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Q9BZS1 (FOXP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 139. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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 P3
Alternative name(s):
Scurfin
Gene names
Name:FOXP3
Synonyms:IPEX
ORF Names:JM2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length431 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Interacts with IKZF3. Ref.8

Subcellular location

Nucleus Potential.

Post-translational modification

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. Ref.9

Involvement in disease

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. Ref.10 Ref.11 Ref.12 Ref.13

Sequence similarities

Contains 1 C2H2-type zinc finger.

Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DiseaseDiabetes mellitus
Disease mutation
   DomainZinc-finger
   LigandDNA-binding
Metal-binding
Zinc
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processB cell homeostasis

Inferred from Biological aspect of Ancestor. Source: RefGenome

CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation

Inferred from electronic annotation. Source: Ensembl

T cell activation

Inferred from direct assay PubMed 15466453. Source: UniProtKB

T cell homeostasis

Non-traceable author statement PubMed 11483607. Source: UniProtKB

T cell mediated immunity

Inferred from electronic annotation. Source: Ensembl

T cell receptor signaling pathway

Inferred from Biological aspect of Ancestor. Source: RefGenome

cardiac muscle cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

chromatin remodeling

Non-traceable author statement PubMed 16903909. Source: UniProtKB

cytokine production

Inferred from electronic annotation. Source: Ensembl

embryo development

Inferred from Biological aspect of Ancestor. Source: RefGenome

immunoglobulin V(D)J recombination

Inferred from Biological aspect of Ancestor. Source: RefGenome

lung development

Inferred from Biological aspect of Ancestor. Source: RefGenome

myeloid cell homeostasis

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of CREB transcription factor activity

Inferred from direct assay PubMed 16652169. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from direct assay PubMed 16652169. Source: UniProtKB

negative regulation of T cell cytokine production

Inferred from direct assay PubMed 15466453. Source: UniProtKB

negative regulation of T cell proliferation

Inferred from direct assay PubMed 15466453. Source: UniProtKB

negative regulation of activated T cell proliferation

Non-traceable author statement PubMed 11483607. Source: UniProtKB

negative regulation of cell proliferation

Inferred from direct assay PubMed 15652505. Source: UniProtKB

negative regulation of chronic inflammatory response

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of cytokine biosynthetic process

Inferred from direct assay PubMed 11483607. Source: UniProtKB

negative regulation of cytokine secretion

Inferred from direct assay PubMed 11483607. Source: UniProtKB

negative regulation of histone acetylation

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of histone deacetylation

Inferred from genetic interaction PubMed 19276356. Source: BHF-UCL

negative regulation of immune response

Inferred from direct assay PubMed 15652505. Source: UniProtKB

negative regulation of interferon-gamma biosynthetic process

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of interferon-gamma production

Inferred from direct assay PubMed 15466453. Source: UniProtKB

negative regulation of interleukin-10 production

Inferred from direct assay PubMed 15466453. Source: UniProtKB

negative regulation of interleukin-2 biosynthetic process

Inferred from mutant phenotype PubMed 16873067. Source: UniProtKB

negative regulation of interleukin-2 production

Inferred from direct assay PubMed 15466453. Source: UniProtKB

negative regulation of interleukin-4 production

Inferred from direct assay PubMed 15466453. Source: UniProtKB

negative regulation of interleukin-5 production

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of interleukin-6 production

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of isotype switching to IgE isotypes

Inferred from Biological aspect of Ancestor. Source: RefGenome

negative regulation of sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 16873067. Source: UniProtKB

negative regulation of transcription, DNA-templated

Inferred from direct assay PubMed 11483607PubMed 16920951. Source: UniProtKB

negative regulation of tumor necrosis factor production

Inferred from Biological aspect of Ancestor. Source: RefGenome

pattern specification process

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of T cell anergy

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of epithelial cell proliferation

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of histone acetylation

Inferred from mutant phenotype PubMed 19276356. Source: BHF-UCL

positive regulation of immature T cell proliferation in thymus

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of immunoglobulin production

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of interleukin-4 production

Inferred from electronic annotation. Source: Ensembl

positive regulation of peripheral T cell tolerance induction

Inferred from Biological aspect of Ancestor. Source: RefGenome

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 19276356. Source: BHF-UCL

positive regulation of transcription, DNA-templated

Inferred from direct assay PubMed 15466453. Source: UniProtKB

positive regulation of transforming growth factor beta1 production

Inferred from Biological aspect of Ancestor. Source: RefGenome

pre-B cell differentiation

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of isotype switching to IgG isotypes

Inferred from Biological aspect of Ancestor. Source: RefGenome

regulation of transcription, DNA-templated

Non-traceable author statement Ref.1. Source: UniProtKB

response to virus

Inferred from expression pattern PubMed 20583921. Source: UniProtKB

tolerance induction to self antigen

Inferred from Biological aspect of Ancestor. Source: RefGenome

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from direct assay PubMed 11483607PubMed 16873067PubMed 16920951. Source: UniProtKB

protein complex

Non-traceable author statement PubMed 16903909. Source: UniProtKB

   Molecular_functionDNA binding, bending

Inferred from Biological aspect of Ancestor. Source: RefGenome

NF-kappaB binding

Non-traceable author statement PubMed 16652169. Source: UniProtKB

NFAT protein binding

Inferred from physical interaction PubMed 16873067. Source: UniProtKB

RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity

Inferred from electronic annotation. Source: Ensembl

chromatin binding

Inferred from Biological aspect of Ancestor. Source: RefGenome

histone acetyltransferase binding

Inferred from physical interaction PubMed 17360565. Source: BHF-UCL

histone deacetylase binding

Inferred from physical interaction PubMed 17360565. Source: BHF-UCL

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein heterodimerization activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

protein homodimerization activity

Inferred from physical interaction PubMed 16920951. Source: UniProtKB

sequence-specific DNA binding

Inferred from direct assay PubMed 11483607PubMed 16873067. Source: UniProtKB

sequence-specific DNA binding transcription factor activity

Inferred from direct assay PubMed 11483607. Source: UniProtKB

transcription corepressor activity

Inferred from Biological aspect of Ancestor. Source: RefGenome

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

IKZF3Q9UKT92EBI-983719,EBI-747204

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9BZS1-1)

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 2 (identifier: Q9BZS1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     72-106: Missing.
Isoform 3 (identifier: Q9BZS1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     72-106: Missing.
     382-382: K → KVSSSEVAVTGMASSAIAAQSGQAWVWAHRHIGEERDVGCWWWLLASEVDAHLLPVPGLPQ
Note: No experimental confirmation available.
Isoform 4 (identifier: Q9BZS1-4)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 431431Forkhead box protein P3
PRO_0000091886

Regions

Zinc finger197 – 22226C2H2-type
DNA binding337 – 42387Fork-head
Region239 – 26022Leucine-zipper

Amino acid modifications

Modified residue311N6-acetyllysine Ref.9
Modified residue2631N6-acetyllysine Ref.9
Modified residue2681N6-acetyllysine Ref.9

Natural variations

Alternative sequence72 – 10635Missing in isoform 2 and isoform 3.
VSP_015796
Alternative sequence246 – 27227Missing in isoform 4.
VSP_047859
Alternative sequence3821K → KVSSSEVAVTGMASSAIAAQ SGQAWVWAHRHIGEERDVGC WWWLLASEVDAHLLPVPGLP Q in isoform 3.
VSP_036418
Natural variant2511Missing in IPEX. Ref.10
VAR_011330
Natural variant3631I → V in IPEX. Ref.11
VAR_023569
Natural variant3711F → C in IPEX. Ref.12
VAR_011331
Natural variant3841A → T in IPEX. Ref.12 Ref.13
VAR_011332
Natural variant3971R → W in IPEX. Ref.12
Corresponds to variant rs28935477 [ dbSNP | Ensembl ].
VAR_011333

Experimental info

Sequence conflict16 – 205LGPSP → MSPIS in CAA06748. Ref.7

Secondary structure

................ 431
Helix Strand Turn

Details...

Sequences

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

Last modified June 1, 2001. Version 1.
Checksum: 91737C3CEA665A15

FASTA43147,244
        10         20         30         40         50         60 
MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL RGGAHASSSS 

        70         80         90        100        110        120 
LNPMPPSQLQ LPTLPLVMVA PSGARLGPLP HLQALLQDRP HFMHQLSTVD AHARTPVLQV 

       130        140        150        160        170        180 
HPLESPAMIS LTPPTTATGV FSLKARPGLP PGINVASLEW VSREPALLCT FPNPSAPRKD 

       190        200        210        220        230        240 
STLSAVPQSS YPLLANGVCK WPGCEKVFEE PEDFLKHCQA DHLLDEKGRA QCLLQREMVQ 

       250        260        270        280        290        300 
SLEQQLVLEK EKLSAMQAHL AGKMALTKAS SVASSDKGSC CIVAAGSQGP VVPAWSGPRE 

       310        320        330        340        350        360 
APDSLFAVRR HLWGSHGNST FPEFLHNMDY FKFHNMRPPF TYATLIRWAI LEAPEKQRTL 

       370        380        390        400        410        420 
NEIYHWFTRM FAFFRNHPAT WKNAIRHNLS LHKCFVRVES EKGAVWTVDE LEFRKKRSQR 

       430 
PSRCSNPTPG P 

« Hide

Isoform 2 [UniParc].

Checksum: BF4DF0DD83D61CD5
Show »

FASTA39643,410
Isoform 3 [UniParc].

Checksum: 39E7483703031335
Show »

FASTA45649,843
Isoform 4 [UniParc].

Checksum: 4D164C39EF069DBB
Show »

FASTA40444,407

References

« Hide 'large scale' references
[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. 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].
[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
RefSeqNP_001107849.1. NM_001114377.1.
NP_054728.2. NM_014009.3.
UniGeneHs.247700.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3QRFX-ray2.80F/G/H/I336-417[»]
ProteinModelPortalQ9BZS1.
SMRQ9BZS1. Positions 202-263, 336-417.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119170. 19 interactions.
DIPDIP-36584N.
IntActQ9BZS1. 1 interaction.
STRING9606.ENSP00000365380.

PTM databases

PhosphoSiteQ9BZS1.

Polymorphism databases

DMDM14548061.

Proteomic databases

PaxDbQ9BZS1.
PRIDEQ9BZS1.

Protocols and materials databases

DNASU50943.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000376197; 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]
GeneID50943.
KEGGhsa:50943.
UCSCuc004dne.4. human. [Q9BZS1-2]
uc004dnf.4. human. [Q9BZS1-1]
uc022bwa.1. human. [Q9BZS1-3]

Organism-specific databases

CTD50943.
GeneCardsGC0XM049106.
HGNCHGNC:6106. FOXP3.
HPACAB026301.
HPA045943.
MIM300292. gene.
304790. phenotype.
neXtProtNX_Q9BZS1.
Orphanet37042. Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome.
PharmGKBPA201094.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5025.
HOGENOMHOG000082490.
HOVERGENHBG051656.
KOK10163.
OMAKHCQADH.
OrthoDBEOG7M6D7G.
PhylomeDBQ9BZS1.
TreeFamTF326978.

Enzyme and pathway databases

SignaLinkQ9BZS1.

Gene expression databases

ArrayExpressQ9BZS1.
BgeeQ9BZS1.
CleanExHS_FOXP3.
GenevestigatorQ9BZS1.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
3.30.160.60. 1 hit.
InterProIPR001766. 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]
PfamPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSPR00053. FORKHEAD.
SMARTSM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9BZS1.
GeneWikiFOXP3.
GenomeRNAi50943.
NextBio35482169.
PROQ9BZS1.
SOURCESearch...

Entry information

Entry nameFOXP3_HUMAN
AccessionPrimary (citable) accession number: Q9BZS1
Secondary accession number(s): A5HJT1 expand/collapse secondary AC list , B7ZLG0, B9UN80, O60827, Q14DD8, Q4ZH51
Entry history
Integrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: April 16, 2014
This is version 139 of the entry and version 1 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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome X

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