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Forkhead box protein P3 (Scurfin) [Cleaved into: Forkhead box protein P3, C-terminally processed; Forkhead box protein P3 41 kDa form]

 FOXP3_HUMAN             Reviewed;         431 AA.
Q9BZS1; A5HJT1; B7ZLG0; B9UN80; O60827; Q14DD8; Q4ZH51;
20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
12-SEP-2018, entry version 185.
RecName: Full=Forkhead box protein P3;
AltName: Full=Scurfin;
Contains:
RecName: Full=Forkhead box protein P3, C-terminally processed;
Contains:
RecName: Full=Forkhead box protein P3 41 kDa form;
Name=FOXP3; Synonyms=IPEX; ORFNames=JM2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=11138001; DOI=10.1038/83784;
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.;
"Disruption of a new forkhead/winged-helix protein, scurfin, results
in the fatal lymphoproliferative disorder of the scurfy mouse.";
Nat. Genet. 27:68-73(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Wang J., Liu Q., Zhang Y., Xu Z., Huang C.;
"Cloning and expression of the cDNA for FOXP3.";
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Kaur G., Goodall J.C., Jarvis L.B., Gaston J.S.H.;
"Functional characterization of FOXP3 splice variants in human
regulatory T cells.";
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Lin L., Nong W., Li H., Ke R., Shen C., Zhong G., Zheng Z., Liang M.,
Huang B., Zhou G., Yang S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15772651; DOI=10.1038/nature03440;
Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A.,
Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G.,
Jones M.C., Hurles M.E., Andrews T.D., Scott C.E., Searle S.,
Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R.,
Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L.,
Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A.,
Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S.,
Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R.,
Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M.,
Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N.,
Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D.,
Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W.,
Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C.,
Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C.,
Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
Corby N., Connor R.E., David R., Davies J., Davis C., Davis J.,
Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S.,
Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I.,
Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L.,
Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P.,
Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S.,
Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A.,
Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J.,
Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J.,
Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S.,
de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z.,
Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C.,
Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W.,
Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T.,
Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I.,
Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N.,
Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J.,
Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E.,
Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S.,
Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T.,
Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S.,
Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L.,
Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A.,
Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L.,
Williams G., Williams L., Williamson A., Williamson H., Wilming L.,
Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H.,
Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A.,
Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A.,
Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T.,
Gibbs R.A., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 16-431 (ISOFORM 3).
Strom T.M., Nyakatura G., Hellebrand H., Drescher B., Rosenthal A.,
Meindl A.;
"Transcription map in Xp11.23.";
Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION, AND INTERACTION WITH RELA AND NFATC2.
PubMed=15790681; DOI=10.1073/pnas.0501675102;
Bettelli E., Dastrange M., Oukka M.;
"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.";
Proc. Natl. Acad. Sci. U.S.A. 102:5138-5143(2005).
[9]
FUNCTION, AND INTERACTION WITH RUNX1.
PubMed=17377532; DOI=10.1038/nature05673;
Ono M., Yaguchi H., Ohkura N., Kitabayashi I., Nagamura Y., Nomura T.,
Miyachi Y., Tsukada T., Sakaguchi S.;
"Foxp3 controls regulatory T-cell function by interacting with
AML1/Runx1.";
Nature 446:685-689(2007).
[10]
FUNCTION, ACETYLATION, INTERACTION WITH KAT5; HDAC7 AND HDAC9, AND
SUBCELLULAR LOCATION.
PubMed=17360565; DOI=10.1073/pnas.0700298104;
Li B., Samanta A., Song X., Iacono K.T., Bembas K., Tao R., Basu S.,
Riley J.L., Hancock W.W., Shen Y., Saouaf S.J., Greene M.I.;
"FOXP3 interactions with histone acetyltransferase and class II
histone deacetylases are required for repression.";
Proc. Natl. Acad. Sci. U.S.A. 104:4571-4576(2007).
[11]
FUNCTION, INTERACTION WITH RORA, SUBCELLULAR LOCATION, AND MUTAGENESIS
OF 95-LEU-LEU-96.
PubMed=18354202; DOI=10.4049/jimmunol.180.7.4785;
Du J., Huang C., Zhou B., Ziegler S.F.;
"Isoform-specific inhibition of ROR alpha-mediated transcriptional
activation by human FOXP3.";
J. Immunol. 180:4785-4792(2008).
[12]
FUNCTION, AND INTERACTION WITH RORC.
PubMed=18368049; DOI=10.1038/nature06878;
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.;
"TGF-beta-induced Foxp3 inhibits T(H)17 cell differentiation by
antagonizing RORgammat function.";
Nature 453:236-240(2008).
[13]
PROTEOLYTIC PROCESSING.
PubMed=19117830; DOI=10.1074/jbc.M807322200;
de Zoeten E.F., Lee I., Wang L., Chen C., Ge G., Wells A.D.,
Hancock W.W., Ozkaynak E.;
"Foxp3 processing by proprotein convertases and control of regulatory
T cell function.";
J. Biol. Chem. 284:5709-5716(2009).
[14]
INTERACTION WITH IKZF3.
PubMed=20676092; DOI=10.1038/ni.1915;
Gandhi R., Kumar D., Burns E.J., Nadeau M., Dake B., Laroni A.,
Kozoriz D., Weiner H.L., Quintana F.J.;
"Activation of the aryl hydrocarbon receptor induces human type 1
regulatory T cell-like and Foxp3(+) regulatory T cells.";
Nat. Immunol. 11:846-853(2010).
[15]
SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL, NUCLEAR EXPORT
SIGNAL, AND MUTAGENESIS OF LEU-69; LEU-71; LEU-74; LEU-76;
415-LYS-LYS-416; LEU-242; LEU-246 AND LEU-248.
PubMed=22678915; DOI=10.1002/eji.201141838;
Magg T., Mannert J., Ellwart J.W., Schmid I., Albert M.H.;
"Subcellular localization of FOXP3 in human regulatory and
nonregulatory T cells.";
Eur. J. Immunol. 42:1627-1638(2012).
[16]
ACETYLATION AT LYS-31; LYS-263 AND LYS-268, AND DEACETYLATION BY
SIRT1.
PubMed=22312127; DOI=10.4049/jimmunol.1100903;
Kwon H.S., Lim H.W., Wu J., Schnolzer M., Verdin E., Ott M.;
"Three novel acetylation sites in the Foxp3 transcription factor
regulate the suppressive activity of regulatory T cells.";
J. Immunol. 188:2712-2721(2012).
[17]
FUNCTION.
PubMed=23169781; DOI=10.1182/blood-2012-05-431023;
McMurchy A.N., Gillies J., Gizzi M.C., Riba M., Garcia-Manteiga J.M.,
Cittaro D., Lazarevic D., Di Nunzio S., Piras I.S., Bulfone A.,
Roncarolo M.G., Stupka E., Bacchetta R., Levings M.K.;
"A novel function for FOXP3 in humans: intrinsic regulation of
conventional T cells.";
Blood 121:1265-1275(2013).
[18]
REVIEW.
PubMed=24350059; DOI=10.3389/fonc.2013.00294;
Lozano T., Casares N., Lasarte J.J.;
"Searching for the Achilles Heel of FOXP3.";
Front. Oncol. 3:294-294(2013).
[19]
UBIQUITINATION, DEUBIQUITINATION, SUBCELLULAR LOCATION, AND
INTERACTION WITH USP7.
PubMed=23973222; DOI=10.1016/j.immuni.2013.05.018;
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.;
"Stabilization of the transcription factor Foxp3 by the deubiquitinase
USP7 increases Treg-cell-suppressive capacity.";
Immunity 39:259-271(2013).
[20]
INTERACTION WITH STUB1; HSPA8 AND HSPA1A/B, SUBCELLULAR LOCATION,
UBIQUITINATION, AND INDUCTION.
PubMed=23973223; DOI=10.1016/j.immuni.2013.08.006;
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.;
"The ubiquitin ligase Stub1 negatively modulates regulatory T cell
suppressive activity by promoting degradation of the transcription
factor Foxp3.";
Immunity 39:272-285(2013).
[21]
INTERACTION WITH ZFP90.
PubMed=23543754; DOI=10.4049/jimmunol.1203561;
Huang C., Martin S., Pfleger C., Du J., Buckner J.H., Bluestone J.A.,
Riley J.L., Ziegler S.F.;
"Cutting Edge: a novel, human-specific interacting protein couples
FOXP3 to a chromatin-remodeling complex that contains KAP1/TRIM28.";
J. Immunol. 190:4470-4473(2013).
[22]
PHOSPHORYLATION AT SER-418, SUBCELLULAR LOCATION, INTERACTION WITH
PPP1CA; PPP1CB AND PPP1CG, MUTAGENESIS OF SER-418 AND SER-422, AND
DEPHOSPHORYLATION.
PubMed=23396208; DOI=10.1038/nm.3085;
Nie H., Zheng Y., Li R., Guo T.B., He D., Fang L., Liu X., Xiao L.,
Chen X., Wan B., Chin Y.E., Zhang J.Z.;
"Phosphorylation of FOXP3 controls regulatory T cell function and is
inhibited by TNF-alpha in rheumatoid arthritis.";
Nat. Med. 19:322-328(2013).
[23]
REVIEW ON FUNCTION.
PubMed=23947341; DOI=10.3109/08830185.2013.811657;
Vent-Schmidt J., Han J.M., MacDonald K.G., Levings M.K.;
"The role of FOXP3 in regulating immune responses.";
Int. Rev. Immunol. 33:110-128(2014).
[24]
REVIEW ON FUNCTION.
PubMed=24354325; DOI=10.3109/08830185.2013.863303;
Passerini L., Santoni de Sio F.R., Roncarolo M.G., Bacchetta R.;
"Forkhead box P3: the peacekeeper of the immune system.";
Int. Rev. Immunol. 33:129-145(2014).
[25]
REVIEW.
PubMed=24722479; DOI=10.1038/nri3650;
Ramsdell F., Ziegler S.F.;
"FOXP3 and scurfy: how it all began.";
Nat. Rev. Immunol. 14:343-349(2014).
[26]
REVIEW ON PTM.
PubMed=25047417; DOI=10.1016/j.it.2014.06.005;
van Loosdregt J., Coffer P.J.;
"Post-translational modification networks regulating FOXP3 function.";
Trends Immunol. 35:368-378(2014).
[27] {ECO:0000244|PDB:3QRF}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 336-417 IN COMPLEX WITH DNA
AND NFATC2, FUNCTION, SUBUNIT, DOMAIN FORK-HEAD, INTERACTION WITH
NFATC2, CHARACTERIZATION OF VARIANTS IPEX GLU-251 DEL; HIS-347;
CYS-371 AND ALA-373, AND MUTAGENESIS OF TRP-348; MET-370 AND ALA-372.
PubMed=21458306; DOI=10.1016/j.immuni.2011.02.017;
Bandukwala H.S., Wu Y., Feuerer M., Chen Y., Barboza B., Ghosh S.,
Stroud J.C., Benoist C., Mathis D., Rao A., Chen L.;
"Structure of a domain-swapped FOXP3 dimer on DNA and its function in
regulatory T cells.";
Immunity 34:479-491(2011).
[28] {ECO:0000244|PDB:4WK8}
X-RAY CRYSTALLOGRAPHY (3.40 ANGSTROMS) OF 336-417 IN COMPLEX WITH DNA,
FUNCTION, AND SUBUNIT.
PubMed=25567984; DOI=10.1093/nar/gku1373;
Chen Y., Chen C., Zhang Z., Liu C.C., Johnson M.E., Espinoza C.A.,
Edsall L.E., Ren B., Zhou X.J., Grant S.F., Wells A.D., Chen L.;
"DNA binding by FOXP3 domain-swapped dimer suggests mechanisms of
long-range chromosomal interactions.";
Nucleic Acids Res. 43:1268-1282(2015).
[29]
VARIANT IPEX GLU-251 DEL.
PubMed=11120765; DOI=10.1172/JCI11679;
Chatila T.A., Blaeser F., Ho N., Lederman H.M., Voulgaropoulos C.,
Helms C., Bowcock A.M.;
"JM2, encoding a fork head-related protein, is mutated in X-linked
autoimmunity-allergic disregulation syndrome.";
J. Clin. Invest. 106:R75-R81(2000).
[30]
VARIANT IPEX VAL-363.
PubMed=11768393; DOI=10.1136/jmg.38.12.874;
Kobayashi I., Shiari R., Yamada M., Kawamura N., Okano M., Yara A.,
Iguchi A., Ishikawa N., Ariga T., Sakiyama Y., Ochs H.D.,
Kobayashi K.;
"Novel mutations of FOXP3 in two Japanese patients with immune
dysregulation, polyendocrinopathy, enteropathy, X linked syndrome
(IPEX).";
J. Med. Genet. 38:874-876(2001).
[31]
VARIANTS IPEX CYS-371; THR-384 AND TRP-397.
PubMed=11137992; DOI=10.1038/83707;
Wildin R.S., Ramsdell F., Peake J., Faravelli F., Casanova J.-L.,
Buist N., Levy-Lahad E., Mazzella M., Goulet O., Perroni L.,
Bricarelli F.D., Byrne G., McEuen M., Proll S., Appleby M.,
Brunkow M.E.;
"X-linked neonatal diabetes mellitus, enteropathy and endocrinopathy
syndrome is the human equivalent of mouse scurfy.";
Nat. Genet. 27:18-20(2001).
[32]
VARIANT IPEX THR-384.
PubMed=11137993; DOI=10.1038/83713;
Bennett C.L., Christie J., Ramsdell F., Brunkow M.E., Ferguson P.J.,
Whitesell L., Kelly T.E., Saulsbury F.T., Chance P.F., Ochs H.D.;
"The immune dysregulation, polyendocrinopathy, enteropathy, X-linked
syndrome (IPEX) is caused by mutations of FOXP3.";
Nat. Genet. 27:20-21(2001).
[33]
VARIANTS IPEX PRO-242; LEU-324; ALA-339; HIS-347; ALA-373; CYS-374 AND
THR-384, AND CHARACTERIZATION OF VARIANTS IPEX PRO-242; LEU-324;
ALA-339; HIS-347; ALA-373; CYS-374 AND THR-384.
PubMed=18951619; DOI=10.1016/j.jaci.2008.09.027;
Gambineri E., Perroni L., Passerini L., Bianchi L., Doglioni C.,
Meschi F., Bonfanti R., Sznajer Y., Tommasini A., Lawitschka A.,
Junker A., Dunstheimer D., Heidemann P.H., Cazzola G., Cipolli M.,
Friedrich W., Janic D., Azzi N., Richmond E., Vignola S., Barabino A.,
Chiumello G., Azzari C., Roncarolo M.G., Bacchetta R.;
"Clinical and molecular profile of a new series of patients with
immune dysregulation, polyendocrinopathy, enteropathy, X-linked
syndrome: inconsistent correlation between forkhead box protein 3
expression and disease severity.";
J. Allergy Clin. Immunol. 122:1105-1112(2008).
-!- FUNCTION: 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).
{ECO:0000250|UniProtKB:Q99JB6, ECO:0000269|PubMed:15790681,
ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17377532,
ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18368049,
ECO:0000269|PubMed:21458306, ECO:0000269|PubMed:23169781}.
-!- SUBUNIT: 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).
{ECO:0000250|UniProtKB:Q99JB6, ECO:0000269|PubMed:15790681,
ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:17377532,
ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:18368049,
ECO:0000269|PubMed:20676092, ECO:0000269|PubMed:21458306,
ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23543754,
ECO:0000269|PubMed:23973222, ECO:0000269|PubMed:23973223,
ECO:0000269|PubMed:25567984}.
-!- INTERACTION:
Q8WUI4:HDAC7; NbExp=2; IntAct=EBI-16338471, EBI-1048378;
P0DMV8:HSPA1A; NbExp=4; IntAct=EBI-983719, EBI-11820565;
Q9UKT9:IKZF3; NbExp=2; IntAct=EBI-983719, EBI-747204;
Q92993:KAT5; NbExp=2; IntAct=EBI-9695448, EBI-399080;
P11309-2:PIM1; NbExp=3; IntAct=EBI-9695448, EBI-1018633;
P62136:PPP1CA; NbExp=2; IntAct=EBI-983719, EBI-357253;
P86479:PRR20C; NbExp=4; IntAct=EBI-983719, EBI-10172814;
P86478:PRR20E; NbExp=3; IntAct=EBI-983719, EBI-12700196;
Q93062:RBPMS; NbExp=4; IntAct=EBI-983719, EBI-740322;
Q93062-3:RBPMS; NbExp=3; IntAct=EBI-983719, EBI-740343;
P35398-4:RORA; NbExp=5; IntAct=EBI-983719, EBI-11295807;
Q9UNE7:STUB1; NbExp=7; IntAct=EBI-983719, EBI-357085;
Q8TF47-3:ZFP90; NbExp=4; IntAct=EBI-983719, EBI-11419904;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00089, ECO:0000269|PubMed:17360565,
ECO:0000269|PubMed:18354202, ECO:0000269|PubMed:22678915,
ECO:0000269|PubMed:23396208, ECO:0000269|PubMed:23973222,
ECO:0000269|PubMed:23973223}. Cytoplasm
{ECO:0000269|PubMed:22678915}. Note=Predominantly expressed in the
cytoplasm in activated conventional T-cells whereas predominantly
expressed in the nucleus in regulatory T-cells (Treg). The 41 kDa
form derived by proteolytic processing is found exclusively in the
chromatin fraction of activated Treg cells (By similarity).
{ECO:0000250|UniProtKB:Q99JB6, ECO:0000269|PubMed:22678915}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9BZS1-1; Sequence=Displayed;
Name=2;
IsoId=Q9BZS1-2; Sequence=VSP_015796;
Name=3;
IsoId=Q9BZS1-3; Sequence=VSP_015796, VSP_036418;
Note=No experimental confirmation available.;
Name=4;
IsoId=Q9BZS1-4; Sequence=VSP_047859;
-!- INDUCTION: Down-regulated in regulatory T-cells (Treg) during
inflammation. {ECO:0000269|PubMed:23973223}.
-!- DOMAIN: The fork-head DNA-binding domain is essential for its
dimerization and interaction with NFATC2.
{ECO:0000269|PubMed:21458306}.
-!- PTM: 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. {ECO:0000269|PubMed:23973222,
ECO:0000269|PubMed:23973223}.
-!- PTM: 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). {ECO:0000250|UniProtKB:Q99JB6,
ECO:0000269|PubMed:23396208}.
-!- PTM: 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. {ECO:0000269|PubMed:17360565, ECO:0000269|PubMed:22312127}.
-!- PTM: 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. {ECO:0000269|PubMed:19117830}.
-!- DISEASE: Immunodeficiency polyendocrinopathy, enteropathy, X-
linked syndrome (IPEX) [MIM:304790]: Characterized by neonatal
onset insulin-dependent diabetes mellitus, infections, secretory
diarrhea, thrombocytopenia, anemia and eczema. It is usually
lethal in infancy. {ECO:0000269|PubMed:11120765,
ECO:0000269|PubMed:11137992, ECO:0000269|PubMed:11137993,
ECO:0000269|PubMed:11768393, ECO:0000269|PubMed:18951619,
ECO:0000269|PubMed:21458306}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FOXP3ID44129chXp11.html";
-!- WEB RESOURCE: Name=FOXP3base; Note=FOXP3 mutation db;
URL="http://structure.bmc.lu.se/idbase/FOXP3base/";
-!- WEB RESOURCE: Name=Wikipedia; Note=FOXP3 entry;
URL="https://en.wikipedia.org/wiki/FOXP3";
-----------------------------------------------------------------------
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EMBL; AF277993; AAG53607.1; -; mRNA.
EMBL; EF534714; ABQ15210.1; -; mRNA.
EMBL; EU855812; ACJ46653.1; -; mRNA.
EMBL; DQ010327; AAY27088.1; -; mRNA.
EMBL; AF235097; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC113401; AAI13402.1; -; mRNA.
EMBL; BC113403; AAI13404.1; -; mRNA.
EMBL; BC143785; AAI43786.1; -; mRNA.
EMBL; AJ005891; CAA06748.1; -; mRNA.
CCDS; CCDS14323.1; -. [Q9BZS1-1]
CCDS; CCDS48109.1; -. [Q9BZS1-2]
RefSeq; NP_001107849.1; NM_001114377.1. [Q9BZS1-2]
RefSeq; NP_054728.2; NM_014009.3. [Q9BZS1-1]
UniGene; Hs.247700; -.
PDB; 3QRF; X-ray; 2.80 A; F/G/H/I=336-417.
PDB; 4WK8; X-ray; 3.40 A; F/G=336-417.
PDBsum; 3QRF; -.
PDBsum; 4WK8; -.
ProteinModelPortal; Q9BZS1; -.
SMR; Q9BZS1; -.
BioGrid; 119170; 70.
DIP; DIP-36584N; -.
IntAct; Q9BZS1; 69.
MINT; Q9BZS1; -.
STRING; 9606.ENSP00000365380; -.
iPTMnet; Q9BZS1; -.
PhosphoSitePlus; Q9BZS1; -.
SwissPalm; Q9BZS1; -.
BioMuta; FOXP3; -.
DMDM; 14548061; -.
MaxQB; Q9BZS1; -.
PaxDb; Q9BZS1; -.
PeptideAtlas; Q9BZS1; -.
PRIDE; Q9BZS1; -.
ProteomicsDB; 79899; -.
ProteomicsDB; 79900; -. [Q9BZS1-2]
ProteomicsDB; 79901; -. [Q9BZS1-3]
TopDownProteomics; Q9BZS1-3; -. [Q9BZS1-3]
DNASU; 50943; -.
Ensembl; ENST00000376199; ENSP00000365372; ENSG00000049768. [Q9BZS1-2]
Ensembl; ENST00000376207; ENSP00000365380; ENSG00000049768. [Q9BZS1-1]
Ensembl; ENST00000518685; ENSP00000428952; ENSG00000049768. [Q9BZS1-2]
Ensembl; ENST00000557224; ENSP00000451208; ENSG00000049768. [Q9BZS1-3]
GeneID; 50943; -.
KEGG; hsa:50943; -.
UCSC; uc004dne.5; human. [Q9BZS1-1]
CTD; 50943; -.
DisGeNET; 50943; -.
EuPathDB; HostDB:ENSG00000049768.14; -.
GeneCards; FOXP3; -.
GeneReviews; FOXP3; -.
HGNC; HGNC:6106; FOXP3.
HPA; CAB026301; -.
HPA; HPA045943; -.
MalaCards; FOXP3; -.
MIM; 300292; gene.
MIM; 304790; phenotype.
neXtProt; NX_Q9BZS1; -.
OpenTargets; ENSG00000049768; -.
Orphanet; 37042; Immune dysregulation-polyendocrinopathy-enteropathy-X-linked syndrome.
PharmGKB; PA201094; -.
eggNOG; KOG4385; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00920000148947; -.
HOGENOM; HOG000082490; -.
HOVERGEN; HBG051656; -.
InParanoid; Q9BZS1; -.
KO; K10163; -.
OMA; SCCIVAT; -.
OrthoDB; EOG091G08HY; -.
PhylomeDB; Q9BZS1; -.
TreeFam; TF326978; -.
Reactome; R-HSA-8877330; RUNX1 and FOXP3 control the development of regulatory T lymphocytes (Tregs).
Reactome; R-HSA-8939256; RUNX1 regulates transcription of genes involved in WNT signaling.
SignaLink; Q9BZS1; -.
SIGNOR; Q9BZS1; -.
EvolutionaryTrace; Q9BZS1; -.
GeneWiki; FOXP3; -.
GenomeRNAi; 50943; -.
PRO; PR:Q9BZS1; -.
Proteomes; UP000005640; Chromosome X.
Bgee; ENSG00000049768; Expressed in 112 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_FOXP3; -.
ExpressionAtlas; Q9BZS1; baseline and differential.
Genevisible; Q9BZS1; HS.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; NAS:UniProtKB.
GO; GO:0003677; F:DNA binding; IMP:UniProtKB.
GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0035035; F:histone acetyltransferase binding; IPI:BHF-UCL.
GO; GO:0042826; F:histone deacetylase binding; IPI:BHF-UCL.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0051059; F:NF-kappaB binding; NAS:UniProtKB.
GO; GO:0051525; F:NFAT protein binding; IPI:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; ISS:UniProtKB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; ISA:NTNU_SB.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0009653; P:anatomical structure morphogenesis; IBA:GO_Central.
GO; GO:0001782; P:B cell homeostasis; IEA:Ensembl.
GO; GO:0002362; P:CD4-positive, CD25-positive, alpha-beta regulatory T cell lineage commitment; TAS:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; NAS:UniProtKB.
GO; GO:0001816; P:cytokine production; IEA:Ensembl.
GO; GO:0002262; P:myeloid cell homeostasis; IEA:Ensembl.
GO; GO:0046007; P:negative regulation of activated T cell proliferation; NAS:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IDA:UniProtKB.
GO; GO:0002677; P:negative regulation of chronic inflammatory response; IEA:Ensembl.
GO; GO:0032792; P:negative regulation of CREB transcription factor activity; IDA:UniProtKB.
GO; GO:0042036; P:negative regulation of cytokine biosynthetic process; IDA:UniProtKB.
GO; GO:0050710; P:negative regulation of cytokine secretion; IDA:UniProtKB.
GO; GO:0043433; P:negative regulation of DNA-binding transcription factor activity; IDA:UniProtKB.
GO; GO:0035067; P:negative regulation of histone acetylation; IEA:Ensembl.
GO; GO:0031064; P:negative regulation of histone deacetylation; IGI:BHF-UCL.
GO; GO:0050777; P:negative regulation of immune response; IDA:UniProtKB.
GO; GO:0045077; P:negative regulation of interferon-gamma biosynthetic process; IEA:Ensembl.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032693; P:negative regulation of interleukin-10 production; IDA:UniProtKB.
GO; GO:0032700; P:negative regulation of interleukin-17 production; IMP:UniProtKB.
GO; GO:0045085; P:negative regulation of interleukin-2 biosynthetic process; IMP:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:UniProtKB.
GO; GO:0032713; P:negative regulation of interleukin-4 production; IDA:UniProtKB.
GO; GO:0032714; P:negative regulation of interleukin-5 production; IEA:Ensembl.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0048294; P:negative regulation of isotype switching to IgE isotypes; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
GO; GO:0002725; P:negative regulation of T cell cytokine production; IDA:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IDA:UniProtKB.
GO; GO:2000320; P:negative regulation of T-helper 17 cell differentiation; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IEA:Ensembl.
GO; GO:0032831; P:positive regulation of CD4-positive, CD25-positive, alpha-beta regulatory T cell differentiation; TAS:UniProtKB.
GO; GO:0035066; P:positive regulation of histone acetylation; IMP:BHF-UCL.
GO; GO:0033092; P:positive regulation of immature T cell proliferation in thymus; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IEA:Ensembl.
GO; GO:0002851; P:positive regulation of peripheral T cell tolerance induction; IEA:Ensembl.
GO; GO:0002669; P:positive regulation of T cell anergy; IEA:Ensembl.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0032914; P:positive regulation of transforming growth factor beta1 production; IEA:Ensembl.
GO; GO:0048302; P:regulation of isotype switching to IgG isotypes; IEA:Ensembl.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; TAS:Reactome.
GO; GO:0002667; P:regulation of T cell anergy; ISS:UniProtKB.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0030111; P:regulation of Wnt signaling pathway; TAS:Reactome.
GO; GO:0009615; P:response to virus; IEP:UniProtKB.
GO; GO:0042110; P:T cell activation; IDA:UniProtKB.
GO; GO:0043029; P:T cell homeostasis; NAS:UniProtKB.
GO; GO:0002456; P:T cell mediated immunity; IEA:Ensembl.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:Ensembl.
GO; GO:0002513; P:tolerance induction to self antigen; IEA:Ensembl.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
CDD; cd00059; FH; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR001766; Fork_head_dom.
InterPro; IPR032354; FOXP-CC.
InterPro; IPR030456; TF_fork_head_CS_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
InterPro; IPR013087; Znf_C2H2_type.
Pfam; PF00250; Forkhead; 1.
Pfam; PF16159; FOXP-CC; 1.
PRINTS; PR00053; FORKHEAD.
SMART; SM00339; FH; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00658; FORK_HEAD_2; 1.
PROSITE; PS50039; FORK_HEAD_3; 1.
PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
Complete proteome; Cytoplasm; Diabetes mellitus; Disease mutation;
DNA-binding; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
Reference proteome; Repressor; Transcription;
Transcription regulation; Ubl conjugation; Zinc; Zinc-finger.
CHAIN 1 431 Forkhead box protein P3.
/FTId=PRO_0000091886.
CHAIN 1 417 Forkhead box protein P3, C-terminally
processed. {ECO:0000305|PubMed:19117830}.
/FTId=PRO_0000432430.
CHAIN 52 417 Forkhead box protein P3 41 kDa form.
{ECO:0000305|PubMed:19117830}.
/FTId=PRO_0000432431.
PROPEP 418 431 {ECO:0000305|PubMed:19117830}.
/FTId=PRO_0000432432.
ZN_FING 197 222 C2H2-type.
DNA_BIND 337 423 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
REGION 106 198 Interaction with ZFP90.
{ECO:0000269|PubMed:23543754}.
REGION 106 190 Essential for transcriptional repressor
activity and for interaction with KAT5
and HDAC7. {ECO:0000269|PubMed:17360565}.
REGION 149 199 Interaction with IKZF4.
{ECO:0000250|UniProtKB:Q99JB6}.
REGION 239 260 Leucine-zipper.
REGION 278 336 Interaction with RUNX1.
{ECO:0000269|PubMed:17377532}.
MOTIF 68 76 Nuclear export signal.
{ECO:0000269|PubMed:22678915}.
MOTIF 92 96 LXXLL motif.
{ECO:0000269|PubMed:18354202}.
MOTIF 239 248 Nuclear export signal.
{ECO:0000269|PubMed:22678915}.
MOTIF 414 417 Nuclear localization signal.
{ECO:0000269|PubMed:22678915}.
SITE 51 52 Cleavage. {ECO:0000269|PubMed:19117830}.
SITE 417 418 Cleavage; by PCSK1 or PCSK2.
{ECO:0000269|PubMed:19117830}.
MOD_RES 19 19 Phosphoserine; by CDK2.
{ECO:0000250|UniProtKB:Q99JB6}.
MOD_RES 31 31 N6-acetyllysine.
{ECO:0000269|PubMed:22312127}.
MOD_RES 263 263 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:22312127}.
MOD_RES 268 268 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:22312127}.
MOD_RES 418 418 Phosphoserine.
{ECO:0000269|PubMed:23396208}.
CROSSLNK 250 250 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q99JB6}.
CROSSLNK 252 252 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q99JB6}.
CROSSLNK 263 263 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q99JB6}.
CROSSLNK 268 268 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin);
alternate.
{ECO:0000250|UniProtKB:Q99JB6}.
CROSSLNK 393 393 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000250|UniProtKB:Q99JB6}.
VAR_SEQ 72 106 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.4, ECO:0000303|Ref.7}.
/FTId=VSP_015796.
VAR_SEQ 246 272 Missing (in isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_047859.
VAR_SEQ 382 382 K -> KVSSSEVAVTGMASSAIAAQSGQAWVWAHRHIGEER
DVGCWWWLLASEVDAHLLPVPGLPQ (in isoform 3).
{ECO:0000303|Ref.7}.
/FTId=VSP_036418.
VARIANT 242 242 L -> P (in IPEX; mild phenotype; no loss
of protein expression).
{ECO:0000269|PubMed:18951619}.
/FTId=VAR_078971.
VARIANT 251 251 Missing (in IPEX; significantly reduces
dimerization).
{ECO:0000269|PubMed:11120765,
ECO:0000269|PubMed:21458306}.
/FTId=VAR_011330.
VARIANT 324 324 F -> L (in IPEX; mild phenotype; no loss
of protein expression;
dbSNP:rs122467173).
{ECO:0000269|PubMed:18951619}.
/FTId=VAR_078972.
VARIANT 339 339 P -> A (in IPEX; no loss of protein
expression; dbSNP:rs886044787).
{ECO:0000269|PubMed:18951619}.
/FTId=VAR_078973.
VARIANT 347 347 R -> 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).
{ECO:0000269|PubMed:18951619,
ECO:0000269|PubMed:21458306}.
/FTId=VAR_078974.
VARIANT 363 363 I -> V (in IPEX).
{ECO:0000269|PubMed:11768393}.
/FTId=VAR_023569.
VARIANT 371 371 F -> C (in IPEX; no effect on
dimerization; dbSNP:rs122467169).
{ECO:0000269|PubMed:11137992,
ECO:0000269|PubMed:21458306}.
/FTId=VAR_011331.
VARIANT 373 373 F -> 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; dbSNP:rs122467172).
{ECO:0000269|PubMed:18951619,
ECO:0000269|PubMed:21458306}.
/FTId=VAR_078975.
VARIANT 374 374 F -> C (in IPEX; no loss of protein
expression).
{ECO:0000269|PubMed:18951619}.
/FTId=VAR_078976.
VARIANT 384 384 A -> T (in IPEX; no loss of protein
expression; dbSNP:rs122467170).
{ECO:0000269|PubMed:11137992,
ECO:0000269|PubMed:11137993,
ECO:0000269|PubMed:18951619}.
/FTId=VAR_011332.
VARIANT 397 397 R -> W (in IPEX; dbSNP:rs28935477).
{ECO:0000269|PubMed:11137992}.
/FTId=VAR_011333.
MUTAGEN 69 69 L->A: Decrease in nuclear export; when
associated with A-71, A-74 and A-76.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 71 71 L->A: Decrease in nuclear export; when
associated with A-69, A-74 and A-76.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 74 74 L->A: Decrease in nuclear export; when
associated with A-69, A-71 and A-76.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 76 76 L->A: Decrease in nuclear export; when
associated with A-69, A-71 and A-74.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 95 96 LL->AA: Loss of interaction with RORA.
{ECO:0000269|PubMed:18354202}.
MUTAGEN 242 242 L->A: Decrease in nuclear export; when
associated with A-246 and A-248.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 246 246 L->A: Decrease in nuclear export; when
associated with A-242 and A-248.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 248 248 L->A: Decrease in nuclear export; when
associated with A-242 and A-246.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 348 348 W->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. {ECO:0000269|PubMed:21458306}.
MUTAGEN 370 370 M->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. {ECO:0000269|PubMed:21458306}.
MUTAGEN 372 372 A->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. {ECO:0000269|PubMed:21458306}.
MUTAGEN 415 416 KK->EE: Loss of nuclear localization.
{ECO:0000269|PubMed:22678915}.
MUTAGEN 418 418 S->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.
{ECO:0000269|PubMed:23396208}.
MUTAGEN 418 418 S->E: Slight increase in transcriptional
repressor activity.
{ECO:0000269|PubMed:23396208}.
MUTAGEN 422 422 S->A: Significant decrease in
phosphorylation and transcriptional
repressor activity; when associated with
A-418. {ECO:0000269|PubMed:23396208}.
CONFLICT 16 20 LGPSP -> MSPIS (in Ref. 7; CAA06748).
{ECO:0000305}.
HELIX 342 351 {ECO:0000244|PDB:3QRF}.
HELIX 360 371 {ECO:0000244|PDB:3QRF}.
TURN 372 375 {ECO:0000244|PDB:3QRF}.
HELIX 381 391 {ECO:0000244|PDB:3QRF}.
STRAND 395 398 {ECO:0000244|PDB:3QRF}.
STRAND 401 403 {ECO:0000244|PDB:3QRF}.
STRAND 405 408 {ECO:0000244|PDB:3QRF}.
HELIX 410 416 {ECO:0000244|PDB:3QRF}.
SEQUENCE 431 AA; 47244 MW; 91737C3CEA665A15 CRC64;
MPNPRPGKPS APSLALGPSP GASPSWRAAP KASDLLGARG PGGTFQGRDL RGGAHASSSS
LNPMPPSQLQ LPTLPLVMVA PSGARLGPLP HLQALLQDRP HFMHQLSTVD AHARTPVLQV
HPLESPAMIS LTPPTTATGV FSLKARPGLP PGINVASLEW VSREPALLCT FPNPSAPRKD
STLSAVPQSS YPLLANGVCK WPGCEKVFEE PEDFLKHCQA DHLLDEKGRA QCLLQREMVQ
SLEQQLVLEK EKLSAMQAHL AGKMALTKAS SVASSDKGSC CIVAAGSQGP VVPAWSGPRE
APDSLFAVRR HLWGSHGNST FPEFLHNMDY FKFHNMRPPF TYATLIRWAI LEAPEKQRTL
NEIYHWFTRM FAFFRNHPAT WKNAIRHNLS LHKCFVRVES EKGAVWTVDE LEFRKKRSQR
PSRCSNPTPG P


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