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O43524

- FOXO3_HUMAN

UniProt

O43524 - FOXO3_HUMAN

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Protein
Forkhead box protein O3
Gene
FOXO3, FKHRL1, FOXO3A
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi157 – 25195Fork-head1 Publication
Add
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. DNA binding, bending Source: RefGenome
  3. chromatin DNA binding Source: UniProtKB
  4. core promoter binding Source: UniProtKB
  5. protein binding Source: UniProtKB
  6. protein kinase binding Source: UniProtKB
  7. sequence-specific DNA binding Source: UniProtKB
  8. sequence-specific DNA binding transcription factor activity Source: MGI

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator Source: Ensembl
  2. Fc-epsilon receptor signaling pathway Source: Reactome
  3. antral ovarian follicle growth Source: Ensembl
  4. cellular response to DNA damage stimulus Source: RefGenome
  5. cellular response to oxidative stress Source: UniProtKB
  6. epidermal growth factor receptor signaling pathway Source: Reactome
  7. extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
  8. fibroblast growth factor receptor signaling pathway Source: Reactome
  9. glucose homeostasis Source: Ensembl
  10. initiation of primordial ovarian follicle growth Source: Ensembl
  11. innate immune response Source: Reactome
  12. insulin receptor signaling pathway Source: RefGenome
  13. negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  14. neurotrophin TRK receptor signaling pathway Source: Reactome
  15. oocyte maturation Source: Ensembl
  16. ovulation from ovarian follicle Source: Ensembl
  17. pattern specification process Source: RefGenome
  18. phosphatidylinositol-mediated signaling Source: Reactome
  19. positive regulation of erythrocyte differentiation Source: MGI
  20. positive regulation of neuron apoptotic process Source: UniProtKB
  21. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  22. positive regulation of transcription, DNA-templated Source: UniProtKB
  23. regulation of cell proliferation Source: RefGenome
  24. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
  25. regulation of translation Source: UniProtKB
  26. tissue development Source: RefGenome
  27. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_111057. Signaling by NODAL.
REACT_12442. AKT phosphorylates targets in the nucleus.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
SignaLinkiO43524.

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein O3
Alternative name(s):
AF6q21 protein
Forkhead in rhabdomyosarcoma-like 1
Gene namesi
Name:FOXO3
Synonyms:FKHRL1, FOXO3A
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:3821. FOXO3.

Subcellular locationi

Cytoplasmcytosol. Nucleus
Note: Translocates to the nucleus upon oxidative stress and in the absence of survival factors.5 Publications

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: RefGenome
  3. membrane Source: Ensembl
  4. nucleoplasm Source: Reactome
  5. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

A chromosomal aberration involving FOXO3 is found in secondary acute leukemias. Translocation t(6;11)(q21;q23) with KMT2A/MLL1.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321T → A: Abolishes YWHAZ-binding; when associated with A-253. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-253 and A-315. 1 Publication
Mutagenesisi179 – 1791T → 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. 1 Publication
Mutagenesisi209 – 2091S → A: Impairs nuclear translocation upon oxidative stress. 1 Publication
Mutagenesisi242 – 2421K → A: Slightly decreases DNA affinity. 1 Publication
Mutagenesisi242 – 2421K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-259; R-290 and R-569.
Mutagenesisi245 – 2451K → A: Decreases DNA affinity. 1 Publication
Mutagenesisi253 – 2531S → A: Abolishes YWHAZ-binding; when associated with A-32. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-315. 1 Publication
Mutagenesisi259 – 2591K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-290 and R-569.
Mutagenesisi269 – 2691K → R: Methylation levels similar to wild-type; when associated with ARG-270. 1 Publication
Mutagenesisi270 – 2701K → R: Methylation levels similar to wild-type; when associated with ARG-269. 1 Publication
Mutagenesisi271 – 2711K → R: Methylation levels strongly reduced. 1 Publication
Mutagenesisi290 – 2901K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-569.
Mutagenesisi315 – 3151S → A: No effect on YWHAZ-binding. Promotes nuclear translocation. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-253. 1 Publication
Mutagenesisi399 – 3991S → 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. 1 Publication
Mutagenesisi413 – 4131S → 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. 1 Publication
Mutagenesisi555 – 5551S → 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. 1 Publication
Mutagenesisi569 – 5691K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-290.
Mutagenesisi588 – 5881S → 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. 1 Publication
Mutagenesisi626 – 6261S → 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. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA28239.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 673673Forkhead box protein O3
PRO_0000091874Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphothreonine; by PKB/AKT11 Publication
Modified residuei46 – 461N6-methyllysine1 Publication
Modified residuei149 – 1491N6-methyllysine1 Publication
Modified residuei179 – 1791Phosphothreonine; by AMPK1 Publication
Modified residuei209 – 2091Phosphoserine; by STK4/MST11 Publication
Modified residuei215 – 2151Phosphoserine; by MAPKAPK51 Publication
Modified residuei230 – 2301N6-methyllysine1 Publication
Modified residuei242 – 2421N6-acetyllysine By similarity
Modified residuei253 – 2531Phosphoserine; by PKB/AKT1 and MAPKAPK52 Publications
Modified residuei262 – 2621N6-methyllysine1 Publication
Modified residuei271 – 2711N6-methyllysine1 Publication
Modified residuei280 – 2801Phosphoserine2 Publications
Modified residuei284 – 2841Phosphoserine1 Publication
Modified residuei290 – 2901N6-methyllysine1 Publication
Modified residuei315 – 3151Phosphoserine; by SGK12 Publications
Modified residuei399 – 3991Phosphoserine; by AMPK1 Publication
Modified residuei413 – 4131Phosphoserine; by AMPK1 Publication
Modified residuei419 – 4191N6-methyllysine1 Publication
Modified residuei421 – 4211Phosphoserine1 Publication
Modified residuei551 – 5511Phosphoserine; by MAPKAPK51 Publication
Modified residuei555 – 5551Phosphoserine; by AMPK and MAPKAPK52 Publications
Modified residuei588 – 5881Phosphoserine; by AMPK1 Publication
Modified residuei626 – 6261Phosphoserine; by AMPK1 Publication

Post-translational modificationi

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.6 Publications
Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional activity in response to oxidative stress By similarity. Deacetylation by SIRT1 or SIRT2 stimulates interaction of FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3 ubiquitination and proteasomal degradation.
Heavyly methylated by SET9 which decreases stability, while moderately increasing transcriptional activity. The main methylation site is Lys-271. Methylation doesn't affect subcellular location.1 Publication
Polyubiquitinated. Ubiquitinated by a SCF complex containing SKP2, leading to proteasomal degradation.

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO43524.
PaxDbiO43524.
PRIDEiO43524.

PTM databases

PhosphoSiteiO43524.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiO43524.
BgeeiO43524.
CleanExiHS_FOXO3.
GenevestigatoriO43524.

Organism-specific databases

HPAiCAB004074.

Interactioni

Subunit structurei

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. Upon oxidative stress, interacts with STK4/MST1, which disrupts interaction with YWHAB/14-3-3-beta and leads to nuclear translocation. Interacts with PIM1. Interacts with DDIT3/CHOP. Interacts (deacetylated form) with SKP2.

Binary interactionsi

WithEntry#Exp.IntActNotes
FOXM1Q080502EBI-1644164,EBI-866480
HCFC1P516102EBI-1644164,EBI-396176
SIRT1Q96EB65EBI-1644164,EBI-1802965
SMAD4Q134854EBI-1644164,EBI-347263

Protein-protein interaction databases

BioGridi108598. 42 interactions.
DIPiDIP-29723N.
IntActiO43524. 22 interactions.
MINTiMINT-89098.
STRINGi9606.ENSP00000339527.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni156 – 1583
Helixi162 – 1698
Beta strandi172 – 1765
Helixi180 – 18910
Beta strandi198 – 2003
Helixi206 – 21611
Beta strandi217 – 22913
Beta strandi233 – 2364
Beta strandi238 – 2403
Beta strandi463 – 4653
Helixi468 – 47710
Turni478 – 4803
Helixi621 – 6233
Helixi624 – 63310

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2K86NMR-A151-251[»]
2LQHNMR-B461-635[»]
2LQINMR-B461-635[»]
2UZKX-ray2.70A/C158-253[»]
ProteinModelPortaliO43524.
SMRiO43524. Positions 158-253.

Miscellaneous databases

EvolutionaryTraceiO43524.

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi242 – 25918Nuclear localization signal1 Publication
Add
BLAST

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG5025.
HOGENOMiHOG000251635.
HOVERGENiHBG057789.
InParanoidiO43524.
KOiK09408.
OMAiNLPVMGH.
OrthoDBiEOG7R2BJD.
PhylomeDBiO43524.
TreeFamiTF315583.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O43524-1 [UniParc]FASTAAdd to Basket

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MAEAPASPAP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE    50
TAADSMIPEE EDDEDDEDGG GRAGSAMAIG GGGGSGTLGS GLLLEDSARV 100
LAPGGQDPGS GPATAAGGLS GGTQALLQPQ QPLPPPQPGA AGGSGQPRKC 150
SSRRNAWGNL SYADLITRAI ESSPDKRLTL SQIYEWMVRC VPYFKDKGDS 200
NSSAGWKNSI RHNLSLHSRF MRVQNEGTGK SSWWIINPDG GKSGKAPRRR 250
AVSMDNSNKY TKSRGRAAKK KAALQTAPES ADDSPSQLSK WPGSPTSRSS 300
DELDAWTDFR SRTNSNASTV SGRLSPIMAS TELDEVQDDD APLSPMLYSS 350
SASLSPSVSK PCTVELPRLT DMAGTMNLND GLTENLMDDL LDNITLPPSQ 400
PSPTGGLMQR SSSFPYTTKG SGLGSPTSSF NSTVFGPSSL NSLRQSPMQT 450
IQENKPATFS SMSHYGNQTL QDLLTSDSLS HSDVMMTQSD PLMSQASTAV 500
SAQNSRRNVM LRNDPMMSFA AQPNQGSLVN QNLLHHQHQT QGALGGSRAL 550
SNSVSNMGLS ESSSLGSAKH QQQSPVSQSM QTLSDSLSGS SLYSTSANLP 600
VMGHEKFPSD LDLDMFNGSL ECDMESIIRS ELMDADGLDF NFDSLISTQN 650
VVGLNVGNFT GAKQASSQSW VPG 673
Length:673
Mass (Da):71,277
Last modified:June 1, 1998 - v1
Checksum:iE5B4E830665A9982
GO

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti156 – 1638AWGNLSYA → WGKPVYS in CAA04860. 1 Publication
Sequence conflicti238 – 2469PDGGKSGKA → LMGEERKT in CAA04860. 1 Publication
Sequence conflicti253 – 2531S → T in CAA04860. 1 Publication
Sequence conflicti271 – 2711Missing in CAA04860. 1 Publication
Sequence conflicti292 – 33039PGSPT…PIMAS → AWQPHVNAAVMSWMRGRTSV HAPILTPAQSVAACRPSWQV in CAA04860. 1 Publication
Add
BLAST
Sequence conflicti345 – 36117PMLYS…SVSKP → AHALQHVSQPVTFSKQA in CAA04860. 1 Publication
Add
BLAST
Sequence conflicti367 – 3671P → R in CAA04860. 1 Publication
Sequence conflicti371 – 3711D → E in CAA04860. 1 Publication
Sequence conflicti382 – 3832LT → AD in CAA04860. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF032886 mRNA. Translation: AAC39592.1.
AL391646, AL365509 Genomic DNA. Translation: CAI16405.1.
AL365509, AL391646 Genomic DNA. Translation: CAI16295.1.
CH471051 Genomic DNA. Translation: EAW48373.1.
CH471051 Genomic DNA. Translation: EAW48374.1.
BC020227 mRNA. Translation: AAH20227.1.
BC021224 mRNA. Translation: AAH21224.1.
BC068552 mRNA. Translation: AAH68552.1.
AJ001589 mRNA. Translation: CAA04860.1.
AJ001590 Genomic DNA. Translation: CAA04861.1.
CCDSiCCDS5068.1.
RefSeqiNP_001446.1. NM_001455.3.
NP_963853.1. NM_201559.2.
UniGeneiHs.220950.

Genome annotation databases

EnsembliENST00000343882; ENSP00000339527; ENSG00000118689.
ENST00000406360; ENSP00000385824; ENSG00000118689.
GeneIDi2309.
KEGGihsa:2309.
UCSCiuc003psk.2. human.

Keywords - Coding sequence diversityi

Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF032886 mRNA. Translation: AAC39592.1 .
AL391646 , AL365509 Genomic DNA. Translation: CAI16405.1 .
AL365509 , AL391646 Genomic DNA. Translation: CAI16295.1 .
CH471051 Genomic DNA. Translation: EAW48373.1 .
CH471051 Genomic DNA. Translation: EAW48374.1 .
BC020227 mRNA. Translation: AAH20227.1 .
BC021224 mRNA. Translation: AAH21224.1 .
BC068552 mRNA. Translation: AAH68552.1 .
AJ001589 mRNA. Translation: CAA04860.1 .
AJ001590 Genomic DNA. Translation: CAA04861.1 .
CCDSi CCDS5068.1.
RefSeqi NP_001446.1. NM_001455.3.
NP_963853.1. NM_201559.2.
UniGenei Hs.220950.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2K86 NMR - A 151-251 [» ]
2LQH NMR - B 461-635 [» ]
2LQI NMR - B 461-635 [» ]
2UZK X-ray 2.70 A/C 158-253 [» ]
ProteinModelPortali O43524.
SMRi O43524. Positions 158-253.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108598. 42 interactions.
DIPi DIP-29723N.
IntActi O43524. 22 interactions.
MINTi MINT-89098.
STRINGi 9606.ENSP00000339527.

Chemistry

ChEMBLi CHEMBL5778.

PTM databases

PhosphoSitei O43524.

Proteomic databases

MaxQBi O43524.
PaxDbi O43524.
PRIDEi O43524.

Protocols and materials databases

DNASUi 2309.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343882 ; ENSP00000339527 ; ENSG00000118689 .
ENST00000406360 ; ENSP00000385824 ; ENSG00000118689 .
GeneIDi 2309.
KEGGi hsa:2309.
UCSCi uc003psk.2. human.

Organism-specific databases

CTDi 2309.
GeneCardsi GC06P108881.
HGNCi HGNC:3821. FOXO3.
HPAi CAB004074.
MIMi 602681. gene.
neXtProti NX_O43524.
PharmGKBi PA28239.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5025.
HOGENOMi HOG000251635.
HOVERGENi HBG057789.
InParanoidi O43524.
KOi K09408.
OMAi NLPVMGH.
OrthoDBi EOG7R2BJD.
PhylomeDBi O43524.
TreeFami TF315583.

Enzyme and pathway databases

Reactomei REACT_111057. Signaling by NODAL.
REACT_12442. AKT phosphorylates targets in the nucleus.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
SignaLinki O43524.

Miscellaneous databases

ChiTaRSi FOXO3. human.
EvolutionaryTracei O43524.
GeneWikii FOXO3.
GenomeRNAii 2309.
NextBioi 9379.
PROi O43524.
SOURCEi Search...

Gene expression databases

ArrayExpressi O43524.
Bgeei O43524.
CleanExi HS_FOXO3.
Genevestigatori O43524.

Family and domain databases

Gene3Di 1.10.10.10. 1 hit.
InterProi IPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view ]
Pfami PF00250. Fork_head. 1 hit.
[Graphical view ]
PRINTSi PR00053. FORKHEAD.
SMARTi SM00339. FH. 1 hit.
[Graphical view ]
PROSITEi PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Rhabdomyosarcoma.
  2. "The DNA sequence and analysis of human chromosome 6."
    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.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle and Placenta.
  5. "AF6q21, a novel partner of the MLL gene in t(6;11)(q21;q23), defines a forkhead transcriptional factor subfamily."
    Hillion J., Le Coniat M., Jonveaux P., Berger R., Bernard O.A.
    Blood 90:3714-3719(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 1-383, INVOLVEMENT IN SECONDARY ACUTE LEUKEMIAS.
  6. "Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor."
    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.
    Cell 96:857-868(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT THR-32; SER-253 AND SER-315, MUTAGENESIS OF THR-32; SER-253 AND SER-315.
  7. "Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)."
    Brunet A., Park J., Tran H., Hu L.S., Hemmings B.A., Greenberg M.E.
    Mol. Cell. Biol. 21:952-965(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-315.
  8. "A conserved MST-FOXO signaling pathway mediates oxidative-stress responses and extends life span."
    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.
    Cell 125:987-1001(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION AT SER-209, INTERACTION WITH STK4/MST1 AND YWHAB, SUBCELLULAR LOCATION, MUTAGENESIS OF SER-209.
  9. "The energy sensor AMP-activated protein kinase directly regulates the mammalian FOXO3 transcription factor."
    Greer E.L., Oskoui P.R., Banko M.R., Maniar J.M., Gygi M.P., Gygi S.P., Brunet A.
    J. Biol. Chem. 282:30107-30119(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: 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, SUBCELLULAR LOCATION.
  10. "Pim kinases promote cell cycle progression by phosphorylating and down-regulating p27Kip1 at the transcriptional and posttranscriptional levels."
    Morishita D., Katayama R., Sekimizu K., Tsuruo T., Fujita N.
    Cancer Res. 68:5076-5085(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PIM1, PHOSPHORYLATION.
  11. "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
    Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
    J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-421, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-284, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "The MK5/PRAK kinase and Myc form a negative feedback loop that is disrupted during colorectal tumorigenesis."
    Kress T.R., Cannell I.G., Brenkman A.B., Samans B., Gaestel M., Roepman P., Burgering B.M., Bushell M., Rosenwald A., Eilers M.
    Mol. Cell 41:445-457(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DNA-BINDING, PHOSPHORYLATION AT SER-215; SER-253; SER-551 AND SER-555.
  17. "Methylation by Set9 modulates FoxO3 stability and transcriptional activity."
    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.
    Aging (Albany NY) 4:462-479(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-46; LYS-149; LYS-230; LYS-262; LYS-271; LYS-290 AND LYS-419, MUTAGENESIS OF LYS-269; LYS-270 AND LYS-271.
  18. "Deacetylation of FOXO3 by SIRT1 or SIRT2 leads to Skp2-mediated FOXO3 ubiquitination and degradation."
    Wang F., Chan C.H., Chen K., Guan X., Lin H.K., Tong Q.
    Oncogene 31:1546-1557(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION, DEACETYLATION BY SIRT2, INTERACTION WITH SKP2, UBIQUITINATION BY SKP2, MUTAGENESIS OF LYS-242; LYS-259; LYS-290 AND LYS-569.
  19. "CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress."
    Ghosh A.P., Klocke B.J., Ballestas M.E., Roth K.A.
    PLoS ONE 7:E39586-E39586(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DDIT3, SUBCELLULAR LOCATION.
  20. "Crystal structure of the human FOXO3a-DBD/DNA complex suggests the effects of post-translational modification."
    Tsai K.-L., Sun Y.-J., Huang C.-Y., Yang J.-Y., Hung M.-C., Hsiao C.-D.
    Nucleic Acids Res. 35:6984-6994(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 158-253 IN COMPLEX WITH DNA, MUTAGENESIS OF LYS-242 AND LYS-245, NUCLEAR LOCALIZATION SIGNAL.

Entry informationi

Entry nameiFOXO3_HUMAN
AccessioniPrimary (citable) accession number: O43524
Secondary accession number(s): E1P5E6
, O15171, Q5T2I7, Q9BZ04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: September 3, 2014
This is version 157 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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