl.2. human.

Organism-specific databases

CTD

2308.

GeneCards

GC13M041129.

H-InvDB

HIX0011258.

HGNC

HGNC:3819. FOXO1.

HPA

CAB022326.
HPA001252.

MIM

136533. gene.
268220. phenotype.

neXtProt

NX_Q12778.

Orphanet

99756. Alveolar rhabdomyosarcoma.

PharmGKB

PA162388858.
PA28237.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG11255.

GeneTree

ENSGT00390000000589.

HOGENOM

HBG714085.

HOVERGEN

HBG057789.

InParanoid

Q12778.

OMA

PPHNDIL.

OrthoDB

EOG49S66C.

PhylomeDB

Q12778.

Enzyme and pathway databases

Pathway_Interaction_DB

angiopoietinreceptor_pathway. Angiopoietin receptor Tie2-mediated signaling.
pi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
foxopathway. FoxO family signaling.
il6_7pathway. IL6-mediated signaling events.
ar_tf_pathway. Regulation of Androgen receptor activity.
smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.
hdac_classiii_pathway. Signaling events mediated by HDAC Class III.

Reactome

REACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q12778.

Bgee

Q12778.

CleanEx

HS_FOXO1.

Genevestigator

Q12778.

GermOnline

ENSG00000150907. Homo sapiens.

Family and domain databases

InterPro

IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]

Gene3D

G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.

KO

K07201.

Pfam

PF00250. Fork_head. 1 hit.
[Graphical view]

PRINTS

PR00053. FORKHEAD.

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

NextBio

9375.

SOURCE

Search...

Entry information

Entry name

FOXO1_HUMAN

Accession

Primary (citable) accession number: Q12778
Secondary accession number(s): O43523, Q5VYC7, Q6NSK6

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	October 17, 2006
Last modified:	January 25, 2012
This is version 124 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.