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P98177

- FOXO4_HUMAN

UniProt

P98177 - FOXO4_HUMAN

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Protein

Forkhead box protein O4

Gene

FOXO4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.8 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
DNA bindingi100 – 18889Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. enzyme binding Source: UniProtKB
  3. sequence-specific DNA binding Source: UniProtKB
  4. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  5. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cell cycle arrest Source: UniProtKB
  2. epidermal growth factor receptor signaling pathway Source: Reactome
  3. Fc-epsilon receptor signaling pathway Source: Reactome
  4. fibroblast growth factor receptor signaling pathway Source: Reactome
  5. innate immune response Source: Reactome
  6. insulin receptor signaling pathway Source: UniProtKB
  7. mitotic G2 DNA damage checkpoint Source: Ensembl
  8. muscle organ development Source: UniProtKB-KW
  9. negative regulation of angiogenesis Source: UniProtKB
  10. negative regulation of cell proliferation Source: UniProtKB
  11. negative regulation of G0 to G1 transition Source: UniProtKB
  12. negative regulation of smooth muscle cell differentiation Source: UniProtKB
  13. neurotrophin TRK receptor signaling pathway Source: Reactome
  14. phosphatidylinositol-mediated signaling Source: Reactome
  15. positive regulation of transcription, DNA-templated Source: Ensembl
  16. regulation of transcription, DNA-templated Source: UniProtKB
  17. stem cell differentiation Source: UniProtKB
  18. transcription from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein

Keywords - Biological processi

Cell cycle, Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_12442. AKT phosphorylates targets in the nucleus.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
SignaLinkiP98177.

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein O4
Alternative name(s):
Fork head domain transcription factor AFX1
Gene namesi
Name:FOXO4
Synonyms:AFX, AFX1, MLLT7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome X

Organism-specific databases

HGNCiHGNC:7139. FOXO4.

Subcellular locationi

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.

GO - Cellular componenti

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

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 usei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi32 – 321T → 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. 3 Publications
Mutagenesisi197 – 1971S → 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. 4 Publications
Mutagenesisi262 – 2621S → 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. 4 Publications

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA162388882.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 505505Forkhead box protein O4PRO_0000091875Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321Phosphothreonine; by PKB/AKT11 Publication
Modified residuei197 – 1971Phosphoserine; by PKB/AKT13 Publications
Modified residuei262 – 2621Phosphoserine; by PKB/AKT13 Publications

Post-translational modificationi

Acetylation by CREBBP/CBP, which is induced by peroxidase stress, inhibits transcriptional activity. Deacetylation by SIRT1 is NAD-dependent and stimulates transcriptional activity.1 Publication
Phosphorylation by PKB/AKT1 inhibits transcriptional activity and is responsible for cytoplasmic localization. May be phosphorylated at multiple sites by NLK.3 Publications
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.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP98177.
PaxDbiP98177.
PRIDEiP98177.

PTM databases

PhosphoSiteiP98177.

Expressioni

Tissue specificityi

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

Gene expression databases

BgeeiP98177.
CleanExiHS_FOXO4.
GenevestigatoriP98177.

Organism-specific databases

HPAiHPA040232.

Interactioni

Subunit structurei

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.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
SIRT1Q96EB63EBI-4481939,EBI-1802965

Protein-protein interaction databases

BioGridi110449. 17 interactions.
IntActiP98177. 4 interactions.
STRINGi9606.ENSP00000363377.

Structurei

Secondary structure

1
505
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 11611Combined sources
Beta strandi117 – 1193Combined sources
Helixi124 – 13411Combined sources
Helixi136 – 1383Combined sources
Helixi139 – 1424Combined sources
Helixi149 – 16012Combined sources
Beta strandi164 – 1674Combined sources
Turni170 – 1723Combined sources
Beta strandi173 – 1753Combined sources
Beta strandi177 – 1804Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1E17NMR-A86-211[»]
3L2CX-ray1.87A86-187[»]
ProteinModelPortaliP98177.
SMRiP98177. Positions 97-181.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP98177.

Family & Domainsi

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00390000000589.
HOGENOMiHOG000251635.
HOVERGENiHBG057789.
InParanoidiP98177.
KOiK12358.
OMAiFSLQHPG.
OrthoDBiEOG7SFHZ8.
PhylomeDBiP98177.
TreeFamiTF315583.

Family and domain databases

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

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P98177-1) [UniParc]FASTAAdd to Basket

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.

« Hide

        10         20         30         40         50
MDPGNENSAT EAAAIIDLDP DFEPQSRPRS CTWPLPRPEI ANQPSEPPEV
60 70 80 90 100
EPDLGEKVHT EGRSEPILLP SRLPEPAGGP QPGILGAVTG PRKGGSRRNA
110 120 130 140 150
WGNQSYAELI SQAIESAPEK RLTLAQIYEW MVRTVPYFKD KGDSNSSAGW
160 170 180 190 200
KNSIRHNLSL HSKFIKVHNE ATGKSSWWML NPEGGKSGKA PRRRAASMDS
210 220 230 240 250
SSKLLRGRSK APKKKPSVLP APPEGATPTS PVGHFAKWSG SPCSRNREEA
260 270 280 290 300
DMWTTFRPRS SSNASSVSTR LSPLRPESEV LAEEIPASVS SYAGGVPPTL
310 320 330 340 350
NEGLELLDGL NLTSSHSLLS RSGLSGFSLQ HPGVTGPLHT YSSSLFSPAE
360 370 380 390 400
GPLSAGEGCF SSSQALEALL TSDTPPPPAD VLMTQVDPIL SQAPTLLLLG
410 420 430 440 450
GLPSSSKLAT GVGLCPKPLE APGPSSLVPT LSMIAPPPVM ASAPIPKALG
460 470 480 490 500
TPVLTPPTEA ASQDRMPQDL DLDMYMENLE CDMDNIISDL MDEGEGLDFN

FEPDP
Length:505
Mass (Da):53,684
Last modified:July 25, 2006 - v5
Checksum:i0C71C8E2167CEE68
GO
Isoform Zeta (identifier: P98177-2) [UniParc]FASTAAdd to Basket

Also known as: AFXzeta, FOXO4b

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

Show »
Length:450
Mass (Da):47,941
Checksum:iD44C18FAD9C2A747
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1 – 1111MDPGNENSATE → MRIQPQK in CAA63819. (PubMed:9010221)CuratedAdd
BLAST
Sequence conflicti25 – 3410QSRPRSCTWP → RAVPLLHLA in CAA72156. (PubMed:9341872)Curated
Sequence conflicti74 – 741P → S in CAA63819. (PubMed:9010221)Curated
Sequence conflicti79 – 791G → A in CAA72156. (PubMed:9341872)Curated
Sequence conflicti109 – 1091L → F in CAA63819. (PubMed:9010221)Curated
Sequence conflicti422 – 4221P → R in CAA63819. (PubMed:9010221)Curated
Sequence conflicti422 – 4221P → R in AAL85197. (PubMed:11779849)Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei58 – 11255Missing in isoform Zeta. 1 PublicationVSP_001552Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS43969.1. [P98177-1]
CCDS55440.1. [P98177-2]
PIRiI38654.
RefSeqiNP_001164402.1. NM_001170931.1. [P98177-2]
NP_005929.2. NM_005938.3. [P98177-1]
UniGeneiHs.584654.

Genome annotation databases

EnsembliENST00000341558; ENSP00000342209; ENSG00000184481. [P98177-2]
ENST00000374259; ENSP00000363377; ENSG00000184481. [P98177-1]
GeneIDi4303.
KEGGihsa:4303.
UCSCiuc004dys.2. human. [P98177-1]
uc004dyt.2. human. [P98177-2]

Polymorphism databases

DMDMi110825720.

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSi CCDS43969.1. [P98177-1 ]
CCDS55440.1. [P98177-2 ]
PIRi I38654.
RefSeqi NP_001164402.1. NM_001170931.1. [P98177-2 ]
NP_005929.2. NM_005938.3. [P98177-1 ]
UniGenei Hs.584654.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1E17 NMR - A 86-211 [» ]
3L2C X-ray 1.87 A 86-187 [» ]
ProteinModelPortali P98177.
SMRi P98177. Positions 97-181.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110449. 17 interactions.
IntActi P98177. 4 interactions.
STRINGi 9606.ENSP00000363377.

PTM databases

PhosphoSitei P98177.

Polymorphism databases

DMDMi 110825720.

Proteomic databases

MaxQBi P98177.
PaxDbi P98177.
PRIDEi P98177.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000341558 ; ENSP00000342209 ; ENSG00000184481 . [P98177-2 ]
ENST00000374259 ; ENSP00000363377 ; ENSG00000184481 . [P98177-1 ]
GeneIDi 4303.
KEGGi hsa:4303.
UCSCi uc004dys.2. human. [P98177-1 ]
uc004dyt.2. human. [P98177-2 ]

Organism-specific databases

CTDi 4303.
GeneCardsi GC0XP070316.
HGNCi HGNC:7139. FOXO4.
HPAi HPA040232.
MIMi 300033. gene.
neXtProti NX_P98177.
PharmGKBi PA162388882.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5025.
GeneTreei ENSGT00390000000589.
HOGENOMi HOG000251635.
HOVERGENi HBG057789.
InParanoidi P98177.
KOi K12358.
OMAi FSLQHPG.
OrthoDBi EOG7SFHZ8.
PhylomeDBi P98177.
TreeFami TF315583.

Enzyme and pathway databases

Reactomei REACT_12442. AKT phosphorylates targets in the nucleus.
REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
SignaLinki P98177.

Miscellaneous databases

ChiTaRSi FOXO4. human.
EvolutionaryTracei P98177.
GeneWikii FOXO4.
GenomeRNAii 4303.
NextBioi 16943.
PROi P98177.
SOURCEi Search...

Gene expression databases

Bgeei P98177.
CleanExi HS_FOXO4.
Genevestigatori P98177.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "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.
    , 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. 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. Cited for: FUNCTION, INTERACTION WITH USP7, UBIQUITINATION, DEUBIQUITINATION BY USP7, SUBCELLULAR LOCATION.
  18. "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.
  19. "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.
  20. "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.
  21. "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.

Entry informationi

Entry nameiFOXO4_HUMAN
AccessioniPrimary (citable) accession number: P98177
Secondary accession number(s): B7WPJ7
, O43821, Q13720, Q3KPF1, Q8TDK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 25, 2006
Last modified: November 26, 2014
This is version 152 of the entry and version 5 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Pharmaceutical, Reference proteome

Documents

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

External Data

Dasty 3