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Forkhead box protein C1 (Forkhead-related protein FKHL7) (Forkhead-related transcription factor 3) (FREAC-3)

 FOXC1_HUMAN             Reviewed;         553 AA.
Q12948; Q86UP7; Q9BYM1; Q9NUE5; Q9UDD0; Q9UP06;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 3.
31-JAN-2018, entry version 179.
RecName: Full=Forkhead box protein C1;
AltName: Full=Forkhead-related protein FKHL7;
AltName: Full=Forkhead-related transcription factor 3;
Short=FREAC-3;
Name=FOXC1; Synonyms=FKHL7, FREAC3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ASGD3 SER-112; MET-126 AND
LEU-131, AND INVOLVEMENT IN ASGD3.
PubMed=9620769; DOI=10.1038/493;
Nishimura D.Y., Swiderski R.E., Alward W.L.M., Searby C.C.,
Patil S.R., Bennet S.R., Kanis A.B., Gastier J.M., Stone E.M.,
Sheffield V.C.;
"The forkhead transcription factor gene FKHL7 is responsible for
glaucoma phenotypes which map to 6p25.";
Nat. Genet. 19:140-147(1998).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS RIEG3 THR-82 AND MET-87,
AND INVOLVEMENT IN RIEG3.
PubMed=9792859; DOI=10.1086/302109;
Mears A.J., Jordan T., Mirzayans F., Dubois S., Kume T., Parlee M.,
Ritch R., Koop B., Kuo W.-L., Collins C., Marshall J., Gould D.B.,
Pearce W., Carlsson P., Enerbaeck S., Morissette J., Bhattacharya S.,
Hogan B., Raymond V., Walter M.A.;
"Mutations of the forkhead/winged-helix gene, FKHL7, in patients with
Axenfeld-Rieger anomaly.";
Am. J. Hum. Genet. 63:1316-1328(1998).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT RIEG3 LYS-161.
PubMed=12592227;
Komatireddy S., Chakrabarti S., Mandal A.K., Reddy A.B.M., Sampath S.,
Panicker S.G., Balasubramanian D.;
"Mutation spectrum of FOXC1 and clinical genetic heterogeneity of
Axenfeld-Rieger anomaly in India.";
Mol. Vis. 9:43-48(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 68-177, AND TISSUE SPECIFICITY.
TISSUE=Erythroleukemia;
PubMed=8499623;
Hromas R., Moore J., Johnston T., Socha C., Klemsz M.;
"Drosophila forkhead homologues are expressed in a lineage-restricted
manner in human hematopoietic cells.";
Blood 81:2854-2859(1993).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 73-178, FUNCTION, AND DNA-BENDING.
PubMed=7957066;
Pierrou S., Hellqvist M., Samuelsson L., Enerbaeck S., Carlsson P.;
"Cloning and characterization of seven human forkhead proteins:
binding site specificity and DNA bending.";
EMBO J. 13:5002-5012(1994).
[7]
FUNCTION, AND INDUCTION.
PubMed=12408963; DOI=10.1016/S0888-7543(02)96860-6;
Zhou Y., Kato H., Asanoma K., Kondo H., Arima T., Kato K., Matsuda T.,
Wake N.;
"Identification of FOXC1 as a TGF-beta1 responsive gene and its
involvement in negative regulation of cell growth.";
Genomics 80:465-472(2002).
[8]
FUNCTION, SUBCELLULAR LOCATION, NUCLEAR LOCALIZATION SIGNAL,
TRANSCRIPTIONAL ACTIVATION/REPRESSION DOMAINS, AND PHOSPHORYLATION.
PubMed=11782474; DOI=10.1074/jbc.M110266200;
Berry F.B., Saleem R.A., Walter M.A.;
"FOXC1 transcriptional regulation is mediated by N- and C-terminal
activation domains and contains a phosphorylated transcriptional
inhibitory domain.";
J. Biol. Chem. 277:10292-10297(2002).
[9]
FUNCTION, AND DNA-BINDING.
PubMed=12533514; DOI=10.1101/gad.1048903;
Yamagishi H., Maeda J., Hu T., McAnally J., Conway S.J., Kume T.,
Meyers E.N., Yamagishi C., Srivastava D.;
"Tbx1 is regulated by tissue-specific forkhead proteins through a
common Sonic hedgehog-responsive enhancer.";
Genes Dev. 17:269-281(2003).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND MUTAGENESIS OF PRO-79; LEU-86;
ILE-87; ILE-91; ILE-126 AND ARG-127.
PubMed=15299087; DOI=10.1093/nar/gkh742;
Saleem R.A., Banerjee-Basu S., Murphy T.C., Baxevanis A., Walter M.A.;
"Essential structural and functional determinants within the forkhead
domain of FOXC1.";
Nucleic Acids Res. 32:4182-4193(2004).
[11]
FUNCTION, DNA-BINDING, INTERACTION WITH FLNA AND PBX1, AND SUBCELLULAR
LOCATION.
PubMed=15684392; DOI=10.1128/MCB.25.4.1415-1424.2005;
Berry F.B., O'Neill M.A., Coca-Prados M., Walter M.A.;
"FOXC1 transcriptional regulatory activity is impaired by PBX1 in a
filamin A-mediated manner.";
Mol. Cell. Biol. 25:1415-1424(2005).
[12]
FUNCTION, UBIQUITINATION, PHOSPHORYLATION AT SER-272, AND MUTAGENESIS
OF THR-68; SER-241; SER-259 AND SER-272.
PubMed=16492674; DOI=10.1074/jbc.M513629200;
Berry F.B., Mirzayans F., Walter M.A.;
"Regulation of FOXC1 stability and transcriptional activity by an
epidermal growth factor-activated mitogen-activated protein kinase
signaling cascade.";
J. Biol. Chem. 281:10098-10104(2006).
[13]
FUNCTION, AND DNA-BINDING.
PubMed=17993506; DOI=10.1093/hmg/ddm326;
Berry F.B., Skarie J.M., Mirzayans F., Fortin Y., Hudson T.J.,
Raymond V., Link B.A., Walter M.A.;
"FOXC1 is required for cell viability and resistance to oxidative
stress in the eye through the transcriptional regulation of FOXO1A.";
Hum. Mol. Genet. 17:490-505(2008).
[14]
INTERACTION WITH C1QBP.
PubMed=18676636; DOI=10.1167/iovs.07-1625;
Huang L., Chi J., Berry F.B., Footz T.K., Sharp M.W., Walter M.A.;
"Human p32 is a novel FOXC1-interacting protein that regulates FOXC1
transcriptional activity in ocular cells.";
Invest. Ophthalmol. Vis. Sci. 49:5243-5249(2008).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-241 AND
SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[19]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20406990; DOI=10.1158/0008-5472.CAN-09-4120;
Ray P.S., Wang J., Qu Y., Sim M.S., Shamonki J., Bagaria S.P., Ye X.,
Liu B., Elashoff D., Hoon D.S., Walter M.A., Martens J.W.,
Richardson A.L., Giuliano A.E., Cui X.;
"FOXC1 is a potential prognostic biomarker with functional
significance in basal-like breast cancer.";
Cancer Res. 70:3870-3876(2010).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320 AND SER-521, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[21]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22991501; DOI=10.7150/ijbs.4769;
Xu Z.Y., Ding S.M., Zhou L., Xie H.Y., Chen K.J., Zhang W., Xing C.Y.,
Guo H.J., Zheng S.S.;
"FOXC1 contributes to microvascular invasion in primary hepatocellular
carcinoma via regulating epithelial-mesenchymal transition.";
Int. J. Biol. Sci. 8:1130-1141(2012).
[22]
SUMOYLATION.
PubMed=22493429; DOI=10.1074/jbc.M112.339424;
Danciu T.E., Chupreta S., Cruz O., Fox J.E., Whitman M.,
Iniguez-Lluhi J.A.;
"Small ubiquitin-like modifier (SUMO) modification mediates function
of the inhibitory domains of developmental regulators FOXC1 and
FOXC2.";
J. Biol. Chem. 287:18318-18329(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[24]
FUNCTION, INTERACTION WITH GLI2, SUBCELLULAR LOCATION, AND TISSUE
SPECIFICITY.
PubMed=26565916; DOI=10.1016/j.celrep.2015.09.063;
Han B., Qu Y., Jin Y., Yu Y., Deng N., Wawrowsky K., Zhang X., Li N.,
Bose S., Wang Q., Sakkiah S., Abrol R., Jensen T.W., Berman B.P.,
Tanaka H., Johnson J., Gao B., Hao J., Liu Z., Buttyan R., Ray P.S.,
Hung M.C., Giuliano A.E., Cui X.;
"FOXC1 activates smoothened-independent Hedgehog signaling in basal-
like breast cancer.";
Cell Rep. 13:1046-1058(2015).
[25]
FUNCTION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=27907090; DOI=10.1371/journal.pone.0167392;
Bin L., Deng L., Yang H., Zhu L., Wang X., Edwards M.G., Richers B.,
Leung D.Y.;
"Forkhead Box C1 regulates human primary keratinocyte terminal
differentiation.";
PLoS ONE 11:E0167392-E0167392(2016).
[26]
VARIANTS RIEG3 LEU-79 AND LEU-131.
PubMed=11170889; DOI=10.1086/318183;
Nishimura D.Y., Searby C.C., Alward W.L., Walton D., Craig J.E.,
Mackey D.A., Kawase K., Kanis A.B., Patil S.R., Stone E.M.,
Sheffield V.C.;
"A spectrum of FOXC1 mutations suggests gene dosage as a mechanism for
developmental defects of the anterior chamber of the eye.";
Am. J. Hum. Genet. 68:364-372(2001).
[27]
VARIANTS RIEG3 THR-82; MET-87; SER-112; MET-126 AND LEU-131, AND
CHARACTERIZATION OF VARIANTS RIEG3 THR-82; MET-87; SER-112; MET-126
AND LEU-131.
PubMed=11179011; DOI=10.1086/318792;
Saleem R.A., Banerjee-Basu S., Berry F.B., Baxevanis A.D.,
Walter M.A.;
"Analyses of the effects that disease-causing missense mutations have
and function of the winged-helix protein FOXC1.";
Am. J. Hum. Genet. 68:627-641(2001).
[28]
VARIANT RIEG3 THR-79.
PubMed=11589884; DOI=10.1016/S0002-9394(01)01059-5;
Suzuki T., Takahashi K., Kuwahara S., Wada Y., Abe T., Tamai M.;
"A novel (Pro79Thr) mutation in the FKHL7 gene in a Japanese family
with Axenfeld-Rieger syndrome.";
Am. J. Ophthalmol. 132:572-575(2001).
[29]
VARIANTS RIEG3 SER-91 AND HIS-127.
PubMed=11740218; DOI=10.1097/00061198-200112000-00007;
Kawase C., Kawase K., Taniguchi T., Sugiyama K., Yamamoto T.,
Kitazawa Y., Alward W.L., Stone E.M., Nishimura D.Y., Sheffield V.C.;
"Screening for mutations of Axenfeld-Rieger syndrome caused by FOXC1
gene in Japanese patients.";
J. Glaucoma 10:477-482(2001).
[30]
VARIANT RIEG3 LYS-161.
PubMed=12454026;
Panicker S.G., Sampath S., Mandal A.K., Reddy A.B.M., Ahmed N.,
Hasnain S.E.;
"Novel mutation in FOXC1 wing region causing Axenfeld-Rieger
anomaly.";
Invest. Ophthalmol. Vis. Sci. 43:3613-3616(2002).
[31]
VARIANT ASGD3 SER-112.
PubMed=12614756; DOI=10.1016/S0002-9394(02)02061-5;
Honkanen R.A., Nishimura D.Y., Swiderski R.E., Bennett S.R., Hong S.,
Kwon Y.H., Stone E.M., Sheffield V.C., Alward W.L.M.;
"A family with Axenfeld-Rieger syndrome and Peters Anomaly caused by a
point mutation (Phe112Ser) in the FOXC1 gene.";
Am. J. Ophthalmol. 135:368-375(2003).
[32]
CHARACTERIZATION OF VARIANTS RIEG3 LEU-79; THR-79; THR-82; SER-91;
THR-91; SER-112; MET-126; HIS-127 AND LEU-131, FUNCTION, AND
DNA-BENDING.
PubMed=14506133; DOI=10.1093/hmg/ddg324;
Saleem R.A., Banerjee-Basu S., Berry F.B., Baxevanis A.D.,
Walter M.A.;
"Structural and functional analyses of disease-causing missense
mutations in the forkhead domain of FOXC1.";
Hum. Mol. Genet. 12:2993-3005(2003).
[33]
VARIANT RIEG3 PHE-86, MUTAGENESIS OF LEU-86, CHARACTERIZATION OF
VARIANT RIEG3 PHE-86, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=14578375; DOI=10.1167/iovs.03-0090;
Saleem R.A., Murphy T.C., Liebmann J.M., Walter M.A.;
"Identification and analysis of a novel mutation in the FOXC1 forkhead
domain.";
Invest. Ophthalmol. Vis. Sci. 44:4608-4612(2003).
[34]
VARIANT RIEG3 THR-91.
PubMed=15477465; DOI=10.1001/archopht.122.10.1527;
Mortemousque B., Amati-Bonneau P., Couture F., Graffan R., Dubois S.,
Colin J., Bonneau D., Morissette J., Lacombe D., Raymond V.;
"Axenfeld-Rieger anomaly: a novel mutation in the forkhead box C1
(FOXC1) gene in a 4-generation family.";
Arch. Ophthalmol. 122:1527-1533(2004).
[35]
VARIANTS RIEG3 ARG-165 AND PRO-169, CHARACTERIZATION OF VARIANTS RIEG3
LYS-161; ARG-165 AND PRO-169, FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=15277473; DOI=10.1167/iovs.04-0167;
Murphy T.C., Saleem R.A., Footz T., Ritch R., McGillivray B.,
Walter M.A.;
"The wing 2 region of the FOXC1 forkhead domain is necessary for
normal DNA-binding and transactivation functions.";
Invest. Ophthalmol. Vis. Sci. 45:2531-2538(2004).
[36]
CHARACTERIZATION OF VARIANTS RIEG3 HIS-127 AND LEU-131, FUNCTION,
INTERACTION WITH PITX2, AND SUBCELLULAR LOCATION.
PubMed=16449236; DOI=10.1093/hmg/ddl008;
Berry F.B., Lines M.A., Oas J.M., Footz T., Underhill D.A., Gage P.J.,
Walter M.A.;
"Functional interactions between FOXC1 and PITX2 underlie the
sensitivity to FOXC1 gene dose in Axenfeld-Rieger syndrome and
anterior segment dysgenesis.";
Hum. Mol. Genet. 15:905-919(2006).
[37]
VARIANTS RIEG3 ARG-79; SER-115; ASP-149 AND VAL-161.
PubMed=16936096; DOI=10.1167/iovs.06-0343;
Weisschuh N., Dressler P., Schuettauf F., Wolf C., Wissinger B.,
Gramer E.;
"Novel mutations of FOXC1 and PITX2 in patients with Axenfeld-Rieger
malformations.";
Invest. Ophthalmol. Vis. Sci. 47:3846-3852(2006).
[38]
ERRATUM.
Weisschuh N., Dressler P., Schuettauf F., Wolf C., Wissinger B.,
Gramer E.;
Invest. Ophthalmol. Vis. Sci. 47:5162-5162(2006).
[39]
VARIANT RIEG3 PHE-130, CHARACTERIZATION OF VARIANT RIEG3 PHE-130,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=17210863; DOI=10.1001/archopht.125.1.128;
Ito Y.A., Footz T.K., Murphy T.C., Courtens W., Walter M.A.;
"Analyses of a novel L130F missense mutation in FOXC1.";
Arch. Ophthalmol. 125:128-135(2007).
[40]
VARIANT RIEG3 PRO-85.
PubMed=17653043;
Fuse N., Takahashi K., Yokokura S., Nishida K.;
"Novel mutations in the FOXC1 gene in Japanese patients with Axenfeld-
Rieger syndrome.";
Mol. Vis. 13:1005-1009(2007).
[41]
VARIANT ASGD3 LYS-161.
PubMed=18484311; DOI=10.1080/13816810801908152;
Khan A.O., Aldahmesh M.A., Al-Amri A.;
"Heterozygous FOXC1 mutation (M161K) associated with congenital
glaucoma and aniridia in an infant and a milder phenotype in her
mother.";
Ophthalmic Genet. 29:67-71(2008).
[42]
VARIANT ASGD3 SER-297, CHARACTERIZATION OF VARIANT ASGD3 SER-297,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=19793056; DOI=10.1111/j.1399-0004.2009.01210.x;
Fetterman C.D., Mirzayans F., Walter M.A.;
"Characterization of a novel FOXC1 mutation, P297S, identified in two
individuals with anterior segment dysgenesis.";
Clin. Genet. 76:296-299(2009).
[43]
VARIANT ASGD3 GLY-152, CHARACTERIZATION OF VARIANT ASGD3 GLY-152,
FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION, AND CHARACTERIZATION
OF VARIANT RIEG3 PHE-130.
PubMed=19279310; DOI=10.1167/iovs.08-3032;
Ito Y.A., Footz T.K., Berry F.B., Mirzayans F., Yu M., Khan A.O.,
Walter M.A.;
"Severe molecular defects of a novel FOXC1 W152G mutation result in
aniridia.";
Invest. Ophthalmol. Vis. Sci. 50:3573-3579(2009).
[44]
VARIANTS ASGD3 VAL-109; TRP-131 AND GLU-138.
PubMed=20881294; DOI=10.1167/iovs.10-5309;
D'haene B., Meire F., Claerhout I., Kroes H.Y., Plomp A., Arens Y.H.,
de Ravel T., Casteels I., De Jaegere S., Hooghe S., Wuyts W.,
van den Ende J., Roulez F., Veenstra-Knol H.E., Oldenburg R.A.,
Giltay J., Verheij J.B., de Faber J.T., Menten B., De Paepe A.,
Kestelyn P., Leroy B.P., De Baere E.;
"Expanding the spectrum of FOXC1 and PITX2 mutations and copy number
changes in patients with anterior segment malformations.";
Invest. Ophthalmol. Vis. Sci. 52:324-333(2011).
[45]
VARIANT RIEG3 TRP-170.
PubMed=23239455; DOI=10.1002/ajmg.a.35697;
Gripp K.W., Hopkins E., Jenny K., Thacker D., Salvin J.;
"Cardiac anomalies in Axenfeld-Rieger syndrome due to a novel FOXC1
mutation.";
Am. J. Med. Genet. A 161A:114-119(2013).
[46]
VARIANT RIEG3 SER-126, CHARACTERIZATION OF VARIANT RIEG3 SER-126,
FUNCTION, SUBCELLULAR LOCATION, AND PHOSPHORYLATION.
PubMed=25786029; DOI=10.1371/journal.pone.0119272;
Medina-Trillo C., Sanchez-Sanchez F., Aroca-Aguilar J.D.,
Ferre-Fernandez J.J., Morales L., Mendez-Hernandez C.D.,
Blanco-Kelly F., Ayuso C., Garcia-Feijoo J., Escribano J.;
"Hypo- and hypermorphic FOXC1 mutations in dominant glaucoma:
transactivation and phenotypic variability.";
PLoS ONE 10:E0119272-E0119272(2015).
[47]
VARIANT RIEG3 LEU-127.
PubMed=24914578; DOI=10.3109/13816810.2014.924016;
Du R.F., Huang H., Fan L.L., Li X.P., Xia K., Xiang R.;
"A novel mutation of FOXC1 (R127L) in an Axenfeld-Rieger syndrome
family with glaucoma and multiple congenital heart diseases.";
Ophthalmic Genet. 37:111-115(2016).
[48]
VARIANTS RIEG3 ARG-128; TYR-135 AND VAL-161, VARIANT ASN-368,
CHARACTERIZATION OF VARIANTS RIEG3 ARG-128; TYR-135 AND VAL-161,
CHARACTERIZATION OF VARIANT ASN-368, FUNCTION, AND SUBCELLULAR
LOCATION.
PubMed=27804176; DOI=10.1002/humu.23141;
Seifi M., Footz T., Taylor S.A., Walter M.A.;
"Comparison of bioinformatics prediction, molecular modeling, and
functional analyses of FOXC1 mutations in patients with Axenfeld-
Rieger syndrome.";
Hum. Mutat. 38:169-179(2017).
-!- FUNCTION: DNA-binding transcriptional factor that plays a role in
a broad range of cellular and developmental processes such as eye,
bones, cardiovascular, kidney and skin development
(PubMed:11782474, PubMed:15299087, PubMed:15684392,
PubMed:16492674, PubMed:27907090, PubMed:14506133,
PubMed:14578375, PubMed:15277473, PubMed:16449236,
PubMed:17210863, PubMed:19793056, PubMed:19279310,
PubMed:25786029, PubMed:27804176). Acts either as a
transcriptional activator or repressor (PubMed:11782474). Binds to
the consensus binding site 5'-[G/C][A/T]AAA[T/C]AA[A/C]-3' in
promoter of target genes (PubMed:7957066, PubMed:11782474,
PubMed:12533514, PubMed:14506133, PubMed:19793056,
PubMed:27804176). Upon DNA-binding, promotes DNA bending
(PubMed:7957066, PubMed:14506133). Acts as a transcriptional
coactivator (PubMed:26565916). Stimulates Indian hedgehog (Ihh)-
induced target gene expression mediated by the transcription
factor GLI2, and hence regulates endochondral ossification (By
similarity). Acts also as a transcriptional coregulator by
increasing DNA-binding capacity of GLI2 in breast cancer cells
(PubMed:26565916). Regulates FOXO1 through binding to a conserved
element, 5'-GTAAACAAA-3' in its promoter region, implicating FOXC1
as an important regulator of cell viability and resistance to
oxidative stress in the eye (PubMed:17993506). Cooperates with
transcription factor FOXC2 in regulating expression of genes that
maintain podocyte integrity (By similarity). Promotes cell growth
inhibition by stopping the cell cycle in the G1 phase through
TGFB1-mediated signals (PubMed:12408963). Involved in epithelial-
mesenchymal transition (EMT) induction by increasing cell
proliferation, migration and invasion (PubMed:20406990,
PubMed:22991501). Involved in chemokine CXCL12-induced endothelial
cell migration through the control of CXCR4 expression (By
similarity). Plays a role in the gene regulatory network essential
for epidermal keratinocyte terminal differentiation
(PubMed:27907090). Essential developmental transcriptional factor
required for mesoderm-derived tissues, such as the somites, skin,
bone and cartilage. Positively regulates CXCL12 and stem cell
factor expression in bone marrow mesenchymal progenitor cells, and
hence plays a role in the development and maintenance of
mesenchymal niches for haematopoietic stem and progenitor cells
(HSPC). Plays a role in corneal transparency by preventing both
blood vessel and lymphatic vessel growth during embryonic
development in a VEGF-dependent manner. Involved in chemokine
CXCL12-induced endothelial cell migration through the control of
CXCR4 expression (By similarity). May function as a tumor
suppressor (PubMed:12408963). {ECO:0000250|UniProtKB:Q61572,
ECO:0000269|PubMed:11782474, ECO:0000269|PubMed:12408963,
ECO:0000269|PubMed:12533514, ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:14578375, ECO:0000269|PubMed:15277473,
ECO:0000269|PubMed:15299087, ECO:0000269|PubMed:15684392,
ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:16492674,
ECO:0000269|PubMed:17210863, ECO:0000269|PubMed:17993506,
ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:19793056,
ECO:0000269|PubMed:20406990, ECO:0000269|PubMed:22991501,
ECO:0000269|PubMed:25786029, ECO:0000269|PubMed:26565916,
ECO:0000269|PubMed:27804176, ECO:0000269|PubMed:27907090,
ECO:0000269|PubMed:7957066}.
-!- SUBUNIT: Monomer. Interacts with C1QBP (PubMed:18676636).
Interacts (via N-terminus) with GLI2 (via C-terminal internal
region); this interaction is direct and increases GLI2 DNA-binding
and transcriptional activity through a smoothened (SMO)-
independent Hedgehog (Hh) signaling pathway (PubMed:26565916).
Interacts (via C-terminus domain) with PITX2 isoform 3 (via
homeobox domain) (PubMed:16449236). Interacts with FLNA and PBX1
(PubMed:15684392). {ECO:0000269|PubMed:15684392,
ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:18676636,
ECO:0000269|PubMed:26565916}.
-!- INTERACTION:
Q07021:C1QBP; NbExp=6; IntAct=EBI-1175253, EBI-347528;
P21333:FLNA; NbExp=8; IntAct=EBI-1175253, EBI-350432;
Q9Q2G4:ORF (xeno); NbExp=3; IntAct=EBI-1175253, EBI-6248094;
P40424:PBX1; NbExp=5; IntAct=EBI-1175253, EBI-301611;
Q99697-3:PITX2; NbExp=6; IntAct=EBI-1175253, EBI-1175243;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11782474,
ECO:0000269|PubMed:14578375, ECO:0000269|PubMed:15277473,
ECO:0000269|PubMed:15299087, ECO:0000269|PubMed:15684392,
ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:17210863,
ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:19793056,
ECO:0000269|PubMed:20406990, ECO:0000269|PubMed:25786029,
ECO:0000269|PubMed:26565916, ECO:0000269|PubMed:27804176}.
Note=Colocalizes with PITX2 isoform 3 in the nucleus at subnuclear
chromatine regions (PubMed:16449236). Colocalizes with CBX5 to a
heterochromatin-rich region of the nucleus (PubMed:15684392).
Colocalizes with GLI2 in the nucleus (By similarity).
{ECO:0000250|UniProtKB:Q61572, ECO:0000269|PubMed:15684392,
ECO:0000269|PubMed:16449236}.
-!- TISSUE SPECIFICITY: Expressed in keratinocytes of epidermis and
hair follicle (PubMed:27907090). Expressed strongly in
microvascular invasion (MVI) formation, basal-like breast cancer
(BLBC) and hepatocellular tumors (PubMed:20406990,
PubMed:22991501). Expressed in breast cancers (at protein level)
(PubMed:26565916). Expressed in hematopoietic cells
(PubMed:8499623). {ECO:0000269|PubMed:20406990,
ECO:0000269|PubMed:22991501, ECO:0000269|PubMed:26565916,
ECO:0000269|PubMed:27907090, ECO:0000269|PubMed:8499623}.
-!- INDUCTION: Up-regulated during the progression of epidermal
keratinocyte differentiation (at protein level) (PubMed:27907090).
Up-regulated upon calcium-mediated keratinocyte differentiation
(PubMed:27907090). Up-regulated by transforming growth factor
TGFB1 (PubMed:12408963). {ECO:0000269|PubMed:12408963,
ECO:0000269|PubMed:27907090}.
-!- PTM: Phosphorylated (PubMed:11782474, PubMed:19279310,
PubMed:25786029). Phosphorylated on Ser-272 in response to
epidermal growth factor (EGF) in a ERK1/2 MAPK-dependent signaling
pathway; phosphorylation contributes to its protein stability and
transcriptional activity (PubMed:16492674).
{ECO:0000269|PubMed:11782474, ECO:0000269|PubMed:16492674,
ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:25786029}.
-!- PTM: Sumoylated preferentially with SUMO2 or SUMO3
(PubMed:22493429). Desumoylated by SENP2 (PubMed:22493429).
{ECO:0000269|PubMed:22493429}.
-!- PTM: Ubiquitinated, leading to its proteasomal degradation
(PubMed:16492674). {ECO:0000269|PubMed:16492674}.
-!- DISEASE: Axenfeld-Rieger syndrome 3 (RIEG3) [MIM:602482]: An
autosomal dominant disorder of morphogenesis that results in
abnormal development of the anterior segment of the eye, and
results in blindness from glaucoma in approximately 50% of
affected individuals. Features include posterior corneal
embryotoxon, prominent Schwalbe line and iris adhesion to the
Schwalbe line, hypertelorism, hypodontia, sensorineural deafness,
redundant periumbilical skin, and cardiovascular defects such as
patent ductus arteriosus and atrial septal defect. When associated
with tooth anomalies, the disorder is known as Rieger syndrome.
{ECO:0000269|PubMed:11170889, ECO:0000269|PubMed:11179011,
ECO:0000269|PubMed:11589884, ECO:0000269|PubMed:11740218,
ECO:0000269|PubMed:12454026, ECO:0000269|PubMed:12592227,
ECO:0000269|PubMed:14506133, ECO:0000269|PubMed:14578375,
ECO:0000269|PubMed:15277473, ECO:0000269|PubMed:15477465,
ECO:0000269|PubMed:16449236, ECO:0000269|PubMed:16936096,
ECO:0000269|PubMed:17210863, ECO:0000269|PubMed:17653043,
ECO:0000269|PubMed:19279310, ECO:0000269|PubMed:23239455,
ECO:0000269|PubMed:24914578, ECO:0000269|PubMed:25786029,
ECO:0000269|PubMed:27804176, ECO:0000269|PubMed:9792859}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Anterior segment dysgenesis 3 (ASGD3) [MIM:601631]: A
form of anterior segment dysgenesis, a group of defects affecting
anterior structures of the eye including cornea, iris, lens,
trabecular meshwork, and Schlemm canal. Anterior segment
dysgeneses result from abnormal migration or differentiation of
the neural crest derived mesenchymal cells that give rise to
components of the anterior chamber during eye development.
Different anterior segment anomalies may exist alone or in
combination, including iris hypoplasia, enlarged or reduced
corneal diameter, corneal vascularization and opacity, posterior
embryotoxon, corectopia, polycoria, abnormal iridocorneal angle,
ectopia lentis, and anterior synechiae between the iris and
posterior corneal surface. Clinical conditions falling within the
phenotypic spectrum of anterior segment dysgeneses include
aniridia, Axenfeld anomaly, Reiger anomaly/syndrome, Peters
anomaly, and iridogoniodysgenesis. ASGD3 inheritance is autosomal
dominant. {ECO:0000269|PubMed:12614756,
ECO:0000269|PubMed:18484311, ECO:0000269|PubMed:19279310,
ECO:0000269|PubMed:19793056, ECO:0000269|PubMed:20881294,
ECO:0000269|PubMed:9620769}. 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/FOXC1ID40624ch6p25.html";
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EMBL; AF048693; AAC18081.1; -; Genomic_DNA.
EMBL; AF078096; AAC72915.1; -; Genomic_DNA.
EMBL; AY228704; AAP15181.1; -; Genomic_DNA.
EMBL; AL034344; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; L12143; AAK13575.1; -; mRNA.
EMBL; U13221; AAA92038.1; -; mRNA.
CCDS; CCDS4473.1; -.
PIR; S51626; S51626.
RefSeq; NP_001444.2; NM_001453.2.
UniGene; Hs.348883; -.
ProteinModelPortal; Q12948; -.
SMR; Q12948; -.
BioGrid; 108585; 51.
IntAct; Q12948; 43.
STRING; 9606.ENSP00000370256; -.
iPTMnet; Q12948; -.
PhosphoSitePlus; Q12948; -.
BioMuta; FOXC1; -.
DMDM; 13638267; -.
PaxDb; Q12948; -.
PeptideAtlas; Q12948; -.
PRIDE; Q12948; -.
Ensembl; ENST00000380874; ENSP00000370256; ENSG00000054598.
GeneID; 2296; -.
KEGG; hsa:2296; -.
CTD; 2296; -.
DisGeNET; 2296; -.
EuPathDB; HostDB:ENSG00000054598.6; -.
GeneCards; FOXC1; -.
H-InvDB; HIX0032962; -.
HGNC; HGNC:3800; FOXC1.
HPA; HPA040670; -.
MalaCards; FOXC1; -.
MIM; 601090; gene.
MIM; 601631; phenotype.
MIM; 602482; phenotype.
neXtProt; NX_Q12948; -.
OpenTargets; ENSG00000054598; -.
Orphanet; 98978; Axenfeld anomaly.
Orphanet; 782; Axenfeld-Rieger syndrome.
Orphanet; 708; Peters anomaly.
Orphanet; 91483; Rieger anomaly.
PharmGKB; PA28217; -.
eggNOG; KOG2294; Eukaryota.
eggNOG; COG5025; LUCA.
GeneTree; ENSGT00760000118904; -.
HOVERGEN; HBG051640; -.
InParanoid; Q12948; -.
KO; K09396; -.
OMA; YSSPCSQ; -.
OrthoDB; EOG091G0HW9; -.
PhylomeDB; Q12948; -.
TreeFam; TF316127; -.
SignaLink; Q12948; -.
SIGNOR; Q12948; -.
GeneWiki; Forkhead_box_C1; -.
GenomeRNAi; 2296; -.
PRO; PR:Q12948; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000054598; -.
CleanEx; HS_FOXC1; -.
ExpressionAtlas; Q12948; baseline and differential.
Genevisible; Q12948; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
GO; GO:0003700; F:DNA binding transcription factor activity; IDA:UniProtKB.
GO; GO:0008301; F:DNA binding, bending; IDA:UniProtKB.
GO; GO:1990841; F:promoter-specific chromatin binding; ISS:UniProtKB.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:NTNU_SB.
GO; GO:0000981; F:RNA polymerase II transcription factor activity, sequence-specific DNA binding; IBA:GO_Central.
GO; GO:0043565; F:sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0001223; F:transcription coactivator binding; ISS:UniProtKB.
GO; GO:0003705; F:transcription factor activity, RNA polymerase II distal enhancer sequence-specific binding; IEA:Ensembl.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0044212; F:transcription regulatory region DNA binding; IDA:UniProtKB.
GO; GO:0001228; F:transcriptional activator activity, RNA polymerase II transcription regulatory region sequence-specific DNA binding; IC:NTNU_SB.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0048844; P:artery morphogenesis; IEA:Ensembl.
GO; GO:0001974; P:blood vessel remodeling; IEA:Ensembl.
GO; GO:0043010; P:camera-type eye development; IEA:Ensembl.
GO; GO:0060038; P:cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:1990869; P:cellular response to chemokine; ISS:UniProtKB.
GO; GO:0071364; P:cellular response to epidermal growth factor stimulus; IMP:UniProtKB.
GO; GO:0021549; P:cerebellum development; ISS:UniProtKB.
GO; GO:0070098; P:chemokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0035050; P:embryonic heart tube development; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; ISS:UniProtKB.
GO; GO:0001654; P:eye development; IDA:MGI.
GO; GO:0008354; P:germ cell migration; IEA:Ensembl.
GO; GO:0072010; P:glomerular epithelium development; ISS:UniProtKB.
GO; GO:0030203; P:glycosaminoglycan metabolic process; IEA:Ensembl.
GO; GO:0007507; P:heart development; IDA:MGI.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0001822; P:kidney development; ISS:UniProtKB.
GO; GO:0032808; P:lacrimal gland development; IEA:Ensembl.
GO; GO:0001945; P:lymph vessel development; IEA:Ensembl.
GO; GO:0036438; P:maintenance of lens transparency; ISS:UniProtKB.
GO; GO:0014031; P:mesenchymal cell development; ISS:UniProtKB.
GO; GO:0016525; P:negative regulation of angiogenesis; ISS:UniProtKB.
GO; GO:1902257; P:negative regulation of apoptotic process involved in outflow tract morphogenesis; IEA:Ensembl.
GO; GO:1901491; P:negative regulation of lymphangiogenesis; ISS:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
GO; GO:0014032; P:neural crest cell development; IEA:Ensembl.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IMP:UniProtKB.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0048341; P:paraxial mesoderm formation; IEA:Ensembl.
GO; GO:1904798; P:positive regulation of core promoter binding; ISS:UniProtKB.
GO; GO:0043388; P:positive regulation of DNA binding; IMP:UniProtKB.
GO; GO:0010718; P:positive regulation of epithelial to mesenchymal transition; IMP:UniProtKB.
GO; GO:1901534; P:positive regulation of hematopoietic progenitor cell differentiation; ISS:UniProtKB.
GO; GO:1902038; P:positive regulation of hematopoietic stem cell differentiation; ISS:UniProtKB.
GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IMP:UniProtKB.
GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0050880; P:regulation of blood vessel size; IEA:Ensembl.
GO; GO:0046620; P:regulation of organ growth; IEA:Ensembl.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
GO; GO:0048010; P:vascular endothelial growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0038084; P:vascular endothelial growth factor signaling pathway; ISS:UniProtKB.
GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; IEA:Ensembl.
CDD; cd00059; FH; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR001766; Fork_head_dom.
InterPro; IPR018122; TF_fork_head_CS_1.
InterPro; IPR030456; TF_fork_head_CS_2.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00250; Forkhead; 1.
PRINTS; PR00053; FORKHEAD.
SMART; SM00339; FH; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS00657; FORK_HEAD_1; 1.
PROSITE; PS00658; FORK_HEAD_2; 1.
PROSITE; PS50039; FORK_HEAD_3; 1.
1: Evidence at protein level;
Activator; Angiogenesis; Complete proteome; Deafness;
Developmental protein; Disease mutation; DNA-binding; Nucleus;
Peters anomaly; Phosphoprotein; Polymorphism; Reference proteome;
Repressor; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 553 Forkhead box protein C1.
/FTId=PRO_0000091806.
DNA_BIND 77 168 Fork-head. {ECO:0000255|PROSITE-
ProRule:PRU00089}.
REGION 1 51 Required for transcriptional activation.
{ECO:0000269|PubMed:11782474}.
REGION 215 366 Required for transcriptional inhibition.
{ECO:0000269|PubMed:11782474}.
REGION 466 553 Required for transcriptional activation.
{ECO:0000269|PubMed:11782474}.
MOTIF 78 93 Nuclear localization signal 1 (NLS 1).
{ECO:0000269|PubMed:11782474}.
MOTIF 168 176 Nuclear localization signal 2 (NLS 2).
{ECO:0000269|PubMed:11782474}.
COMPBIAS 28 33 Poly-Ala.
COMPBIAS 169 173 Poly-Arg.
COMPBIAS 194 197 Poly-Pro.
COMPBIAS 262 272 Poly-Ser.
COMPBIAS 292 297 Poly-Pro.
COMPBIAS 375 382 Poly-Gly.
COMPBIAS 438 445 Poly-Ser.
COMPBIAS 447 456 Poly-Gly.
COMPBIAS 486 495 Poly-Ala.
MOD_RES 235 235 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:18691976}.
MOD_RES 241 241 Phosphoserine.
{ECO:0000244|PubMed:18691976}.
MOD_RES 272 272 Phosphoserine.
{ECO:0000269|PubMed:16492674}.
MOD_RES 320 320 Phosphoserine.
{ECO:0000244|PubMed:18691976,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 521 521 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
VARIANT 79 79 P -> L (in RIEG3; decreased location at
the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity; no change
on DNA bending activity).
{ECO:0000269|PubMed:11170889,
ECO:0000269|PubMed:14506133}.
/FTId=VAR_058722.
VARIANT 79 79 P -> R (in RIEG3).
{ECO:0000269|PubMed:16936096}.
/FTId=VAR_058723.
VARIANT 79 79 P -> T (in RIEG3; decreased location at
the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity; no change
on DNA bending activity).
{ECO:0000269|PubMed:11589884,
ECO:0000269|PubMed:14506133}.
/FTId=VAR_058724.
VARIANT 82 82 S -> T (in RIEG3; decreased location at
the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity;
dbSNP:rs104893953).
{ECO:0000269|PubMed:11179011,
ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:9792859}.
/FTId=VAR_007944.
VARIANT 85 85 A -> P (in RIEG3; unknown pathological
significance).
{ECO:0000269|PubMed:17653043}.
/FTId=VAR_078501.
VARIANT 86 86 L -> F (in RIEG3; no change in location
at the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity;
dbSNP:rs886039568).
{ECO:0000269|PubMed:14578375}.
/FTId=VAR_058725.
VARIANT 87 87 I -> M (in RIEG3; loss of protein
stability; dbSNP:rs104893954).
{ECO:0000269|PubMed:11179011,
ECO:0000269|PubMed:9792859}.
/FTId=VAR_007945.
VARIANT 91 91 I -> S (in RIEG3; decreased location at
the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity; no change
on DNA bending activity).
{ECO:0000269|PubMed:11740218,
ECO:0000269|PubMed:14506133}.
/FTId=VAR_058726.
VARIANT 91 91 I -> T (in RIEG3; decreased location at
the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity; no change
on DNA bending activity).
{ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:15477465}.
/FTId=VAR_058727.
VARIANT 109 109 M -> V (in ASGD3; dbSNP:rs917382067).
{ECO:0000269|PubMed:20881294}.
/FTId=VAR_078502.
VARIANT 112 112 F -> S (in ASGD3 and RIEG3; decreased
location at the nucleus; decreased
transcription regulatory region DNA
binding; decreased sequence-specific DNA
binding transcription factor activity;
dbSNP:rs104893951).
{ECO:0000269|PubMed:11179011,
ECO:0000269|PubMed:12614756,
ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:9620769}.
/FTId=VAR_007815.
VARIANT 115 115 Y -> S (in RIEG3).
{ECO:0000269|PubMed:16936096}.
/FTId=VAR_058728.
VARIANT 126 126 I -> M (in ASGD3 and RIEG3; with
glaucoma; decreased location at the
nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity;
dbSNP:rs104893958).
{ECO:0000269|PubMed:11179011,
ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:9620769}.
/FTId=VAR_007816.
VARIANT 126 126 I -> S (in RIEG3; hypomorphic mutation;
decreased protein abundance; decreased
protein stability; changed post-
translational phosphorylation; decreased
location at the nucleus; novel location
at the cytoplasm; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity;
dbSNP:rs483352810).
{ECO:0000269|PubMed:25786029}.
/FTId=VAR_078503.
VARIANT 127 127 R -> H (in RIEG3; decreased location at
the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity).
{ECO:0000269|PubMed:11740218,
ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:16449236}.
/FTId=VAR_058729.
VARIANT 127 127 R -> L (in RIEG3).
{ECO:0000269|PubMed:24914578}.
/FTId=VAR_078504.
VARIANT 128 128 H -> R (in RIEG3; no effect on protein
abundance; increased protein stability;
decreased location at nucleus; loss of
transcription regulatory region DNA
binding; loss of sequence-specific DNA
binding transcription factor activity).
{ECO:0000269|PubMed:27804176}.
/FTId=VAR_078505.
VARIANT 130 130 L -> F (in RIEG3; no effect on protein
abundance; changed post-translational
phosphorylation; novel location at
aggresome, aggregation correspond to
microtubule-dependent inclusion bodies;
decreased location at the nucleus;
decreased transcription regulatory region
DNA binding; decreased sequence-specific
DNA binding transcription factor
activity; dbSNP:rs121909338).
{ECO:0000269|PubMed:17210863,
ECO:0000269|PubMed:19279310}.
/FTId=VAR_058730.
VARIANT 131 131 S -> L (in RIEG3 and ASGD3; with
glaucoma; decreased location at the
nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity;
dbSNP:rs104893957).
{ECO:0000269|PubMed:11170889,
ECO:0000269|PubMed:11179011,
ECO:0000269|PubMed:14506133,
ECO:0000269|PubMed:16449236,
ECO:0000269|PubMed:9620769}.
/FTId=VAR_007817.
VARIANT 131 131 S -> W (in ASGD3).
{ECO:0000269|PubMed:20881294}.
/FTId=VAR_078506.
VARIANT 135 135 C -> Y (in RIEG3; decreased protein
abundance; decreased protein stability;
decreased location at nucleus; loss of
transcription regulatory region DNA
binding; loss of sequence-specific DNA
binding transcription factor activity).
{ECO:0000269|PubMed:27804176}.
/FTId=VAR_078507.
VARIANT 138 138 K -> E (in ASGD3).
{ECO:0000269|PubMed:20881294}.
/FTId=VAR_078508.
VARIANT 149 149 G -> D (in RIEG3).
{ECO:0000269|PubMed:16936096}.
/FTId=VAR_058731.
VARIANT 152 152 W -> G (in ASGD3; no change in protein
abundance; changed post-translational
phosphorylation; changed protein
structure; decreased location at the
nucleus; novel location at the cytoplasm;
increased protein aggregation,
aggregation do not correspond to
microtubule-dependent inclusion bodies;
loss of transcription regulatory region
DNA binding; loss of sequence-specific
DNA binding transcription factor
activity). {ECO:0000269|PubMed:19279310}.
/FTId=VAR_078509.
VARIANT 161 161 M -> K (in RIEG3 and ASGD3; no change in
location at the nucleus; decreased
transcription regulatory region DNA
binding; decreased sequence-specific DNA
binding transcription factor activity).
{ECO:0000269|PubMed:12454026,
ECO:0000269|PubMed:12592227,
ECO:0000269|PubMed:15277473,
ECO:0000269|PubMed:18484311}.
/FTId=VAR_018150.
VARIANT 161 161 M -> V (in RIEG3; no effect on protein
abundance; no effect on protein
stability; no effect on location at
nucleus; no effect on transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity).
{ECO:0000269|PubMed:16936096,
ECO:0000269|PubMed:27804176}.
/FTId=VAR_058732.
VARIANT 165 165 G -> R (in RIEG3; no change in location
at the nucleus; no effect on
transcription regulatory region DNA
binding; decreased sequence-specific DNA
binding transcription factor activity).
{ECO:0000269|PubMed:15277473}.
/FTId=VAR_058733.
VARIANT 169 169 R -> P (in RIEG3; no change in location
at the nucleus; decreased transcription
regulatory region DNA binding; decreased
sequence-specific DNA binding
transcription factor activity).
{ECO:0000269|PubMed:15277473}.
/FTId=VAR_058734.
VARIANT 170 170 R -> W (in RIEG3; unknown pathological
significance).
{ECO:0000269|PubMed:23239455}.
/FTId=VAR_078510.
VARIANT 297 297 P -> S (in ASGD3; no effect on protein
abundance; increased protein stability;
no effect on nuclear location; no effect
on transcription regulatory region DNA
binding; decreased sequence-specific DNA
binding transcription factor activity;
dbSNP:rs79691946).
{ECO:0000269|PubMed:19793056}.
/FTId=VAR_078511.
VARIANT 368 368 T -> N (no effect on protein abundance;
no effect on protein stability; no effect
on nuclear location; no effect on
transcription regulatory region DNA
binding; no effect on sequence-specific
DNA binding transcription factor
activity). {ECO:0000269|PubMed:27804176}.
/FTId=VAR_078512.
MUTAGEN 68 68 T->A: No effect on protein stability. No
effect on transcriptional activity.
{ECO:0000269|PubMed:16492674}.
MUTAGEN 79 79 P->A: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 79 79 P->E: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 79 79 P->K: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 86 86 L->A: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 86 86 L->E: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 86 86 L->K: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 86 86 L->P: Severely disrupts the protein
function. {ECO:0000269|PubMed:14578375}.
MUTAGEN 87 87 I->A,E,K: Loss of protein stability.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 91 91 I->A: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 91 91 I->E: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 91 91 I->K: Decreased nuclear localization. No
effect on DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 126 126 I->A: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 126 126 I->E: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 126 126 I->K: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 127 127 R->A: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 127 127 R->E: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 127 127 R->K: Decreased nuclear localization.
Decreased DNA-binding activity. Decreased
transcriptional activity.
{ECO:0000269|PubMed:15299087}.
MUTAGEN 241 241 S->A: Decreased protein stability. No
effect on transcriptional activity.
{ECO:0000269|PubMed:16492674}.
MUTAGEN 259 259 S->A: No effect on protein stability. No
effect on transcriptional activity.
{ECO:0000269|PubMed:16492674}.
MUTAGEN 272 272 S->A: Decreased protein stability.
Decreased transcriptional activity.
{ECO:0000269|PubMed:16492674}.
CONFLICT 70 77 QPQPKDMV -> RSRSPRHG (in Ref. 5;
AAK13575). {ECO:0000305}.
CONFLICT 101 101 L -> Q (in Ref. 5; AAK13575).
{ECO:0000305}.
CONFLICT 180 180 V -> L (in Ref. 2; AAC72915).
{ECO:0000305}.
CONFLICT 199 202 RQPP -> ASPR (in Ref. 2; AAC72915).
{ECO:0000305}.
CONFLICT 426 426 D -> N (in Ref. 1; AAC18081 and 3;
AAP15181). {ECO:0000305}.
SEQUENCE 553 AA; 56789 MW; 59C6FB94303ED59A CRC64;
MQARYSVSSP NSLGVVPYLG GEQSYYRAAA AAAGGGYTAM PAPMSVYSHP AHAEQYPGGM
ARAYGPYTPQ PQPKDMVKPP YSYIALITMA IQNAPDKKIT LNGIYQFIMD RFPFYRDNKQ
GWQNSIRHNL SLNECFVKVP RDDKKPGKGS YWTLDPDSYN MFENGSFLRR RRRFKKKDAV
KDKEEKDRLH LKEPPPPGRQ PPPAPPEQAD GNAPGPQPPP VRIQDIKTEN GTCPSPPQPL
SPAAALGSGS AAAVPKIESP DSSSSSLSSG SSPPGSLPSA RPLSLDGADS APPPPAPSAP
PPHHSQGFSV DNIMTSLRGS PQSAAAELSS GLLASAAASS RAGIAPPLAL GAYSPGQSSL
YSSPCSQTSS AGSSGGGGGG AGAAGGAGGA GTYHCNLQAM SLYAAGERGG HLQGAPGGAG
GSAVDDPLPD YSLPPVTSSS SSSLSHGGGG GGGGGGQEAG HHPAAHQGRL TSWYLNQAGG
DLGHLASAAA AAAAAGYPGQ QQNFHSVREM FESQRIGLNN SPVNGNSSCQ MAFPSSQSLY
RTSGAFVYDC SKF


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