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Q12948 (FOXC1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 120. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
Protein existenceEvidence 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 processTranscription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityPolymorphism
   DiseaseDisease mutation
Peters anomaly
   LigandDNA-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Uncategorizedpromoter 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 processNotch 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 componentcytoplasm

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 functionDNA 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

PITX2Q99697-36EBI-1175253,EBI-1175243

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 553553Forkhead box protein C1
PRO_0000091806

Regions

DNA binding77 – 16892Fork-head
Compositional bias28 – 336Poly-Ala
Compositional bias169 – 1735Poly-Arg
Compositional bias194 – 1974Poly-Pro
Compositional bias262 – 27211Poly-Ser
Compositional bias292 – 2976Poly-Pro
Compositional bias375 – 3828Poly-Gly
Compositional bias438 – 4458Poly-Ser
Compositional bias447 – 45610Poly-Gly
Compositional bias486 – 49510Poly-Ala

Amino acid modifications

Modified residue2281Phosphothreonine Ref.9
Modified residue2321Phosphothreonine Ref.9
Modified residue2351Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue2411Phosphoserine Ref.7 Ref.8 Ref.9
Modified residue3201Phosphoserine Ref.7

Natural variations

Natural variant791P → L in Rieger syndrome. Ref.10
VAR_058722
Natural variant791P → R in ARS. Ref.18
VAR_058723
Natural variant791P → T in ARS. Ref.11
VAR_058724
Natural variant821S → T in ARS. Ref.2
VAR_007944
Natural variant861L → F in ARS; does not affect nuclear localization of the protein; reduces DNA binding and significantly reduces transactivation. Ref.15
VAR_058725
Natural variant871I → M in ARS. Ref.2
VAR_007945
Natural variant911I → S in ARS. Ref.12
VAR_058726
Natural variant911I → T in ARS. Ref.16
VAR_058727
Natural variant1121F → S in IGDA and PAN. Ref.1 Ref.14
VAR_007815
Natural variant1151Y → S in ARS. Ref.18
VAR_058728
Natural variant1261I → M in ARS; with glaucoma. Ref.1
VAR_007816
Natural variant1271R → H in ARS. Ref.12
VAR_058729
Natural variant1301L → 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 variant1311S → L in ARS; with glaucoma. Ref.1 Ref.10
VAR_007817
Natural variant1491G → D in ARS. Ref.18
VAR_058731
Natural variant1611M → 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 variant1611M → V in ARS. Ref.18
VAR_058732
Natural variant1651G → 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 variant1691R → P in ARS; localized correctly to the nucleus; displays reduced DNA binding ability; disrupts FOXC1's transactivation ability. Ref.17
VAR_058734

Experimental info

Mutagenesis861L → P: Severely disrupts the protein function. Ref.15
Sequence conflict70 – 778QPQPKDMV → RSRSPRHG in AAK13575. Ref.5
Sequence conflict1011L → Q in AAK13575. Ref.5
Sequence conflict1801V → L in AAC72915. Ref.2
Sequence conflict199 – 2024RQPP → ASPR in AAC72915. Ref.2
Sequence conflict4261D → N in AAC18081. Ref.1
Sequence conflict4261D → N in AAP15181. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Q12948 [UniParc].

Last modified April 27, 2001. Version 3.
Checksum: 59C6FB94303ED59A

FASTA55356,789
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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

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.
IPIIPI00290377.
PIRS51626.
RefSeqNP_001444.2. NM_001453.2.
UniGeneHs.348883.

3D structure databases

ProteinModelPortalQ12948.
SMRQ12948. Positions 76-168.
ModBaseSearch...

Protein-protein interaction databases

IntActQ12948. 1 interaction.
STRINGQ12948.

PTM databases

PhosphoSiteQ12948.

Polymorphism databases

DMDM13638267.

Proteomic databases

PRIDEQ12948.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000380874; ENSP00000370256; ENSG00000054598.
GeneID2296.
KEGGhsa:2296.
UCSCuc003mtp.1. human.

Organism-specific databases

CTD2296.
GeneCardsGC06P001610.
H-InvDBHIX0032962.
HGNCHGNC:3800. FOXC1.
HPAHPA040670.
MIM601090. gene.
601631. phenotype.
602482. phenotype.
604229. phenotype.
neXtProtNX_Q12948.
Orphanet782. Axenfeld-Rieger syndrome.
708. Peters anomaly.
91483. Rieger-Axenfeld anomaly.
PharmGKBPA28217.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG05733.
HOGENOMHBG269707.
HOVERGENHBG051640.
InParanoidQ12948.
OMAQRIGLNN.
OrthoDBEOG479F8T.
PhylomeDBQ12948.

Gene expression databases

ArrayExpressQ12948.
BgeeQ12948.
CleanExHS_FOXC1.
GenevestigatorQ12948.
GermOnlineENSG00000054598. Homo sapiens.

Family and domain databases

InterProIPR001766. TF_fork_head.
IPR018122. TF_fork_head_CS.
IPR011991. WHTH_trsnscrt_rep_DNA-bd.
[Graphical view]
Gene3DG3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KOK09396.
PfamPF00250. Fork_head. 1 hit.
[Graphical view]
PRINTSPR00053. FORKHEAD.
SMARTSM00339. FH. 1 hit.
[Graphical view]
PROSITEPS00657. FORK_HEAD_1. 1 hit.
PS00658. FORK_HEAD_2. 1 hit.
PS50039. FORK_HEAD_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio9319.
SOURCESearch...

Entry information

Entry nameFOXC1_HUMAN
AccessionPrimary (citable) accession number: Q12948
Secondary accession number(s): Q86UP7 expand/collapse secondary AC list , 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 statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families