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Protein

Forkhead box protein P3

Gene

FOXP3

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

Functioni

Transcriptional regulator which is crucial for the development and inhibitory function of regulatory T-cells (Treg). Plays an essential role in maintaining homeostasis of the immune system by allowing the acquisition of full suppressive function and stability of the Treg lineage, and by directly modulating the expansion and function of conventional T-cells. Can act either as a transcriptional repressor or a transcriptional activator depending on its interactions with other transcription factors, histone acetylases and deacetylases. The suppressive activity of Treg involves the coordinate activation of many genes, including CTLA4 and TNFRSF18 by FOXP3 along with repression of genes encoding cytokines such as interleukin-2 (IL2) and interferon-gamma (IFNG). Inhibits cytokine production and T-cell effector function by repressing the activity of two key transcription factors, RELA and NFATC2 (PubMed:15790681). Mediates transcriptional repression of IL2 via its association with histone acetylase KAT5 and histone deacetylase HDAC7 (PubMed:17360565). Can activate the expression of TNFRSF18, IL2RA and CTLA4 and repress the expression of IL2 and IFNG via its association with transcription factor RUNX1 (PubMed:17377532). Inhibits the differentiation of IL17 producing helper T-cells (Th17) by antagonizing RORC function, leading to down-regulation of IL17 expression, favoring Treg development (PubMed:18368049). Inhibits the transcriptional activator activity of RORA (PubMed:18354202). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (By similarity).By similarity6 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 222C2H2-typeAdd BLAST26
DNA bindingi337 – 423Fork-headPROSITE-ProRule annotationAdd BLAST87

GO - Molecular functioni

  • core promoter binding Source: UniProtKB
  • histone acetyltransferase binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • metal ion binding Source: UniProtKB-KW
  • NFAT protein binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • RNA polymerase II transcription factor activity, sequence-specific DNA binding Source: GO_Central
  • sequence-specific DNA binding Source: UniProtKB
  • transcription corepressor activity Source: Ensembl
  • transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding Source: Ensembl
  • transcription factor activity, sequence-specific DNA binding Source: UniProtKB

GO - Biological processi

  • B cell homeostasis Source: Ensembl
  • CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment Source: UniProtKB
  • chromatin remodeling Source: UniProtKB
  • cytokine production Source: Ensembl
  • myeloid cell homeostasis Source: Ensembl
  • negative regulation of activated T cell proliferation Source: UniProtKB
  • negative regulation of cell proliferation Source: UniProtKB
  • negative regulation of chronic inflammatory response Source: Ensembl
  • negative regulation of CREB transcription factor activity Source: UniProtKB
  • negative regulation of cytokine biosynthetic process Source: UniProtKB
  • negative regulation of cytokine secretion Source: UniProtKB
  • negative regulation of histone acetylation Source: Ensembl
  • negative regulation of histone deacetylation Source: BHF-UCL
  • negative regulation of immune response Source: UniProtKB
  • negative regulation of interferon-gamma biosynthetic process Source: Ensembl
  • negative regulation of interferon-gamma production Source: UniProtKB
  • negative regulation of interleukin-10 production Source: UniProtKB
  • negative regulation of interleukin-17 production Source: UniProtKB
  • negative regulation of interleukin-2 biosynthetic process Source: UniProtKB
  • negative regulation of interleukin-2 production Source: UniProtKB
  • negative regulation of interleukin-4 production Source: UniProtKB
  • negative regulation of interleukin-5 production Source: Ensembl
  • negative regulation of interleukin-6 production Source: Ensembl
  • negative regulation of isotype switching to IgE isotypes Source: Ensembl
  • negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  • negative regulation of T cell cytokine production Source: UniProtKB
  • negative regulation of T cell proliferation Source: UniProtKB
  • negative regulation of T-helper 17 cell differentiation Source: UniProtKB
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: Ensembl
  • negative regulation of tumor necrosis factor production Source: Ensembl
  • positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: UniProtKB
  • positive regulation of histone acetylation Source: BHF-UCL
  • positive regulation of immature T cell proliferation in thymus Source: Ensembl
  • positive regulation of interleukin-4 production Source: Ensembl
  • positive regulation of peripheral T cell tolerance induction Source: Ensembl
  • positive regulation of T cell anergy Source: Ensembl
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transforming growth factor beta1 production Source: Ensembl
  • regulation of isotype switching to IgG isotypes Source: Ensembl
  • regulation of T cell anergy Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • response to virus Source: UniProtKB
  • T cell activation Source: UniProtKB
  • T cell homeostasis Source: UniProtKB
  • T cell mediated immunity Source: Ensembl
  • T cell receptor signaling pathway Source: Ensembl
  • tolerance induction to self antigen Source: Ensembl
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciZFISH:ENSG00000049768-MONOMER.
SignaLinkiQ9BZS1.
SIGNORiQ9BZS1.

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein P3
Alternative name(s):
Scurfin
Cleaved into the following 2 chains:
Gene namesi
Name:FOXP3
Synonyms:IPEX
ORF Names:JM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:6106. FOXP3.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Involvement in diseasei

Immunodeficiency polyendocrinopathy, enteropathy, X-linked syndrome (IPEX)4 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by neonatal onset insulin-dependent diabetes mellitus, infections, secretory diarrhea, thrombocytopenia, anemia and eczema. It is usually lethal in infancy.
See also OMIM:304790
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011330251Missing in IPEX. 1 Publication1
Natural variantiVAR_023569363I → V in IPEX. 1 Publication1
Natural variantiVAR_011331371F → C in IPEX. 1 PublicationCorresponds to variant rs122467169dbSNPEnsembl.1
Natural variantiVAR_011332384A → T in IPEX. 2 PublicationsCorresponds to variant rs122467170dbSNPEnsembl.1
Natural variantiVAR_011333397R → W in IPEX. 1 PublicationCorresponds to variant rs28935477dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi69L → A: Decrease in nuclear export; when associated with A-71, A-74 and A-76. 1 Publication1
Mutagenesisi71L → A: Decrease in nuclear export; when associated with A-69, A-74 and A-76. 1 Publication1
Mutagenesisi74L → A: Decrease in nuclear export; when associated with A-69, A-71 and A-76. 1 Publication1
Mutagenesisi76L → A: Decrease in nuclear export; when associated with A-69, A-71 and A-74. 1 Publication1
Mutagenesisi95 – 96LL → AA: Loss of interaction with RORA. 1 Publication2
Mutagenesisi242L → A: Decrease in nuclear export; when associated with A-246 and A-248. 1 Publication1
Mutagenesisi246L → A: Decrease in nuclear export; when associated with A-242 and A-248. 1 Publication1
Mutagenesisi248L → A: Decrease in nuclear export; when associated with A-242 and A-246. 1 Publication1
Mutagenesisi415 – 416KK → EE: Loss of nuclear localization. 1 Publication2
Mutagenesisi418S → A: Decrease in phosphorylation, significant decrease in transcriptional repressor activity and reduced interaction with PP1CA, PP1CB and PP1CG. Significant decrease in phosphorylation and transcriptional repressor activity; when associated with A-422. 1 Publication1
Mutagenesisi418S → E: Slight increase in transcriptional repressor activity. 1 Publication1
Mutagenesisi422S → A: Significant decrease in phosphorylation and transcriptional repressor activity; when associated with A-418. 1 Publication1

Keywords - Diseasei

Diabetes mellitus, Disease mutation

Organism-specific databases

DisGeNETi50943.
MalaCardsiFOXP3.
MIMi304790. phenotype.
OpenTargetsiENSG00000049768.
Orphaneti37042. Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome.
PharmGKBiPA201094.

Polymorphism and mutation databases

BioMutaiFOXP3.
DMDMi14548061.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000918861 – 431Forkhead box protein P3Add BLAST431
ChainiPRO_00004324301 – 417Forkhead box protein P3, C-terminally processed1 PublicationAdd BLAST417
ChainiPRO_000043243152 – 417Forkhead box protein P3 41 kDa form1 PublicationAdd BLAST366
PropeptideiPRO_0000432432418 – 4311 PublicationAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei19Phosphoserine; by CDK2By similarity1
Modified residuei31N6-acetyllysine1 Publication1
Cross-linki250Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki252Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei263N6-acetyllysine; alternate1 Publication1
Cross-linki263Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Modified residuei268N6-acetyllysine; alternate1 Publication1
Cross-linki268Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternateBy similarity
Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei418Phosphoserine1 Publication1

Post-translational modificationi

Polyubiquitinated, leading to its proteasomal degradation in regulatory T-cells (Treg) which is mediated by STUB1 in a HSPA1A/B-dependent manner. Deubiquitinated by USP7 leading to increase in protein stability.2 Publications
Phosphorylation at Ser-418 regulates its transcriptional repressor activity and consequently, regulatory T-cells (Treg) suppressive function. Dephosphorylated at Ser-418 by protein phosphatase 1 (PP1) in Treg cells derived from patients with rheumatoid arthritis. Phosphorylation by CDK2 negatively regulates its transcriptional activity and protein stability (By similarity).By similarity1 Publication
Acetylation on lysine residues stabilizes FOXP3 and promotes differentiation of T-cells into induced regulatory T-cells (iTregs) associated with suppressive functions. Deacetylated by SIRT1.2 Publications
Undergoes proteolytic cleavage in activated regulatory T-cells (Treg), and can be cleaved at either the N- or C-terminal site, or at both sites.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei51 – 52Cleavage1 Publication2
Sitei417 – 418Cleavage; by PCSK1 or PCSK21 Publication2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiQ9BZS1.
PaxDbiQ9BZS1.
PeptideAtlasiQ9BZS1.
PRIDEiQ9BZS1.
TopDownProteomicsiQ9BZS1-3. [Q9BZS1-3]

PTM databases

iPTMnetiQ9BZS1.
PhosphoSitePlusiQ9BZS1.
SwissPalmiQ9BZS1.

Expressioni

Inductioni

Down-regulated in regulatory T-cells (Treg) during inflammation.1 Publication

Gene expression databases

BgeeiENSG00000049768.
CleanExiHS_FOXP3.
ExpressionAtlasiQ9BZS1. baseline and differential.
GenevisibleiQ9BZS1. HS.

Organism-specific databases

HPAiCAB026301.
HPA045943.

Interactioni

Subunit structurei

Homodimer (By similarity). Interacts with IKZF3. Isoform 1 (via LXXLL motif), but not isoform 2, interacts with isoform 4 of RORA (via AF-2 motif). Interacts with STUB1, HSPA8 and HSPA1A/B. Interacts with PPP1CA, PPP1CB and PPP1CG. Interacts with KAT5 and HDAC7. Interacts with HDAC9 in the absence of T-cell stimulation. Interacts with USP7. Interacts with isoform 2 of ZFP90 and can form a complex with TRIM28 in the presence of isoform 2 of ZFP90. Interacts with RUNX1. Interacts with RORC. Interacts with RELA and NFATC2. Interacts with RUNX2, RUNX3 and IKZF4 (By similarity).By similarity10 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HDAC7Q8WUI42EBI-9695448,EBI-1048378
IKZF3Q9UKT92EBI-983719,EBI-747204
KAT5Q929932EBI-9695448,EBI-399080
PIM1P11309-23EBI-9695448,EBI-1018633
PPP1CAP621362EBI-983719,EBI-357253
PRR20CP864796EBI-983719,EBI-10172814
RBPMSQ930624EBI-983719,EBI-740322
RORAP35398-45EBI-983719,EBI-11295807
STUB1Q9UNE77EBI-983719,EBI-357085

GO - Molecular functioni

  • histone acetyltransferase binding Source: BHF-UCL
  • histone deacetylase binding Source: BHF-UCL
  • NFAT protein binding Source: UniProtKB
  • NF-kappaB binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi119170. 70 interactors.
DIPiDIP-36584N.
IntActiQ9BZS1. 59 interactors.
STRINGi9606.ENSP00000365380.

Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi342 – 351Combined sources10
Helixi360 – 371Combined sources12
Turni372 – 375Combined sources4
Helixi381 – 391Combined sources11
Beta strandi395 – 398Combined sources4
Beta strandi401 – 403Combined sources3
Beta strandi405 – 408Combined sources4
Helixi410 – 416Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QRFX-ray2.80F/G/H/I336-417[»]
4WK8X-ray3.40F/G336-417[»]
ProteinModelPortaliQ9BZS1.
SMRiQ9BZS1.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9BZS1.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni106 – 198Interaction with ZFP901 PublicationAdd BLAST93
Regioni106 – 190Essential for transcriptional repressor activity and for interaction with KAT5 and HDAC71 PublicationAdd BLAST85
Regioni149 – 199Interaction with IKZF4By similarityAdd BLAST51
Regioni239 – 260Leucine-zipperAdd BLAST22
Regioni278 – 336Interaction with RUNX11 PublicationAdd BLAST59

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi68 – 76Nuclear export signal1 Publication9
Motifi92 – 96LXXLL motif1 Publication5
Motifi239 – 248Nuclear export signal1 Publication10
Motifi414 – 417Nuclear localization signal1 Publication4

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri197 – 222C2H2-typeAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiKOG4385. Eukaryota.
COG5025. LUCA.
GeneTreeiENSGT00800000124014.
HOGENOMiHOG000082490.
HOVERGENiHBG051656.
InParanoidiQ9BZS1.
KOiK10163.
OMAiFKEPEDF.
OrthoDBiEOG091G08HY.
PhylomeDBiQ9BZS1.
TreeFamiTF326978.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.160.60. 1 hit.
InterProiIPR001766. Fork_head_dom.
IPR032354. FOXP-CC.
IPR030456. TF_fork_head_CS_2.
IPR011991. WHTH_DNA-bd_dom.
IPR007087. Znf_C2H2.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00250. Forkhead. 1 hit.
PF16159. FOXP-CC. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
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.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

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

        10         20         30         40         50
MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL
60 70 80 90 100
RGGAHASSSS LNPMPPSQLQ LPTLPLVMVA PSGARLGPLP HLQALLQDRP
110 120 130 140 150
HFMHQLSTVD AHARTPVLQV HPLESPAMIS LTPPTTATGV FSLKARPGLP
160 170 180 190 200
PGINVASLEW VSREPALLCT FPNPSAPRKD STLSAVPQSS YPLLANGVCK
210 220 230 240 250
WPGCEKVFEE PEDFLKHCQA DHLLDEKGRA QCLLQREMVQ SLEQQLVLEK
260 270 280 290 300
EKLSAMQAHL AGKMALTKAS SVASSDKGSC CIVAAGSQGP VVPAWSGPRE
310 320 330 340 350
APDSLFAVRR HLWGSHGNST FPEFLHNMDY FKFHNMRPPF TYATLIRWAI
360 370 380 390 400
LEAPEKQRTL NEIYHWFTRM FAFFRNHPAT WKNAIRHNLS LHKCFVRVES
410 420 430
EKGAVWTVDE LEFRKKRSQR PSRCSNPTPG P
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)DescriptionActionsGraphical viewLength
Sequence conflicti16 – 20LGPSP → MSPIS in CAA06748 (Ref. 7) Curated5

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_011330251Missing in IPEX. 1 Publication1
Natural variantiVAR_023569363I → V in IPEX. 1 Publication1
Natural variantiVAR_011331371F → C in IPEX. 1 PublicationCorresponds to variant rs122467169dbSNPEnsembl.1
Natural variantiVAR_011332384A → T in IPEX. 2 PublicationsCorresponds to variant rs122467170dbSNPEnsembl.1
Natural variantiVAR_011333397R → W in IPEX. 1 PublicationCorresponds to variant rs28935477dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_01579672 – 106Missing in isoform 2 and isoform 3. 3 PublicationsAdd BLAST35
Alternative sequenceiVSP_047859246 – 272Missing in isoform 4. 1 PublicationAdd BLAST27
Alternative sequenceiVSP_036418382K → KVSSSEVAVTGMASSAIAAQ SGQAWVWAHRHIGEERDVGC WWWLLASEVDAHLLPVPGLP Q in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000376199; ENSP00000365372; ENSG00000049768. [Q9BZS1-2]
ENST00000376207; ENSP00000365380; ENSG00000049768. [Q9BZS1-1]
ENST00000518685; ENSP00000428952; ENSG00000049768. [Q9BZS1-2]
ENST00000557224; ENSP00000451208; ENSG00000049768. [Q9BZS1-3]
GeneIDi50943.
KEGGihsa:50943.
UCSCiuc004dne.5. human. [Q9BZS1-1]

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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QRFX-ray2.80F/G/H/I336-417[»]
4WK8X-ray3.40F/G336-417[»]
ProteinModelPortaliQ9BZS1.
SMRiQ9BZS1.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119170. 70 interactors.
DIPiDIP-36584N.
IntActiQ9BZS1. 59 interactors.
STRINGi9606.ENSP00000365380.

PTM databases

iPTMnetiQ9BZS1.
PhosphoSitePlusiQ9BZS1.
SwissPalmiQ9BZS1.

Polymorphism and mutation databases

BioMutaiFOXP3.
DMDMi14548061.

Proteomic databases

MaxQBiQ9BZS1.
PaxDbiQ9BZS1.
PeptideAtlasiQ9BZS1.
PRIDEiQ9BZS1.
TopDownProteomicsiQ9BZS1-3. [Q9BZS1-3]

Protocols and materials databases

DNASUi50943.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000376199; ENSP00000365372; ENSG00000049768. [Q9BZS1-2]
ENST00000376207; ENSP00000365380; ENSG00000049768. [Q9BZS1-1]
ENST00000518685; ENSP00000428952; ENSG00000049768. [Q9BZS1-2]
ENST00000557224; ENSP00000451208; ENSG00000049768. [Q9BZS1-3]
GeneIDi50943.
KEGGihsa:50943.
UCSCiuc004dne.5. human. [Q9BZS1-1]

Organism-specific databases

CTDi50943.
DisGeNETi50943.
GeneCardsiFOXP3.
GeneReviewsiFOXP3.
HGNCiHGNC:6106. FOXP3.
HPAiCAB026301.
HPA045943.
MalaCardsiFOXP3.
MIMi300292. gene.
304790. phenotype.
neXtProtiNX_Q9BZS1.
OpenTargetsiENSG00000049768.
Orphaneti37042. Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome.
PharmGKBiPA201094.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4385. Eukaryota.
COG5025. LUCA.
GeneTreeiENSGT00800000124014.
HOGENOMiHOG000082490.
HOVERGENiHBG051656.
InParanoidiQ9BZS1.
KOiK10163.
OMAiFKEPEDF.
OrthoDBiEOG091G08HY.
PhylomeDBiQ9BZS1.
TreeFamiTF326978.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000049768-MONOMER.
SignaLinkiQ9BZS1.
SIGNORiQ9BZS1.

Miscellaneous databases

EvolutionaryTraceiQ9BZS1.
GeneWikiiFOXP3.
GenomeRNAii50943.
PROiQ9BZS1.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000049768.
CleanExiHS_FOXP3.
ExpressionAtlasiQ9BZS1. baseline and differential.
GenevisibleiQ9BZS1. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.160.60. 1 hit.
InterProiIPR001766. Fork_head_dom.
IPR032354. FOXP-CC.
IPR030456. TF_fork_head_CS_2.
IPR011991. WHTH_DNA-bd_dom.
IPR007087. Znf_C2H2.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00250. Forkhead. 1 hit.
PF16159. FOXP-CC. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 167 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.