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Entry version 170 (07 Oct 2020)
Sequence version 1 (01 Jun 2001)
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Protein

Forkhead box protein P3

Gene

Foxp3

Organism
Mus musculus (Mouse)
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 (By similarity). 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 (By similarity). Can repress the expression of IL2 and IFNG via its association with transcription factor IKZF4 (PubMed:19696312).By similarity4 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 fingeri196 – 221C2H2-typeAdd BLAST26
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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-MMU-8877330, RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)

<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%5Fand%5Ftaxonomy%5Fsection">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%5Fand%5Ftaxonomy%5Fsection">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
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1891436, Foxp3

<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

Defects in Foxp3 are the cause of the scurfy phenotype (sf). It results in a lethal disorder of immunoregulation, characterized by infections, diarrhea, anemia, thrombocytopenia, hypogonadism, gastrointestinal bleeding, lymphadenopathy and leukocytosis.

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi19S → A: Loss of phosphorylation. Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-88; A-114 and A-175. 1 Publication1
Mutagenesisi48 – 51RDLR → HDLH: Loss of proteolytic processing. 1 Publication4
Mutagenesisi88S → A: Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-19; A-114 and A-175. 1 Publication1
Mutagenesisi114T → A: Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-19; A-88 and A-175. 1 Publication1
Mutagenesisi175T → A: Increase in protein stability, transcriptional activity and the ability to suppress the proliferation of conventional T-cells in vitro; when associated with A-19; A-88 and A-114. 1 Publication1
Mutagenesisi250Missing : Loss of homodimerization, decrease in transcriptional repressor activity, elimination of its Treg suppressor activity, defects in Th1 and Th2 cytokine secretion and down-regulation of cell surface markers on regulatory T-cells. 1 Publication1
Mutagenesisi329 – 330DY → VH: Reduced interaction with RUNX1, decrease in its ability to regulate the expression of IL2, TNFRSF18, IL2RA and CTLA4 in a RUNX1-dependent manner. Loss of interaction with RUNX1 but no effect on interaction with NFATC2 and loss of its ability to regulate the expression of IL2, TNFRSF18, IL2RA and CTLA4 in a RUNX1-dependent manner; when associated with L-332. 1 Publication2
Mutagenesisi332K → L: Loss of interaction with RUNX1 but no effect on interaction with NFATC2 and loss of its ability to regulate the expression of IL2, TNFRSF18, IL2RA and CTLA4 in a RUNX1-dependent manner; when associated with 329-VH-330. 1 Publication1
Mutagenesisi414 – 417RKKR → PNNW: Loss of ability to suppress the proliferation of effector T-cells. 1 Publication4
Mutagenesisi414 – 417RKKR → QNKS: Loss of proteolytic processing. 1 Publication4

<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 or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000918881 – 429Forkhead box protein P3Add BLAST429
ChainiPRO_00004324361 – 417Forkhead box protein P3, C-terminally processed1 PublicationAdd BLAST417
ChainiPRO_000043243752 – 417Forkhead box protein P3 41 kDa form1 PublicationAdd BLAST366
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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_0000432438418 – 4291 PublicationAdd BLAST12

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 CDK21 Publication1
Modified residuei31N6-acetyllysine1 Publication1
Modified residuei175Phosphothreonine; by CDK21 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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-linki249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei262N6-acetyllysine; alternate1 Publication1
Cross-linki262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Modified residuei267N6-acetyllysine; alternate1 Publication1
Cross-linki267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei418PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

Acetylation on lysine residues stabilizes FOXP3 and promotes differentiation of T-cells into induced regulatory T-cells (iTregs) associated with suppressive functions. Deacetylated by SIRT1.1 Publication
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 (By similarity). Phosphorylation by CDK2 negatively regulates its transcriptional activity and protein stability.By similarity1 Publication
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. Treg expressing the form cleaved at C-terminal site or both N- and C-terminal sites exhibit an increased induction of IL10 and an increased capacity to suppress proliferation of conventional T-cells in vitro. Treg expressing the form cleaved at only the C-terminal site are highly effective at preventing experimental colitis in an in vivo model of inflammatory bowel disease.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

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

More...
PaxDbi
Q99JB6

PRoteomics IDEntifications database

More...
PRIDEi
Q99JB6

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q99JB6

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

More...
PhosphoSitePlusi
Q99JB6

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

High level of expression in thymus and spleen.

<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

By TGFB1 in T-cells. Down-regulated in regulatory T-cells (Treg) during inflammation.2 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSMUSG00000039521, Expressed in thymus and 85 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q99JB6, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q99JB6, MM

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Homodimer. Dimerization is essential for its transcriptional regulator activity.

Interacts with IKZF3 (By similarity).

Interacts (via LXXLL motif) with isoform 4 of RORA (via AF-2 motif) (By similarity).

Interacts with STUB1 and HSPA1A/B.

Interacts with IKZF4, HDAC7 and KAT5.

Interacts with RUNX1, RUNX2, RUNX3 and NFATC2.

Interacts with RORC.

Interacts with HDAC9 in the absence of T-cell stimulation (By similarity).

Interacts with RELA, PPP1CA, PPP1CB, PPP1CG, HSPA8 and USP7 (By similarity).

By similarity5 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">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="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<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
203183, 368 interactors

Database of interacting proteins

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DIPi
DIP-59739N

Protein interaction database and analysis system

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IntActi
Q99JB6, 13 interactors

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000111405

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
Q99JB6, protein

<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

1429
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
Q99JB6

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<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>Regioni105 – 189Essential for transcriptional repressor activity and for interaction with KAT5 and HDAC7By similarityAdd BLAST85
Regioni148 – 198Interaction with IKZF41 PublicationAdd BLAST51
Regioni238 – 259Leucine-zipperAdd BLAST22
Regioni277 – 336Interaction with RUNX1By similarityAdd BLAST60

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>Motifi67 – 75Nuclear export signalBy similarity9
Motifi91 – 95LXXLL motifBy similarity5
Motifi238 – 247Nuclear export signalBy similarity10
Motifi414 – 417Nuclear localization signalBy similarity4

<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.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri196 – 221C2H2-typeAdd BLAST26

Keywords - Domaini

Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG4385, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000161807

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_019502_1_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q99JB6

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
Q99JB6

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

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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

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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

More...
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%5Flength">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

Q99JB6-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MPNPRPAKPM APSLALGPSP GVLPSWKTAP KGSELLGTRG SGGPFQGRDL
60 70 80 90 100
RSGAHTSSSL NPLPPSQLQL PTVPLVMVAP SGARLGPSPH LQALLQDRPH
110 120 130 140 150
FMHQLSTVDA HAQTPVLQVR PLDNPAMISL PPPSAATGVF SLKARPGLPP
160 170 180 190 200
GINVASLEWV SREPALLCTF PRSGTPRKDS NLLAAPQGSY PLLANGVCKW
210 220 230 240 250
PGCEKVFEEP EEFLKHCQAD HLLDEKGKAQ CLLQREVVQS LEQQLELEKE
260 270 280 290 300
KLGAMQAHLA GKMALAKAPS VASMDKSSCC IVATSTQGSV LPAWSAPREA
310 320 330 340 350
PDGGLFAVRR HLWGSHGNSS FPEFFHNMDY FKYHNMRPPF TYATLIRWAI
360 370 380 390 400
LEAPERQRTL NEIYHWFTRM FAYFRNHPAT WKNAIRHNLS LHKCFVRVES
410 420
EKGAVWTVDE FEFRKKRSQR PNKCSNPCP
Length:429
Mass (Da):47,346
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:i28D5B8E67891840C
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 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A3Q4L2R0A0A3Q4L2R0_MOUSE
Forkhead box protein P3
Foxp3
394Annotation 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>
A0A3Q4EC46A0A3Q4EC46_MOUSE
Forkhead box protein P3
Foxp3
402Annotation 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>
A0A3Q4EC35A0A3Q4EC35_MOUSE
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>
A0A3Q4EI60A0A3Q4EI60_MOUSE
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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AF277994 Genomic DNA Translation: AAG53608.1
AF277991 mRNA Translation: AAG53605.1
AF277992 mRNA Translation: AAG53606.1

The Consensus CDS (CCDS) project

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CCDSi
CCDS29965.1

NCBI Reference Sequences

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RefSeqi
NP_001186276.1, NM_001199347.1
NP_001186277.1, NM_001199348.1
NP_473380.1, NM_054039.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENSMUST00000045566; ENSMUSP00000041953; ENSMUSG00000039521
ENSMUST00000115738; ENSMUSP00000111403; ENSMUSG00000039521
ENSMUST00000115739; ENSMUSP00000111404; ENSMUSG00000039521
ENSMUST00000115740; ENSMUSP00000111405; ENSMUSG00000039521
ENSMUST00000234363; ENSMUSP00000157093; ENSMUSG00000039521
ENSMUST00000235116; ENSMUSP00000157059; ENSMUSG00000039521

Database of genes from NCBI RefSeq genomes

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GeneIDi
20371

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
mmu:20371

UCSC genome browser

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UCSCi
uc009sll.2, mouse

<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

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF277994 Genomic DNA Translation: AAG53608.1
AF277991 mRNA Translation: AAG53605.1
AF277992 mRNA Translation: AAG53606.1
CCDSiCCDS29965.1
RefSeqiNP_001186276.1, NM_001199347.1
NP_001186277.1, NM_001199348.1
NP_473380.1, NM_054039.2

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4I1LX-ray2.10A189-276[»]
SMRiQ99JB6
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi203183, 368 interactors
DIPiDIP-59739N
IntActiQ99JB6, 13 interactors
STRINGi10090.ENSMUSP00000111405

PTM databases

iPTMnetiQ99JB6
PhosphoSitePlusiQ99JB6

Proteomic databases

PaxDbiQ99JB6
PRIDEiQ99JB6

Protocols and materials databases

Antibodypedia a portal for validated antibodies

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Antibodypediai
485, 1867 antibodies

Genome annotation databases

EnsembliENSMUST00000045566; ENSMUSP00000041953; ENSMUSG00000039521
ENSMUST00000115738; ENSMUSP00000111403; ENSMUSG00000039521
ENSMUST00000115739; ENSMUSP00000111404; ENSMUSG00000039521
ENSMUST00000115740; ENSMUSP00000111405; ENSMUSG00000039521
ENSMUST00000234363; ENSMUSP00000157093; ENSMUSG00000039521
ENSMUST00000235116; ENSMUSP00000157059; ENSMUSG00000039521
GeneIDi20371
KEGGimmu:20371
UCSCiuc009sll.2, mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
50943
MGIiMGI:1891436, Foxp3

Phylogenomic databases

eggNOGiKOG4385, Eukaryota
GeneTreeiENSGT00940000161807
HOGENOMiCLU_019502_1_0_1
InParanoidiQ99JB6
KOiK10163
OMAiFAYFRNH
OrthoDBi836427at2759
PhylomeDBiQ99JB6
TreeFamiTF326978

Enzyme and pathway databases

ReactomeiR-MMU-8877330, RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs)

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
20371, 1 hit in 22 CRISPR screens

Protein Ontology

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PROi
PR:Q99JB6
RNActiQ99JB6, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000039521, Expressed in thymus and 85 other tissues
ExpressionAtlasiQ99JB6, baseline and differential
GenevisibleiQ99JB6, MM

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

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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_MOUSE
<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: Q99JB6
<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%5Fand%5Fisoforms">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 7, 2020
This is version 170 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

<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, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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