Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P98177 (FOXO4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Forkhead box protein O4
Alternative name(s):
Fork head domain transcription factor AFX1
Gene names
Name:FOXO4
Synonyms:AFX, AFX1, MLLT7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length505 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transcription factor involved in the regulation of the insulin signaling pathway. Binds to insulin-response elements (IREs) and can activate transcription of IGFBP1. Down-regulates expression of HIF1A and suppresses hypoxia-induced transcriptional activation of HIF1A-modulated genes. Also involved in negative regulation of the cell cycle. Involved in increased proteasome activity in embryonic stem cells (ESCs) by activating expression of PSMD11 in ESCs, leading to enhanced assembly of the 26S proteasome, followed by higher proteasome activity. Ref.8 Ref.10 Ref.11 Ref.12 Ref.14 Ref.17 Ref.19 Ref.20

Subunit structure

Interacts with CREBBP/CBP, CTNNB1, MYOCD, SIRT1, SRF and YWHAZ. Acetylated by CREBBP/CBP and deacetylated by SIRT1. Binding of YWHAZ inhibits DNA-binding. Interacts with USP7; the interaction is enhanced in presence of hydrogen peroxide and occurs independently of TP53. Interacts with NLK, and this inhibits monoubiquitination and transcriptional activity. Ref.12 Ref.13 Ref.14 Ref.17 Ref.19

Subcellular location

Cytoplasm. Nucleus. Note: When phosphorylated, translocated from nucleus to cytoplasm. Dephosphorylation triggers nuclear translocation. Monoubiquitination increases nuclear localization. When deubiquitinated, translocated from nucleus to cytoplasm. Ref.9 Ref.13 Ref.17

Tissue specificity

Heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. Isoform zetais most abundant in the liver, kidney, and pancreas.

Post-translational modification

Acetylation by CREBBP/CBP, which is induced by peroxidase stress, inhibits transcriptional activity. Deacetylation by SIRT1 is NAD-dependent and stimulates transcriptional activity. Ref.12

Phosphorylation by PKB/AKT1 inhibits transcriptional activity and is responsible for cytoplasmic localization. May be phosphorylated at multiple sites by NLK. Ref.8 Ref.9 Ref.15 Ref.18

Monoubiquitinated; monoubiquitination is induced by oxidative stress and reduced by deacetylase inhibitors; results in its relocalization to the nucleus and its increased transcriptional activity. Deubiquitinated by USP7; deubiquitination is induced by oxidative stress; enhances its interaction with USP7 and consequently, deubiquitination; increases its translocation to the cytoplasm and inhibits its transcriptional activity. Hydrogene-peroxide-induced ubiquitination and USP7-mediated deubiquitination have no major effect on its protein stability.

Involvement in disease

A chromosomal aberration involving FOXO4 is found in acute leukemias. Translocation t(X;11)(q13;q23) with KMT2A/MLL1. The result is a rogue activator protein.

Pharmaceutical use

A constitutively active FOXO4 mutant where phosphorylation sites Thr-32, Ser-197 and Ser-262 have been mutated to alanine may have therapeutic potential in ERBB2/HER2-overexpressing cancers as it inhibits ERBB2-mediated cell survival, transformation and tumorigenicity.

Sequence similarities

Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
   Biological processCell cycle
Differentiation
Myogenesis
Transcription
Transcription regulation
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
   DiseaseProto-oncogene
   LigandDNA-binding
   Molecular functionActivator
Developmental protein
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Pharmaceutical
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

cell cycle arrest

Inferred from direct assay Ref.10. Source: UniProtKB

embryo development

Inferred from Biological aspect of Ancestor. Source: RefGenome

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

innate immune response

Traceable author statement. Source: Reactome

insulin receptor signaling pathway

Inferred from direct assay Ref.8. Source: UniProtKB

mitotic G2 DNA damage checkpoint

Inferred from Biological aspect of Ancestor. Source: RefGenome

muscle organ development

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of G0 to G1 transition

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of angiogenesis

Inferred from direct assay Ref.11. Source: UniProtKB

negative regulation of apoptotic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of cell proliferation

Inferred from direct assay Ref.10. Source: UniProtKB

negative regulation of smooth muscle cell differentiation

Inferred from direct assay Ref.14. Source: UniProtKB

negative regulation of stress-activated MAPK cascade

Inferred from Biological aspect of Ancestor. Source: RefGenome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

pattern specification process

Inferred from Biological aspect of Ancestor. Source: RefGenome

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: Ensembl

regulation of transcription, DNA-templated

Inferred from direct assay Ref.12. Source: UniProtKB

stem cell differentiation

Inferred from mutant phenotype Ref.20. Source: UniProtKB

tissue development

Inferred from Biological aspect of Ancestor. Source: RefGenome

transcription from RNA polymerase II promoter

Traceable author statement Ref.10. Source: ProtInc

   Cellular_componentcytoplasm

Inferred from direct assay Ref.17. Source: UniProtKB

cytosol

Inferred from direct assay Ref.15. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.15Ref.17. Source: UniProtKB

   Molecular_functionDNA binding

Inferred from direct assay Ref.10. Source: UniProtKB

DNA binding, bending

Inferred from Biological aspect of Ancestor. Source: RefGenome

enzyme binding

Inferred from physical interaction Ref.12Ref.17. Source: UniProtKB

sequence-specific DNA binding

Inferred from mutant phenotype Ref.20. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay Ref.10. Source: UniProtKB

transcription factor binding

Inferred from physical interaction Ref.14. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

SIRT1Q96EB63EBI-4481939,EBI-1802965

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P98177-1)

Also known as: FOXO4a;

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.
Isoform Zeta (identifier: P98177-2)

Also known as: AFXzeta; FOXO4b;

The sequence of this isoform differs from the canonical sequence as follows:
     58-112: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 505505Forkhead box protein O4
PRO_0000091875

Regions

DNA binding100 – 18889Fork-head

Amino acid modifications

Modified residue321Phosphothreonine; by PKB/AKT1 Ref.15
Modified residue1971Phosphoserine; by PKB/AKT1 Ref.8 Ref.9 Ref.15 Ref.18
Modified residue2001Phosphoserine Ref.18
Modified residue2621Phosphoserine; by PKB/AKT1 Ref.8 Ref.9 Ref.15

Natural variations

Alternative sequence58 – 11255Missing in isoform Zeta.
VSP_001552

Experimental info

Mutagenesis321T → A: Abolishes phosphorylation. Protein is located mainly in nucleus and shows increased transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-197 and A-262. Ref.9 Ref.15 Ref.20
Mutagenesis1971S → A: Abolishes phosphorylation. Protein is located mainly in nucleus and shows increased transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-32 and A-262. Ref.8 Ref.9 Ref.15 Ref.20
Mutagenesis2621S → A: Abolishes phosphorylation. No effect on cellular location or transcriptional activity. Increased transcriptional and proteasome activities in embryonic stem cells; when associated with A-32 and A-197. Ref.8 Ref.9 Ref.15 Ref.20
Sequence conflict1 – 1111MDPGNENSATE → MRIQPQK in CAA63819. Ref.2
Sequence conflict25 – 3410QSRPRSCTWP → RAVPLLHLA in CAA72156. Ref.1
Sequence conflict741P → S in CAA63819. Ref.2
Sequence conflict791G → A in CAA72156. Ref.1
Sequence conflict1091L → F in CAA63819. Ref.2
Sequence conflict4221P → R in CAA63819. Ref.2
Sequence conflict4221P → R in AAL85197. Ref.3

Secondary structure

.................. 505
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (FOXO4a) [UniParc].

Last modified July 25, 2006. Version 5.
Checksum: 0C71C8E2167CEE68

FASTA50553,684
        10         20         30         40         50         60 
MDPGNENSAT EAAAIIDLDP DFEPQSRPRS CTWPLPRPEI ANQPSEPPEV EPDLGEKVHT 

        70         80         90        100        110        120 
EGRSEPILLP SRLPEPAGGP QPGILGAVTG PRKGGSRRNA WGNQSYAELI SQAIESAPEK 

       130        140        150        160        170        180 
RLTLAQIYEW MVRTVPYFKD KGDSNSSAGW KNSIRHNLSL HSKFIKVHNE ATGKSSWWML 

       190        200        210        220        230        240 
NPEGGKSGKA PRRRAASMDS SSKLLRGRSK APKKKPSVLP APPEGATPTS PVGHFAKWSG 

       250        260        270        280        290        300 
SPCSRNREEA DMWTTFRPRS SSNASSVSTR LSPLRPESEV LAEEIPASVS SYAGGVPPTL 

       310        320        330        340        350        360 
NEGLELLDGL NLTSSHSLLS RSGLSGFSLQ HPGVTGPLHT YSSSLFSPAE GPLSAGEGCF 

       370        380        390        400        410        420 
SSSQALEALL TSDTPPPPAD VLMTQVDPIL SQAPTLLLLG GLPSSSKLAT GVGLCPKPLE 

       430        440        450        460        470        480 
APGPSSLVPT LSMIAPPPVM ASAPIPKALG TPVLTPPTEA ASQDRMPQDL DLDMYMENLE 

       490        500 
CDMDNIISDL MDEGEGLDFN FEPDP 

« Hide

Isoform Zeta (AFXzeta) (FOXO4b) [UniParc].

Checksum: D44C18FAD9C2A747
Show »

FASTA45047,941

References

« Hide 'large scale' references
[1]"AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as candidate genes of X-linked dystonia parkinsonism."
Peters U., Haberhausen G., Kostrzewa M., Nolte D., Mueller U.
Hum. Genet. 100:569-572(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.
[2]"Cloning and characterization of AFX, the gene that fuses to MLL in acute leukemias with a t(X;11)(q13;q23)."
Borkhardt A., Repp R., Haas O.A., Leis T., Harbott J., Kreuder J., Hammermann J., Henn T., Lampert F.
Oncogene 14:195-202(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"An mRNA splice variant of the AFX gene with altered transcriptional activity."
Yang Z., Whelan J., Babb R., Bowen B.R.
J. Biol. Chem. 277:8068-8075(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ZETA).
[4]"The DNA sequence of the human X chromosome."
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. expand/collapse author list , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[7]"Cloning and characterization of the t(X;11) breakpoint from a leukemic cell line identify a new member of the forkhead gene family."
Parry P., Wei Y., Evans G.
Genes Chromosomes Cancer 11:79-84(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION.
Tissue: Bone marrow.
[8]"Direct control of the forkhead transcription factor AFX by protein kinase B."
Kops G.J.P.L., de Ruiter N.D., De Vries-Smits A.M.M., Powell D.R., Bos J.L., Burgering B.M.T.
Nature 398:630-634(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-262, MUTAGENESIS OF SER-197 AND SER-262.
[9]"Regulation of nuclear translocation of forkhead transcription factor AFX by protein kinase B."
Takaishi H., Konishi H., Matsuzaki H., Ono Y., Shirai Y., Saito N., Kitamura T., Ogawa W., Kasuga M., Kikkawa U., Nishizuka Y.
Proc. Natl. Acad. Sci. U.S.A. 96:11836-11841(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-197 AND SER-262, MUTAGENESIS OF THR-32; SER-197 AND SER-262.
[10]"AFX-like forkhead transcription factors mediate cell-cycle regulation by Ras and PKB through p27kip1."
Medema R.H., Kops G.J.P.L., Bos J.L., Burgering B.M.T.
Nature 404:782-787(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[11]"The forkhead transcription factor FOXO4 induces the down-regulation of hypoxia-inducible factor 1 alpha by a von Hippel-Lindau protein-independent mechanism."
Tang T.T.-L., Lasky L.A.
J. Biol. Chem. 278:30125-30135(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"FOXO4 is acetylated upon peroxide stress and deacetylated by the longevity protein hSir2(SIRT1)."
van der Horst A., Tertoolen L.G.J., de Vries-Smits L.M.M., Frye R.A., Medema R.H., Burgering B.M.T.
J. Biol. Chem. 279:28873-28879(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CREBBP AND SIRT1, ACETYLATION.
[13]"14-3-3 protein interacts with nuclear localization sequence of forkhead transcription factor FoxO4."
Obsilova V., Vecer J., Herman P., Pabianova A., Sulc M., Teisinger J., Boura E., Obsil T.
Biochemistry 44:11608-11617(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH YWHAZ, SUBCELLULAR LOCATION.
[14]"Phenotypic modulation of smooth muscle cells through interaction of Foxo4 and myocardin."
Liu Z.-P., Wang Z., Yanagisawa H., Olson E.N.
Dev. Cell 9:261-270(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH MYOCD AND SRF.
[15]"Regulation of intracellular localization and transcriptional activity of FOXO4 by protein kinase B through phosphorylation at the motif sites conserved among the FOXO family."
Matsuzaki H., Ichino A., Hayashi T., Yamamoto T., Kikkawa U.
J. Biochem. 138:485-491(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT THR-32; SER-197 AND SER-262, MUTAGENESIS OF THR-32; SER-197 AND SER-262.
[16]"Constitutively active FOXO4 inhibits Akt activity, regulates p27 Kip1 stability, and suppresses HER2-mediated tumorigenicity."
Yang H., Zhao R., Yang H.-Y., Lee M.-H.
Oncogene 24:1924-1935(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: PHARMACEUTICAL USE.
[17]"FOXO4 transcriptional activity is regulated by monoubiquitination and USP7/HAUSP."
van der Horst A., de Vries-Smits A.M., Brenkman A.B., van Triest M.H., van den Broek N., Colland F., Maurice M.M., Burgering B.M.
Nat. Cell Biol. 8:1064-1073(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH USP7, UBIQUITINATION, DEUBIQUITINATION BY USP7, SUBCELLULAR LOCATION.
[18]Carrascal M., Abian J.
Submitted (JAN-2008) to UniProtKB
Cited for: PHOSPHORYLATION AT SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
[19]"Oxidative stress-dependent regulation of Forkhead box O4 activity by nemo-like kinase."
Szypowska A.A., de Ruiter H., Meijer L.A.T., Smits L.M.M., Burgering B.M.T.
Antioxid. Redox Signal. 14:563-578(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH NLK; CTNNB1 AND CREBBP.
[20]"Increased proteasome activity in human embryonic stem cells is regulated by PSMD11."
Vilchez D., Boyer L., Morantte I., Lutz M., Merkwirth C., Joyce D., Spencer B., Page L., Masliah E., Berggren W.T., Gage F.H., Dillin A.
Nature 489:304-308(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF THR-32; SER-197 AND SER-262.
[21]"1H, 13C and 15N resonance assignments of the DNA binding domain of the human forkhead transcription factor AFX."
Weigelt J., Climent I., Dahlman-Wright K., Wikstrom M.
J. Biomol. NMR 17:181-182(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 86-211.
[22]"Solution structure of the DNA binding domain of the human forkhead transcription factor AFX (FOXO4)."
Weigelt J., Climent I., Dahlman-Wright K., Wikstrom M.
Biochemistry 40:5861-5869(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 86-211.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11284, Y11285, Y11286 Genomic DNA. Translation: CAA72156.1.
X93996 mRNA. Translation: CAA63819.1.
AF384029 mRNA. Translation: AAL85197.1.
AL590764 Genomic DNA. No translation available.
CH471132 Genomic DNA. Translation: EAX05321.1.
BC106761 mRNA. Translation: AAI06762.1.
U10072 mRNA. Translation: AAA82171.1. Sequence problems.
PIRI38654.
RefSeqNP_001164402.1. NM_001170931.1.
NP_005929.2. NM_005938.3.
UniGeneHs.584654.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1E17NMR-A86-211[»]
3L2CX-ray1.87A86-187[»]
ProteinModelPortalP98177.
SMRP98177. Positions 97-181.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid110449. 16 interactions.
IntActP98177. 4 interactions.
STRING9606.ENSP00000363377.

PTM databases

PhosphoSiteP98177.

Polymorphism databases

DMDM110825720.

Proteomic databases

PaxDbP98177.
PRIDEP98177.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341558; ENSP00000342209; ENSG00000184481. [P98177-2]
ENST00000374259; ENSP00000363377; ENSG00000184481. [P98177-1]
GeneID4303.
KEGGhsa:4303.
UCSCuc004dys.2. human. [P98177-1]
uc004dyt.2. human. [P98177-2]

Organism-specific databases

CTD4303.
GeneCardsGC0XP070316.
HGNCHGNC:7139. FOXO4.
HPAHPA040232.
MIM300033. gene.
neXtProtNX_P98177.
PharmGKBPA162388882.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5025.
HOGENOMHOG000251635.
HOVERGENHBG057789.
KOK12358.
OMAFSLQHPG.
OrthoDBEOG7SFHZ8.
PhylomeDBP98177.
TreeFamTF315583.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP98177.

Gene expression databases

BgeeP98177.
CleanExHS_FOXO4.
GenevestigatorP98177.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSPR00053. FORKHEAD.
SMARTSM00339. FH. 1 hit.
[Graphical view]
PROSITEPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP98177.
GeneWikiFOXO4.
GenomeRNAi4303.
NextBio16943.
PROP98177.
SOURCESearch...

Entry information

Entry nameFOXO4_HUMAN
AccessionPrimary (citable) accession number: P98177
Secondary accession number(s): B7WPJ7 expand/collapse secondary AC list , O43821, Q13720, Q3KPF1, Q8TDK9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 25, 2006
Last modified: April 16, 2014
This is version 145 of the entry and version 5 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome X

Human chromosome X: entries, gene names and cross-references to MIM