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Entry version 195 (16 Oct 2019)
Sequence version 1 (01 Jun 2001)
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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

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 similarity7 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri197 – 222C2H2-typeAdd BLAST26
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi337 – 423Fork-headPROSITE-ProRule annotationAdd BLAST87

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionActivator, DNA-binding, Repressor
Biological processTranscription, Transcription regulation
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8939256 RUNX1 regulates transcription of genes involved in WNT signaling

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q9BZS1

SIGNOR Signaling Network Open Resource

More...
SIGNORi
Q9BZS1

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Forkhead box protein P3
Alternative name(s):
Scurfin
Cleaved into the following 2 chains:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FOXP3
Synonyms:IPEX
ORF Names:JM2
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome X

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:6106 FOXP3

Online Mendelian Inheritance in Man (OMIM)

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MIMi
300292 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q9BZS1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>Involvement in diseasei

Immunodeficiency polyendocrinopathy, enteropathy, X-linked syndrome (IPEX)6 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.
Related information in OMIM
Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_078971242L → P in IPEX; mild phenotype; no loss of protein expression. 1 Publication1
Natural variantiVAR_011330251Missing in IPEX; significantly reduces dimerization. 2 Publications1
Natural variantiVAR_078972324F → L in IPEX; mild phenotype; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs122467173EnsemblClinVar.1
Natural variantiVAR_078973339P → A in IPEX; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs886044787EnsemblClinVar.1
Natural variantiVAR_078974347R → H in IPEX; mild phenotype; no loss of protein expression; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with A-373. 2 Publications1
Natural variantiVAR_023569363I → V in IPEX. 1 Publication1
Natural variantiVAR_011331371F → C in IPEX; no effect on dimerization. 2 PublicationsCorresponds to variant dbSNP:rs122467169EnsemblClinVar.1
Natural variantiVAR_078975373F → A in IPEX; requires 2 nucleotide substitutions; no loss of protein expression; disrupts dimerization; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with H-347. 2 PublicationsCorresponds to variant dbSNP:rs122467172EnsemblClinVar.1
Natural variantiVAR_078976374F → C in IPEX; no loss of protein expression. 1 Publication1
Natural variantiVAR_011332384A → T in IPEX; no loss of protein expression. 3 PublicationsCorresponds to variant dbSNP:rs122467170EnsemblClinVar.1
Natural variantiVAR_011333397R → W in IPEX. 1 PublicationCorresponds to variant dbSNP:rs28935477EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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
Mutagenesisi348W → Q: No loss of DNA-binding. Disrupts dimerization but does not affect DNA-binding; when associated with T-370. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with T-370 and P-372. 1 Publication1
Mutagenesisi370M → T: Disrupts dimerization but does not affect DNA-binding; when associated with Q-348. Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and P-372. 1 Publication1
Mutagenesisi372A → P: Disrupts dimerization, does not affect DNA-binding, causes dysregulated expression of a subset of FOXP3 target genes and impairs its ability to confer inhibitory function to regulatory T-cells; when associated with Q-348 and T-370. 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

DisGeNET

More...
DisGeNETi
50943

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
FOXP3

MalaCards human disease database

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MalaCardsi
FOXP3
MIMi304790 phenotype

Open Targets

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OpenTargetsi
ENSG00000049768

Orphanet; a database dedicated to information on rare diseases and orphan drugs

More...
Orphaneti
37042 Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA201094

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...
Pharosi
Q9BZS1

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FOXP3

Domain mapping of disease mutations (DMDM)

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DMDMi
14548061

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>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
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000432432418 – 4311 PublicationAdd BLAST14

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei19Phosphoserine; by CDK2By similarity1
Modified residuei31N6-acetyllysine1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>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

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei51 – 52Cleavage1 Publication2
Sitei417 – 418Cleavage; by PCSK1 or PCSK21 Publication2

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q9BZS1

MaxQB - The MaxQuant DataBase

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MaxQBi
Q9BZS1

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q9BZS1

PeptideAtlas

More...
PeptideAtlasi
Q9BZS1

PRoteomics IDEntifications database

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PRIDEi
Q9BZS1

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
7545
79899 [Q9BZS1-1]
79900 [Q9BZS1-2]
79901 [Q9BZS1-3]

Consortium for Top Down Proteomics

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TopDownProteomicsi
Q9BZS1-3 [Q9BZS1-3]

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q9BZS1

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q9BZS1

SwissPalm database of S-palmitoylation events

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SwissPalmi
Q9BZS1

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000049768 Expressed in 112 organ(s), highest expression level in amniotic fluid

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q9BZS1 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q9BZS1 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB026301
HPA045943

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer (PubMed:21458306, PubMed:25567984). Dimerization is essential for its transcriptional regulator activity (PubMed:21458306).

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 similarity12 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
119170, 70 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
Q9BZS1

Database of interacting proteins

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DIPi
DIP-36584N

Protein interaction database and analysis system

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IntActi
Q9BZS1, 71 interactors

Molecular INTeraction database

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MINTi
Q9BZS1

STRING: functional protein association networks

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STRINGi
9606.ENSP00000365380

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1431
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q9BZS1

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q9BZS1

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi68 – 76Nuclear export signal1 Publication9
Motifi92 – 96LXXLL motif1 Publication5
Motifi239 – 248Nuclear export signal1 Publication10
Motifi414 – 417Nuclear localization signal1 Publication4

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The fork-head DNA-binding domain is essential for its dimerization and interaction with NFATC2.1 Publication

Zinc finger

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

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4385 Eukaryota
COG5025 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000161807

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000082490

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q9BZS1

KEGG Orthology (KO)

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KOi
K10163

Identification of Orthologs from Complete Genome Data

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OMAi
FAYFRNH

Database of Orthologous Groups

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OrthoDBi
836427at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q9BZS1

TreeFam database of animal gene trees

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TreeFami
TF326978

Family and domain databases

Conserved Domains Database

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CDDi
cd00059 FH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR001766 Fork_head_dom
IPR032354 FOXP-CC
IPR030456 TF_fork_head_CS_2
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
IPR013087 Znf_C2H2_type

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00250 Forkhead, 1 hit
PF16159 FOXP-CC, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00053 FORKHEAD

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00339 FH, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46785 SSF46785, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit
PS00028 ZINC_FINGER_C2H2_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (4+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 4 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

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

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali 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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> 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

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
B7ZLG1B7ZLG1_HUMAN
FOXP3 protein
FOXP3
454Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0C4DFW6A0A0C4DFW6_HUMAN
Forkhead box P3, isoform CRA_b
FOXP3 hCG_19830
441Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A494C0B0A0A494C0B0_HUMAN
Forkhead box protein P3
FOXP3
335Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A494BZV0A0A494BZV0_HUMAN
Forkhead box protein P3
FOXP3
154Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A494C1K1A0A494C1K1_HUMAN
Forkhead box protein P3
FOXP3
54Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti16 – 20LGPSP → MSPIS in CAA06748 (Ref. 7) Curated5

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078971242L → P in IPEX; mild phenotype; no loss of protein expression. 1 Publication1
Natural variantiVAR_011330251Missing in IPEX; significantly reduces dimerization. 2 Publications1
Natural variantiVAR_078972324F → L in IPEX; mild phenotype; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs122467173EnsemblClinVar.1
Natural variantiVAR_078973339P → A in IPEX; no loss of protein expression. 1 PublicationCorresponds to variant dbSNP:rs886044787EnsemblClinVar.1
Natural variantiVAR_078974347R → H in IPEX; mild phenotype; no loss of protein expression; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with A-373. 2 Publications1
Natural variantiVAR_023569363I → V in IPEX. 1 Publication1
Natural variantiVAR_011331371F → C in IPEX; no effect on dimerization. 2 PublicationsCorresponds to variant dbSNP:rs122467169EnsemblClinVar.1
Natural variantiVAR_078975373F → A in IPEX; requires 2 nucleotide substitutions; no loss of protein expression; disrupts dimerization; impairs its ability to confer inhibitory function to regulatory T-cells; no loss of DNA-binding when associated with H-347. 2 PublicationsCorresponds to variant dbSNP:rs122467172EnsemblClinVar.1
Natural variantiVAR_078976374F → C in IPEX; no loss of protein expression. 1 Publication1
Natural variantiVAR_011332384A → T in IPEX; no loss of protein expression. 3 PublicationsCorresponds to variant dbSNP:rs122467170EnsemblClinVar.1
Natural variantiVAR_011333397R → W in IPEX. 1 PublicationCorresponds to variant dbSNP:rs28935477EnsemblClinVar.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>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:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
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

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS14323.1 [Q9BZS1-1]
CCDS48109.1 [Q9BZS1-2]

NCBI Reference Sequences

More...
RefSeqi
NP_001107849.1, NM_001114377.1 [Q9BZS1-2]
NP_054728.2, NM_014009.3 [Q9BZS1-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000376199; ENSP00000365372; ENSG00000049768 [Q9BZS1-2]
ENST00000376207; ENSP00000365380; ENSG00000049768 [Q9BZS1-1]
ENST00000518685; ENSP00000428952; ENSG00000049768 [Q9BZS1-4]
ENST00000557224; ENSP00000451208; ENSG00000049768 [Q9BZS1-3]

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
50943

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:50943

UCSC genome browser

More...
UCSCi
uc004dne.5 human [Q9BZS1-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>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]

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3QRFX-ray2.80F/G/H/I336-417[»]
4WK8X-ray3.40F/G336-417[»]
SMRiQ9BZS1
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi119170, 70 interactors
CORUMiQ9BZS1
DIPiDIP-36584N
IntActiQ9BZS1, 71 interactors
MINTiQ9BZS1
STRINGi9606.ENSP00000365380

PTM databases

iPTMnetiQ9BZS1
PhosphoSitePlusiQ9BZS1
SwissPalmiQ9BZS1

Polymorphism and mutation databases

BioMutaiFOXP3
DMDMi14548061

Proteomic databases

MassIVEiQ9BZS1
MaxQBiQ9BZS1
PaxDbiQ9BZS1
PeptideAtlasiQ9BZS1
PRIDEiQ9BZS1
ProteomicsDBi7545
79899 [Q9BZS1-1]
79900 [Q9BZS1-2]
79901 [Q9BZS1-3]
TopDownProteomicsiQ9BZS1-3 [Q9BZS1-3]

Protocols and materials databases

The DNASU plasmid repository

More...
DNASUi
50943

Genome annotation databases

EnsembliENST00000376199; ENSP00000365372; ENSG00000049768 [Q9BZS1-2]
ENST00000376207; ENSP00000365380; ENSG00000049768 [Q9BZS1-1]
ENST00000518685; ENSP00000428952; ENSG00000049768 [Q9BZS1-4]
ENST00000557224; ENSP00000451208; ENSG00000049768 [Q9BZS1-3]
GeneIDi50943
KEGGihsa:50943
UCSCiuc004dne.5 human [Q9BZS1-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
50943
DisGeNETi50943

GeneCards: human genes, protein and diseases

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

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG4385 Eukaryota
COG5025 LUCA
GeneTreeiENSGT00940000161807
HOGENOMiHOG000082490
InParanoidiQ9BZS1
KOiK10163
OMAiFAYFRNH
OrthoDBi836427at2759
PhylomeDBiQ9BZS1
TreeFamiTF326978

Enzyme and pathway databases

ReactomeiR-HSA-8877330 RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)
R-HSA-8939256 RUNX1 regulates transcription of genes involved in WNT signaling
SignaLinkiQ9BZS1
SIGNORiQ9BZS1

Miscellaneous databases

EvolutionaryTraceiQ9BZS1

The Gene Wiki collection of pages on human genes and proteins

More...
GeneWikii
FOXP3

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...
GenomeRNAii
50943
PharosiQ9BZS1

Protein Ontology

More...
PROi
PR:Q9BZS1

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSG00000049768 Expressed in 112 organ(s), highest expression level in amniotic fluid
ExpressionAtlasiQ9BZS1 baseline and differential
GenevisibleiQ9BZS1 HS

Family and domain databases

CDDicd00059 FH, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR001766 Fork_head_dom
IPR032354 FOXP-CC
IPR030456 TF_fork_head_CS_2
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
IPR013087 Znf_C2H2_type
PfamiView protein in Pfam
PF00250 Forkhead, 1 hit
PF16159 FOXP-CC, 1 hit
PRINTSiPR00053 FORKHEAD
SMARTiView protein in SMART
SM00339 FH, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit
PS00028 ZINC_FINGER_C2H2_1, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOXP3_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q9BZS1
Secondary accession number(s): A5HJT1
, B7ZLG0, B9UN80, O60827, Q14DD8, Q4ZH51
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 20, 2001
Last sequence update: June 1, 2001
Last modified: October 16, 2019
This is version 195 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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