Q12948 (FOXC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Forkhead box protein C1

Alternative name(s):
Forkhead-related protein FKHL7
Forkhead-related transcription factor 3
Short name=FREAC-3

Gene names

Name:	FOXC1
Synonyms:	FKHL7, FREAC3

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	553 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Binding of FREAC-3 and FREAC-4 to their cognate sites results in bending of the DNA at an angle of 80-90 degrees.
Subunit structure	Monomer.
Subcellular location	Nucleus.
Tissue specificity	Expressed in all tissues and cell lines examined. Ref.5
Involvement in disease	Defects in FOXC1 are the cause of Axenfeld-Rieger syndrome type 3 (RIEG3) [MIM:602482]; also known as Axenfeld-Rieger syndrome (ARS) or Axenfeld syndrome or Axenfeld anomaly. It is characterized by posterior corneal embryotoxon, prominent Schwalbe line and iris adhesion to the Schwalbe line. Other features may be hypertelorism (wide spacing of the eyes), hypoplasia of the malar bones, congenital absence of some teeth and mental retardation. When associated with tooth anomalies, the disorder is known as Rieger syndrome. Glaucoma is a progressive blinding condition that occurs in approximately half of patients with Axenfeld-Rieger malformations. Ref.20 Defects in FOXC1 are the cause of iridogoniodysgenesis anomaly (IGDA) [MIM:601631]. IGDA is an autosomal dominant phenotype characterized by iris hypoplasia, goniodysgenesis, and juvenile glaucoma. Defects in FOXC1 are a cause of Peters anomaly (PAN) [MIM:604229]. Peters anomaly consists of a central corneal leukoma, absence of the posterior corneal stroma and Descemet membrane, and a variable degree of iris and lenticular attachments to the central aspect of the posterior cornea. Ref.14
Sequence similarities	Contains 1 fork-head DNA-binding domain.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Polymorphism
Disease	Disease mutation Peters anomaly
Ligand	DNA-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Uncategorized	promoter binding Inferred from Biological aspect of Ancestor. Source: RefGenome specific RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome specific transcriptional repressor activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription activator activity Inferred from Biological aspect of Ancestor. Source: RefGenome
Biological process	Notch signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome anti-apoptosis Inferred from Biological aspect of Ancestor. Source: RefGenome artery morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome blood vessel remodeling Inferred from Biological aspect of Ancestor. Source: RefGenome brain development Inferred from Biological aspect of Ancestor. Source: RefGenome camera-type eye development Inferred from Biological aspect of Ancestor. Source: RefGenome cardiac muscle cell proliferation Inferred from Biological aspect of Ancestor. Source: RefGenome collagen fibril organization Inferred from Biological aspect of Ancestor. Source: RefGenome embryonic heart tube development Inferred from Biological aspect of Ancestor. Source: RefGenome germ cell migration Inferred from Biological aspect of Ancestor. Source: RefGenome glycosaminoglycan metabolic process Inferred from Biological aspect of Ancestor. Source: RefGenome lacrimal gland development Inferred from Biological aspect of Ancestor. Source: RefGenome lymphangiogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome metanephros development Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of mitotic cell cycle Inferred from direct assay. Source: UniProtKB neural crest cell fate commitment Inferred from Biological aspect of Ancestor. Source: RefGenome odontogenesis of dentin-containing tooth Inferred from mutant phenotype Ref.14. Source: UniProtKB ossification Inferred from Biological aspect of Ancestor. Source: RefGenome ovarian follicle development Inferred from Biological aspect of Ancestor. Source: RefGenome paraxial mesodermal cell fate commitment Inferred from Biological aspect of Ancestor. Source: RefGenome positive regulation of transcription from RNA polymerase II promoter Inferred from direct assay. Source: BHF-UCL regulation of blood vessel size Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of organ growth Inferred from Biological aspect of Ancestor. Source: RefGenome regulation of sequence-specific DNA binding transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome somitogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome ureteric bud development Inferred from Biological aspect of Ancestor. Source: RefGenome vascular endothelial growth factor receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome vasculogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome ventricular cardiac muscle tissue morphogenesis Inferred from Biological aspect of Ancestor. Source: RefGenome
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nuclear heterochromatin Inferred from direct assay. Source: UniProtKB transcription factor complex Inferred from Biological aspect of Ancestor. Source: RefGenome
Molecular function	DNA binding, bending Inferred from direct assay Ref.6. Source: UniProtKB chromatin DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome double-stranded DNA binding Inferred from Biological aspect of Ancestor. Source: RefGenome sequence-specific DNA binding Inferred from direct assay Ref.17Ref.6. Source: UniProtKB sequence-specific distal enhancer binding RNA polymerase II transcription factor activity Inferred from Biological aspect of Ancestor. Source: RefGenome transcription factor binding Inferred from physical interaction. Source: UniProtKB transcription regulatory region DNA binding Inferred from sequence or structural similarity. Source: BHF-UCL
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PITX2	Q99697-3	6	EBI-1175253,EBI-1175243

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 553	553	Forkhead box protein C1		PRO_0000091806
Regions
	DNA binding	77 – 168	92	Fork-head
	Compositional bias	28 – 33	6	Poly-Ala
	Compositional bias	169 – 173	5	Poly-Arg
	Compositional bias	194 – 197	4	Poly-Pro
	Compositional bias	262 – 272	11	Poly-Ser
	Compositional bias	292 – 297	6	Poly-Pro
	Compositional bias	375 – 382	8	Poly-Gly
	Compositional bias	438 – 445	8	Poly-Ser
	Compositional bias	447 – 456	10	Poly-Gly
	Compositional bias	486 – 495	10	Poly-Ala
Amino acid modifications
	Modified residue	228	1	Phosphothreonine Ref.9
	Modified residue	232	1	Phosphothreonine Ref.9
	Modified residue	235	1	Phosphoserine Ref.7 Ref.8 Ref.9
	Modified residue	241	1	Phosphoserine Ref.7 Ref.8 Ref.9
	Modified residue	320	1	Phosphoserine Ref.7
Natural variations
	Natural variant	79	1	P → L in Rieger syndrome. Ref.10		VAR_058722
	Natural variant	79	1	P → R in ARS. Ref.18		VAR_058723
	Natural variant	79	1	P → T in ARS. Ref.11		VAR_058724
	Natural variant	82	1	S → T in ARS. Ref.2		VAR_007944
	Natural variant	86	1	L → F in ARS; does not affect nuclear localization of the protein; reduces DNA binding and significantly reduces transactivation. Ref.15		VAR_058725
	Natural variant	87	1	I → M in ARS. Ref.2		VAR_007945
	Natural variant	91	1	I → S in ARS. Ref.12		VAR_058726
	Natural variant	91	1	I → T in ARS. Ref.16		VAR_058727
	Natural variant	112	1	F → S in IGDA and PAN. Ref.1 Ref.14		VAR_007815
	Natural variant	115	1	Y → S in ARS. Ref.18		VAR_058728
	Natural variant	126	1	I → M in ARS; with glaucoma. Ref.1		VAR_007816
	Natural variant	127	1	R → H in ARS. Ref.12		VAR_058729
	Natural variant	130	1	L → F in RIEG3; expressed at levels similar to those of wild-type protein; migrates at an apparent reduced molecular weight compared with wild-type; has significantly impaired capacity to localize to the nucleus, binds DNA and transactivates reporter genes. Ref.20		VAR_058730
	Natural variant	131	1	S → L in ARS; with glaucoma. Ref.1 Ref.10		VAR_007817
	Natural variant	149	1	G → D in ARS. Ref.18		VAR_058731
	Natural variant	161	1	M → K in ARS; localized correctly to the nucleus; displays reduced DNA binding ability; disrupts FOXC1's transactivation ability. Ref.3 Ref.13 Ref.17		VAR_018150
	Natural variant	161	1	M → V in ARS. Ref.18		VAR_058732
	Natural variant	165	1	G → R in ARS; localized correctly to the nucleus; maintains wild-type levels of DNA binding; disrupts FOXC1's transactivation ability. Ref.17		VAR_058733
	Natural variant	169	1	R → P in ARS; localized correctly to the nucleus; displays reduced DNA binding ability; disrupts FOXC1's transactivation ability. Ref.17		VAR_058734
Experimental info
	Mutagenesis	86	1	L → P: Severely disrupts the protein function. Ref.15
	Sequence conflict	70 – 77	8	QPQPKDMV → RSRSPRHG in AAK13575. Ref.5
	Sequence conflict	101	1	L → Q in AAK13575. Ref.5
	Sequence conflict	180	1	V → L in AAC72915. Ref.2
	Sequence conflict	199 – 202	4	RQPP → ASPR in AAC72915. Ref.2
	Sequence conflict	426	1	D → N in AAC18081. Ref.1
	Sequence conflict	426	1	D → N in AAP15181. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q12948 [UniParc]. Last modified April 27, 2001. Version 3. Checksum: 59C6FB94303ED59A	FASTA	553	56,789
	10 20 30 40 50 60 MQARYSVSSP NSLGVVPYLG GEQSYYRAAA AAAGGGYTAM PAPMSVYSHP AHAEQYPGGM 70 80 90 100 110 120 ARAYGPYTPQ PQPKDMVKPP YSYIALITMA IQNAPDKKIT LNGIYQFIMD RFPFYRDNKQ 130 140 150 160 170 180 GWQNSIRHNL SLNECFVKVP RDDKKPGKGS YWTLDPDSYN MFENGSFLRR RRRFKKKDAV 190 200 210 220 230 240 KDKEEKDRLH LKEPPPPGRQ PPPAPPEQAD GNAPGPQPPP VRIQDIKTEN GTCPSPPQPL 250 260 270 280 290 300 SPAAALGSGS AAAVPKIESP DSSSSSLSSG SSPPGSLPSA RPLSLDGADS APPPPAPSAP 310 320 330 340 350 360 PPHHSQGFSV DNIMTSLRGS PQSAAAELSS GLLASAAASS RAGIAPPLAL GAYSPGQSSL 370 380 390 400 410 420 YSSPCSQTSS AGSSGGGGGG AGAAGGAGGA GTYHCNLQAM SLYAAGERGG HLQGAPGGAG 430 440 450 460 470 480 GSAVDDPLPD YSLPPVTSSS SSSLSHGGGG GGGGGGQEAG HHPAAHQGRL TSWYLNQAGG 490 500 510 520 530 540 DLGHLASAAA AAAAAGYPGQ QQNFHSVREM FESQRIGLNN SPVNGNSSCQ MAFPSSQSLY 550 RTSGAFVYDC SKF

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"The forkhead transcription factor gene FKHL7 is responsible for glaucoma phenotypes which map to 6p25." 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. Nat. Genet. 19:140-147(1998) [PubMed: 9620769] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-112; MET-126 AND LEU-131.
[2]	"Mutations of the forkhead/winged-helix gene, FKHL7, in patients with Axenfeld-Rieger anomaly." 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. Am. J. Hum. Genet. 63:1316-1328(1998) [PubMed: 9792859] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARS THR-82 AND MET-87.
[3]	"Mutation spectrum of FOXC1 and clinical genetic heterogeneity of Axenfeld-Rieger anomaly in India." Komatireddy S., Chakrabarti S., Mandal A.K., Reddy A.B.M., Sampath S., Panicker S.G., Balasubramanian D. Mol. Vis. 9:43-48(2003) [PubMed: 12592227] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT ARS LYS-161.
[4]	"The DNA sequence and analysis of human chromosome 6." 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. Nature 425:805-811(2003) [PubMed: 14574404] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	"Drosophila forkhead homologues are expressed in a lineage-restricted manner in human hematopoietic cells." Hromas R., Moore J., Johnston T., Socha C., Klemsz M. Blood 81:2854-2859(1993) [PubMed: 8499623] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 68-177, TISSUE SPECIFICITY. Tissue: Erythroleukemia.
[6]	"Cloning and characterization of seven human forkhead proteins: binding site specificity and DNA bending." Pierrou S., Hellqvist M., Samuelsson L., Enerbaeck S., Carlsson P. EMBO J. 13:5002-5012(1994) [PubMed: 7957066] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 73-178.
[7]	"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle." Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M. Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235; SER-241 AND SER-320, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-235 AND SER-241, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-228; THR-232; SER-235 AND SER-241, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"A spectrum of FOXC1 mutations suggests gene dosage as a mechanism for developmental defects of the anterior chamber of the eye." 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. Am. J. Hum. Genet. 68:364-372(2001) [PubMed: 11170889] [Abstract] Cited for: VARIANTS RIEGER SYNDROME LEU-79 AND LEU-131.
[11]	"A novel (Pro79Thr) mutation in the FKHL7 gene in a Japanese family with Axenfeld-Rieger syndrome." Suzuki T., Takahashi K., Kuwahara S., Wada Y., Abe T., Tamai M. Am. J. Ophthalmol. 132:572-575(2001) [PubMed: 11589884] [Abstract] Cited for: VARIANT ARS THR-79.
[12]	"Screening for mutations of Axenfeld-Rieger syndrome caused by FOXC1 gene in Japanese patients." Kawase C., Kawase K., Taniguchi T., Sugiyama K., Yamamoto T., Kitazawa Y., Alward W.L., Stone E.M., Nishimura D.Y., Sheffield V.C. J. Glaucoma 10:477-482(2001) [PubMed: 11740218] [Abstract] Cited for: VARIANTS ARS SER-91 AND HIS-127.
[13]	"Novel mutation in FOXC1 wing region causing Axenfeld-Rieger anomaly." Panicker S.G., Sampath S., Mandal A.K., Reddy A.B.M., Ahmed N., Hasnain S.E. Invest. Ophthalmol. Vis. Sci. 43:3613-3616(2002) [PubMed: 12454026] [Abstract] Cited for: VARIANT ARS LYS-161.
[14]	"A family with Axenfeld-Rieger syndrome and Peters Anomaly caused by a point mutation (Phe112Ser) in the FOXC1 gene." 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. Am. J. Ophthalmol. 135:368-375(2003) [PubMed: 12614756] [Abstract] Cited for: VARIANT PAN SER-112.
[15]	"Identification and analysis of a novel mutation in the FOXC1 forkhead domain." Saleem R.A., Murphy T.C., Liebmann J.M., Walter M.A. Invest. Ophthalmol. Vis. Sci. 44:4608-4612(2003) [PubMed: 14578375] [Abstract] Cited for: VARIANT ARS PHE-86, MUTAGENESIS OF LEU-86, CHARACTERIZATION OF VARIANT ARS PHE-86.
[16]	"Axenfeld-Rieger anomaly: a novel mutation in the forkhead box C1 (FOXC1) gene in a 4-generation family." Mortemousque B., Amati-Bonneau P., Couture F., Graffan R., Dubois S., Colin J., Bonneau D., Morissette J., Lacombe D., Raymond V. Arch. Ophthalmol. 122:1527-1533(2004) [PubMed: 15477465] [Abstract] Cited for: VARIANT ARS THR-91.
[17]	"The wing 2 region of the FOXC1 forkhead domain is necessary for normal DNA-binding and transactivation functions." Murphy T.C., Saleem R.A., Footz T., Ritch R., McGillivray B., Walter M.A. Invest. Ophthalmol. Vis. Sci. 45:2531-2538(2004) [PubMed: 15277473] [Abstract] Cited for: VARIANTS ARS ARG-165 AND PRO-169, CHARACTERIZATION OF VARIANTS ARS LYS-161; ARG-165 AND PRO-169.
[18]	"Novel mutations of FOXC1 and PITX2 in patients with Axenfeld-Rieger malformations." Weisschuh N., Dressler P., Schuettauf F., Wolf C., Wissinger B., Gramer E. Invest. Ophthalmol. Vis. Sci. 47:3846-3852(2006) [PubMed: 16936096] [Abstract] Cited for: VARIANTS ARS ARG-79; SER-115; ASP-149 AND VAL-161.
[19]	Erratum Weisschuh N., Dressler P., Schuettauf F., Wolf C., Wissinger B., Gramer E. Invest. Ophthalmol. Vis. Sci. 47:5162-5162(2006)
[20]	"Analyses of a novel L130F missense mutation in FOXC1." Ito Y.A., Footz T.K., Murphy T.C., Courtens W., Walter M.A. Arch. Ophthalmol. 125:128-135(2007) [PubMed: 17210863] [Abstract] Cited for: VARIANT RIEG3 PHE-130, CHARACTERIZATION OF VARIANT RIEG3 PHE-130.
+	Additional computationally mapped references.

Web resources

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF048693 Genomic DNA. Translation: AAC18081.1. AF078096 Genomic DNA. Translation: AAC72915.1. AY228704 Genomic DNA. Translation: AAP15181.1. AL034344 Genomic DNA. Translation: CAB81658.1. L12143 mRNA. Translation: AAK13575.1. U13221 mRNA. Translation: AAA92038.1.
IPI	IPI00290377.
PIR	S51626.
RefSeq	NP_001444.2. NM_001453.2.
UniGene	Hs.348883.
3D structure databases
ProteinModelPortal	Q12948.
SMR	Q12948. Positions 76-168.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q12948. 1 interaction.
STRING	Q12948.
PTM databases
PhosphoSite	Q12948.
Polymorphism databases
DMDM	13638267.
Proteomic databases
PRIDE	Q12948.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000380874; ENSP00000370256; ENSG00000054598.
GeneID	2296.
KEGG	hsa:2296.
UCSC	uc003mtp.1. human.
Organism-specific databases
CTD	2296.
GeneCards	GC06P001610.
H-InvDB	HIX0032962.
HGNC	HGNC:3800. FOXC1.
HPA	HPA040670.
MIM	601090. gene. 601631. phenotype. 602482. phenotype. 604229. phenotype.
neXtProt	NX_Q12948.
Orphanet	782. Axenfeld-Rieger syndrome. 708. Peters anomaly. 91483. Rieger-Axenfeld anomaly.
PharmGKB	PA28217.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05733.
HOGENOM	HBG269707.
HOVERGEN	HBG051640.
InParanoid	Q12948.
OMA	QRIGLNN.
OrthoDB	EOG479F8T.
PhylomeDB	Q12948.
Gene expression databases
ArrayExpress	Q12948.
Bgee	Q12948.
CleanEx	HS_FOXC1.
Genevestigator	Q12948.
GermOnline	ENSG00000054598. Homo sapiens.
Family and domain databases
InterPro	IPR001766. TF_fork_head. IPR018122. TF_fork_head_CS. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K09396.
Pfam	PF00250. Fork_head. 1 hit. [Graphical view]
PRINTS	PR00053. FORKHEAD.
SMART	SM00339. FH. 1 hit. [Graphical view]
PROSITE	PS00657. FORK_HEAD_1. 1 hit. PS00658. FORK_HEAD_2. 1 hit. PS50039. FORK_HEAD_3. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	9319.
SOURCE	Search...

Entry information

Entry name

FOXC1_HUMAN

Accession

Primary (citable) accession number: Q12948
Secondary accession number(s): Q86UP7 , Q9BYM1, Q9NUE5, Q9UDD0, Q9UP06

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	April 27, 2001
Last modified:	January 25, 2012
This is version 120 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.