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Protein

Forkhead box protein C1

Gene

FOXC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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).By similarity21 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
DNA bindingi77 – 168Fork-headPROSITE-ProRule annotationAdd BLAST92

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionActivator, Developmental protein, DNA-binding, Repressor
Biological processAngiogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

SignaLinkiQ12948
SIGNORiQ12948

Names & Taxonomyi

Protein namesi
Recommended name:
Forkhead box protein C1
Alternative name(s):
Forkhead-related protein FKHL7
Forkhead-related transcription factor 3
Short name:
FREAC-3
Gene namesi
Name:FOXC1
Synonyms:FKHL7, FREAC3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

EuPathDBiHostDB:ENSG00000054598.6
HGNCiHGNC:3800 FOXC1
MIMi601090 gene
neXtProtiNX_Q12948

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Axenfeld-Rieger syndrome 3 (RIEG3)20 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:602482
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05872279P → 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. 2 Publications1
Natural variantiVAR_05872379P → R in RIEG3. 1 Publication1
Natural variantiVAR_05872479P → 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. 2 Publications1
Natural variantiVAR_00794482S → T in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 3 PublicationsCorresponds to variant dbSNP:rs104893953EnsemblClinVar.1
Natural variantiVAR_07850185A → P in RIEG3; unknown pathological significance. 1 Publication1
Natural variantiVAR_05872586L → F in RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 1 PublicationCorresponds to variant dbSNP:rs886039568EnsemblClinVar.1
Natural variantiVAR_00794587I → M in RIEG3; loss of protein stability. 2 PublicationsCorresponds to variant dbSNP:rs104893954EnsemblClinVar.1
Natural variantiVAR_05872691I → 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. 2 Publications1
Natural variantiVAR_05872791I → 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. 2 Publications1
Natural variantiVAR_058728115Y → S in RIEG3. 1 Publication1
Natural variantiVAR_078503126I → 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. 1 PublicationCorresponds to variant dbSNP:rs483352810EnsemblClinVar.1
Natural variantiVAR_058729127R → H in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 3 Publications1
Natural variantiVAR_078504127R → L in RIEG3. 1 Publication1
Natural variantiVAR_078505128H → 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. 1 Publication1
Natural variantiVAR_058730130L → 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. 2 PublicationsCorresponds to variant dbSNP:rs121909338EnsemblClinVar.1
Natural variantiVAR_078507135C → 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. 1 Publication1
Natural variantiVAR_058731149G → D in RIEG3. 1 Publication1
Natural variantiVAR_058732161M → 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. 2 Publications1
Natural variantiVAR_058733165G → 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. 1 Publication1
Natural variantiVAR_058734169R → P in RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 1 Publication1
Natural variantiVAR_078510170R → W in RIEG3; unknown pathological significance. 1 Publication1
Anterior segment dysgenesis 3 (ASGD3)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:601631
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_078502109M → V in ASGD3. 1 PublicationCorresponds to variant dbSNP:rs917382067Ensembl.1
Natural variantiVAR_078506131S → W in ASGD3. 1 Publication1
Natural variantiVAR_078508138K → E in ASGD3. 1 Publication1
Natural variantiVAR_078509152W → 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. 1 Publication1
Natural variantiVAR_078511297P → 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. 1 PublicationCorresponds to variant dbSNP:rs79691946EnsemblClinVar.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi68T → A: No effect on protein stability. No effect on transcriptional activity. 1 Publication1
Mutagenesisi79P → A: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi79P → E: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi79P → K: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi86L → A: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi86L → E: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi86L → K: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi86L → P: Severely disrupts the protein function. 1 Publication1
Mutagenesisi87I → A, E or K: Loss of protein stability. 1 Publication1
Mutagenesisi91I → A: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi91I → E: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi91I → K: Decreased nuclear localization. No effect on DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi126I → A: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi126I → E: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi126I → K: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi127R → A: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi127R → E: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi127R → K: Decreased nuclear localization. Decreased DNA-binding activity. Decreased transcriptional activity. 1 Publication1
Mutagenesisi241S → A: Decreased protein stability. No effect on transcriptional activity. 1 Publication1
Mutagenesisi259S → A: No effect on protein stability. No effect on transcriptional activity. 1 Publication1
Mutagenesisi272S → A: Decreased protein stability. Decreased transcriptional activity. 1 Publication1

Keywords - Diseasei

Deafness, Disease mutation, Peters anomaly

Organism-specific databases

DisGeNETi2296
MalaCardsiFOXC1
MIMi601631 phenotype
602482 phenotype
OpenTargetsiENSG00000054598
Orphaneti98978 Axenfeld anomaly
782 Axenfeld-Rieger syndrome
708 Peters anomaly
91483 Rieger anomaly
PharmGKBiPA28217

Polymorphism and mutation databases

BioMutaiFOXC1
DMDMi13638267

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000918061 – 553Forkhead box protein C1Add BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei235PhosphoserineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei272Phosphoserine1 Publication1
Modified residuei320PhosphoserineCombined sources1
Modified residuei521PhosphoserineCombined sources1

Post-translational modificationi

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).4 Publications
Sumoylated preferentially with SUMO2 or SUMO3 (PubMed:22493429). Desumoylated by SENP2 (PubMed:22493429).1 Publication
Ubiquitinated, leading to its proteasomal degradation (PubMed:16492674).1 Publication

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiQ12948
PeptideAtlasiQ12948
PRIDEiQ12948

PTM databases

iPTMnetiQ12948
PhosphoSitePlusiQ12948

Expressioni

Tissue specificityi

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).5 Publications

Inductioni

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).2 Publications

Gene expression databases

BgeeiENSG00000054598
CleanExiHS_FOXC1
ExpressionAtlasiQ12948 baseline and differential
GenevisibleiQ12948 HS

Organism-specific databases

HPAiHPA040670

Interactioni

Subunit structurei

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).4 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • transcription coactivator binding Source: UniProtKB
  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108585, 51 interactors
IntActiQ12948, 43 interactors
MINTiQ12948
STRINGi9606.ENSP00000370256

Structurei

3D structure databases

ProteinModelPortaliQ12948
SMRiQ12948
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 51Required for transcriptional activation1 PublicationAdd BLAST51
Regioni215 – 366Required for transcriptional inhibition1 PublicationAdd BLAST152
Regioni466 – 553Required for transcriptional activation1 PublicationAdd BLAST88

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi78 – 93Nuclear localization signal 1 (NLS 1)1 PublicationAdd BLAST16
Motifi168 – 176Nuclear localization signal 2 (NLS 2)1 Publication9

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi28 – 33Poly-Ala6
Compositional biasi169 – 173Poly-Arg5
Compositional biasi194 – 197Poly-Pro4
Compositional biasi262 – 272Poly-SerAdd BLAST11
Compositional biasi292 – 297Poly-Pro6
Compositional biasi375 – 382Poly-Gly8
Compositional biasi438 – 445Poly-Ser8
Compositional biasi447 – 456Poly-Gly10
Compositional biasi486 – 495Poly-Ala10

Phylogenomic databases

eggNOGiKOG2294 Eukaryota
COG5025 LUCA
GeneTreeiENSGT00760000118904
HOVERGENiHBG051640
InParanoidiQ12948
KOiK09396
OMAiYSSPCSQ
OrthoDBiEOG091G0HW9
PhylomeDBiQ12948
TreeFamiTF316127

Family and domain databases

CDDicd00059 FH, 1 hit
Gene3Di1.10.10.10, 1 hit
InterProiView protein in InterPro
IPR001766 Fork_head_dom
IPR018122 TF_fork_head_CS_1
IPR030456 TF_fork_head_CS_2
IPR036388 WH-like_DNA-bd_sf
IPR036390 WH_DNA-bd_sf
PfamiView protein in Pfam
PF00250 Forkhead, 1 hit
PRINTSiPR00053 FORKHEAD
SMARTiView protein in SMART
SM00339 FH, 1 hit
SUPFAMiSSF46785 SSF46785, 1 hit
PROSITEiView protein in PROSITE
PS00657 FORK_HEAD_1, 1 hit
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit

Sequencei

Sequence statusi: Complete.

Q12948-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQARYSVSSP NSLGVVPYLG GEQSYYRAAA AAAGGGYTAM PAPMSVYSHP
60 70 80 90 100
AHAEQYPGGM ARAYGPYTPQ PQPKDMVKPP YSYIALITMA IQNAPDKKIT
110 120 130 140 150
LNGIYQFIMD RFPFYRDNKQ GWQNSIRHNL SLNECFVKVP RDDKKPGKGS
160 170 180 190 200
YWTLDPDSYN MFENGSFLRR RRRFKKKDAV KDKEEKDRLH LKEPPPPGRQ
210 220 230 240 250
PPPAPPEQAD GNAPGPQPPP VRIQDIKTEN GTCPSPPQPL SPAAALGSGS
260 270 280 290 300
AAAVPKIESP DSSSSSLSSG SSPPGSLPSA RPLSLDGADS APPPPAPSAP
310 320 330 340 350
PPHHSQGFSV DNIMTSLRGS PQSAAAELSS GLLASAAASS RAGIAPPLAL
360 370 380 390 400
GAYSPGQSSL YSSPCSQTSS AGSSGGGGGG AGAAGGAGGA GTYHCNLQAM
410 420 430 440 450
SLYAAGERGG HLQGAPGGAG GSAVDDPLPD YSLPPVTSSS SSSLSHGGGG
460 470 480 490 500
GGGGGGQEAG HHPAAHQGRL TSWYLNQAGG DLGHLASAAA AAAAAGYPGQ
510 520 530 540 550
QQNFHSVREM FESQRIGLNN SPVNGNSSCQ MAFPSSQSLY RTSGAFVYDC

SKF
Length:553
Mass (Da):56,789
Last modified:April 27, 2001 - v3
Checksum:i59C6FB94303ED59A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti70 – 77QPQPKDMV → RSRSPRHG in AAK13575 (PubMed:8499623).Curated8
Sequence conflicti101L → Q in AAK13575 (PubMed:8499623).Curated1
Sequence conflicti180V → L in AAC72915 (PubMed:9792859).Curated1
Sequence conflicti199 – 202RQPP → ASPR in AAC72915 (PubMed:9792859).Curated4
Sequence conflicti426D → N in AAC18081 (PubMed:9620769).Curated1
Sequence conflicti426D → N in AAP15181 (PubMed:12592227).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05872279P → 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. 2 Publications1
Natural variantiVAR_05872379P → R in RIEG3. 1 Publication1
Natural variantiVAR_05872479P → 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. 2 Publications1
Natural variantiVAR_00794482S → T in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 3 PublicationsCorresponds to variant dbSNP:rs104893953EnsemblClinVar.1
Natural variantiVAR_07850185A → P in RIEG3; unknown pathological significance. 1 Publication1
Natural variantiVAR_05872586L → F in RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 1 PublicationCorresponds to variant dbSNP:rs886039568EnsemblClinVar.1
Natural variantiVAR_00794587I → M in RIEG3; loss of protein stability. 2 PublicationsCorresponds to variant dbSNP:rs104893954EnsemblClinVar.1
Natural variantiVAR_05872691I → 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. 2 Publications1
Natural variantiVAR_05872791I → 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. 2 Publications1
Natural variantiVAR_078502109M → V in ASGD3. 1 PublicationCorresponds to variant dbSNP:rs917382067Ensembl.1
Natural variantiVAR_007815112F → S in ASGD3 and RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 4 PublicationsCorresponds to variant dbSNP:rs104893951EnsemblClinVar.1
Natural variantiVAR_058728115Y → S in RIEG3. 1 Publication1
Natural variantiVAR_007816126I → 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. 3 PublicationsCorresponds to variant dbSNP:rs104893958EnsemblClinVar.1
Natural variantiVAR_078503126I → 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. 1 PublicationCorresponds to variant dbSNP:rs483352810EnsemblClinVar.1
Natural variantiVAR_058729127R → H in RIEG3; decreased location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 3 Publications1
Natural variantiVAR_078504127R → L in RIEG3. 1 Publication1
Natural variantiVAR_078505128H → 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. 1 Publication1
Natural variantiVAR_058730130L → 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. 2 PublicationsCorresponds to variant dbSNP:rs121909338EnsemblClinVar.1
Natural variantiVAR_007817131S → 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. 5 PublicationsCorresponds to variant dbSNP:rs104893957EnsemblClinVar.1
Natural variantiVAR_078506131S → W in ASGD3. 1 Publication1
Natural variantiVAR_078507135C → 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. 1 Publication1
Natural variantiVAR_078508138K → E in ASGD3. 1 Publication1
Natural variantiVAR_058731149G → D in RIEG3. 1 Publication1
Natural variantiVAR_078509152W → 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. 1 Publication1
Natural variantiVAR_018150161M → 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. 4 Publications1
Natural variantiVAR_058732161M → 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. 2 Publications1
Natural variantiVAR_058733165G → 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. 1 Publication1
Natural variantiVAR_058734169R → P in RIEG3; no change in location at the nucleus; decreased transcription regulatory region DNA binding; decreased sequence-specific DNA binding transcription factor activity. 1 Publication1
Natural variantiVAR_078510170R → W in RIEG3; unknown pathological significance. 1 Publication1
Natural variantiVAR_078511297P → 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. 1 PublicationCorresponds to variant dbSNP:rs79691946EnsemblClinVar.1
Natural variantiVAR_078512368T → 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. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF048693 Genomic DNA Translation: AAC18081.1
AF078096 Genomic DNA Translation: AAC72915.1
AY228704 Genomic DNA Translation: AAP15181.1
AL034344 Genomic DNA No translation available.
L12143 mRNA Translation: AAK13575.1
U13221 mRNA Translation: AAA92038.1
CCDSiCCDS4473.1
PIRiS51626
RefSeqiNP_001444.2, NM_001453.2
UniGeneiHs.348883

Genome annotation databases

EnsembliENST00000380874; ENSP00000370256; ENSG00000054598
GeneIDi2296
KEGGihsa:2296

Keywords - Coding sequence diversityi

Polymorphism

Similar proteinsi

Entry informationi

Entry nameiFOXC1_HUMAN
AccessioniPrimary (citable) accession number: Q12948
Secondary accession number(s): Q86UP7
, Q9BYM1, Q9NUE5, Q9UDD0, Q9UP06
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: May 23, 2018
This is version 182 of the entry and version 3 of the sequence. See complete history.
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

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