FOXC1
entrez
2296
canonical
uniprot
Q12948
canonical
ensembl
ENSG00000054598
resolver
ensp
ENSP00000493906
resolver
enst
ENST00000645831
resolver
genesymbol
FOXC1
resolver
genesymbol_syn
FKHL7
resolver
genesymbol_syn
FREAC3
resolver
hgnc
HGNC:3800
resolver
uniprot
Q86UP7
resolver
uniprot
Q9BYM1
resolver
uniprot
Q9NUE5
resolver
uniprot
Q9UDD0
resolver
uniprot
Q9UP06
resolver
uniprot_entry
FOXC1_HUMAN
resolver
uniprot_sec
Q86UP7
resolver
uniprot_sec
Q9BYM1
resolver
uniprot_sec
Q9NUE5
resolver
uniprot_sec
Q9UDD0
resolver
uniprot_sec
Q9UP06
resolver
amino_acid_sequence
MQARYSVSSPNSLGVVPYLGGEQSYYRAAAAAAGGGYTAMPAPMSVYSHPAHAEQYPGGMARAYGPYTPQPQPKDMVKPPYSYIALITMAIQNAPDKKITLNGIYQFIMDRFPFYRDNKQGWQNSIRHNLSLNECFVKVPRDDKKPGKGSYWTLDPDSYNMFENGSFLRRRRRFKKKDAVKDKEEKDRLHLKEPPPPGRQPPPAPPEQADGNAPGPQPPPVRIQDIKTENGTCPSPPQPLSPAAALGSGSAAAVPKIESPDSSSSSLSSGSSPPGSLPSARPLSLDGADSAPPPPAPSAPPPHHSQGFSVDNIMTSLRGSPQSAAAELSSGLLASAAASSRAGIAPPLALGAYSPGQSSLYSSPCSQTSSAGSSGGGGGGAGAAGGAGGAGTYHCNLQAMSLYAAGERGGHLQGAPGGAGGSAVDDPLPDYSLPPVTSSSSSSLSHGGGGGGGGGGQEAGHHPAAHQGRLTSWYLNQAGGDLGHLASAAAAAAAAGYPGQQQNFHSVREMFESQRIGLNNSPVNGNSSCQMAFPSSQSLYRTSGAFVYDCSKF
uniprot
proteins
disease_involvement
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 variants 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 variants affecting the gene represented in this entry.
uniprot
proteins
function
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:14506133, PubMed:14578375, PubMed:15277473, PubMed:15299087, PubMed:15684392, PubMed:16449236, PubMed:16492674, PubMed:17210863, PubMed:19279310, PubMed:19793056, PubMed:25786029, PubMed:27804176, PubMed:27907090). 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:11782474, PubMed:12533514, PubMed:14506133, PubMed:19793056, PubMed:27804176, PubMed:7957066). Upon DNA-binding, promotes DNA bending (PubMed:14506133, PubMed:7957066). 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). Also acts 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}.
uniprot
proteins
mass_dalton
56789
uniprot
proteins
mutagenesis
MUTAGEN 68; /note="T->A: No effect on protein stability. No effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:16492674"; MUTAGEN 79; /note="P->A: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 79; /note="P->E: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 79; /note="P->K: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 86; /note="L->A: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 86; /note="L->E: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 86; /note="L->K: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 86; /note="L->P: Severely disrupts the protein function."; /evidence="ECO:0000269|PubMed:14578375"; MUTAGEN 87; /note="I->A,E,K: Loss of protein stability."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 91; /note="I->A: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 91; /note="I->E: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 91; /note="I->K: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 126; /note="I->A: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 126; /note="I->E: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 126; /note="I->K: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 127; /note="R->A: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 127; /note="R->E: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 127; /note="R->K: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:15299087"; MUTAGEN 241; /note="S->A: Decreased protein stability. No effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:16492674"; MUTAGEN 259; /note="S->A: No effect on protein stability. No effect on transcriptional activity."; /evidence="ECO:0000269|PubMed:16492674"; MUTAGEN 272; /note="S->A: Decreased protein stability. Decreased transcriptional activity."; /evidence="ECO:0000269|PubMed:16492674
uniprot
proteins
post_translational_modification
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}.
uniprot
proteins
pubmed
11170889
uniprot
proteins
pubmed
11179011
uniprot
proteins
pubmed
11589884
uniprot
proteins
pubmed
11740218
uniprot
proteins
pubmed
11782474
uniprot
proteins
pubmed
12408963
uniprot
proteins
pubmed
12454026
uniprot
proteins
pubmed
12533514
uniprot
proteins
pubmed
12592227
uniprot
proteins
pubmed
12614756
uniprot
proteins
pubmed
14506133
uniprot
proteins
pubmed
14574404
uniprot
proteins
pubmed
14578375
uniprot
proteins
pubmed
15277473
uniprot
proteins
pubmed
15299087
uniprot
proteins
pubmed
15477465
uniprot
proteins
pubmed
15684392
uniprot
proteins
pubmed
16449236
uniprot
proteins
pubmed
16492674
uniprot
proteins
pubmed
16936096
uniprot
proteins
pubmed
17210863
uniprot
proteins
pubmed
17653043
uniprot
proteins
pubmed
17993506
uniprot
proteins
pubmed
18484311
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18676636
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19279310
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
19793056
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20406990
uniprot
proteins
pubmed
20881294
uniprot
proteins
pubmed
22493429
uniprot
proteins
pubmed
22991501
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23239455
uniprot
proteins
pubmed
24914578
uniprot
proteins
pubmed
25786029
uniprot
proteins
pubmed
26565916
uniprot
proteins
pubmed
27804176
uniprot
proteins
pubmed
27907090
uniprot
proteins
pubmed
7957066
uniprot
proteins
pubmed
8499623
uniprot
proteins
pubmed
9620769
uniprot
proteins
pubmed
9792859
uniprot
proteins
sequence_length
553
uniprot
proteins
subcellular_location
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}.
uniprot
proteins