O43524 (FOXO3_HUMAN) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 142.
History...
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Forkhead box protein O3 Alternative name(s): AF6q21 protein Forkhead in rhabdomyosarcoma-like 1 | ||||
| Gene names |
| ||||
| Organism | Homo sapiens (Human) [Reference proteome] | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo![]() |
Protein attributes
| Sequence length | 673 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | 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. Ref.6 Ref.8 Ref.16 |
| Subunit structure | 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. Ref.8 Ref.10 Ref.18 |
| Subcellular location | Cytoplasm › cytosol. Nucleus. Note: Translocates to the nucleus upon oxidative stress and in the absence of survival factors. Ref.6 Ref.8 Ref.9 Ref.16 Ref.18 |
| Tissue specificity | Ubiquitous. Ref.1 |
| Post-translational modification | 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.16 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. Ref.17 |
| Involvement in disease | A chromosomal aberration involving FOXO3 is found in secondary acute leukemias. Translocation t(6;11)(q21;q23) with MLL/HRX. |
| Sequence similarities | Contains 1 fork-head DNA-binding domain. |
Ontologies
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| FOXM1 | Q08050 | 2 | EBI-1644164,EBI-866480 | |
| HCFC1 | P51610 | 2 | EBI-1644164,EBI-396176 | |
| SIRT1 | Q96EB6 | 5 | EBI-1644164,EBI-1802965 | |
| SMAD4 | Q13485 | 4 | EBI-1644164,EBI-347263 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Initiator methionine | 1 | 1 | Removed Ref.14 | |||||||||||||||||||||||||||||||
| Chain | 2 – 673 | 672 | Forkhead box protein O3 | PRO_0000091874 | ||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||
| DNA binding | 157 – 251 | 95 | Fork-head Ref.16 | |||||||||||||||||||||||||||||||
| Motif | 242 – 259 | 18 | Nuclear localization signal Ref.19 | |||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||
| Modified residue | 2 | 1 | N-acetylalanine Ref.14 | |||||||||||||||||||||||||||||||
| Modified residue | 7 | 1 | Phosphoserine Ref.13 Ref.14 | |||||||||||||||||||||||||||||||
| Modified residue | 12 | 1 | Phosphoserine Ref.13 Ref.14 | |||||||||||||||||||||||||||||||
| Modified residue | 32 | 1 | Phosphothreonine; by PKB/AKT1 Ref.6 | |||||||||||||||||||||||||||||||
| Modified residue | 46 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 149 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 179 | 1 | Phosphothreonine; by AMPK Ref.9 | |||||||||||||||||||||||||||||||
| Modified residue | 209 | 1 | Phosphoserine; by STK4/MST1 Ref.8 | |||||||||||||||||||||||||||||||
| Modified residue | 215 | 1 | Phosphoserine; by MAPKAPK5 Ref.16 | |||||||||||||||||||||||||||||||
| Modified residue | 230 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 253 | 1 | Phosphoserine; by PKB/AKT1 and MAPKAPK5 Ref.6 Ref.16 | |||||||||||||||||||||||||||||||
| Modified residue | 262 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 271 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 280 | 1 | Phosphoserine Ref.12 Ref.13 | |||||||||||||||||||||||||||||||
| Modified residue | 284 | 1 | Phosphoserine Ref.12 | |||||||||||||||||||||||||||||||
| Modified residue | 290 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 315 | 1 | Phosphoserine; by SGK1 Ref.6 Ref.7 | |||||||||||||||||||||||||||||||
| Modified residue | 399 | 1 | Phosphoserine; by AMPK Ref.9 | |||||||||||||||||||||||||||||||
| Modified residue | 413 | 1 | Phosphoserine; by AMPK Ref.9 | |||||||||||||||||||||||||||||||
| Modified residue | 419 | 1 | N6-methyllysine Ref.17 | |||||||||||||||||||||||||||||||
| Modified residue | 421 | 1 | Phosphoserine Ref.11 | |||||||||||||||||||||||||||||||
| Modified residue | 551 | 1 | Phosphoserine; by MAPKAPK5 Ref.16 | |||||||||||||||||||||||||||||||
| Modified residue | 555 | 1 | Phosphoserine; by AMPK and MAPKAPK5 Ref.9 Ref.16 | |||||||||||||||||||||||||||||||
| Modified residue | 588 | 1 | Phosphoserine; by AMPK Ref.9 | |||||||||||||||||||||||||||||||
| Modified residue | 626 | 1 | Phosphoserine; by AMPK Ref.9 | |||||||||||||||||||||||||||||||
Experimental info | ||||||||||||||||||||||||||||||||||
| Mutagenesis | 32 | 1 | T → A: Abolishes YWHAZ-binding; when associated with A-253. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-253 and A-315. Ref.6 | |||||||||||||||||||||||||||||||
| Mutagenesis | 179 | 1 | T → 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. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 209 | 1 | S → A: Impairs nuclear translocation upon oxidative stress. Ref.8 | |||||||||||||||||||||||||||||||
| Mutagenesis | 242 | 1 | K → A: Slightly decreases DNA affinity. Ref.19 | |||||||||||||||||||||||||||||||
| Mutagenesis | 245 | 1 | K → A: Decreases DNA affinity. Ref.19 | |||||||||||||||||||||||||||||||
| Mutagenesis | 253 | 1 | S → A: Abolishes YWHAZ-binding; when associated with A-32. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-315. Ref.6 | |||||||||||||||||||||||||||||||
| Mutagenesis | 269 | 1 | K → R: Methylation levels similar to wild-type; when associated with ARG-270. Ref.17 | |||||||||||||||||||||||||||||||
| Mutagenesis | 270 | 1 | K → R: Methylation levels similar to wild-type; when associated with ARG-269. Ref.17 | |||||||||||||||||||||||||||||||
| Mutagenesis | 271 | 1 | K → R: Methylation levels strongly reduced. Ref.17 | |||||||||||||||||||||||||||||||
| Mutagenesis | 315 | 1 | S → A: No effect on YWHAZ-binding. Promotes nuclear translocation. Exclusively nuclear, induces transcription and promotes apoptosis; when associated with A-32 and A-253. Ref.6 | |||||||||||||||||||||||||||||||
| Mutagenesis | 399 | 1 | S → 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. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 413 | 1 | S → 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. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 555 | 1 | S → 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. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 588 | 1 | S → 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. Ref.9 | |||||||||||||||||||||||||||||||
| Mutagenesis | 626 | 1 | S → 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. Ref.9 | |||||||||||||||||||||||||||||||
| Sequence conflict | 156 – 163 | 8 | AWGNLSYA → WGKPVYS in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 238 – 246 | 9 | PDGGKSGKA → LMGEERKT in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 253 | 1 | S → T in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 271 | 1 | Missing in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 292 – 330 | 39 | PGSPT…PIMAS → AWQPHVNAAVMSWMRGRTSV HAPILTPAQSVAACRPSWQV in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 345 – 361 | 17 | PMLYS…SVSKP → AHALQHVSQPVTFSKQA in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 367 | 1 | P → R in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 371 | 1 | D → E in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
| Sequence conflict | 382 – 383 | 2 | LT → AD in CAA04860. Ref.5 | |||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||
| Turn | 156 – 158 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 162 – 169 | 8 | ||||||||||||||||||||||||||||||||
| Beta strand | 172 – 176 | 5 | ||||||||||||||||||||||||||||||||
| Helix | 180 – 189 | 10 | ||||||||||||||||||||||||||||||||
| Beta strand | 198 – 200 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 206 – 216 | 11 | ||||||||||||||||||||||||||||||||
| Beta strand | 217 – 229 | 13 | ||||||||||||||||||||||||||||||||
| Beta strand | 233 – 236 | 4 | ||||||||||||||||||||||||||||||||
| Beta strand | 238 – 240 | 3 | ||||||||||||||||||||||||||||||||
| Beta strand | 463 – 465 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 468 – 477 | 10 | ||||||||||||||||||||||||||||||||
| Turn | 478 – 480 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 621 – 623 | 3 | ||||||||||||||||||||||||||||||||
| Helix | 624 – 633 | 10 | ||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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. Beck S.Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [3] | Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. Venter J.C.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [12] | "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-284, MASS SPECTROMETRY. Tissue: Cervix carcinoma. |
| [13] | "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-7; SER-12 AND SER-280, MASS SPECTROMETRY. Tissue: Leukemic T-cell. |
| [14] | "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-7 AND SER-12, MASS SPECTROMETRY, CLEAVAGE OF INITIATOR METHIONINE. Tissue: Cervix carcinoma. |
| [15] | "Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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] | "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. |
| [19] | "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. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | 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. | ||||||||||||||||||||||||||||||
| IPI | IPI00012856. | ||||||||||||||||||||||||||||||
| RefSeq | NP_001446.1. NM_001455.3. NP_963853.1. NM_201559.2. | ||||||||||||||||||||||||||||||
| UniGene | Hs.220950. | ||||||||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||||||||
| PDBe RCSB PDB PDBj |
| ||||||||||||||||||||||||||||||
| ProteinModelPortal | O43524. | ||||||||||||||||||||||||||||||
| ModBase | Search... | ||||||||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||||||||
| DIP | DIP-29723N. | ||||||||||||||||||||||||||||||
| IntAct | O43524. 18 interactions. | ||||||||||||||||||||||||||||||
| MINT | MINT-89098. | ||||||||||||||||||||||||||||||
| STRING | 9606.ENSP00000339527. | ||||||||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||||||||
| PhosphoSite | O43524. | ||||||||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||||||||
| PaxDb | O43524. | ||||||||||||||||||||||||||||||
| PRIDE | O43524. | ||||||||||||||||||||||||||||||
Protocols and materials databases | |||||||||||||||||||||||||||||||
| DNASU | 2309. | ||||||||||||||||||||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||||||||
| Ensembl | ENST00000343882; ENSP00000339527; ENSG00000118689. ENST00000406360; ENSP00000385824; ENSG00000118689. | ||||||||||||||||||||||||||||||
| GeneID | 2309. | ||||||||||||||||||||||||||||||
| KEGG | hsa:2309. | ||||||||||||||||||||||||||||||
| UCSC | uc003psk.2. human. | ||||||||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||||||||
| CTD | 2309. | ||||||||||||||||||||||||||||||
| GeneCards | GC06P108881. | ||||||||||||||||||||||||||||||
| HGNC | HGNC:3821. FOXO3. | ||||||||||||||||||||||||||||||
| HPA | CAB004074. | ||||||||||||||||||||||||||||||
| MIM | 602681. gene. | ||||||||||||||||||||||||||||||
| neXtProt | NX_O43524. | ||||||||||||||||||||||||||||||
| PharmGKB | PA28239. | ||||||||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||||||||
| eggNOG | COG5025. | ||||||||||||||||||||||||||||||
| HOGENOM | HOG000251635. | ||||||||||||||||||||||||||||||
| HOVERGEN | HBG057789. | ||||||||||||||||||||||||||||||
| InParanoid | O43524. | ||||||||||||||||||||||||||||||
| KO | K09408. | ||||||||||||||||||||||||||||||
| OMA | NLPVMGH. | ||||||||||||||||||||||||||||||
| OrthoDB | EOG4N8R4G. | ||||||||||||||||||||||||||||||
| PhylomeDB | O43524. | ||||||||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||||||||
| Pathway_Interaction_DB | pi3kcipathway. Class I PI3K signaling events. pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. foxopathway. FoxO family signaling. il2_pi3kpathway. IL2 signaling events mediated by PI3K. insulin_pathway. Insulin Pathway. smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling. hdac_classiii_pathway. Signaling events mediated by HDAC Class III. kitpathway. Signaling events mediated by Stem cell factor receptor (c-Kit). pi3kplctrkpathway. Trk receptor signaling mediated by PI3K and PLC-gamma. | ||||||||||||||||||||||||||||||
| Reactome | REACT_111045. Developmental Biology. REACT_111102. Signal Transduction. REACT_116125. Disease. REACT_6900. Immune System. | ||||||||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||||||||
| ArrayExpress | O43524. | ||||||||||||||||||||||||||||||
| Bgee | O43524. | ||||||||||||||||||||||||||||||
| CleanEx | HS_FOXO3. | ||||||||||||||||||||||||||||||
| Genevestigator | O43524. | ||||||||||||||||||||||||||||||
| GermOnline | ENSG00000118689. Homo sapiens. | ||||||||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||||||||
| Gene3D | 1.10.10.10. 1 hit. | ||||||||||||||||||||||||||||||
| InterPro | IPR001766. TF_fork_head. IPR018122. TF_fork_head_CS. IPR011991. WHTH_DNA-bd_dom. [Graphical view] | ||||||||||||||||||||||||||||||
| 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 | |||||||||||||||||||||||||||||||
| ChEMBL | CHEMBL5778. | ||||||||||||||||||||||||||||||
| ChiTaRS | FOXO3. human. | ||||||||||||||||||||||||||||||
| EvolutionaryTrace | O43524. | ||||||||||||||||||||||||||||||
| GenomeRNAi | 2309. | ||||||||||||||||||||||||||||||
| NextBio | 9379. | ||||||||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||||||||
Entry information
| Entry name | FOXO3_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O43524 Secondary accession number(s): E1P5E6 Q9BZ04 | ||||||||
| Entry 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. | ||||||||
Relevant documents
| Human chromosome 6 Human chromosome 6: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with
