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Protein

Fibroblast growth factor receptor 1

Gene

FGFR1

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

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation.By similarity18 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by sequential autophosphorylation on tyrosine residues. Inhibited by ARQ 069; this compound maintains the kinase in an inactive conformation and inhibits autophosphorylation. Inhibited by PD173074.4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei514ATP1
Binding sitei568ATP1
<p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei623Proton acceptorPROSITE-ProRule annotation1 Publication1
Binding sitei627ATP1
Binding sitei641ATP1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei766Mediates interaction with PLCG1 and SHB1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi484 – 490ATP7
Nucleotide bindingi562 – 564ATP3

<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 functionHeparin-binding, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processTranscription, Transcription regulation
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

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BRENDAi
2.7.10.1 2681

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-109704 PI3K Cascade
R-HSA-1257604 PIP3 activates AKT signaling
R-HSA-1839120 Signaling by FGFR1 amplification mutants
R-HSA-1839122 Signaling by activated point mutants of FGFR1
R-HSA-190370 FGFR1b ligand binding and activation
R-HSA-190373 FGFR1c ligand binding and activation
R-HSA-190374 FGFR1c and Klotho ligand binding and activation
R-HSA-2219530 Constitutive Signaling by Aberrant PI3K in Cancer
R-HSA-375165 NCAM signaling for neurite out-growth
R-HSA-445144 Signal transduction by L1
R-HSA-5654219 Phospholipase C-mediated cascade: FGFR1
R-HSA-5654687 Downstream signaling of activated FGFR1
R-HSA-5654688 SHC-mediated cascade:FGFR1
R-HSA-5654689 PI-3K cascade:FGFR1
R-HSA-5654693 FRS-mediated FGFR1 signaling
R-HSA-5654726 Negative regulation of FGFR1 signaling
R-HSA-5655302 Signaling by FGFR1 in disease
R-HSA-5673001 RAF/MAP kinase cascade
R-HSA-6811558 PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling
R-HSA-8853336 Signaling by plasma membrane FGFR1 fusions

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

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SignaLinki
P11362

SIGNOR Signaling Network Open Resource

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SIGNORi
P11362

Protein family/group databases

Transport Classification Database

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TCDBi
8.A.23.1.7 the basigin (basigin) family

<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:
Fibroblast growth factor receptor 1 (EC:2.7.10.17 Publications)
Short name:
FGFR-1
Alternative name(s):
Basic fibroblast growth factor receptor 1
Short name:
BFGFR
Short name:
bFGF-R-1
Fms-like tyrosine kinase 2
Short name:
FLT-2
N-sam
Proto-oncogene c-Fgr
CD_antigen: CD331
<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:FGFR1
Synonyms:BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR
<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 8

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000077782.19

Human Gene Nomenclature Database

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HGNCi
HGNC:3688 FGFR1

Online Mendelian Inheritance in Man (OMIM)

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MIMi
136350 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P11362

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini22 – 376ExtracellularSequence analysisAdd BLAST355
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei377 – 397HelicalSequence analysisAdd BLAST21
Topological domaini398 – 822CytoplasmicSequence analysisAdd BLAST425

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Cytoplasmic vesicle, Membrane, 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

Pfeiffer syndrome (PS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by the association of craniosynostosis, broad and deviated thumbs and big toes, and partial syndactyly of the fingers and toes. Three subtypes are known: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).
See also OMIM:101600
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_004111252P → R in PS and JWS. 2 PublicationsCorresponds to variant dbSNP:rs121909627EnsemblClinVar.1
Hypogonadotropic hypogonadism 2 with or without anosmia (HH2)15 Publications
The disease is caused by mutations affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FGFR1 also have a mutation other HH-associated genes including DUSP6, FGF8, FGF17, FLRT3, GNRH1, GNRHR, HS6ST1, IL17RD, ANOS1, KISS1R, NSMF, PROKR2, SPRY4 and TACR3 (PubMed:23643382).1 Publication
Disease descriptionA disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH).
See also OMIM:147950
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0740124W → C in HH2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs760884357Ensembl.1
Natural variantiVAR_03096848G → S in HH2; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism. 1 PublicationCorresponds to variant dbSNP:rs121909640EnsemblClinVar.1
Natural variantiVAR_07299370G → R in HH2. 1 PublicationCorresponds to variant dbSNP:rs140254426Ensembl.1
Natural variantiVAR_03097078R → C in HH2. 1 Publication1
Natural variantiVAR_07401396S → C in HH2; unknown pathological significance. 1 Publication1
Natural variantiVAR_01788597G → D in HH2. 1 Publication1
Natural variantiVAR_01788699Y → C in HH2; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression. 2 PublicationsCorresponds to variant dbSNP:rs727505373EnsemblClinVar.1
Natural variantiVAR_030971101C → F in HH2. 1 Publication1
Natural variantiVAR_030972102V → I in HH2. 2 PublicationsCorresponds to variant dbSNP:rs55642501EnsemblClinVar.1
Natural variantiVAR_072994116V → I in HH2. 1 PublicationCorresponds to variant dbSNP:rs747842199Ensembl.1
Natural variantiVAR_069288117N → S in HH2; some patients also carry GNRHR mutations. 2 PublicationsCorresponds to variant dbSNP:rs780765366Ensembl.1
Natural variantiVAR_030973129D → A in HH2. 1 PublicationCorresponds to variant dbSNP:rs765615419EnsemblClinVar.1
Natural variantiVAR_017887167A → S in HH2; with cleft palate, corpus callosum agenesis, unilateral deafness and fusion of fourth and fifth metacarpal bones. 1 PublicationCorresponds to variant dbSNP:rs121909630EnsemblClinVar.1
Natural variantiVAR_072995174V → A in HH2. 1 Publication1
Natural variantiVAR_030974178C → S in HH2; with severe ear anomalies. 1 Publication1
Natural variantiVAR_030976224D → H in HH2. 1 Publication1
Natural variantiVAR_069289228Y → D in HH2; some patients also carry KISS1R mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression. 2 Publications1
Natural variantiVAR_030977237G → D in HH2. 1 Publication1
Natural variantiVAR_030978237G → S in HH2; with or without anosmia; also found in a family member with isolated anosmia; may impair proper folding. 1 PublicationCorresponds to variant dbSNP:rs121909635EnsemblClinVar.1
Natural variantiVAR_069290239I → T in HH2; some patients also carry PROKR2 and GNRH1 mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression. 2 Publications1
Natural variantiVAR_030979245L → P in HH2. 1 Publication1
Natural variantiVAR_069291250R → Q in HH2; with or without anosmia; results in Kallmann syndrome in the presence of HS6ST1 mutation TRP-306; reduces receptor affinity for fibroblast growth factor. 4 PublicationsCorresponds to variant dbSNP:rs121909645EnsemblClinVar.1
Natural variantiVAR_030980250R → W in HH2. 2 Publications1
Natural variantiVAR_030981254R → Q in HH2. 1 Publication1
Natural variantiVAR_030982270G → D in HH2. 1 Publication1
Natural variantiVAR_030983273V → M in HH2. 2 PublicationsCorresponds to variant dbSNP:rs1131691929Ensembl.1
Natural variantiVAR_030984274E → G in HH2; also found in a family member with isolated anosmia. Corresponds to variant dbSNP:rs727505369EnsemblClinVar.1
Natural variantiVAR_017888277C → Y in HH2. 1 Publication1
Natural variantiVAR_030985283P → R in HH2. 1 Publication1
Natural variantiVAR_080328324 – 822Missing in HH2. 1 PublicationAdd BLAST499
Natural variantiVAR_030988332S → C in HH2. 1 Publication1
Natural variantiVAR_030989339Y → C in HH2. 1 Publication1
Natural variantiVAR_069954342L → S in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a splice site mutation in NSMF. 1 PublicationCorresponds to variant dbSNP:rs121909638EnsemblClinVar.1
Natural variantiVAR_030990343A → V in HH2. 1 Publication1
Natural variantiVAR_030991346S → C in HH2; also found in a family member with isolated anosmia. 1 Publication1
Natural variantiVAR_069955348G → R in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in IL17RD. 2 PublicationsCorresponds to variant dbSNP:rs886037634EnsemblClinVar.1
Natural variantiVAR_030992366P → L in HH2; with or without anosmia. 1 PublicationCorresponds to variant dbSNP:rs121909641EnsemblClinVar.1
Natural variantiVAR_069292470R → L in HH2; some patients also carry GNRHR mutations. 2 PublicationsCorresponds to variant dbSNP:rs121909637EnsemblClinVar.1
Natural variantiVAR_069956483P → T in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in SPRY4. 1 PublicationCorresponds to variant dbSNP:rs397515444EnsemblClinVar.1
Natural variantiVAR_030995520A → T in HH2. 1 PublicationCorresponds to variant dbSNP:rs749758370Ensembl.1
Natural variantiVAR_030996538I → V in HH2. 1 Publication1
Natural variantiVAR_017889607V → M in HH2; with bimanual synkinesis. 1 PublicationCorresponds to variant dbSNP:rs121909629EnsemblClinVar.1
Natural variantiVAR_069293618K → N in HH2; some patients also carry GNRHR mutations; impairs tyrosine kinase activity. 2 Publications1
Natural variantiVAR_030997621H → R in HH2. 1 Publication1
Natural variantiVAR_080329622 – 822Missing in HH2. 1 PublicationAdd BLAST201
Natural variantiVAR_030998622R → G in HH2; with severe ear anomalies. 1 PublicationCorresponds to variant dbSNP:rs121909628EnsemblClinVar.1
Natural variantiVAR_030999622R → Q in HH2. 1 Publication1
Natural variantiVAR_080330661 – 822Missing in HH2. 1 PublicationAdd BLAST162
Natural variantiVAR_017890666W → R in HH2; with cleft palate. 1 Publication1
Natural variantiVAR_069957670E → K in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in FLRT3. 1 PublicationCorresponds to variant dbSNP:rs397515446EnsemblClinVar.1
Natural variantiVAR_069294671A → P in HH2. 1 Publication1
Natural variantiVAR_031000685S → F in HH2. 1 Publication1
Natural variantiVAR_031001687G → R in HH2. 2 PublicationsCorresponds to variant dbSNP:rs727505376EnsemblClinVar.1
Natural variantiVAR_069958692E → G in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in DUSP6. 1 PublicationCorresponds to variant dbSNP:rs397515445EnsemblClinVar.1
Natural variantiVAR_031002693I → F in HH2. 1 Publication1
Natural variantiVAR_031003703G → R in HH2. 1 Publication1
Natural variantiVAR_031004703G → S in HH2. 1 PublicationCorresponds to variant dbSNP:rs768957161Ensembl.1
Natural variantiVAR_017891719M → R in HH2. 1 Publication1
Natural variantiVAR_074014719M → V in HH2; unknown pathological significance. 1 PublicationCorresponds to variant dbSNP:rs1085307879Ensembl.1
Natural variantiVAR_031005722P → H in HH2; associated with K-724; also found in a family member with isolated anosmia; reduced tyrosine kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs267606805EnsemblClinVar.1
Natural variantiVAR_031006722P → S in HH2. 1 PublicationCorresponds to variant dbSNP:rs121909642EnsemblClinVar.1
Natural variantiVAR_031007724N → K in HH2; associated with H-722; also found in a family member with isolated anosmia; reduced tyrosine kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs267606806EnsemblClinVar.1
Natural variantiVAR_031008745P → S in HH2. 2 Publications1
Natural variantiVAR_069959768D → Y in HH2; the patient also carries a rare variant in FGF8. 1 PublicationCorresponds to variant dbSNP:rs121909644EnsemblClinVar.1
Natural variantiVAR_031010795V → I in HH2; also found in a family member with isolated anosmia. 1 PublicationCorresponds to variant dbSNP:rs781328162Ensembl.1
Isoform 19 (identifier: P11362-19)
Natural varianti353A → T in HH2, unknown pathological significance. 1 Publication1
Osteoglophonic dysplasia (OGD)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionCharacterized by craniosynostosis, prominent supraorbital ridge, and depressed nasal bridge, as well as by rhizomelic dwarfism and nonossifying bone lesions. Inheritance is autosomal dominant.
See also OMIM:166250
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030987330N → I in OGD. 2 PublicationsCorresponds to variant dbSNP:rs121909632EnsemblClinVar.1
Natural variantiVAR_030993374Y → C in OGD; elevated basal activity and increased FGF2-mediated activity. 1 PublicationCorresponds to variant dbSNP:rs121909631EnsemblClinVar.1
Natural variantiVAR_030994381C → R in OGD. 2 PublicationsCorresponds to variant dbSNP:rs121909634EnsemblClinVar.1
Hartsfield syndrome (HRTFDS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA syndrome characterized by the triad of holoprosencephaly, ectrodactyly, and cleft/lip palate. Profound mental retardation is also present. Multiple other congenital anomalies usually occur.
See also OMIM:615465
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_070851165L → S in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs397515481EnsemblClinVar.1
Natural variantiVAR_070852191L → S in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs869025669EnsemblClinVar.1
Natural variantiVAR_070853490G → R in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs869025670EnsemblClinVar.1
Natural variantiVAR_070854623D → Y in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs398122946EnsemblClinVar.1
Natural variantiVAR_071460627R → T in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs869025671EnsemblClinVar.1
Natural variantiVAR_070855628N → K in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs869025672EnsemblClinVar.1
Natural variantiVAR_070856725C → Y in HRTFDS. 1 PublicationCorresponds to variant dbSNP:rs398122945EnsemblClinVar.1
Trigonocephaly 1 (TRIGNO1)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head.
See also OMIM:190440
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_030986300I → T in TRIGNO1. 1 PublicationCorresponds to variant dbSNP:rs121909633EnsemblClinVar.1
A chromosomal aberration involving FGFR1 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with ZMYM2. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow.1 Publication
A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1OP. Insertion ins(12;8)(p11;p11p22) with FGFR1OP2. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion proteins FGFR1OP2-FGFR1, FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity.5 Publications
A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with CNTRL. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein CNTRL-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.
Encephalocraniocutaneous lipomatosis (ECCL)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA sporadically occurring, neurocutaneous disorder characterized by ocular anomalies, skin lesions, and central nervous system anomalies. Clinical features include a well-demarcated hairless fatty nevus on the scalp, benign ocular tumors, intracranial and intraspinal lipomas, and congenital abnormalities of the meninges. Seizures, spasticity, and intellectual disability can be present.
See also OMIM:613001
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075853546N → K in ECCL; somatic mutation; activating mutation; strongly increased speed of the first autophosphorylation and loss of the normal sequential order of autophosphorylation. 2 PublicationsCorresponds to variant dbSNP:rs779707422EnsemblClinVar.1
Natural variantiVAR_075855656K → E in ECCL; somatic mutation. 1 PublicationCorresponds to variant dbSNP:rs869320694EnsemblClinVar.1
Jackson-Weiss syndrome (JWS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.
See also OMIM:123150
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004111252P → R in PS and JWS. 2 PublicationsCorresponds to variant dbSNP:rs121909627EnsemblClinVar.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>Mutagenesisi514K → A: Loss of kinase activity. 1 Publication1
Mutagenesisi577R → E: Strongly reduced autophosphorylation in response to FGF signaling. No effect on in vitro kinase activity. 1 Publication1
Mutagenesisi609R → V: Abolishes interaction with PLCG1. 1
Mutagenesisi623D → A: Loss of kinase activity. 1 Publication1
Mutagenesisi653Y → F: No effect on kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-654. 1 Publication1
Mutagenesisi654Y → F: Reduced kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-653. 1 Publication1
Mutagenesisi755D → V: Abolishes interaction with PLCG1. 1
Mutagenesisi766Y → F: Abolishes interaction with PLCG1 and SHB. Decreases phosphorylation of FRS2, activation of RAS and MAP kinase signaling and stimulation of cell proliferation. 4 Publications1

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei428 – 429Breakpoint for translocation to form CNTRL-FGFR1 OR FGFR1-CNTRL fusion proteins1 Publication2
Sitei428 – 429Breakpoint for translocation to form FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion proteins1 Publication2
Sitei428 – 429Breakpoint for translocation to form FGFR1OP2-FGFR13 Publications2

Keywords - Diseasei

Craniosynostosis, Disease mutation, Dwarfism, Holoprosencephaly, Hypogonadotropic hypogonadism, Kallmann syndrome, Mental retardation

Organism-specific databases

DisGeNET

More...
DisGeNETi
2260

GeneReviews a resource of expert-authored, peer-reviewed disease descriptions.

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GeneReviewsi
FGFR1

MalaCards human disease database

More...
MalaCardsi
FGFR1
MIMi101600 phenotype
123150 phenotype
147950 phenotype
166250 phenotype
190440 phenotype
613001 phenotype
615465 phenotype

Open Targets

More...
OpenTargetsi
ENSG00000077782

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

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Orphaneti
2396 Encephalocraniocutaneous lipomatosis
251579 Giant cell glioblastoma
251576 Gliosarcoma
2117 Hartsfield syndrome
3366 Isolated trigonocephaly
478 Kallmann syndrome
93924 Lobar holoprosencephaly
280200 Microform holoprosencephaly
168953 Myeloid/lymphoid neoplasm associated with FGFR1 rearrangement
2227 NON RARE IN EUROPE: Hypodontia
432 Normosmic congenital hypogonadotropic hypogonadism
99798 Oligodontia
2645 Osteoglosphonic dysplasia
93258 Pfeiffer syndrome type 1
251615 Pilomyxoid astrocytoma
314950 Primary hypereosinophilic syndrome
220386 Semilobar holoprosencephaly
3157 Septo-optic dysplasia spectrum

The Pharmacogenetics and Pharmacogenomics Knowledge Base

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PharmGKBi
PA28127

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL3650

Drug and drug target database

More...
DrugBanki
DB08577 3-[(3-(2-CARBOXYETHYL)-4-METHYLPYRROL-2-YL)METHYLENE]-2-INDOLINONE
DB09078 Lenvatinib
DB09079 Nintedanib
DB00039 Palifermin
DB08901 Ponatinib
DB08896 Regorafenib
DB00398 Sorafenib
DB02058 SU4984
DB05014 XL999

IUPHAR/BPS Guide to PHARMACOLOGY

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GuidetoPHARMACOLOGYi
1808

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
FGFR1

Domain mapping of disease mutations (DMDM)

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DMDMi
120046

<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 denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 21Add BLAST21
<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_000001678022 – 822Fibroblast growth factor receptor 1Add BLAST801

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi55 ↔ 101PROSITE-ProRule annotation
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi77N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi117N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi178 ↔ 230
Glycosylationi227N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi240N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi264N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi277 ↔ 341
Glycosylationi296N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi317N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi330N-linked (GlcNAc...) asparagineSequence analysis1
<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 residuei463Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei583Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei585Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei653Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei654Phosphotyrosine; by autocatalysis4 Publications1
Modified residuei730Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei766Phosphotyrosine; by autocatalysis1 Publication1

<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

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer and proceeds in a highly ordered manner. Initial autophosphorylation at Tyr-653 increases the kinase activity by a factor of 50 to 100. After this, Tyr-583 becomes phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is autophosphorylated, resulting in a further tenfold increase of kinase activity. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation.4 Publications
Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after autophosphorylation, leading to internalization and lysosomal degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and mediates ubiquitination and subsequent degradation of FGFR1.2 Publications
N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P11362

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P11362

MaxQB - The MaxQuant DataBase

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MaxQBi
P11362

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

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PaxDbi
P11362

PeptideAtlas

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PeptideAtlasi
P11362

PRoteomics IDEntifications database

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PRIDEi
P11362

ProteomicsDB human proteome resource

More...
ProteomicsDBi
52745
52746 [P11362-10]
52747 [P11362-11]
52748 [P11362-12]
52749 [P11362-13]
52750 [P11362-14]
52751 [P11362-15]
52752 [P11362-16]
52753 [P11362-17]
52754 [P11362-18]
52755 [P11362-19]
52756 [P11362-2]
52757 [P11362-20]
52758 [P11362-21]
52759 [P11362-3]
52760 [P11362-4]
52761 [P11362-5]
52762 [P11362-6]
52763 [P11362-7]
52764 [P11362-8]
52765 [P11362-9]

PTM databases

CarbonylDB database of protein carbonylation sites

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CarbonylDBi
P11362

GlyConnect protein glycosylation platform

More...
GlyConnecti
1239

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P11362

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

More...
PhosphoSitePlusi
P11362

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
P11362

Miscellaneous databases

CutDB - Proteolytic event database

More...
PMAP-CutDBi
P11362

<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

Detected in astrocytoma, neuroblastoma and adrenal cortex cell lines. Some isoforms are detected in foreskin fibroblast cell lines, however isoform 17, isoform 18 and isoform 19 are not detected in these cells.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000077782 Expressed in 240 organ(s), highest expression level in body of pancreas

CleanEx database of gene expression profiles

More...
CleanExi
HS_FGFR1
HS_FLG

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P11362 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P11362 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB033614
HPA056402
HPA076274

<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. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro) (PubMed:1697263, PubMed:1722683, PubMed:8663044, PubMed:9655399, PubMed:12181353, PubMed:16597617, PubMed:17623664). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and FGF23 (PubMed:19966287). Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains) (PubMed:1656221, PubMed:1379697, PubMed:21765395). Interacts with FRS2 (PubMed:21765395). Interacts with RPS6KA1 (PubMed:15117958). Interacts (via C-terminus) with NEDD4 (via WW3 domain) (PubMed:21765395). Interacts with KL (By similarity). Interacts with SHB (via SH2 domain) (PubMed:12181353). Interacts with GRB10 (PubMed:10454568). Interacts with ANOS1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2 (PubMed:19696444). Interacts with SOX2 and SOX3. Interacts with FLRT1, FLRT2 and FLRT3 (By similarity). Found in a ternary complex with FGF1 and ITGAV:ITGB3 (PubMed:20422052, PubMed:18441324).By similarity16 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)

More...
BioGridi
108551, 178 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P11362

Database of interacting proteins

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DIPi
DIP-4019N

Protein interaction database and analysis system

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IntActi
P11362, 30 interactors

Molecular INTeraction database

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MINTi
P11362

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000393312

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
P11362

<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

Secondary structure

1822
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AGWX-ray2.40A/B456-765[»]
1CVSX-ray2.80C/D141-365[»]
1EVTX-ray2.80C/D141-365[»]
1FGIX-ray2.50A/B456-765[»]
1FGKX-ray2.00A/B456-765[»]
1FQ9X-ray3.00C/D141-365[»]
1XR0NMR-A409-430[»]
2CR3NMR-A38-123[»]
2FGIX-ray2.50A/B456-765[»]
3C4FX-ray2.07A/B464-765[»]
3DPKX-ray1.95A577-615[»]
3GQIX-ray2.50A458-774[»]
3GQLX-ray2.80A/B/C458-774[»]
3JS2X-ray2.20A/B458-765[»]
3KRJX-ray2.10A577-597[»]
3KRLX-ray2.40A577-597[»]
3KXXX-ray3.20A/B/C/D458-765[»]
3KY2X-ray2.70A/B458-765[»]
3OJVX-ray2.60C/D142-365[»]
3RHXX-ray2.01A/B461-765[»]
3TT0X-ray2.80A/B456-765[»]
4F63X-ray2.55A/B458-765[»]
4F64X-ray2.05A/B458-765[»]
4F65X-ray2.26A/B458-765[»]
4NK9X-ray2.57A/B458-765[»]
4NKAX-ray2.19A/B458-765[»]
4NKSX-ray2.50A/B458-765[»]
4RWIX-ray2.29A/B458-765[»]
4RWJX-ray2.49A/B458-765[»]
4RWKX-ray2.98A/B458-765[»]
4RWLX-ray2.19A/B458-765[»]
4UWBX-ray2.31A/B458-765[»]
4UWCX-ray1.96A/B458-765[»]
4UWYX-ray2.31A/B458-765[»]
4V01X-ray2.33A/B458-765[»]
4V04X-ray2.12A/B458-765[»]
4V05X-ray2.57A/B458-765[»]
4WUNX-ray1.65A/B459-765[»]
4ZSAX-ray2.00A/B458-765[»]
5A46X-ray2.63A/B437-822[»]
5A4CX-ray2.09A/B461-765[»]
5AM6X-ray1.96A/B458-765[»]
5AM7X-ray1.96A/B458-765[»]
5B7VX-ray2.15A/B456-765[»]
5EW8X-ray1.63A/B458-765[»]
5FLFX-ray2.58A/B/C/D/E458-765[»]
5O49X-ray1.91A/B458-765[»]
5O4AX-ray2.01A/B458-765[»]
5UQ0X-ray2.30A/B459-765[»]
5UR1X-ray2.20A/B459-765[»]
5VNDX-ray2.20A/B458-765[»]
5W21X-ray3.00C142-365[»]
5W59X-ray2.50B142-365[»]
5ZV2X-ray2.86A/B461-764[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

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ProteinModelPortali
P11362

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

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SMRi
P11362

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...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P11362

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini25 – 119Ig-like C2-type 1Add BLAST95
Domaini158 – 246Ig-like C2-type 2Add BLAST89
Domaini255 – 357Ig-like C2-type 3Add BLAST103
Domaini478 – 767Protein kinasePROSITE-ProRule annotationAdd BLAST290

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>Regioni160 – 177Heparin-bindingAdd BLAST18

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains.

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0200 Eukaryota
COG0515 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000155860

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000263410

The HOVERGEN Database of Homologous Vertebrate Genes

More...
HOVERGENi
HBG000345

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P11362

KEGG Orthology (KO)

More...
KOi
K04362

Identification of Orthologs from Complete Genome Data

More...
OMAi
YPEKMEK

Database of Orthologous Groups

More...
OrthoDBi
220433at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P11362

TreeFam database of animal gene trees

More...
TreeFami
TF316307

Family and domain databases

Conserved Domains Database

More...
CDDi
cd05098 PTKc_FGFR1, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
2.60.40.10, 3 hits

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR028174 FGF_rcpt_1
IPR016248 FGF_rcpt_fam
IPR007110 Ig-like_dom
IPR036179 Ig-like_dom_sf
IPR013783 Ig-like_fold
IPR013098 Ig_I-set
IPR003599 Ig_sub
IPR003598 Ig_sub2
IPR013151 Immunoglobulin
IPR011009 Kinase-like_dom_sf
IPR000719 Prot_kinase_dom
IPR017441 Protein_kinase_ATP_BS
IPR001245 Ser-Thr/Tyr_kinase_cat_dom
IPR008266 Tyr_kinase_AS
IPR020635 Tyr_kinase_cat_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF07679 I-set, 2 hits
PF00047 ig, 1 hit
PF07714 Pkinase_Tyr, 1 hit

PIRSF; a whole-protein classification database

More...
PIRSFi
PIRSF000628 FGFR, 1 hit

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00109 TYRKINASE

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00409 IG, 3 hits
SM00408 IGc2, 3 hits
SM00219 TyrKc, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48726 SSF48726, 3 hits
SSF56112 SSF56112, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS50835 IG_LIKE, 3 hits
PS00107 PROTEIN_KINASE_ATP, 1 hit
PS50011 PROTEIN_KINASE_DOM, 1 hit
PS00109 PROTEIN_KINASE_TYR, 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>Sequences (21+)i

<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.

<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 in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 21 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 21 described isoforms and 13 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P11362-1) [UniParc]FASTAAdd to basket
Also known as: Alpha A1, IV

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL
60 70 80 90 100
LQLRCRLRDD VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA
110 120 130 140 150
CVTSSPSGSD TTYFSVNVSD ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP
160 170 180 190 200
VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS SGTPNPTLRW LKNGKEFKPD
210 220 230 240 250
HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN HTYQLDVVER
260 270 280 290 300
SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
310 320 330 340 350
GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS
360 370 380 390 400
HHSAWLTVLE ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK
410 420 430 440 450
SGTKKSDFHS QMAVHKLAKS IPLRRQVTVS ADSSASMNSG VLLVRPSRLS
460 470 480 490 500
SSGTPMLAGV SEYELPEDPR WELPRDRLVL GKPLGEGCFG QVVLAEAIGL
510 520 530 540 550
DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK HKNIINLLGA
560 570 580 590 600
CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL
610 620 630 640 650
VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH
660 670 680 690 700
IDYYKKTTNG RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP
710 720 730 740 750
YPGVPVEELF KLLKEGHRMD KPSNCTNELY MMMRDCWHAV PSQRPTFKQL
760 770 780 790 800
VEDLDRIVAL TSNQEYLDLS MPLDQYSPSF PDTRSSTCSS GEDSVFSHEP
810 820
LPEEPCLPRH PAQLANGGLK RR
Length:822
Mass (Da):91,868
Last modified:May 1, 1991 - 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:i93A01B5D78C3E72C
GO
Isoform 2 (identifier: P11362-8) [UniParc]FASTAAdd to basket
Also known as: Alpha A2

The sequence of this isoform differs from the canonical sequence as follows:
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

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Length:662
Mass (Da):73,475
Checksum:iE9419E4DCB3D8A15
GO
Isoform 3 (identifier: P11362-17) [UniParc]FASTAAdd to basket
Also known as: Alpha A3

The sequence of this isoform differs from the canonical sequence as follows:
     32-61: QPWGAPVEVESFLVHPGDLLQLRCRLRDDV → CPDLQEAKSCSASFHSITPLPFGLGTRLSD
     62-822: Missing.

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Length:61
Mass (Da):6,682
Checksum:i13F5DEE578AF5D86
GO
Isoform 4 (identifier: P11362-2) [UniParc]FASTAAdd to basket
Also known as: Alpha B1

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.

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Length:820
Mass (Da):91,668
Checksum:i16B07518ECFC98F5
GO
Isoform 5 (identifier: P11362-9) [UniParc]FASTAAdd to basket
Also known as: Alpha B2

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Show »
Length:660
Mass (Da):73,274
Checksum:i2D2E9EEAC7BDDE3F
GO
Isoform 6 (identifier: P11362-3) [UniParc]FASTAAdd to basket
Also known as: Beta A1, II, H2

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.

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Length:733
Mass (Da):82,162
Checksum:iED3CD2B1CA825F7E
GO
Isoform 7 (identifier: P11362-10) [UniParc]FASTAAdd to basket
Also known as: Beta A2

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Show »
Length:573
Mass (Da):63,769
Checksum:iBA9898B9E682D31C
GO
Isoform 8 (identifier: P11362-4) [UniParc]FASTAAdd to basket
Also known as: Beta B1

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     428-429: Missing.

Show »
Length:731
Mass (Da):81,962
Checksum:iEF5CC75954AEC7FC
GO
Isoform 9 (identifier: P11362-11) [UniParc]FASTAAdd to basket
Also known as: Beta B2

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Show »
Length:571
Mass (Da):63,569
Checksum:i0BDAB3559EB4B141
GO
Isoform 10 (identifier: P11362-5) [UniParc]FASTAAdd to basket
Also known as: Gamma A1

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.

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Length:662
Mass (Da):74,133
Checksum:iF51EB57977705DE1
GO
Isoform 11 (identifier: P11362-12) [UniParc]FASTAAdd to basket
Also known as: Gamma A2

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.

Show »
Length:502
Mass (Da):55,740
Checksum:i3D3E866B4D4CEBEF
GO
Isoform 12 (identifier: P11362-6) [UniParc]FASTAAdd to basket
Also known as: Gamma B1

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     428-429: Missing.

Show »
Length:660
Mass (Da):73,933
Checksum:iE8947AAB5631D58E
GO
Isoform 13 (identifier: P11362-13) [UniParc]FASTA