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Protein

Forkhead box protein C1

Gene

FOXC1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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
<p>This subsection of the ‘Function’ section specifies the position and type of each DNA-binding domain present within the protein.<p><a href='/help/dna_bind' target='_top'>More...</a></p>DNA bindingi77 – 168Fork-headPROSITE-ProRule annotationAdd BLAST92

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

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

Enzyme and pathway databases

SignaLink: a signaling pathway resource with multi-layered regulatory networks

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SignaLinki
Q12948

SIGNOR Signaling Network Open Resource

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SIGNORi
Q12948

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Forkhead box protein C1
Alternative name(s):
Forkhead-related protein FKHL7
Forkhead-related transcription factor 3
Short name:
FREAC-3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:FOXC1
Synonyms:FKHL7, FREAC3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 6

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000054598.6

Human Gene Nomenclature Database

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HGNCi
HGNC:3800 FOXC1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
601090 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_Q12948

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section provides information on the disease(s) associated with genetic variations in a given protein. The information is extracted from the scientific literature and diseases that are also described in the <a href="http://www.ncbi.nlm.nih.gov/sites/entrez?db=omim">OMIM</a> database are represented with a <a href="http://www.uniprot.org/diseases">controlled vocabulary</a> in the following way:<p><a href='/help/involvement_in_disease' target='_top'>More...</a></p>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
<p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>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_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 PublicationCorresponds to variant dbSNP:rs1085307884Ensembl.1
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_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_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
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_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_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_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_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_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_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
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>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

DisGeNET

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DisGeNETi
2296

MalaCards human disease database

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MalaCardsi
FOXC1
MIMi601631 phenotype
602482 phenotype

Open Targets

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OpenTargetsi
ENSG00000054598

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
98978 Axenfeld anomaly
782 Axenfeld-Rieger syndrome
250923 Isolated aniridia
708 Peters anomaly
91483 Rieger anomaly

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28217

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FOXC1

Domain mapping of disease mutations (DMDM)

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DMDMi
13638267

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000918061 – 553Forkhead box protein C1Add BLAST553

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei235PhosphoserineCombined sources1
Modified residuei241PhosphoserineCombined sources1
Modified residuei272Phosphoserine1 Publication1
Modified residuei320PhosphoserineCombined sources1
Modified residuei521PhosphoserineCombined sources1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

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EPDi
Q12948

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q12948

PaxDb, a database of protein abundance averages across all three domains of life

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PaxDbi
Q12948

PeptideAtlas

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PeptideAtlasi
Q12948

PRoteomics IDEntifications database

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PRIDEi
Q12948

ProteomicsDB human proteome resource

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ProteomicsDBi
59043

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
Q12948

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

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PhosphoSitePlusi
Q12948

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>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

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000054598 Expressed in 219 organ(s), highest expression level in parotid gland

CleanEx database of gene expression profiles

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CleanExi
HS_FOXC1

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q12948 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q12948 HS

Organism-specific databases

Human Protein Atlas

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HPAi
HPA040670

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>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

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
108585, 53 interactors

Protein interaction database and analysis system

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IntActi
Q12948, 43 interactors

Molecular INTeraction database

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MINTi
Q12948

STRING: functional protein association networks

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STRINGi
9606.ENSP00000370256

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
Q12948

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q12948

Database of comparative protein structure models

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ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>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
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2294 Eukaryota
COG5025 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00940000162303

The HOVERGEN Database of Homologous Vertebrate Genes

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HOVERGENi
HBG051640

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q12948

KEGG Orthology (KO)

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KOi
K09396

Identification of Orthologs from Complete Genome Data

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OMAi
GRLTSWY

Database of Orthologous Groups

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OrthoDBi
1270467at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q12948

TreeFam database of animal gene trees

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TreeFami
TF316127

Family and domain databases

Conserved Domains Database

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CDDi
cd00059 FH, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
1.10.10.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View 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

Pfam protein domain database

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Pfami
View protein in Pfam
PF00250 Forkhead, 1 hit

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00053 FORKHEAD

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00339 FH, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF46785 SSF46785, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS00657 FORK_HEAD_1, 1 hit
PS00658 FORK_HEAD_2, 1 hit
PS50039 FORK_HEAD_3, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i59C6FB94303ED59A
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>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 PublicationCorresponds to variant dbSNP:rs1085307884Ensembl.1
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:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS4473.1

Protein sequence database of the Protein Information Resource

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PIRi
S51626

NCBI Reference Sequences

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RefSeqi
NP_001444.2, NM_001453.2

UniGene gene-oriented nucleotide sequence clusters

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UniGenei
Hs.348883

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000380874; ENSP00000370256; ENSG00000054598
ENST00000645831; ENSP00000493906; ENSG00000054598

Database of genes from NCBI RefSeq genomes

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GeneIDi
2296

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:2296

Keywords - Coding sequence diversityi

Polymorphism

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

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

3D structure databases

ProteinModelPortaliQ12948
SMRiQ12948
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108585, 53 interactors
IntActiQ12948, 43 interactors
MINTiQ12948
STRINGi9606.ENSP00000370256

PTM databases

iPTMnetiQ12948
PhosphoSitePlusiQ12948

Polymorphism and mutation databases

BioMutaiFOXC1
DMDMi13638267

Proteomic databases

EPDiQ12948
jPOSTiQ12948
PaxDbiQ12948
PeptideAtlasiQ12948
PRIDEiQ12948
ProteomicsDBi59043

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000380874; ENSP00000370256; ENSG00000054598
ENST00000645831; ENSP00000493906; ENSG00000054598
GeneIDi2296
KEGGihsa:2296

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
2296
DisGeNETi2296
EuPathDBiHostDB:ENSG00000054598.6

GeneCards: human genes, protein and diseases

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GeneCardsi
FOXC1

H-Invitational Database, human transcriptome db

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H-InvDBi
HIX0032962
HGNCiHGNC:3800 FOXC1
HPAiHPA040670
MalaCardsiFOXC1
MIMi601090 gene
601631 phenotype
602482 phenotype
neXtProtiNX_Q12948
OpenTargetsiENSG00000054598
Orphaneti98978 Axenfeld anomaly
782 Axenfeld-Rieger syndrome
250923 Isolated aniridia
708 Peters anomaly
91483 Rieger anomaly
PharmGKBiPA28217

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2294 Eukaryota
COG5025 LUCA
GeneTreeiENSGT00940000162303
HOVERGENiHBG051640
InParanoidiQ12948
KOiK09396
OMAiGRLTSWY
OrthoDBi1270467at2759
PhylomeDBiQ12948
TreeFamiTF316127

Enzyme and pathway databases

SignaLinkiQ12948
SIGNORiQ12948

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Forkhead_box_C1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
2296

Protein Ontology

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PROi
PR:Q12948

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000054598 Expressed in 219 organ(s), highest expression level in parotid gland
CleanExiHS_FOXC1
ExpressionAtlasiQ12948 baseline and differential
GenevisibleiQ12948 HS

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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiFOXC1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q12948
Secondary accession number(s): Q86UP7
, Q9BYM1, Q9NUE5, Q9UDD0, Q9UP06
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: April 27, 2001
Last modified: January 16, 2019
This is version 188 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

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