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Q9BZS1

- FOXP3_HUMAN

UniProt

Q9BZS1 - FOXP3_HUMAN

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Protein

Forkhead box protein P3

Gene
FOXP3, IPEX, JM2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-headAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

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

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 Reviewed prediction

GO - Cellular componenti

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

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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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.

Miscellaneous databases

EvolutionaryTraceiQ9BZS1.

Family & Domainsi

Region

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

Sequence similaritiesi

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

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. VSP_015796Add
BLAST
Alternative sequencei246 – 27227Missing in isoform 4. VSP_047859Add
BLAST
Alternative sequencei382 – 3821K → KVSSSEVAVTGMASSAIAAQ SGQAWVWAHRHIGEERDVGC WWWLLASEVDAHLLPVPGLP Q in isoform 3. VSP_036418

Sequence conflict

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

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]
ENST00000595256; ENSP00000472792; ENSG00000269002. [Q9BZS1-4]
ENST00000596575; ENSP00000470454; ENSG00000269002. [Q9BZS1-1]
ENST00000599169; ENSP00000470432; ENSG00000269002. [Q9BZS1-2]
ENST00000599600; ENSP00000469715; ENSG00000269002. [Q9BZS1-2]
ENST00000600505; ENSP00000470672; ENSG00000269002.
ENST00000602054; ENSP00000471366; ENSG00000269002. [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 ]
ENST00000595256 ; ENSP00000472792 ; ENSG00000269002 . [Q9BZS1-4 ]
ENST00000596575 ; ENSP00000470454 ; ENSG00000269002 . [Q9BZS1-1 ]
ENST00000599169 ; ENSP00000470432 ; ENSG00000269002 . [Q9BZS1-2 ]
ENST00000599600 ; ENSP00000469715 ; ENSG00000269002 . [Q9BZS1-2 ]
ENST00000600505 ; ENSP00000470672 ; ENSG00000269002 .
ENST00000602054 ; ENSP00000471366 ; ENSG00000269002 . [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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 142 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

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