Q9BZS1 (FOXP3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Forkhead box protein P3

Alternative name(s):
Scurfin

Gene names

Name:	FOXP3
Synonyms:	IPEX
ORF Names:	JM2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	431 AA.
Sequence status	Complete.
Protein existence	Evidence 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.7
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.
Involvement in disease	Immunodeficiency polyendocrinopathy, enteropathy, X-linked syndrome (IPEX) [MIM:304790]: Characterized by neonatal onset insulin-dependent diabetes mellitus, infections, secretory diarrhea, trombocytopenia, anemia and eczema. It is usually lethal in infancy. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.9 Ref.10 Ref.11 Ref.12
Sequence similarities	Contains 1 C2H2-type zinc finger. Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Disease	Diabetes mellitus Disease mutation
Domain	Zinc-finger
Ligand	DNA-binding Metal-binding Zinc
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	B 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: Compara 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: Compara T cell receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome cerebellum development 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: Compara embryo 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 activated T cell proliferation Non-traceable author statement PubMed 11483607. Source: UniProtKB negative regulation of chronic inflammatory response Inferred from Biological aspect of Ancestor. Source: RefGenome 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 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 transcription, DNA-dependent 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 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 interleukin-4 production Inferred from electronic annotation. Source: Compara 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 transforming growth factor beta1 production Inferred from Biological aspect of Ancestor. Source: RefGenome post-embryonic development Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of isotype switching to IgG isotypes Inferred from Biological aspect of Ancestor. Source: RefGenome 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_component	cytoplasm Inferred from Biological aspect of Ancestor. Source: RefGenome nucleus Non-traceable author statement PubMed 16903909PubMed 16903909. Source: UniProtKB transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular_function	DNA binding, bending Inferred from Biological aspect of Ancestor. Source: RefGenome NF-kappaB binding Non-traceable author statement PubMed 16652169. Source: UniProtKB RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome chromatin binding Inferred from Biological aspect of Ancestor. Source: RefGenome double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome protein heterodimerization activity Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from direct assay PubMed 11483607PubMed 16873067. Source: UniProtKB transcription corepressor activity Inferred from Biological aspect of Ancestor. Source: RefGenome zinc ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
IKZF3	Q9UKT9	2	EBI-983719,EBI-747204

Alternative products

This entry describes 3 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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 431

431

Forkhead box protein P3

PRO_0000091886

Regions

Zinc finger

197 – 222

26

C2H2-type

DNA binding

337 – 423

87

Fork-head

Region

239 – 260

22

Leucine-zipper

Amino acid modifications

Modified residue

31

1

N6-acetyllysine Ref.8

Modified residue

263

1

N6-acetyllysine Ref.8

Modified residue

268

1

N6-acetyllysine Ref.8

Natural variations

Alternative sequence

72 – 106

35

Missing in isoform 2 and isoform 3.

VSP_015796

Alternative sequence

382

1

K → KVSSSEVAVTGMASSAIAAQ SGQAWVWAHRHIGEERDVGC WWWLLASEVDAHLLPVPGLP Q in isoform 3.

VSP_036418

Natural variant

251

1

Missing in IPEX. Ref.9

VAR_011330

Natural variant

363

1

I → V in IPEX. Ref.10

VAR_023569

Natural variant

371

1

F → C in IPEX. Ref.11

VAR_011331

Natural variant

384

1

A → T in IPEX. Ref.11 Ref.12

VAR_011332

Natural variant

397

1

R → W in IPEX. Ref.11
Corresponds to variant rs28935477 [ dbSNP | Ensembl ].

VAR_011333

Experimental info

Sequence conflict

16 – 20

5

LGPSP → MSPIS in CAA06748. Ref.6

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

431

Helix Strand Turn

Details...

Helix

342 – 351

10

Helix

360 – 371

12

Turn

372 – 375

4

Helix

381 – 391

11

Beta strand

395 – 398

4

Beta strand

401 – 403

3

Beta strand

405 – 408

4

Helix

410 – 416

7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2001. Version 1. Checksum: 91737C3CEA665A15	FASTA	431	47,244
	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
	Isoform 2 [UniParc]. Checksum: BF4DF0DD83D61CD5	FASTA	396	43,410
	10 20 30 40 50 60 MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL RGGAHASSSS 70 80 90 100 110 120 LNPMPPSQLQ LSTVDAHART PVLQVHPLES PAMISLTPPT TATGVFSLKA RPGLPPGINV 130 140 150 160 170 180 ASLEWVSREP ALLCTFPNPS APRKDSTLSA VPQSSYPLLA NGVCKWPGCE KVFEEPEDFL 190 200 210 220 230 240 KHCQADHLLD EKGRAQCLLQ REMVQSLEQQ LVLEKEKLSA MQAHLAGKMA LTKASSVASS 250 260 270 280 290 300 DKGSCCIVAA GSQGPVVPAW SGPREAPDSL FAVRRHLWGS HGNSTFPEFL HNMDYFKFHN 310 320 330 340 350 360 MRPPFTYATL IRWAILEAPE KQRTLNEIYH WFTRMFAFFR NHPATWKNAI RHNLSLHKCF 370 380 390 VRVESEKGAV WTVDELEFRK KRSQRPSRCS NPTPGP
	Isoform 3 [UniParc]. Checksum: 39E7483703031335	FASTA	456	49,843
	10 20 30 40 50 60 MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL RGGAHASSSS 70 80 90 100 110 120 LNPMPPSQLQ LSTVDAHART PVLQVHPLES PAMISLTPPT TATGVFSLKA RPGLPPGINV 130 140 150 160 170 180 ASLEWVSREP ALLCTFPNPS APRKDSTLSA VPQSSYPLLA NGVCKWPGCE KVFEEPEDFL 190 200 210 220 230 240 KHCQADHLLD EKGRAQCLLQ REMVQSLEQQ LVLEKEKLSA MQAHLAGKMA LTKASSVASS 250 260 270 280 290 300 DKGSCCIVAA GSQGPVVPAW SGPREAPDSL FAVRRHLWGS HGNSTFPEFL HNMDYFKFHN 310 320 330 340 350 360 MRPPFTYATL IRWAILEAPE KQRTLNEIYH WFTRMFAFFR NHPATWKVSS SEVAVTGMAS 370 380 390 400 410 420 SAIAAQSGQA WVWAHRHIGE ERDVGCWWWL LASEVDAHLL PVPGLPQNAI RHNLSLHKCF 430 440 450 VRVESEKGAV WTVDELEFRK KRSQRPSRCS NPTPGP

References

	« Hide 'large scale' referencesShow '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]	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).
[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]	"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).
[6]	"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).
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"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.
[12]	"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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

FOXP3base

FOXP3 mutation db

GeneReviews

Wikipedia

FOXP3 entry

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

AF277993 mRNA. Translation: AAG53607.1.
EF534714 mRNA. Translation: ABQ15210.1.
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.

IPI

IPI00328094.
IPI00604500.
IPI00644203.

RefSeq

NP_001107849.1. NM_001114377.1.
NP_054728.2. NM_014009.3.

UniGene

Hs.247700.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3QRF	X-ray	2.80	F/G/H/I	336-417	[»]

ProteinModelPortal

Q9BZS1.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q9BZS1. 1 interaction.

STRING

9606.ENSP00000365380.

PTM databases

PhosphoSite

Q9BZS1.

Polymorphism databases

DMDM

14548061.

Proteomic databases

PaxDb

Q9BZS1.

PRIDE

Q9BZS1.

Protocols and materials databases

DNASU

50943.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000376197; ENSP00000365369; ENSG00000049768.
ENST00000376199; ENSP00000365372; ENSG00000049768.
ENST00000376207; ENSP00000365380; ENSG00000049768.
ENST00000518685; ENSP00000428952; ENSG00000049768.
ENST00000557224; ENSP00000451208; ENSG00000049768.
ENST00000596575; ENSP00000470454; ENSG00000269002.
ENST00000599169; ENSP00000470432; ENSG00000269002.
ENST00000599600; ENSP00000469715; ENSG00000269002.
ENST00000600505; ENSP00000470672; ENSG00000269002.
ENST00000602054; ENSP00000471366; ENSG00000269002.

GeneID

50943.

KEGG

hsa:50943.

UCSC

uc004dne.4. human.
uc004dnf.4. human.
uc022bwa.1. human.

Organism-specific databases

CTD

50943.

GeneCards

GC0XM049106.

HGNC

HGNC:6106. FOXP3.

HPA

CAB026301.

MIM

300292. gene.
304790. phenotype.

neXtProt

NX_Q9BZS1.

Orphanet

37042. X-linked immune dysregulation - polyendocrinopathy - enteropathy.

PharmGKB

PA201094.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5025.

HOGENOM

HOG000082490.

HOVERGEN

HBG051656.

KO

K10163.

OMA

PSRCSNP.

OrthoDB

EOG4F7NK4.

PhylomeDB

Q9BZS1.

Enzyme and pathway databases

Pathway_Interaction_DB

nfat_tfpathway. Calcineurin-regulated NFAT-dependent transcription in lymphocytes.
il2_stat5pathway. IL2 signaling events mediated by STAT5.

Gene expression databases

ArrayExpress

Q9BZS1.

Bgee

Q9BZS1.

CleanEx

HS_FOXP3.

Genevestigator

Q9BZS1.

GermOnline

ENSG00000049768. Homo sapiens.

Family and domain databases

Gene3D

1.10.10.10. 1 hit.
3.30.160.60. 1 hit.

InterPro

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]

Pfam

PF00250. Fork_head. 1 hit.
[Graphical view]

PRINTS

PR00053. FORKHEAD.

SMART

SM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]

PROSITE

PS00657. FORK_HEAD_1. False negative.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
PS50157. ZINC_FINGER_C2H2_2. False negative.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

Q9BZS1.

GenomeRNAi

50943.

NextBio

53405.

SOURCE

Search...

Entry information

Entry name

FOXP3_HUMAN

Accession

Primary (citable) accession number: Q9BZS1
Secondary accession number(s): A5HJT1 , B7ZLG0, O60827, Q14DD8, Q4ZH51

Entry history

Integrated into UniProtKB/Swiss-Prot:	June 20, 2001
Last sequence update:	June 1, 2001
Last modified:	May 1, 2013
This is version 129 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.