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Protein

Forkhead box protein O3

Gene

FOXO3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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)DescriptionActionsGraphical viewLength
DNA bindingi157 – 251Fork-headPROSITE-ProRule annotationAdd BLAST95

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • chromatin DNA binding Source: UniProtKB
  • core promoter binding Source: UniProtKB
  • DNA binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • sequence-specific DNA binding Source: UniProtKB
  • transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: Ensembl
  • transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific binding Source: BHF-UCL
  • transcription factor activity, sequence-specific DNA binding Source: MGI

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Apoptosis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000118689-MONOMER.
ReactomeiR-HSA-1181150. Signaling by NODAL.
R-HSA-198693. AKT phosphorylates targets in the nucleus.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
R-HSA-5687128. MAPK6/MAPK4 signaling.
SignaLinkiO43524.
SIGNORiO43524.

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein O3Curated
Alternative name(s):
AF6q21 protein1 Publication
Forkhead in rhabdomyosarcoma-like 11 Publication
Gene namesi
Name:FOXO3Imported
Synonyms:FKHRL11 Publication, FOXO3A1 Publication
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:3821. FOXO3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: FlyBase
  • membrane Source: Ensembl
  • mitochondrion Source: Ensembl
  • nucleoplasm Source: HPA
  • 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)DescriptionActionsGraphical viewLength
Mutagenesisi32T → 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 Publication1
Mutagenesisi179T → 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 Publication1
Mutagenesisi209S → A: Impairs nuclear translocation upon oxidative stress. 1 Publication1
Mutagenesisi242K → A: Slightly decreases DNA affinity. 2 Publications1
Mutagenesisi242K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-259; R-290 and R-569. 2 Publications1
Mutagenesisi245K → A: Decreases DNA affinity. 1 Publication1
Mutagenesisi253S → 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 Publication1
Mutagenesisi259K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-290 and R-569. 1 Publication1
Mutagenesisi269K → R: Methylation levels similar to wild-type; when associated with ARG-270. 1 Publication1
Mutagenesisi270K → R: Methylation levels similar to wild-type; when associated with ARG-269. 1 Publication1
Mutagenesisi271K → R: Methylation levels strongly reduced. 1 Publication1
Mutagenesisi290K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-569. 1 Publication1
Mutagenesisi315S → 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 Publication1
Mutagenesisi399S → 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 Publication1
Mutagenesisi413S → 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 Publication1
Mutagenesisi555S → 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 Publication1
Mutagenesisi569K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-290. 1 Publication1
Mutagenesisi588S → 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 Publication1
Mutagenesisi626S → 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 Publication1
Mutagenesisi644S → A: Loss of phosphorylation by IKKB. 1 Publication1

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

DisGeNETi2309.
OpenTargetsiENSG00000118689.
PharmGKBiPA28239.

Chemistry databases

ChEMBLiCHEMBL5778.

Polymorphism and mutation databases

BioMutaiFOXO3.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000918741 – 673Forkhead box protein O3Add BLAST673

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei32Phosphothreonine; by PKB/AKT11 Publication1
Modified residuei46N6-methyllysine1 Publication1
Modified residuei149N6-methyllysine1 Publication1
Modified residuei179Phosphothreonine; by AMPK1 Publication1
Modified residuei209Phosphoserine; by STK4/MST11 Publication1
Modified residuei215Phosphoserine; by MAPKAPK51 Publication1
Modified residuei230N6-methyllysine1 Publication1
Modified residuei242N6-acetyllysineBy similarity1
Modified residuei253Phosphoserine; by PKB/AKT1 and MAPKAPK52 Publications1
Modified residuei262N6-methyllysine1 Publication1
Modified residuei271N6-methyllysine1 Publication1
Modified residuei280PhosphoserineCombined sources1
Modified residuei284PhosphoserineCombined sources1
Modified residuei290N6-methyllysine1 Publication1
Modified residuei294PhosphoserineBy similarity1
Modified residuei299Phosphoserine; by CaMK2ACombined sources1 Publication1
Modified residuei311PhosphoserineCombined sources1
Modified residuei315Phosphoserine; by SGK12 Publications1
Modified residuei399Phosphoserine; by AMPK1 Publication1
Modified residuei413Phosphoserine; by AMPKCombined sources1 Publication1
Modified residuei419N6-methyllysine1 Publication1
Modified residuei421PhosphoserineCombined sources1
Modified residuei551Phosphoserine; by MAPKAPK5Combined sources1 Publication1
Modified residuei555Phosphoserine; by AMPK and MAPKAPK52 Publications1
Modified residuei588Phosphoserine; by AMPK1 Publication1
Modified residuei626Phosphoserine; by AMPK1 Publication1
Modified residuei644Phosphoserine; by IKKB1 Publication1

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 (PubMed:10102273, PubMed:11154281, PubMed:16751106, PubMed:17711846, PubMed:18593906, PubMed:21329882). Phosphorylated by CHUK/IKKA and IKBKB/IKKB. TNF-induced inactivation of FOXO3 requires its phosphorylation at Ser-644 by IKBKB/IKKB which promotes FOXO3 retention in the cytoplasm, polyubiquitination and ubiquitin-mediated proteasomal degradation (PubMed:15084260). May be dephosphorylated by calcineurin A on Ser-299 which abolishes FOXO3 transcriptional activity (By similarity).By similarity7 Publications
Deacetylation by SIRT1 or SIRT2 stimulates interaction of FOXO3 with SKP2 and facilitates SCF(SKP2)-mediated FOXO3 ubiquitination and proteasomal degradation (PubMed:21841822). Deacetylation by SIRT2 stimulates FOXO3-mediated transcriptional activity in response to oxidative stress (By similarity).By similarity1 Publication
Heavily methylated by SET9 which decreases stability, while moderately increasing transcriptional activity. The main methylation site is Lys-271. Methylation doesn't affect subcellular location.1 Publication
Polyubiquitinated. Ubiquitinated by a SCF complex containing SKP2, leading to proteasomal degradation.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO43524.
MaxQBiO43524.
PaxDbiO43524.
PeptideAtlasiO43524.
PRIDEiO43524.

PTM databases

iPTMnetiO43524.
PhosphoSitePlusiO43524.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

BgeeiENSG00000118689.
CleanExiHS_FOXO3.
GenevisibleiO43524. HS.

Organism-specific databases

HPAiCAB004074.
HPA063104.

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 (PubMed:16751106). Upon oxidative stress, interacts with STK4/MST1, which disrupts interaction with YWHAB/14-3-3-beta and leads to nuclear translocation (PubMed:16751106). Interacts with PIM1 (PubMed:18593906). Interacts with DDIT3/CHOP (PubMed:22761832). Interacts (deacetylated form) with SKP2 (PubMed:21841822). Interacts with CHUK and IKBKB (PubMed:15084260, PubMed:22313691). Interacts with CAMK2A, CAMK2B and calcineurin A (By similarity).By similarity6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ARHGEF2Q929742EBI-1644164,EBI-302405
CDC27P302602EBI-1644164,EBI-994813
CREBBPQ927933EBI-1644164,EBI-81215
Foxg1Q609875EBI-1644164,EBI-11166131From a different organism.
FOXK1P850372EBI-1644164,EBI-2509974
FOXM1Q080502EBI-1644164,EBI-866480
HCFC1P516102EBI-1644164,EBI-396176
PIM1P113092EBI-1644164,EBI-696621
PNKPQ96T602EBI-1644164,EBI-1045072
RB1P064002EBI-1644164,EBI-491274
RBL1P287493EBI-1644164,EBI-971402
SIRT1Q96EB65EBI-1644164,EBI-1802965
SMAD3P840225EBI-1644164,EBI-347161
SMAD4Q134859EBI-1644164,EBI-347263
TAF5LO755292EBI-1644164,EBI-1785876
TP53P046372EBI-1644164,EBI-366083

GO - Molecular functioni

  • beta-catenin binding Source: ParkinsonsUK-UCL
  • protein kinase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108598. 62 interactors.
DIPiDIP-29723N.
IntActiO43524. 38 interactors.
MINTiMINT-89098.
STRINGi9606.ENSP00000339527.

Chemistry databases

BindingDBiO43524.

Structurei

Secondary structure

1673
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni156 – 158Combined sources3
Helixi162 – 169Combined sources8
Beta strandi172 – 176Combined sources5
Helixi180 – 189Combined sources10
Beta strandi198 – 200Combined sources3
Helixi206 – 216Combined sources11
Beta strandi217 – 229Combined sources13
Beta strandi233 – 236Combined sources4
Beta strandi238 – 240Combined sources3
Beta strandi463 – 465Combined sources3
Helixi468 – 477Combined sources10
Turni478 – 480Combined sources3
Helixi621 – 623Combined sources3
Helixi624 – 633Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K86NMR-A151-251[»]
2LQHNMR-B461-635[»]
2LQINMR-B461-635[»]
2UZKX-ray2.70A/C158-253[»]
ProteinModelPortaliO43524.
SMRiO43524.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO43524.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni300 – 673Mediates interaction with CHUK/IKKA and IKBKB/IKKB1 PublicationAdd BLAST374

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi242 – 259Nuclear localization signal1 PublicationAdd BLAST18

Sequence similaritiesi

Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2294. Eukaryota.
COG5025. LUCA.
GeneTreeiENSGT00790000123003.
HOGENOMiHOG000251635.
HOVERGENiHBG057789.
InParanoidiO43524.
KOiK09408.
OMAiWMINPDG.
OrthoDBiEOG091G06K3.
PhylomeDBiO43524.
TreeFamiTF315583.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. Fork_head_dom.
IPR032067. FOXO-TAD.
IPR032068. FOXO_KIX-bd.
IPR030456. TF_fork_head_CS_2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Forkhead. 1 hit.
PF16676. FOXO-TAD. 1 hit.
PF16675. FOXO_KIX_bdg. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O43524-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MAEAPASPAP LSPLEVELDP EFEPQSRPRS CTWPLQRPEL QASPAKPSGE
60 70 80 90 100
TAADSMIPEE EDDEDDEDGG GRAGSAMAIG GGGGSGTLGS GLLLEDSARV
110 120 130 140 150
LAPGGQDPGS GPATAAGGLS GGTQALLQPQ QPLPPPQPGA AGGSGQPRKC
160 170 180 190 200
SSRRNAWGNL SYADLITRAI ESSPDKRLTL SQIYEWMVRC VPYFKDKGDS
210 220 230 240 250
NSSAGWKNSI RHNLSLHSRF MRVQNEGTGK SSWWIINPDG GKSGKAPRRR
260 270 280 290 300
AVSMDNSNKY TKSRGRAAKK KAALQTAPES ADDSPSQLSK WPGSPTSRSS
310 320 330 340 350
DELDAWTDFR SRTNSNASTV SGRLSPIMAS TELDEVQDDD APLSPMLYSS
360 370 380 390 400
SASLSPSVSK PCTVELPRLT DMAGTMNLND GLTENLMDDL LDNITLPPSQ
410 420 430 440 450
PSPTGGLMQR SSSFPYTTKG SGLGSPTSSF NSTVFGPSSL NSLRQSPMQT
460 470 480 490 500
IQENKPATFS SMSHYGNQTL QDLLTSDSLS HSDVMMTQSD PLMSQASTAV
510 520 530 540 550
SAQNSRRNVM LRNDPMMSFA AQPNQGSLVN QNLLHHQHQT QGALGGSRAL
560 570 580 590 600
SNSVSNMGLS ESSSLGSAKH QQQSPVSQSM QTLSDSLSGS SLYSTSANLP
610 620 630 640 650
VMGHEKFPSD LDLDMFNGSL ECDMESIIRS ELMDADGLDF NFDSLISTQN
660 670
VVGLNVGNFT GAKQASSQSW VPG
Length:673
Mass (Da):71,277
Last modified:June 1, 1998 - v1
Checksum:iE5B4E830665A9982
GO
Isoform 2 (identifier: O43524-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-220: Missing.

Note: No experimental confirmation available.
Show »
Length:453
Mass (Da):48,406
Checksum:iE093364532E78AE1
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti156 – 163AWGNLSYA → WGKPVYS in CAA04860 (PubMed:9345057).Curated8
Sequence conflicti238 – 246PDGGKSGKA → LMGEERKT in CAA04860 (PubMed:9345057).Curated9
Sequence conflicti253S → T in CAA04860 (PubMed:9345057).Curated1
Sequence conflicti271Missing in CAA04860 (PubMed:9345057).Curated1
Sequence conflicti292 – 330PGSPT…PIMAS → AWQPHVNAAVMSWMRGRTSV HAPILTPAQSVAACRPSWQV in CAA04860 (PubMed:9345057).CuratedAdd BLAST39
Sequence conflicti345 – 361PMLYS…SVSKP → AHALQHVSQPVTFSKQA in CAA04860 (PubMed:9345057).CuratedAdd BLAST17
Sequence conflicti367P → R in CAA04860 (PubMed:9345057).Curated1
Sequence conflicti371D → E in CAA04860 (PubMed:9345057).Curated1
Sequence conflicti382 – 383LT → AD in CAA04860 (PubMed:9345057).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0562251 – 220Missing in isoform 2. 1 PublicationAdd BLAST220

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032886 mRNA. Translation: AAC39592.1.
AK301304 mRNA. Translation: BAG62858.1.
AL096818 Genomic DNA. No translation available.
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. [O43524-1]
RefSeqiNP_001446.1. NM_001455.3. [O43524-1]
NP_963853.1. NM_201559.2. [O43524-1]
XP_005266925.1. XM_005266868.3. [O43524-2]
XP_011533930.1. XM_011535628.2. [O43524-2]
XP_011533931.1. XM_011535629.2. [O43524-2]
XP_016866075.1. XM_017010586.1. [O43524-2]
UniGeneiHs.220950.

Genome annotation databases

EnsembliENST00000343882; ENSP00000339527; ENSG00000118689. [O43524-1]
ENST00000406360; ENSP00000385824; ENSG00000118689. [O43524-1]
ENST00000540898; ENSP00000446316; ENSG00000118689. [O43524-2]
GeneIDi2309.
KEGGihsa:2309.
UCSCiuc003psk.3. human. [O43524-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF032886 mRNA. Translation: AAC39592.1.
AK301304 mRNA. Translation: BAG62858.1.
AL096818 Genomic DNA. No translation available.
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. [O43524-1]
RefSeqiNP_001446.1. NM_001455.3. [O43524-1]
NP_963853.1. NM_201559.2. [O43524-1]
XP_005266925.1. XM_005266868.3. [O43524-2]
XP_011533930.1. XM_011535628.2. [O43524-2]
XP_011533931.1. XM_011535629.2. [O43524-2]
XP_016866075.1. XM_017010586.1. [O43524-2]
UniGeneiHs.220950.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2K86NMR-A151-251[»]
2LQHNMR-B461-635[»]
2LQINMR-B461-635[»]
2UZKX-ray2.70A/C158-253[»]
ProteinModelPortaliO43524.
SMRiO43524.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108598. 62 interactors.
DIPiDIP-29723N.
IntActiO43524. 38 interactors.
MINTiMINT-89098.
STRINGi9606.ENSP00000339527.

Chemistry databases

BindingDBiO43524.
ChEMBLiCHEMBL5778.

PTM databases

iPTMnetiO43524.
PhosphoSitePlusiO43524.

Polymorphism and mutation databases

BioMutaiFOXO3.

Proteomic databases

EPDiO43524.
MaxQBiO43524.
PaxDbiO43524.
PeptideAtlasiO43524.
PRIDEiO43524.

Protocols and materials databases

DNASUi2309.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000343882; ENSP00000339527; ENSG00000118689. [O43524-1]
ENST00000406360; ENSP00000385824; ENSG00000118689. [O43524-1]
ENST00000540898; ENSP00000446316; ENSG00000118689. [O43524-2]
GeneIDi2309.
KEGGihsa:2309.
UCSCiuc003psk.3. human. [O43524-1]

Organism-specific databases

CTDi2309.
DisGeNETi2309.
GeneCardsiFOXO3.
HGNCiHGNC:3821. FOXO3.
HPAiCAB004074.
HPA063104.
MIMi602681. gene.
neXtProtiNX_O43524.
OpenTargetsiENSG00000118689.
PharmGKBiPA28239.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2294. Eukaryota.
COG5025. LUCA.
GeneTreeiENSGT00790000123003.
HOGENOMiHOG000251635.
HOVERGENiHBG057789.
InParanoidiO43524.
KOiK09408.
OMAiWMINPDG.
OrthoDBiEOG091G06K3.
PhylomeDBiO43524.
TreeFamiTF315583.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000118689-MONOMER.
ReactomeiR-HSA-1181150. Signaling by NODAL.
R-HSA-198693. AKT phosphorylates targets in the nucleus.
R-HSA-5674400. Constitutive Signaling by AKT1 E17K in Cancer.
R-HSA-5687128. MAPK6/MAPK4 signaling.
SignaLinkiO43524.
SIGNORiO43524.

Miscellaneous databases

ChiTaRSiFOXO3. human.
EvolutionaryTraceiO43524.
GeneWikiiFOXO3.
GenomeRNAii2309.
PROiO43524.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000118689.
CleanExiHS_FOXO3.
GenevisibleiO43524. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR001766. Fork_head_dom.
IPR032067. FOXO-TAD.
IPR032068. FOXO_KIX-bd.
IPR030456. TF_fork_head_CS_2.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00250. Forkhead. 1 hit.
PF16676. FOXO-TAD. 1 hit.
PF16675. FOXO_KIX_bdg. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
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Entry informationi

Entry nameiFOXO3_HUMAN
AccessioniPrimary (citable) accession number: O43524
Secondary accession number(s): B4DVZ6
, E1P5E6, O15171, Q5T2I7, Q9BZ04
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: June 1, 1998
Last modified: November 30, 2016
This is version 183 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.