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Q9BZS1

- FOXP3_HUMAN

UniProt

Q9BZS1 - FOXP3_HUMAN

Protein

Forkhead box protein P3

Gene

FOXP3

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Jun 2001)
      Previous versions | rss
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    Functioni

    Probable transcription factor. Plays a critical role in the control of immune response.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri197 – 22226C2H2-typeAdd
    BLAST
    DNA bindingi337 – 42387Fork-headPROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. histone acetyltransferase binding Source: BHF-UCL
    2. histone deacetylase binding Source: BHF-UCL
    3. metal ion binding Source: UniProtKB-KW
    4. NFAT protein binding Source: UniProtKB
    5. NF-kappaB binding Source: UniProtKB
    6. protein binding Source: UniProtKB
    7. protein homodimerization activity Source: UniProtKB
    8. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: Ensembl
    9. sequence-specific DNA binding Source: UniProtKB
    10. sequence-specific DNA binding transcription factor activity Source: UniProtKB
    11. transcription corepressor activity Source: Ensembl

    GO - Biological processi

    1. B cell homeostasis Source: Ensembl
    2. CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: Ensembl
    3. chromatin remodeling Source: UniProtKB
    4. cytokine production Source: Ensembl
    5. myeloid cell homeostasis Source: Ensembl
    6. negative regulation of activated T cell proliferation Source: UniProtKB
    7. negative regulation of cell proliferation Source: UniProtKB
    8. negative regulation of chronic inflammatory response Source: Ensembl
    9. negative regulation of CREB transcription factor activity Source: UniProtKB
    10. negative regulation of cytokine biosynthetic process Source: UniProtKB
    11. negative regulation of cytokine secretion Source: UniProtKB
    12. negative regulation of histone acetylation Source: Ensembl
    13. negative regulation of histone deacetylation Source: BHF-UCL
    14. negative regulation of immune response Source: UniProtKB
    15. negative regulation of interferon-gamma biosynthetic process Source: Ensembl
    16. negative regulation of interferon-gamma production Source: UniProtKB
    17. negative regulation of interleukin-10 production Source: UniProtKB
    18. negative regulation of interleukin-2 biosynthetic process Source: UniProtKB
    19. negative regulation of interleukin-2 production Source: UniProtKB
    20. negative regulation of interleukin-4 production Source: UniProtKB
    21. negative regulation of interleukin-5 production Source: Ensembl
    22. negative regulation of interleukin-6 production Source: Ensembl
    23. negative regulation of isotype switching to IgE isotypes Source: Ensembl
    24. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
    25. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
    26. negative regulation of T cell cytokine production Source: UniProtKB
    27. negative regulation of T cell proliferation Source: UniProtKB
    28. negative regulation of transcription, DNA-templated Source: UniProtKB
    29. negative regulation of tumor necrosis factor production Source: Ensembl
    30. positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: Ensembl
    31. positive regulation of histone acetylation Source: BHF-UCL
    32. positive regulation of immature T cell proliferation in thymus Source: Ensembl
    33. positive regulation of interleukin-4 production Source: Ensembl
    34. positive regulation of peripheral T cell tolerance induction Source: Ensembl
    35. positive regulation of T cell anergy Source: Ensembl
    36. positive regulation of transcription, DNA-templated Source: UniProtKB
    37. positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
    38. positive regulation of transforming growth factor beta1 production Source: Ensembl
    39. regulation of isotype switching to IgG isotypes Source: Ensembl
    40. regulation of transcription, DNA-templated Source: UniProtKB
    41. response to virus Source: UniProtKB
    42. T cell activation Source: UniProtKB
    43. T cell homeostasis Source: UniProtKB
    44. T cell mediated immunity Source: Ensembl
    45. T cell receptor signaling pathway Source: Ensembl
    46. tolerance induction to self antigen Source: Ensembl

    Keywords - Biological processi

    Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, Metal-binding, Zinc

    Enzyme and pathway databases

    SignaLinkiQ9BZS1.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Forkhead box protein P3
    Alternative name(s):
    Scurfin
    Gene namesi
    Name:FOXP3
    Synonyms:IPEX
    ORF Names:JM2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome X

    Organism-specific databases

    HGNCiHGNC:6106. FOXP3.

    Subcellular locationi

    Nucleus PROSITE-ProRule annotation

    GO - Cellular componenti

    1. cytoplasm Source: Ensembl
    2. nucleus Source: UniProtKB
    3. protein complex Source: UniProtKB

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Immunodeficiency polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) [MIM:304790]: Characterized by neonatal onset insulin-dependent diabetes mellitus, infections, secretory diarrhea, thrombocytopenia, anemia and eczema. It is usually lethal in infancy.4 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti251 – 2511Missing in IPEX. 1 Publication
    VAR_011330
    Natural varianti363 – 3631I → V in IPEX. 1 Publication
    VAR_023569
    Natural varianti371 – 3711F → C in IPEX. 1 Publication
    VAR_011331
    Natural varianti384 – 3841A → T in IPEX. 2 Publications
    VAR_011332
    Natural varianti397 – 3971R → W in IPEX. 1 Publication
    Corresponds to variant rs28935477 [ dbSNP | Ensembl ].
    VAR_011333

    Keywords - Diseasei

    Diabetes mellitus, Disease mutation

    Organism-specific databases

    MIMi304790. phenotype.
    Orphaneti37042. Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome.
    PharmGKBiPA201094.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 431431Forkhead box protein P3PRO_0000091886Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei31 – 311N6-acetyllysine1 Publication
    Modified residuei263 – 2631N6-acetyllysine1 Publication
    Modified residuei268 – 2681N6-acetyllysine1 Publication

    Post-translational modificationi

    Acetylation on lysine residues stabilizes FOXP3 and promotes differentiation of T-cells into induced regulatory T-cells (iTregs) associated with suppressive functions. Deacetylated by SIRT1.1 Publication

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9BZS1.
    PRIDEiQ9BZS1.

    PTM databases

    PhosphoSiteiQ9BZS1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9BZS1.
    BgeeiQ9BZS1.
    CleanExiHS_FOXP3.
    GenevestigatoriQ9BZS1.

    Organism-specific databases

    HPAiCAB026301.
    HPA045943.

    Interactioni

    Subunit structurei

    Interacts with IKZF3.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    IKZF3Q9UKT92EBI-983719,EBI-747204

    Protein-protein interaction databases

    BioGridi119170. 19 interactions.
    DIPiDIP-36584N.
    IntActiQ9BZS1. 1 interaction.
    STRINGi9606.ENSP00000365380.

    Structurei

    Secondary structure

    1
    431
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi342 – 35110
    Helixi360 – 37112
    Turni372 – 3754
    Helixi381 – 39111
    Beta strandi395 – 3984
    Beta strandi401 – 4033
    Beta strandi405 – 4084
    Helixi410 – 4167

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3QRFX-ray2.80F/G/H/I336-417[»]
    ProteinModelPortaliQ9BZS1.
    SMRiQ9BZS1. Positions 202-263, 336-417.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9BZS1.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni239 – 26022Leucine-zipperAdd
    BLAST

    Sequence similaritiesi

    Contains 1 C2H2-type zinc finger.Curated
    Contains 1 fork-head DNA-binding domain.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri197 – 22226C2H2-typeAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5025.
    HOGENOMiHOG000082490.
    HOVERGENiHBG051656.
    KOiK10163.
    OMAiKHCQADH.
    OrthoDBiEOG7M6D7G.
    PhylomeDBiQ9BZS1.
    TreeFamiTF326978.

    Family and domain databases

    Gene3Di1.10.10.10. 1 hit.
    3.30.160.60. 1 hit.
    InterProiIPR001766. TF_fork_head.
    IPR018122. TF_fork_head_CS.
    IPR011991. WHTH_DNA-bd_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view]
    PfamiPF00250. Fork_head. 1 hit.
    [Graphical view]
    PRINTSiPR00053. FORKHEAD.
    SMARTiSM00339. FH. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view]
    PROSITEiPS00658. FORK_HEAD_2. 1 hit.
    PS50039. FORK_HEAD_3. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9BZS1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL    50
    RGGAHASSSS LNPMPPSQLQ LPTLPLVMVA PSGARLGPLP HLQALLQDRP 100
    HFMHQLSTVD AHARTPVLQV HPLESPAMIS LTPPTTATGV FSLKARPGLP 150
    PGINVASLEW VSREPALLCT FPNPSAPRKD STLSAVPQSS YPLLANGVCK 200
    WPGCEKVFEE PEDFLKHCQA DHLLDEKGRA QCLLQREMVQ SLEQQLVLEK 250
    EKLSAMQAHL AGKMALTKAS SVASSDKGSC CIVAAGSQGP VVPAWSGPRE 300
    APDSLFAVRR HLWGSHGNST FPEFLHNMDY FKFHNMRPPF TYATLIRWAI 350
    LEAPEKQRTL NEIYHWFTRM FAFFRNHPAT WKNAIRHNLS LHKCFVRVES 400
    EKGAVWTVDE LEFRKKRSQR PSRCSNPTPG P 431
    Length:431
    Mass (Da):47,244
    Last modified:June 1, 2001 - v1
    Checksum:i91737C3CEA665A15
    GO
    Isoform 2 (identifier: Q9BZS1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-106: Missing.

    Show »
    Length:396
    Mass (Da):43,410
    Checksum:iBF4DF0DD83D61CD5
    GO
    Isoform 3 (identifier: Q9BZS1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         72-106: Missing.
         382-382: K → KVSSSEVAVTGMASSAIAAQSGQAWVWAHRHIGEERDVGCWWWLLASEVDAHLLPVPGLPQ

    Note: No experimental confirmation available.

    Show »
    Length:456
    Mass (Da):49,843
    Checksum:i39E7483703031335
    GO
    Isoform 4 (identifier: Q9BZS1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         246-272: Missing.

    Show »
    Length:404
    Mass (Da):44,407
    Checksum:i4D164C39EF069DBB
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti16 – 205LGPSP → MSPIS in CAA06748. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti251 – 2511Missing in IPEX. 1 Publication
    VAR_011330
    Natural varianti363 – 3631I → V in IPEX. 1 Publication
    VAR_023569
    Natural varianti371 – 3711F → C in IPEX. 1 Publication
    VAR_011331
    Natural varianti384 – 3841A → T in IPEX. 2 Publications
    VAR_011332
    Natural varianti397 – 3971R → W in IPEX. 1 Publication
    Corresponds to variant rs28935477 [ dbSNP | Ensembl ].
    VAR_011333

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei72 – 10635Missing in isoform 2 and isoform 3. 3 PublicationsVSP_015796Add
    BLAST
    Alternative sequencei246 – 27227Missing in isoform 4. 1 PublicationVSP_047859Add
    BLAST
    Alternative sequencei382 – 3821K → KVSSSEVAVTGMASSAIAAQ SGQAWVWAHRHIGEERDVGC WWWLLASEVDAHLLPVPGLP Q in isoform 3. 1 PublicationVSP_036418

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF277993 mRNA. Translation: AAG53607.1.
    EF534714 mRNA. Translation: ABQ15210.1.
    EU855812 mRNA. Translation: ACJ46653.1.
    DQ010327 mRNA. Translation: AAY27088.1.
    AF235097 Genomic DNA. No translation available.
    BC113401 mRNA. Translation: AAI13402.1.
    BC113403 mRNA. Translation: AAI13404.1.
    BC143785 mRNA. Translation: AAI43786.1.
    AJ005891 mRNA. Translation: CAA06748.1.
    CCDSiCCDS14323.1. [Q9BZS1-1]
    CCDS48109.1. [Q9BZS1-2]
    RefSeqiNP_001107849.1. NM_001114377.1. [Q9BZS1-2]
    NP_054728.2. NM_014009.3. [Q9BZS1-1]
    UniGeneiHs.247700.

    Genome annotation databases

    EnsembliENST00000376197; ENSP00000365369; ENSG00000049768.
    ENST00000376199; ENSP00000365372; ENSG00000049768. [Q9BZS1-2]
    ENST00000376207; ENSP00000365380; ENSG00000049768. [Q9BZS1-1]
    ENST00000455775; ENSP00000396415; ENSG00000049768. [Q9BZS1-4]
    ENST00000518685; ENSP00000428952; ENSG00000049768. [Q9BZS1-2]
    ENST00000557224; ENSP00000451208; ENSG00000049768. [Q9BZS1-3]
    GeneIDi50943.
    KEGGihsa:50943.
    UCSCiuc004dne.4. human. [Q9BZS1-2]
    uc004dnf.4. human. [Q9BZS1-1]
    uc022bwa.1. human. [Q9BZS1-3]

    Polymorphism databases

    DMDMi14548061.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    FOXP3base

    FOXP3 mutation db

    Wikipedia

    FOXP3 entry

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF277993 mRNA. Translation: AAG53607.1 .
    EF534714 mRNA. Translation: ABQ15210.1 .
    EU855812 mRNA. Translation: ACJ46653.1 .
    DQ010327 mRNA. Translation: AAY27088.1 .
    AF235097 Genomic DNA. No translation available.
    BC113401 mRNA. Translation: AAI13402.1 .
    BC113403 mRNA. Translation: AAI13404.1 .
    BC143785 mRNA. Translation: AAI43786.1 .
    AJ005891 mRNA. Translation: CAA06748.1 .
    CCDSi CCDS14323.1. [Q9BZS1-1 ]
    CCDS48109.1. [Q9BZS1-2 ]
    RefSeqi NP_001107849.1. NM_001114377.1. [Q9BZS1-2 ]
    NP_054728.2. NM_014009.3. [Q9BZS1-1 ]
    UniGenei Hs.247700.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3QRF X-ray 2.80 F/G/H/I 336-417 [» ]
    ProteinModelPortali Q9BZS1.
    SMRi Q9BZS1. Positions 202-263, 336-417.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119170. 19 interactions.
    DIPi DIP-36584N.
    IntActi Q9BZS1. 1 interaction.
    STRINGi 9606.ENSP00000365380.

    PTM databases

    PhosphoSitei Q9BZS1.

    Polymorphism databases

    DMDMi 14548061.

    Proteomic databases

    PaxDbi Q9BZS1.
    PRIDEi Q9BZS1.

    Protocols and materials databases

    DNASUi 50943.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000376197 ; ENSP00000365369 ; ENSG00000049768 .
    ENST00000376199 ; ENSP00000365372 ; ENSG00000049768 . [Q9BZS1-2 ]
    ENST00000376207 ; ENSP00000365380 ; ENSG00000049768 . [Q9BZS1-1 ]
    ENST00000455775 ; ENSP00000396415 ; ENSG00000049768 . [Q9BZS1-4 ]
    ENST00000518685 ; ENSP00000428952 ; ENSG00000049768 . [Q9BZS1-2 ]
    ENST00000557224 ; ENSP00000451208 ; ENSG00000049768 . [Q9BZS1-3 ]
    GeneIDi 50943.
    KEGGi hsa:50943.
    UCSCi uc004dne.4. human. [Q9BZS1-2 ]
    uc004dnf.4. human. [Q9BZS1-1 ]
    uc022bwa.1. human. [Q9BZS1-3 ]

    Organism-specific databases

    CTDi 50943.
    GeneCardsi GC0XM049106.
    GeneReviewsi FOXP3.
    HGNCi HGNC:6106. FOXP3.
    HPAi CAB026301.
    HPA045943.
    MIMi 300292. gene.
    304790. phenotype.
    neXtProti NX_Q9BZS1.
    Orphaneti 37042. Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome.
    PharmGKBi PA201094.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5025.
    HOGENOMi HOG000082490.
    HOVERGENi HBG051656.
    KOi K10163.
    OMAi KHCQADH.
    OrthoDBi EOG7M6D7G.
    PhylomeDBi Q9BZS1.
    TreeFami TF326978.

    Enzyme and pathway databases

    SignaLinki Q9BZS1.

    Miscellaneous databases

    EvolutionaryTracei Q9BZS1.
    GeneWikii FOXP3.
    GenomeRNAii 50943.
    NextBioi 35482169.
    PROi Q9BZS1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9BZS1.
    Bgeei Q9BZS1.
    CleanExi HS_FOXP3.
    Genevestigatori Q9BZS1.

    Family and domain databases

    Gene3Di 1.10.10.10. 1 hit.
    3.30.160.60. 1 hit.
    InterProi IPR001766. TF_fork_head.
    IPR018122. TF_fork_head_CS.
    IPR011991. WHTH_DNA-bd_dom.
    IPR007087. Znf_C2H2.
    IPR015880. Znf_C2H2-like.
    IPR013087. Znf_C2H2/integrase_DNA-bd.
    [Graphical view ]
    Pfami PF00250. Fork_head. 1 hit.
    [Graphical view ]
    PRINTSi PR00053. FORKHEAD.
    SMARTi SM00339. FH. 1 hit.
    SM00355. ZnF_C2H2. 1 hit.
    [Graphical view ]
    PROSITEi PS00658. FORK_HEAD_2. 1 hit.
    PS50039. FORK_HEAD_3. 1 hit.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Disruption of a new forkhead/winged-helix protein, scurfin, results in the fatal lymphoproliferative disorder of the scurfy mouse."
      Brunkow M.E., Jeffery E.W., Hjerrild K.A., Paeper B., Clark L.B., Yasayko S.-A., Wilkinson J.E., Galas D., Ziegler S.F., Ramsdell F.
      Nat. Genet. 27:68-73(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Cloning and expression of the cDNA for FOXP3."
      Wang J., Liu Q., Zhang Y., Xu Z., Huang C.
      Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Functional characterization of FOXP3 splice variants in human regulatory T cells."
      Kaur G., Goodall J.C., Jarvis L.B., Gaston J.S.H.
      Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
    4. Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M., Huang B., Zhou G., Yang S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    5. "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].
    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] (ISOFORMS 1 AND 2).
    7. "Transcription map in Xp11.23."
      Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A., Meindl A.
      Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-431 (ISOFORM 3).
    8. "Activation of the aryl hydrocarbon receptor induces human type 1 regulatory T cell-like and Foxp3(+) regulatory T cells."
      Gandhi R., Kumar D., Burns E.J., Nadeau M., Dake B., Laroni A., Kozoriz D., Weiner H.L., Quintana F.J.
      Nat. Immunol. 11:846-853(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH IKZF3.
    9. "Three novel acetylation sites in the Foxp3 transcription factor regulate the suppressive activity of regulatory T cells."
      Kwon H.S., Lim H.W., Wu J., Schnolzer M., Verdin E., Ott M.
      J. Immunol. 188:2712-2721(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION AT LYS-31; LYS-263 AND LYS-268, DEACETYLATION BY SIRT1.
    10. "JM2, encoding a fork head-related protein, is mutated in X-linked autoimmunity-allergic disregulation syndrome."
      Chatila T.A., Blaeser F., Ho N., Lederman H.M., Voulgaropoulos C., Helms C., Bowcock A.M.
      J. Clin. Invest. 106:R75-R81(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IPEX GLU-251 DEL.
    11. "Novel mutations of FOXP3 in two Japanese patients with immune dysregulation, polyendocrinopathy, enteropathy, X linked syndrome (IPEX)."
      Kobayashi I., Shiari R., Yamada M., Kawamura N., Okano M., Yara A., Iguchi A., Ishikawa N., Ariga T., Sakiyama Y., Ochs H.D., Kobayashi K.
      J. Med. Genet. 38:874-876(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IPEX VAL-363.
    12. "X-linked neonatal diabetes mellitus, enteropathy and endocrinopathy syndrome is the human equivalent of mouse scurfy."
      Wildin R.S., Ramsdell F., Peake J., Faravelli F., Casanova J.-L., Buist N., Levy-Lahad E., Mazzella M., Goulet O., Perroni L., Bricarelli F.D., Byrne G., McEuen M., Proll S., Appleby M., Brunkow M.E.
      Nat. Genet. 27:18-20(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS IPEX CYS-371; THR-384 AND TRP-397.
    13. "The immune dysregulation, polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) is caused by mutations of FOXP3."
      Bennett C.L., Christie J., Ramsdell F., Brunkow M.E., Ferguson P.J., Whitesell L., Kelly T.E., Saulsbury F.T., Chance P.F., Ochs H.D.
      Nat. Genet. 27:20-21(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT IPEX THR-384.

    Entry informationi

    Entry nameiFOXP3_HUMAN
    AccessioniPrimary (citable) accession number: Q9BZS1
    Secondary accession number(s): A5HJT1
    , B7ZLG0, B9UN80, O60827, Q14DD8, Q4ZH51
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 20, 2001
    Last sequence update: June 1, 2001
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    External Data

    Dasty 3