UniProtKB - O43524 (FOXO3_HUMAN)
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- BLAST>sp|O43524|FOXO3_HUMAN Forkhead box protein O3 OS=Homo sapiens OX=9606 GN=FOXO3 PE=1 SV=1 MAEAPASPAPLSPLEVELDPEFEPQSRPRSCTWPLQRPELQASPAKPSGETAADSMIPEE EDDEDDEDGGGRAGSAMAIGGGGGSGTLGSGLLLEDSARVLAPGGQDPGSGPATAAGGLS GGTQALLQPQQPLPPPQPGAAGGSGQPRKCSSRRNAWGNLSYADLITRAIESSPDKRLTL SQIYEWMVRCVPYFKDKGDSNSSAGWKNSIRHNLSLHSRFMRVQNEGTGKSSWWIINPDG GKSGKAPRRRAVSMDNSNKYTKSRGRAAKKKAALQTAPESADDSPSQLSKWPGSPTSRSS DELDAWTDFRSRTNSNASTVSGRLSPIMASTELDEVQDDDAPLSPMLYSSSASLSPSVSK PCTVELPRLTDMAGTMNLNDGLTENLMDDLLDNITLPPSQPSPTGGLMQRSSSFPYTTKG SGLGSPTSSFNSTVFGPSSLNSLRQSPMQTIQENKPATFSSMSHYGNQTLQDLLTSDSLS HSDVMMTQSDPLMSQASTAVSAQNSRRNVMLRNDPMMSFAAQPNQGSLVNQNLLHHQHQT QGALGGSRALSNSVSNMGLSESSSLGSAKHQQQSPVSQSMQTLSDSLSGSSLYSTSANLP VMGHEKFPSDLDLDMFNGSLECDMESIIRSELMDADGLDFNFDSLISTQNVVGLNVGNFT GAKQASSQSWVPG
- Align
Forkhead box protein O3
FOXO3
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"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. - Ref.10"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. - Ref.18"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. - Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION.
Regions
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi | 157 – 251 | Fork-headPROSITE-ProRule annotation <p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi Add BLAST | 95 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- beta-catenin binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- chromatin DNA binding Source: UniProtKB
- core promoter binding Source: UniProtKB
- DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- DNA binding transcription factor activity Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- mitochondrial sequence-specific DNA binding transcription factor activity Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: NTNU_SB
- sequence-specific DNA binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: Ensembl
- transcriptional repressor activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- transcription cofactor binding Source: Ensembl
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- aging Source: Ensembl
- anatomical structure morphogenesis Source: GO_Central
- antral ovarian follicle growth Source: Ensembl
- brain morphogenesis Source: Ensembl
- cellular response to amyloid-beta Source: Ensembl
- cellular response to corticosterone stimulus Source: Ensembl
- cellular response to glucose stimulus Source: Ensembl
- cellular response to hypoxia Source: Ensembl
- cellular response to nerve growth factor stimulus Source: Ensembl
- cellular response to oxidative stress Source: UniProtKB
- cytokine-mediated signaling pathway Source: Reactome
- DNA damage response, signal transduction by p53 class mediator Source: Ensembl
- extrinsic apoptotic signaling pathway in absence of ligand Source: Ensembl
- initiation of primordial ovarian follicle growth Source: Ensembl
- mitochondrial transcription Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- negative regulation of canonical Wnt signaling pathway Source: Ensembl
- negative regulation of neuron differentiation Source: Ensembl
- negative regulation of transcription by RNA polymerase II Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- neuronal stem cell population maintenance Source: Ensembl
- oocyte maturation Source: Ensembl
- ovulation from ovarian follicle Source: Ensembl
- positive regulation of apoptotic process Source: BHF-UCL <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of endothelial cell apoptotic process Source: Ensembl
- positive regulation of erythrocyte differentiation Source: MGI <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of hydrogen peroxide-mediated programmed cell death Source: Ensembl
- positive regulation of neuron apoptotic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- positive regulation of reactive oxygen species biosynthetic process Source: Ensembl
- positive regulation of transcription, DNA-templated Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of transcription by RNA polymerase II Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- regulation of neural precursor cell proliferation Source: Ensembl
- regulation of transcription by RNA polymerase II Source: UniProtKB
- regulation of translation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- response to dexamethasone Source: Ensembl
- response to nutrient levels Source: Ensembl
- response to water-immersion restraint stress Source: Ensembl
- tumor necrosis factor-mediated signaling pathway Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Activator, DNA-binding |
| Biological process | Apoptosis, Transcription, Transcription regulation |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-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 R-HSA-6785807 Interleukin-4 and 13 signaling R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation R-HSA-8952158 RUNX3 regulates BCL2L11 (BIM) transcription |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O43524 |
SIGNOR Signaling Network Open Resource More...SIGNORi | O43524 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Forkhead box protein O3CuratedAlternative name(s): AF6q21 protein1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
Forkhead in rhabdomyosarcoma-like 11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
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| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:FOXO3Imported <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More...</a></p> Manual assertion inferred from database entriesi Synonyms:FKHRL11 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
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| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
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Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000118689.14 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3821 FOXO3 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602681 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O43524 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Nucleus
- Nucleus 9 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"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. - Ref.9"IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a."
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y., Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.
Cell 117:225-237(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHUK AND IKBKB, REGION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-644, MUTAGENESIS OF SER-644. - Ref.10"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. - Ref.11"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. - Ref.18"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. - Ref.20"IKK-beta mediates chemoresistance by sequestering FOXO3; a critical factor for cell survival and death."
Tezil T., Bodur C., Kutuk O., Basaga H.
Cell. Signal. 24:1361-1368(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IKBKB, SUBCELLULAR LOCATION. - Ref.22"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. - Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION. - Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
- Nucleus 9 Publications
Cytosol
- cytosol 8 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"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. - Ref.9"IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a."
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y., Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.
Cell 117:225-237(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHUK AND IKBKB, REGION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-644, MUTAGENESIS OF SER-644. - Ref.10"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. - Ref.11"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. - Ref.18"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. - Ref.20"IKK-beta mediates chemoresistance by sequestering FOXO3; a critical factor for cell survival and death."
Tezil T., Bodur C., Kutuk O., Basaga H.
Cell. Signal. 24:1361-1368(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IKBKB, SUBCELLULAR LOCATION. - Ref.22"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. - Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION.
- cytosol 8 Publications
Mitochondrion
- Mitochondrion matrix 2 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION. - Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
- Mitochondrion outer membrane 1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
Note: Retention in the cytoplasm contributes to its inactivation (PubMed:10102273, PubMed:15084260, PubMed:16751106). Translocates to the nucleus upon oxidative stress and in the absence of survival factors (PubMed:10102273, PubMed:16751106). Translocates in a AMPK-dependent manner into the mitochondrion in response to metabolic stress (PubMed:23283301, PubMed:29445193).5 Publications- Mitochondrion matrix 2 Publications
- Ref.7"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. - Ref.9"IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a."
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y., Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.
Cell 117:225-237(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHUK AND IKBKB, REGION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-644, MUTAGENESIS OF SER-644. - Ref.10"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. - Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION. - Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Cytosol
- cytosol Source: FlyBase <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Mitochondrion
- mitochondrial matrix Source: UniProtKB-SubCell
- mitochondrial outer membrane Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Nucleus
- nucleoplasm Source: HPA
- nucleus Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Other locations
- cytoplasm Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein-containing complex Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Membrane, Mitochondrion, Mitochondrion outer membrane, Nucleus<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 2 – 148 | Missing : Loss of localization to the mitochondrion outer membrane and loss of translocation into the mitochondrion following metabolic stress. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 147 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 2 – 30 | Missing : Loss of translocation into the mitochondrion following metabolic stress. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 29 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 12 | S → A in normal cells, no defect in mitochondrion import following metabolic stress. In cancer cells, defective mitochondrion import following metabolic stress and abolition of ERK-mediated phosphorylation. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 30 | S → A: Abolishes phosphorylation. Loss of localization to the mitochondrion outer membrane and loss of translocation into the mitochondrion following metabolic stress. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 32 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 80 – 108 | Missing : Loss of translocation into the mitochondrion following metabolic stress. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 29 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 179 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 209 | S → A: Impairs nuclear translocation upon oxidative stress. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 242 – 271 | Missing : Loss of nuclear import. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 30 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 242 | K → A: Slightly decreases DNA affinity. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 242 | K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-259; R-290 and R-569. 2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 245 | K → A: Decreases DNA affinity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 253 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 259 | K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-290 and R-569. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 269 | K → R: Methylation levels similar to wild-type; when associated with ARG-270. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 270 | K → R: Methylation levels similar to wild-type; when associated with ARG-269. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 271 | K → R: Methylation levels strongly reduced. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 290 | K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-569. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 315 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 399 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 413 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 555 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 569 | K → R: Reduces acetylation, increases interaction with SKP2 and inhibits FOXO3 ubiquitination and degradation; when associated with R-242; R-259 and R-290. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 588 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 626 | 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. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 644 | S → A: Loss of phosphorylation by IKKB. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Diseasei
Proto-oncogeneOrganism-specific databases
DisGeNET More...DisGeNETi | 2309 |
Open Targets More...OpenTargetsi | ENSG00000118689 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA28239 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5778 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | FOXO3 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000091874 | 1 – 673 | Forkhead box protein O3Add BLAST | 673 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 30 | Phosphoserine; by AMPK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 32 | Phosphothreonine; by PKB/AKT11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 46 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 149 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 179 | Phosphothreonine; by AMPK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 209 | Phosphoserine; by STK4/MST11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 215 | Phosphoserine; by MAPKAPK51 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 230 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 242 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 253 | Phosphoserine; by PKB/AKT1 and MAPKAPK52 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 262 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 271 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 280 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 284 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 290 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 294 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 299 | Phosphoserine; by CaMK2ACombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 311 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 315 | Phosphoserine; by SGK12 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 399 | Phosphoserine; by AMPK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 413 | Phosphoserine; by AMPKCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 419 | N6-methyllysine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 421 | PhosphoserineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 551 | Phosphoserine; by MAPKAPK5Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 555 | Phosphoserine; by AMPK and MAPKAPK52 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 588 | Phosphoserine; by AMPK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 626 | Phosphoserine; by AMPK1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 644 | Phosphoserine; by IKKB1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
8 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.7"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. - Ref.8"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. - Ref.9"IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a."
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y., Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.
Cell 117:225-237(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHUK AND IKBKB, REGION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-644, MUTAGENESIS OF SER-644. - Ref.10"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. - Ref.11"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. - Ref.12"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. - Ref.18"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. - Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
2 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"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. - Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.21"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.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Methylation, Phosphoprotein, Ubl conjugationProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O43524 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O43524 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O43524 |
PeptideAtlas More...PeptideAtlasi | O43524 |
PRoteomics IDEntifications database More...PRIDEi | O43524 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 49029 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O43524 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O43524 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.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] (ISOFORM 1), TISSUE SPECIFICITY.
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000118689 |
CleanEx database of gene expression profiles More...CleanExi | HS_FOXO3 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O43524 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | CAB004074 HPA063104 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
8 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.9"IkappaB kinase promotes tumorigenesis through inhibition of forkhead FOXO3a."
Hu M.C., Lee D.F., Xia W., Golfman L.S., Ou-Yang F., Yang J.Y., Zou Y., Bao S., Hanada N., Saso H., Kobayashi R., Hung M.C.
Cell 117:225-237(2004) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH CHUK AND IKBKB, REGION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-644, MUTAGENESIS OF SER-644. - Ref.10"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. - Ref.12"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. - Ref.20"IKK-beta mediates chemoresistance by sequestering FOXO3; a critical factor for cell survival and death."
Tezil T., Bodur C., Kutuk O., Basaga H.
Cell. Signal. 24:1361-1368(2012) [PubMed] [Europe PMC] [Abstract]Cited for: INTERACTION WITH IKBKB, SUBCELLULAR LOCATION. - Ref.21"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. - Ref.22"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. - Ref.23"A novel AMPK-dependent FoxO3A-SIRT3 intramitochondrial complex sensing glucose levels."
Peserico A., Chiacchiera F., Grossi V., Matrone A., Latorre D., Simonatto M., Fusella A., Ryall J.G., Finley L.W., Haigis M.C., Villani G., Puri P.L., Sartorelli V., Simone C.
Cell. Mol. Life Sci. 70:2015-2029(2013) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH SIRT3 AND POLRMT, SUBCELLULAR LOCATION, ACETYLATION. - Ref.26"Uncoupling FoxO3A mitochondrial and nuclear functions in cancer cells undergoing metabolic stress and chemotherapy."
Celestini V., Tezil T., Russo L., Fasano C., Sanese P., Forte G., Peserico A., Lepore Signorile M., Longo G., De Rasmo D., Signorile A., Gadaleta R.M., Scialpi N., Terao M., Garattini E., Cocco T., Villani G., Moschetta A., Grossi V., Simone C.
Cell Death Dis. 9:231-231(2018) [PubMed] [Europe PMC] [Abstract]Cited for: IDENTIFICATION IN A COMPLEX WITH SIRT3; TFAM AND POLRMT, SUBCELLULAR LOCATION, PROTEOLYTIC CLEAVAGE, PHOSPHORYLATION AT SER-30, NUCLEAR LOCALIZATION SIGNAL, MUTAGENESIS OF 2-ALA--SER-30; 2-ALA--ARG-148; SER-12; SER-30; 80-GLY--PRO-108 AND 241-LYS--LYS-271.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
| With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| AKT1 | P31749 | 3 | EBI-1644164,EBI-296087 | |
| ARHGEF2 | Q92974 | 2 | EBI-1644164,EBI-302405 | |
| CDC27 | P30260 | 2 | EBI-1644164,EBI-994813 | |
| CREBBP | Q92793 | 3 | EBI-1644164,EBI-81215 | |
| Foxg1 | Q60987 | 5 | EBI-1644164,EBI-11166131 | From Mus musculus. |
| FOXK1 | P85037 | 2 | EBI-1644164,EBI-2509974 | |
| FOXM1 | Q08050 | 2 | EBI-1644164,EBI-866480 | |
| HCFC1 | P51610 | 2 | EBI-1644164,EBI-396176 | |
| MYC | P01106 | 3 | EBI-1644164,EBI-447544 | |
| PIM1 | P11309 | 2 | EBI-1644164,EBI-696621 | |
| PNKP | Q96T60 | 2 | EBI-1644164,EBI-1045072 | |
| RB1 | P06400 | 2 | EBI-1644164,EBI-491274 | |
| RBL1 | P28749 | 3 | EBI-1644164,EBI-971402 | |
| SIRT1 | Q96EB6 | 5 | EBI-1644164,EBI-1802965 | |
| SMAD3 | P84022 | 5 | EBI-1644164,EBI-347161 | |
| SMAD4 | Q13485 | 9 | EBI-1644164,EBI-347263 | |
| TAF5L | O75529 | 2 | EBI-1644164,EBI-1785876 | |
| TP53 | P04637 | 2 | EBI-1644164,EBI-366083 | |
| YWHAZ | P63104 | 2 | EBI-1644164,EBI-347088 | |
| Ywhaz | P63101 | 2 | EBI-1644164,EBI-354751 | From Mus musculus. |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- beta-catenin binding Source: ParkinsonsUK-UCL <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- protein kinase binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- transcription cofactor binding Source: Ensembl
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108598, 65 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1123 FOXO3-MYC complex CPX-1147 FOXO3-YWHAZ complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O43524 |
Database of interacting proteins More...DIPi | DIP-29723N |
Protein interaction database and analysis system More...IntActi | O43524, 43 interactors |
Molecular INTeraction database More...MINTi | O43524 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000339527 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O43524 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 156 – 158 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 162 – 169 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 172 – 176 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 180 – 189 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 198 – 200 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 206 – 216 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 217 – 229 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 233 – 236 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 238 – 240 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 463 – 465 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 468 – 477 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 478 – 480 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB 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 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O43524 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O43524 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O43524 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 80 – 108 | Required for mitochondrial import1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 29 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 300 – 673 | Mediates interaction with CHUK/IKKA and IKBKB/IKKB1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 374 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 242 – 259 | Nuclear localization signal2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 18 |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2294 Eukaryota COG5025 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149005 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000251635 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057789 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O43524 |
KEGG Orthology (KO) More...KOi | K09408 |
Identification of Orthologs from Complete Genome Data More...OMAi | PSVSKPC |
Database of Orthologous Groups More...OrthoDBi | EOG091G06K3 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O43524 |
TreeFam database of animal gene trees More...TreeFami | TF315583 |
Family and domain databases
Conserved Domains Database More...CDDi | cd00059 FH, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001766 Fork_head_dom IPR032067 FOXO-TAD IPR032068 FOXO_KIX-bd IPR030456 TF_fork_head_CS_2 IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00250 Forkhead, 1 hit PF16676 FOXO-TAD, 1 hit PF16675 FOXO_KIX_bdg, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00053 FORKHEAD |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00339 FH, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46785 SSF46785, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00658 FORK_HEAD_2, 1 hit PS50039 FORK_HEAD_3, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (2)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 2 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded 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.
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
The sequence of this isoform differs from the canonical sequence as follows:
1-220: Missing.
10 20 30 40 50
MRVQNEGTGK SSWWIINPDG GKSGKAPRRR AVSMDNSNKY TKSRGRAAKK
60 70 80 90 100
KAALQTAPES ADDSPSQLSK WPGSPTSRSS DELDAWTDFR SRTNSNASTV
110 120 130 140 150
SGRLSPIMAS TELDEVQDDD APLSPMLYSS SASLSPSVSK PCTVELPRLT
160 170 180 190 200
DMAGTMNLND GLTENLMDDL LDNITLPPSQ PSPTGGLMQR SSSFPYTTKG
210 220 230 240 250
SGLGSPTSSF NSTVFGPSSL NSLRQSPMQT IQENKPATFS SMSHYGNQTL
260 270 280 290 300
QDLLTSDSLS HSDVMMTQSD PLMSQASTAV SAQNSRRNVM LRNDPMMSFA
310 320 330 340 350
AQPNQGSLVN QNLLHHQHQT QGALGGSRAL SNSVSNMGLS ESSSLGSAKH
360 370 380 390 400
QQQSPVSQSM QTLSDSLSGS SLYSTSANLP VMGHEKFPSD LDLDMFNGSL
410 420 430 440 450
ECDMESIIRS ELMDADGLDF NFDSLISTQN VVGLNVGNFT GAKQASSQSW
VPG
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 156 – 163 | AWGNLSYA → WGKPVYS in CAA04860 (PubMed:9345057).Curated | 8 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 238 – 246 | PDGGKSGKA → LMGEERKT in CAA04860 (PubMed:9345057).Curated | 9 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 253 | S → T in CAA04860 (PubMed:9345057).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 271 | Missing in CAA04860 (PubMed:9345057).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 292 – 330 | PGSPT…PIMAS → AWQPHVNAAVMSWMRGRTSV HAPILTPAQSVAACRPSWQV in CAA04860 (PubMed:9345057).CuratedAdd BLAST | 39 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 345 – 361 | PMLYS…SVSKP → AHALQHVSQPVTFSKQA in CAA04860 (PubMed:9345057).CuratedAdd BLAST | 17 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 367 | P → R in CAA04860 (PubMed:9345057).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 371 | D → E in CAA04860 (PubMed:9345057).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 382 – 383 | LT → AD in CAA04860 (PubMed:9345057).Curated | 2 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF032886 mRNA Translation: AAC39592.1 AK301304 mRNA Translation: BAG62858.1 AL096818 Genomic DNA No translation available. AL391646 Genomic DNA No translation available. AL365509 Genomic DNA No translation available. 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS5068.1 [O43524-1] |
NCBI Reference Sequences More...RefSeqi | NP_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] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.220950 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000343882; ENSP00000339527; ENSG00000118689 [O43524-1] ENST00000406360; ENSP00000385824; ENSG00000118689 [O43524-1] ENST00000540898; ENSP00000446316; ENSG00000118689 [O43524-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2309 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2309 |
UCSC genome browser More...UCSCi | uc003psk.3 human [O43524-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Chromosomal rearrangement<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O43524 | FOXO3 isoform 3 | 453 | |||
| FOXO3 isoform 3 | 453 | ||||
| UPI0006438190 | 688 | ||||
| UPI000333380D | 676 | ||||
| Forkhead box O3 | 675 | ||||
| +96 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| O43524 | FOXO3 isoform 3 | 453 | |||
| FOXO3 isoform 3 | 453 | ||||
| UPI0006438190 | 688 | ||||
| UPI000333380D | 676 | ||||
| Forkhead box O3 | 675 | ||||
| +113 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| Atlas of Genetics and Cytogenetics in Oncology and Haematology |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AF032886 mRNA Translation: AAC39592.1 AK301304 mRNA Translation: BAG62858.1 AL096818 Genomic DNA No translation available. AL391646 Genomic DNA No translation available. AL365509 Genomic DNA No translation available. 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 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS5068.1 [O43524-1] |
NCBI Reference Sequences More...RefSeqi | NP_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] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.220950 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB 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 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | O43524 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | O43524 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108598, 65 interactors |
ComplexPortal: manually curated resource of macromolecular complexes More...ComplexPortali | CPX-1123 FOXO3-MYC complex CPX-1147 FOXO3-YWHAZ complex |
CORUM comprehensive resource of mammalian protein complexes More...CORUMi | O43524 |
Database of interacting proteins More...DIPi | DIP-29723N |
Protein interaction database and analysis system More...IntActi | O43524, 43 interactors |
Molecular INTeraction database More...MINTi | O43524 |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000339527 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | O43524 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL5778 |
PTM databases
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | O43524 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | O43524 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | FOXO3 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | O43524 |
MaxQB - The MaxQuant DataBase More...MaxQBi | O43524 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | O43524 |
PeptideAtlas More...PeptideAtlasi | O43524 |
PRoteomics IDEntifications database More...PRIDEi | O43524 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 49029 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 2309 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000343882; ENSP00000339527; ENSG00000118689 [O43524-1] ENST00000406360; ENSP00000385824; ENSG00000118689 [O43524-1] ENST00000540898; ENSP00000446316; ENSG00000118689 [O43524-2] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2309 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2309 |
UCSC genome browser More...UCSCi | uc003psk.3 human [O43524-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 2309 |
DisGeNET More...DisGeNETi | 2309 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000118689.14 |
GeneCards: human genes, protein and diseases More...GeneCardsi | FOXO3 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3821 FOXO3 |
Human Protein Atlas More...HPAi | CAB004074 HPA063104 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 602681 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_O43524 |
Open Targets More...OpenTargetsi | ENSG00000118689 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA28239 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG2294 Eukaryota COG5025 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00920000149005 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000251635 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG057789 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | O43524 |
KEGG Orthology (KO) More...KOi | K09408 |
Identification of Orthologs from Complete Genome Data More...OMAi | PSVSKPC |
Database of Orthologous Groups More...OrthoDBi | EOG091G06K3 |
Database for complete collections of gene phylogenies More...PhylomeDBi | O43524 |
TreeFam database of animal gene trees More...TreeFami | TF315583 |
Enzyme and pathway databases
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-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 R-HSA-6785807 Interleukin-4 and 13 signaling R-HSA-8862803 Deregulated CDK5 triggers multiple neurodegenerative pathways in Alzheimer's disease models R-HSA-8950505 Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation R-HSA-8952158 RUNX3 regulates BCL2L11 (BIM) transcription |
SignaLink: a signaling pathway resource with multi-layered regulatory networks More...SignaLinki | O43524 |
SIGNOR Signaling Network Open Resource More...SIGNORi | O43524 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | FOXO3 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | O43524 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | FOXO3 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 2309 |
Protein Ontology More...PROi | PR:O43524 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000118689 |
CleanEx database of gene expression profiles More...CleanExi | HS_FOXO3 |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | O43524 HS |
Family and domain databases
Conserved Domains Database More...CDDi | cd00059 FH, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.10.10, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR001766 Fork_head_dom IPR032067 FOXO-TAD IPR032068 FOXO_KIX-bd IPR030456 TF_fork_head_CS_2 IPR036388 WH-like_DNA-bd_sf IPR036390 WH_DNA-bd_sf |
Pfam protein domain database More...Pfami | View protein in Pfam PF00250 Forkhead, 1 hit PF16676 FOXO-TAD, 1 hit PF16675 FOXO_KIX_bdg, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00053 FORKHEAD |
Simple Modular Architecture Research Tool; a protein domain database More...SMARTi | View protein in SMART SM00339 FH, 1 hit |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF46785 SSF46785, 1 hit |
PROSITE; a protein domain and family database More...PROSITEi | View protein in PROSITE PS00658 FORK_HEAD_2, 1 hit PS50039 FORK_HEAD_3, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | FOXO3_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | O43524Primary (citable) accession number: O43524 Secondary accession number(s): B4DVZ6 , E1P5E6, O15171, Q5T2I7, Q9BZ04 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | May 30, 2000 |
| Last sequence update: | June 1, 1998 | |
| Last modified: | June 20, 2018 | |
| This is version 200 of the entry and version 1 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Reference proteomeDocuments
- 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
