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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-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 (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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei51 – 522Cleavage1 Publication
Sitei417 – 4182Cleavage; by PCSK1 or PCSK21 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri196 – 22126C2H2-typeAdd
BLAST
DNA bindingi337 – 42387Fork-headPROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  1. core promoter binding Source: UniProtKB
  2. histone acetyltransferase binding Source: MGI
  3. histone deacetylase binding Source: MGI
  4. metal ion binding Source: UniProtKB-KW
  5. NFAT protein binding Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: MGI
  8. sequence-specific DNA binding Source: UniProtKB
  9. sequence-specific DNA binding transcription factor activity Source: UniProtKB
  10. transcription corepressor activity Source: MGI

GO - Biological processi

  1. B cell homeostasis Source: MGI
  2. CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: MGI
  3. CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment Source: UniProtKB
  4. cytokine production Source: MGI
  5. myeloid cell homeostasis Source: MGI
  6. negative regulation of cell proliferation Source: UniProtKB
  7. negative regulation of chronic inflammatory response Source: MGI
  8. negative regulation of CREB transcription factor activity Source: UniProtKB
  9. negative regulation of cytokine biosynthetic process Source: UniProtKB
  10. negative regulation of cytokine secretion Source: UniProtKB
  11. negative regulation of histone acetylation Source: MGI
  12. negative regulation of histone deacetylation Source: MGI
  13. negative regulation of immune response Source: UniProtKB
  14. negative regulation of inflammatory response Source: MGI
  15. negative regulation of interferon-gamma biosynthetic process Source: MGI
  16. negative regulation of interferon-gamma production Source: UniProtKB
  17. negative regulation of interleukin-10 production Source: UniProtKB
  18. negative regulation of interleukin-17 production Source: UniProtKB
  19. negative regulation of interleukin-2 biosynthetic process Source: UniProtKB
  20. negative regulation of interleukin-2 production Source: UniProtKB
  21. negative regulation of interleukin-4 production Source: UniProtKB
  22. negative regulation of interleukin-5 production Source: MGI
  23. negative regulation of interleukin-6 production Source: MGI
  24. negative regulation of isotype switching to IgE isotypes Source: MGI
  25. negative regulation of lymphocyte proliferation Source: MGI
  26. negative regulation of NF-kappaB transcription factor activity Source: UniProtKB
  27. negative regulation of sequence-specific DNA binding transcription factor activity Source: UniProtKB
  28. negative regulation of T cell cytokine production Source: UniProtKB
  29. negative regulation of T cell proliferation Source: UniProtKB
  30. negative regulation of T-helper 17 cell differentiation Source: UniProtKB
  31. negative regulation of transcription, DNA-templated Source: UniProtKB
  32. negative regulation of transcription from RNA polymerase II promoter Source: MGI
  33. negative regulation of tumor necrosis factor production Source: MGI
  34. positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation Source: UniProtKB
  35. positive regulation of gene expression Source: MGI
  36. positive regulation of histone acetylation Source: MGI
  37. positive regulation of immature T cell proliferation in thymus Source: MGI
  38. positive regulation of interleukin-4 production Source: MGI
  39. positive regulation of peripheral T cell tolerance induction Source: MGI
  40. positive regulation of regulatory T cell differentiation Source: MGI
  41. positive regulation of T cell anergy Source: MGI
  42. positive regulation of T cell tolerance induction Source: MGI
  43. positive regulation of transcription, DNA-templated Source: UniProtKB
  44. positive regulation of transcription from RNA polymerase II promoter Source: MGI
  45. positive regulation of transforming growth factor beta1 production Source: MGI
  46. regulation of immunoglobulin production Source: MGI
  47. regulation of isotype switching to IgG isotypes Source: MGI
  48. regulation of T cell anergy Source: UniProtKB
  49. regulation of transcription from RNA polymerase II promoter Source: MGI
  50. regulatory T cell differentiation Source: MGI
  51. response to virus Source: Ensembl
  52. T cell activation Source: UniProtKB
  53. T cell mediated immunity Source: MGI
  54. T cell receptor signaling pathway Source: MGI
  55. tolerance induction Source: MGI
  56. tolerance induction to self antigen Source: MGI
  57. transcription from RNA polymerase II promoter Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Activator, Repressor

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein P3
Alternative name(s):
Scurfin
Cleaved into the following 2 chains:
Gene namesi
Name:Foxp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome X

Organism-specific databases

MGIiMGI:1891436. Foxp3.

Subcellular locationi

Nucleus PROSITE-ProRule annotation2 Publications. Cytoplasm By similarity
Note: Predominantly expressed in the cytoplasm in activated conventional T-cells whereas predominantly expressed in the nucleus in regulatory T-cells (Treg) (By similarity). The 41 kDa form derived by proteolytic processing is found exclusively in the chromatin fraction of activated Treg cells.By similarity1 Publication

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. intracellular Source: MGI
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi19 – 191S → 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 Publication
Mutagenesisi48 – 514RDLR → HDLH: Loss of proteolytic processing. 1 Publication
Mutagenesisi88 – 881S → 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 Publication
Mutagenesisi114 – 1141T → 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 Publication
Mutagenesisi175 – 1751T → 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 Publication
Mutagenesisi250 – 2501Missing : 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 Publication
Mutagenesisi329 – 3302DY → 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 Publication
Mutagenesisi332 – 3321K → 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 Publication
Mutagenesisi414 – 4174RKKR → PNNW: Loss of ability to suppress the proliferation of effector T-cells. 1 Publication
Mutagenesisi414 – 4174RKKR → QNKS: Loss of proteolytic processing. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 429429Forkhead box protein P3PRO_0000091888Add
BLAST
Chaini1 – 417417Forkhead box protein P3, C-terminally processed1 PublicationPRO_0000432436Add
BLAST
Chaini52 – 417366Forkhead box protein P3 41 kDa form1 PublicationPRO_0000432437Add
BLAST
Propeptidei418 – 429121 PublicationPRO_0000432438Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei19 – 191Phosphoserine; by CDK21 Publication
Modified residuei31 – 311N6-acetyllysine1 Publication
Modified residuei175 – 1751Phosphothreonine; by CDK21 Publication
Cross-linki249 – 249Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki251 – 251Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei262 – 2621N6-acetyllysine1 Publication
Cross-linki262 – 262Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei267 – 2671N6-acetyllysine1 Publication
Cross-linki267 – 267Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki393 – 393Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei418 – 4181PhosphoserineBy similarity

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

Keywords - PTMi

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ99JB6.

PTM databases

PhosphoSiteiQ99JB6.

Expressioni

Tissue specificityi

High level of expression in thymus and spleen.

Inductioni

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

Gene expression databases

BgeeiQ99JB6.
CleanExiMM_FOXP3.
ExpressionAtlasiQ99JB6. baseline and differential.
GenevestigatoriQ99JB6.

Interactioni

Subunit structurei

Homodimer. 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

Protein-protein interaction databases

BioGridi203183. 369 interactions.
DIPiDIP-59739N.

Structurei

Secondary structure

1
429
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni204 – 2074Combined sources
Helixi208 – 25750Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I1LX-ray2.10A189-276[»]
ProteinModelPortaliQ99JB6.
SMRiQ99JB6. Positions 201-262, 336-417.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni105 – 18985Essential for transcriptional repressor activity and for interaction with KAT5 and HDAC7By similarityAdd
BLAST
Regioni148 – 19851Interaction with IKZF41 PublicationAdd
BLAST
Regioni238 – 25922Leucine-zipperAdd
BLAST
Regioni277 – 33660Interaction with RUNX1By similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi67 – 759Nuclear export signalBy similarity
Motifi91 – 955LXXLL motifBy similarity
Motifi238 – 24710Nuclear export signalBy similarity
Motifi414 – 4174Nuclear localization signalBy similarity

Sequence similaritiesi

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

Zinc finger

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri196 – 22126C2H2-typeAdd
BLAST

Keywords - Domaini

Zinc-finger

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000082490.
HOVERGENiHBG051656.
InParanoidiQ99JB6.
KOiK10163.
OMAiKHCQADH.
OrthoDBiEOG7M6D7G.
PhylomeDBiQ99JB6.
TreeFamiTF326978.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.160.60. 1 hit.
InterProiIPR001766. TF_fork_head.
IPR011991. WHTH_DNA-bd_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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:May 31, 2001 - v1
Checksum:i28D5B8E67891840C
GO

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.
UniGeneiMm.182291.
Mm.288192.

Genome annotation databases

EnsembliENSMUST00000045566; ENSMUSP00000041953; ENSMUSG00000039521.
ENSMUST00000115738; ENSMUSP00000111403; ENSMUSG00000039521.
ENSMUST00000115739; ENSMUSP00000111404; ENSMUSG00000039521.
ENSMUST00000115740; ENSMUSP00000111405; ENSMUSG00000039521.
GeneIDi20371.
KEGGimmu:20371.
UCSCiuc009sll.2. mouse.

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.
UniGeneiMm.182291.
Mm.288192.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4I1LX-ray2.10A189-276[»]
ProteinModelPortaliQ99JB6.
SMRiQ99JB6. Positions 201-262, 336-417.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi203183. 369 interactions.
DIPiDIP-59739N.

PTM databases

PhosphoSiteiQ99JB6.

Proteomic databases

PRIDEiQ99JB6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000045566; ENSMUSP00000041953; ENSMUSG00000039521.
ENSMUST00000115738; ENSMUSP00000111403; ENSMUSG00000039521.
ENSMUST00000115739; ENSMUSP00000111404; ENSMUSG00000039521.
ENSMUST00000115740; ENSMUSP00000111405; ENSMUSG00000039521.
GeneIDi20371.
KEGGimmu:20371.
UCSCiuc009sll.2. mouse.

Organism-specific databases

CTDi50943.
MGIiMGI:1891436. Foxp3.

Phylogenomic databases

eggNOGiCOG5025.
GeneTreeiENSGT00780000121840.
HOGENOMiHOG000082490.
HOVERGENiHBG051656.
InParanoidiQ99JB6.
KOiK10163.
OMAiKHCQADH.
OrthoDBiEOG7M6D7G.
PhylomeDBiQ99JB6.
TreeFamiTF326978.

Miscellaneous databases

NextBioi298278.
PROiQ99JB6.
SOURCEiSearch...

Gene expression databases

BgeeiQ99JB6.
CleanExiMM_FOXP3.
ExpressionAtlasiQ99JB6. baseline and differential.
GenevestigatoriQ99JB6.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
3.30.160.60. 1 hit.
InterProiIPR001766. TF_fork_head.
IPR011991. WHTH_DNA-bd_dom.
IPR007087. Znf_C2H2.
IPR015880. Znf_C2H2-like.
IPR013087. Znf_C2H2/integrase_DNA-bd.
[Graphical view]
PfamiPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSiPR00053. FORKHEAD.
SMARTiSM00339. FH. 1 hit.
SM00355. ZnF_C2H2. 1 hit.
[Graphical view]
PROSITEiPS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Disruption of a new forkhead/winged-helix protein, scurfin, results in the fatal lymphoproliferative disorder of the scurfy mouse."
    Brunkow M.E., Jeffery E.W., Hjerrild K.A., Paeper B., Clark L.B., Yasayko S.-A., Wilkinson J.E., Galas D., Ziegler S.F., Ramsdell F.
    Nat. Genet. 27:68-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
  2. "Foxp3 interacts with nuclear factor of activated T cells and NF-kappa B to repress cytokine gene expression and effector functions of T helper cells."
    Bettelli E., Dastrange M., Oukka M.
    Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "The mutant leucine-zipper domain impairs both dimerization and suppressive function of Foxp3 in T cells."
    Chae W.J., Henegariu O., Lee S.K., Bothwell A.L.
    Proc. Natl. Acad. Sci. U.S.A. 103:9631-9636(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: HOMODIMERIZATION, MUTAGENESIS OF GLU-250.
  4. "Foxp3 controls regulatory T-cell function by interacting with AML1/Runx1."
    Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T., Miyachi Y., Tsukada T., Sakaguchi S.
    Nature 446:685-689(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RUNX1; RUNX2; RUNX3 AND NFATC2, SUBCELLULAR LOCATION, MUTAGENESIS OF 329-ASP-TYR-330 AND LYS-332.
  5. "TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by antagonizing RORgammat function."
    Zhou L., Lopes J.E., Chong M.M., Ivanov I.I., Min R., Victora G.D., Shen Y., Du J., Rubtsov Y.P., Rudensky A.Y., Ziegler S.F., Littman D.R.
    Nature 453:236-240(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH RORC, INDUCTION.
  6. "Foxp3 processing by proprotein convertases and control of regulatory T cell function."
    de Zoeten E.F., Lee I., Wang L., Chen C., Ge G., Wells A.D., Hancock W.W., Ozkaynak E.
    J. Biol. Chem. 284:5709-5716(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEOLYTIC PROCESSING, SUBCELLULAR LOCATION, MUTAGENESIS OF 48-ARG--ARG-51 AND 414-ARG--ARG-417.
  7. Cited for: FUNCTION, INTERACTION WITH IKZF4; HDAC7 AND KAT5.
  8. "Three novel acetylation sites in the Foxp3 transcription factor regulate the suppressive activity of regulatory T cells."
    Kwon H.S., Lim H.W., Wu J., Schnolzer M., Verdin E., Ott M.
    J. Immunol. 188:2712-2721(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-31; LYS-262 AND LYS-267, DEACETYLATION BY SIRT1.
  9. "Stabilization of the transcription factor Foxp3 by the deubiquitinase USP7 increases Treg-cell-suppressive capacity."
    van Loosdregt J., Fleskens V., Fu J., Brenkman A.B., Bekker C.P., Pals C.E., Meerding J., Berkers C.R., Barbi J., Grone A., Sijts A.J., Maurice M.M., Kalkhoven E., Prakken B.J., Ovaa H., Pan F., Zaiss D.M., Coffer P.J.
    Immunity 39:259-271(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-249; LYS-251; LYS-262; LYS-267 AND LYS-393, DEUBIQUITINATION.
  10. "The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3."
    Chen Z., Barbi J., Bu S., Yang H.Y., Li Z., Gao Y., Jinasena D., Fu J., Lin F., Chen C., Zhang J., Yu N., Li X., Shan Z., Nie J., Gao Z., Tian H., Li Y.
    , Yao Z., Zheng Y., Park B.V., Pan Z., Zhang J., Dang E., Li Z., Wang H., Luo W., Li L., Semenza G.L., Zheng S.G., Loser K., Tsun A., Greene M.I., Pardoll D.M., Pan F., Li B.
    Immunity 39:272-285(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION, INTERACTION WITH STUB1 AND HSPA1A/B, INDUCTION.
  11. "Foxp3 protein stability is regulated by cyclin-dependent kinase 2."
    Morawski P.A., Mehra P., Chen C., Bhatti T., Wells A.D.
    J. Biol. Chem. 288:24494-24502(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-19 AND THR-175, MUTAGENESIS OF SER-19; SER-88; THR-114 AND THR-175.
  12. Cited for: REVIEW.

Entry informationi

Entry nameiFOXP3_MOUSE
AccessioniPrimary (citable) accession number: Q99JB6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 19, 2001
Last sequence update: May 31, 2001
Last modified: March 31, 2015
This is version 124 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, 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
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.