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Protein

Fibroblast growth factor receptor 3

Gene

FGFR3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Required for normal development of the inner ear. Phosphorylates PLCG1, CBL and FRS2. 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. Plays a role in the regulation of vitamin D metabolism. Mutations that lead to constitutive kinase activation or impair normal FGFR3 maturation, internalization and degradation lead to aberrant signaling. Over-expressed or constitutively activated FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling.13 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation2 Publications

Enzyme regulationi

Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by SU5402.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei508ATPPROSITE-ProRule annotation1
Active sitei617Proton acceptorPROSITE-ProRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi478 – 486ATPPROSITE-ProRule annotation9

GO - Molecular functioni

  • 1-phosphatidylinositol-3-kinase activity Source: Reactome
  • ATP binding Source: UniProtKB-KW
  • fibroblast growth factor-activated receptor activity Source: UniProtKB
  • fibroblast growth factor binding Source: UniProtKB
  • phosphatidylinositol-4,5-bisphosphate 3-kinase activity Source: Reactome
  • protein tyrosine kinase activity Source: UniProtKB
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome

GO - Biological processi

  • bone maturation Source: BHF-UCL
  • bone mineralization Source: BHF-UCL
  • bone morphogenesis Source: UniProtKB
  • cell-cell signaling Source: Ensembl
  • chondrocyte differentiation Source: UniProtKB
  • chondrocyte proliferation Source: UniProtKB
  • endochondral bone growth Source: UniProtKB
  • endochondral ossification Source: UniProtKB
  • fibroblast growth factor receptor apoptotic signaling pathway Source: UniProtKB
  • fibroblast growth factor receptor signaling pathway Source: UniProtKB
  • JAK-STAT cascade Source: ProtInc
  • MAPK cascade Source: Reactome
  • negative regulation of developmental growth Source: BHF-UCL
  • peptidyl-tyrosine phosphorylation Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of cell proliferation Source: UniProtKB
  • positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
  • positive regulation of MAPK cascade Source: UniProtKB
  • positive regulation of phosphatidylinositol 3-kinase activity Source: UniProtKB
  • positive regulation of phospholipase activity Source: UniProtKB
  • positive regulation of tyrosine phosphorylation of Stat1 protein Source: UniProtKB
  • positive regulation of tyrosine phosphorylation of Stat3 protein Source: UniProtKB
  • protein autophosphorylation Source: UniProtKB
  • regulation of phosphatidylinositol 3-kinase signaling Source: Reactome
  • skeletal system development Source: ProtInc
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Receptor, Transferase, Tyrosine-protein kinase

Keywords - Biological processi

Apoptosis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:HS00929-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1839130. Signaling by activated point mutants of FGFR3.
R-HSA-190371. FGFR3b ligand binding and activation.
R-HSA-190372. FGFR3c ligand binding and activation.
R-HSA-2033514. FGFR3 mutant receptor activation.
R-HSA-2033515. t(4;14) translocations of FGFR3.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654710. PI-3K cascade:FGFR3.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8853334. Signaling by FGFR3 fusions in cancer.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP22607.
SIGNORiP22607.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 3 (EC:2.7.10.1)
Short name:
FGFR-3
Alternative name(s):
CD_antigen: CD333
Gene namesi
Name:FGFR3
Synonyms:JTK4
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:3690. FGFR3.

Subcellular locationi

Isoform 1 :

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini23 – 375ExtracellularSequence analysisAdd BLAST353
Transmembranei376 – 396HelicalSequence analysisAdd BLAST21
Topological domaini397 – 806CytoplasmicSequence analysisAdd BLAST410

GO - Cellular componenti

  • cell surface Source: Ensembl
  • endoplasmic reticulum Source: HPA
  • extracellular region Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB
  • integral component of plasma membrane Source: UniProtKB
  • nucleus Source: Ensembl
  • plasma membrane Source: UniProtKB
  • transport vesicle Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Endoplasmic reticulum, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Achondroplasia (ACH)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA frequent form of short-limb dwarfism. It is characterized by a long, narrow trunk, short extremities, particularly in the proximal (rhizomelic) segments, a large head with frontal bossing, hypoplasia of the midface and a trident configuration of the hands.
See also OMIM:100800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004154375G → C in ACH. 1 PublicationCorresponds to variant rs75790268dbSNPEnsembl.1
Natural variantiVAR_004155380G → R in keratinocytic non-epidermolytic nevus and ACH; very common mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 7 PublicationsCorresponds to variant rs28931614dbSNPEnsembl.1
Natural variantiVAR_004161650K → M in KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 6 PublicationsCorresponds to variant rs121913105dbSNPEnsembl.1
Crouzon syndrome with acanthosis nigricans (CAN)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionClassic Crouzon disease which is caused by mutations in the FGFR2 gene is characterized by craniosynostosis (premature fusion of the skull sutures), and facial hypoplasia. Crouzon syndrome with acanthosis nigricans (a skin disorder characterized by pigmentation anomalies), CAN, is considered to be an independent disorder from classic Crouzon syndrome. CAN is characterized by additional more severe physical manifestation, such as Chiari malformation, hydrocephalus, and atresia or stenosis of the choanas, and is caused by a specific mutation (Ala-391 to Glu) in the transmembrane domain of FGFR3. It is proposed to have an autosomal dominant mode of inheritance.
See also OMIM:612247
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004156391A → E in CAN. 2 PublicationsCorresponds to variant rs28931615dbSNPEnsembl.1
Thanatophoric dysplasia 1 (TD1)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neonatal lethal skeletal dysplasia. Affected individuals manifest severe shortening of the limbs with macrocephaly, narrow thorax, short ribs, and curved femurs.
See also OMIM:187600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004148248R → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1; severe and lethal; also found as somatic mutation in one patient with multiple myeloma; constitutive dimerization and kinase activation. 8 PublicationsCorresponds to variant rs121913482dbSNPEnsembl.1
Natural variantiVAR_004149249S → C in KERSEB, BLC, cervical cancer and TD1. 5 PublicationsCorresponds to variant rs121913483dbSNPEnsembl.1
Natural variantiVAR_004151370G → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1. 5 PublicationsCorresponds to variant rs121913479dbSNPEnsembl.1
Natural variantiVAR_004152371S → C in KERSEB and TD1. 2 PublicationsCorresponds to variant rs121913484dbSNPEnsembl.1
Natural variantiVAR_004153373Y → C in KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation. 5 PublicationsCorresponds to variant rs121913485dbSNPEnsembl.1
Natural variantiVAR_004161650K → M in KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 6 PublicationsCorresponds to variant rs121913105dbSNPEnsembl.1
Thanatophoric dysplasia 2 (TD2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA neonatal lethal skeletal dysplasia causing severe shortening of the limbs, narrow thorax and short ribs. Patients with thanatophoric dysplasia type 2 have straight femurs and cloverleaf skull.
See also OMIM:187601
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004160650K → E in KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 12 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Hypochondroplasia (HCH)6 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAutosomal dominant disease and is characterized by disproportionate short stature. It resembles achondroplasia, but with a less severe phenotype.
See also OMIM:146000
Bladder cancer (BLC)2 Publications
Disease susceptibility is associated with variations affecting the gene represented in this entry. Somatic mutations can constitutively activate FGFR3.
Disease descriptionA malignancy originating in tissues of the urinary bladder. It often presents with multiple tumors appearing at different times and at different sites in the bladder. Most bladder cancers are transitional cell carcinomas that begin in cells that normally make up the inner lining of the bladder. Other types of bladder cancer include squamous cell carcinoma (cancer that begins in thin, flat cells) and adenocarcinoma (cancer that begins in cells that make and release mucus and other fluids). Bladder cancer is a complex disorder with both genetic and environmental influences.
See also OMIM:109800
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004148248R → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1; severe and lethal; also found as somatic mutation in one patient with multiple myeloma; constitutive dimerization and kinase activation. 8 PublicationsCorresponds to variant rs121913482dbSNPEnsembl.1
Natural variantiVAR_004149249S → C in KERSEB, BLC, cervical cancer and TD1. 5 PublicationsCorresponds to variant rs121913483dbSNPEnsembl.1
Natural variantiVAR_004151370G → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1. 5 PublicationsCorresponds to variant rs121913479dbSNPEnsembl.1
Natural variantiVAR_004160650K → E in KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 12 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Natural variantiVAR_018390650K → Q in hypochondroplasia and BLC; in hypochondroplasia the form is milder than that seen in individuals with the K-540 or M-650 mutations; constitutively activated kinase. 3 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Cervical cancer (CERCA)1 Publication
The gene represented in this entry is involved in disease pathogenesis.
Disease descriptionA malignant neoplasm of the cervix, typically originating from a dysplastic or premalignant lesion previously present at the active squamocolumnar junction. The transformation from mild dysplastic to invasive carcinoma generally occurs slowly within several years, although the rate of this process varies widely. Carcinoma in situ is particularly known to precede invasive cervical cancer in most cases. Cervical cancer is strongly associated with infection by oncogenic types of human papillomavirus.
See also OMIM:603956
Camptodactyly, tall stature, and hearing loss syndrome (CATSHLS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant syndrome characterized by permanent and irreducible flexion of one or more fingers of the hand and/or feet, tall stature, scoliosis and/or a pectus excavatum, and hearing loss. Affected individuals have developmental delay and/or mental retardation, and several of these have microcephaly. Radiographic findings included tall vertebral bodies with irregular borders and broad femoral metaphyses with long tubular shafts. On audiological exam, each tested member have bilateral sensorineural hearing loss and absent otoacoustic emissions. The hearing loss was congenital or developed in early infancy, progressed variably in early childhood, and range from mild to severe. Computed tomography and magnetic resonance imaging reveal that the brain, middle ear, and inner ear are structurally normal.
See also OMIM:610474
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029108621R → H in CATSHLS. 1 PublicationCorresponds to variant rs121913113dbSNPEnsembl.1
Multiple myeloma (MM)2 Publications
The gene represented in this entry may be involved in disease pathogenesis. A chromosomal aberration involving FGFR3 is found in multiple myeloma. Translocation t(4;14)(p16.3;q32.3) with the IgH locus.
Disease descriptionA malignant tumor of plasma cells usually arising in the bone marrow and characterized by diffuse involvement of the skeletal system, hyperglobulinemia, Bence-Jones proteinuria and anemia. Complications of multiple myeloma are bone pain, hypercalcemia, renal failure and spinal cord compression. The aberrant antibodies that are produced lead to impaired humoral immunity and patients have a high prevalence of infection. Amyloidosis may develop in some patients. Multiple myeloma is part of a spectrum of diseases ranging from monoclonal gammopathy of unknown significance (MGUS) to plasma cell leukemia.
See also OMIM:254500
Lacrimo-auriculo-dento-digital syndrome (LADDS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. Lacrimo-auriculo-dento-digital syndrome is characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.
See also OMIM:149730
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029887513D → N in LADDS. 1 PublicationCorresponds to variant rs121913112dbSNPEnsembl.1
Keratinocytic non-epidermolytic nevus (KNEN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionEpidermal nevi of the common, non-organoid and non-epidermolytic type are benign skin lesions and may vary in their extent from a single (usually linear) lesion to widespread and systematized involvement. They may be present at birth or develop early during childhood.
See also OMIM:162900
Muenke syndrome (MNKS)3 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA condition characterized by premature closure of coronal suture of skull during development (coronal craniosynostosis), which affects the shape of the head and face. It may be uni- or bilateral. When bilateral, it is characterized by a skull with a small antero-posterior diameter (brachycephaly), often with a decrease in the depth of the orbits and hypoplasia of the maxillae. Unilateral closure of the coronal sutures leads to flattening of the orbit on the involved side (plagiocephaly). The intellect is normal. In addition to coronal craniosynostosis some affected individuals show skeletal abnormalities of hands and feet, sensorineural hearing loss, mental retardation and respiratory insufficiency.
See also OMIM:602849
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004150250P → R in MNKS; also some individuals with autosomal dominant congenital sensorineural deafness without craniosynostosis. 4 PublicationsCorresponds to variant rs4647924dbSNPEnsembl.1
Keratosis, seborrheic (KERSEB)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA common benign skin tumor. Seborrheic keratoses usually begin with the appearance of one or more sharply defined, light brown, flat macules. The lesions may be sparse or numerous. As they initially grow, they develop a velvety to finely verrucous surface, followed by an uneven warty surface with multiple plugged follicles and a dull or lackluster appearance.
See also OMIM:182000
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004148248R → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1; severe and lethal; also found as somatic mutation in one patient with multiple myeloma; constitutive dimerization and kinase activation. 8 PublicationsCorresponds to variant rs121913482dbSNPEnsembl.1
Natural variantiVAR_004149249S → C in KERSEB, BLC, cervical cancer and TD1. 5 PublicationsCorresponds to variant rs121913483dbSNPEnsembl.1
Natural variantiVAR_004151370G → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1. 5 PublicationsCorresponds to variant rs121913479dbSNPEnsembl.1
Natural variantiVAR_004152371S → C in KERSEB and TD1. 2 PublicationsCorresponds to variant rs121913484dbSNPEnsembl.1
Natural variantiVAR_004153373Y → C in KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation. 5 PublicationsCorresponds to variant rs121913485dbSNPEnsembl.1
Natural variantiVAR_004160650K → E in KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 12 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Natural variantiVAR_004161650K → M in KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 6 PublicationsCorresponds to variant rs121913105dbSNPEnsembl.1
Testicular germ cell tumor (TGCT)1 Publication
The gene represented in this entry may be involved in disease pathogenesis.
Disease descriptionA common malignancy in males representing 95% of all testicular neoplasms. TGCTs have various pathologic subtypes including: unclassified intratubular germ cell neoplasia, seminoma (including cases with syncytiotrophoblastic cells), spermatocytic seminoma, embryonal carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
See also OMIM:273300
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004160650K → E in KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 12 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Achondroplasia, severe, with developmental delay and acanthosis nigricans (SADDAN)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA severe form of achondroplasia associated with developmental delay and acanthosis nigricans. Patients manifest short-limb dwarfism, with a long, narrow trunk, short extremities, particularly in the proximal (rhizomelic) segments, a large head with frontal bossing, hypoplasia of the midface and a trident configuration of the hands. Acanthosis nigricans is a skin condition characterized by brown-pigmented, velvety verrucosities in body folds and creases.
See also OMIM:616482
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004161650K → M in KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 6 PublicationsCorresponds to variant rs121913105dbSNPEnsembl.1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi508K → A: Loss of kinase activity. Abolishes ubiquitination. 2 Publications1
Mutagenesisi577Y → F: Minor effect on kinase activity. 1 Publication1
Mutagenesisi650K → D: Constitutively activated kinase. 1
Mutagenesisi650K → L: Constitutively activated kinase. 1
Mutagenesisi724Y → F: Strongly reduced kinase activity. Strongly reduced mitogen activity. 1 Publication1
Mutagenesisi760Y → F: Minor effect on kinase activity. 1 Publication1
Mutagenesisi770Y → F: Minor effect on kinase activity. Increased mitogen activity. 1 Publication1

Keywords - Diseasei

Craniosynostosis, Deafness, Disease mutation, Dwarfism, Ectodermal dysplasia, Lacrimo-auriculo-dento-digital syndrome

Organism-specific databases

DisGeNETi2261.
MalaCardsiFGFR3.
MIMi100800. phenotype.
109800. phenotype.
146000. phenotype.
149730. phenotype.
162900. phenotype.
182000. phenotype.
187600. phenotype.
187601. phenotype.
254500. phenotype.
273300. phenotype.
602849. phenotype.
603956. phenotype.
610474. phenotype.
612247. phenotype.
616482. phenotype.
OpenTargetsiENSG00000068078.
Orphaneti15. Achondroplasia.
85164. Camptodactyly - tall stature - scoliosis - hearing loss.
93262. Crouzon syndrome - acanthosis nigricans.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
429. Hypochondroplasia.
35099. Isolated brachycephaly.
35098. Isolated plagiocephaly.
2363. Lacrimoauriculodentodigital syndrome.
53271. Muenke syndrome.
794. Saethre-Chotzen syndrome.
85165. Severe achondroplasia - developmental delay - acanthosis nigricans.
1860. Thanatophoric dysplasia type 1.
93274. Thanatophoric dysplasia type 2.
PharmGKBiPA28129.

Chemistry databases

ChEMBLiCHEMBL2742.
DrugBankiDB09078. Lenvatinib.
DB09079. Nintedanib.
DB00039. Palifermin.
DB06589. Pazopanib.
DB08901. Ponatinib.
GuidetoPHARMACOLOGYi1810.

Polymorphism and mutation databases

BioMutaiFGFR3.
DMDMi120050.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 22Add BLAST22
ChainiPRO_000001678523 – 806Fibroblast growth factor receptor 3Add BLAST784

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi61 ↔ 109PROSITE-ProRule annotation
Glycosylationi98N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi176 ↔ 228PROSITE-ProRule annotation
Glycosylationi225N-linked (GlcNAc...)Sequence analysis1
Glycosylationi262N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi275 ↔ 339PROSITE-ProRule annotation
Glycosylationi294N-linked (GlcNAc...)Sequence analysis1
Glycosylationi315N-linked (GlcNAc...)Sequence analysis1
Glycosylationi328N-linked (GlcNAc...)Sequence analysis1
Modified residuei444PhosphoserineBy similarity1
Modified residuei445PhosphoserineBy similarity1
Modified residuei647Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei648Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei724Phosphotyrosine; by autocatalysis1 Publication1
Modified residuei760Phosphotyrosine; by autocatalysis1 Publication1

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. Phosphorylation at Tyr-724 is essential for stimulation of cell proliferation and activation of PIK3R1, STAT1 and MAP kinase signaling. Phosphorylation at Tyr-760 is required for interaction with PIK3R1 and PLCG1.2 Publications
Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation.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.4 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP22607.
PeptideAtlasiP22607.
PRIDEiP22607.

PTM databases

iPTMnetiP22607.
PhosphoSitePlusiP22607.

Expressioni

Tissue specificityi

Expressed in brain, kidney and testis. Very low or no expression in spleen, heart, and muscle. In 20- to 22-week old fetuses it is expressed at high level in kidney, lung, small intestine and brain, and to a lower degree in spleen, liver, and muscle. Isoform 2 is detected in epithelial cells. Isoform 1 is not detected in epithelial cells. Isoform 1 and isoform 2 are detected in fibroblastic cells.1 Publication

Gene expression databases

BgeeiENSG00000068078.
CleanExiHS_FGFR3.
ExpressionAtlasiP22607. baseline and differential.
GenevisibleiP22607. HS.

Organism-specific databases

HPAiCAB004231.
HPA067204.

Interactioni

Subunit structurei

Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19, FGF20 and FGF23 (in vitro). Interacts with KLB. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19 and FGF21. Interacts with PIK3R1, PLCG1, SOCS1 and SOCS3. Isoform 3 forms disulfide-linked dimers.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
FGF1P052303EBI-348399,EBI-698068
HSP90AB1P082382EBI-348399,EBI-352572

GO - Molecular functioni

  • fibroblast growth factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108552. 42 interactors.
DIPiDIP-4016N.
IntActiP22607. 27 interactors.
MINTiMINT-1034697.
STRINGi9606.ENSP00000339824.

Chemistry databases

BindingDBiP22607.

Structurei

Secondary structure

1806
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi163 – 167Combined sources5
Beta strandi172 – 175Combined sources4
Beta strandi185 – 187Combined sources3
Turni208 – 211Combined sources4
Beta strandi212 – 215Combined sources4
Helixi220 – 222Combined sources3
Beta strandi226 – 232Combined sources7
Beta strandi235 – 246Combined sources12
Beta strandi263 – 268Combined sources6
Beta strandi271 – 273Combined sources3
Beta strandi283 – 289Combined sources7
Helixi293 – 295Combined sources3
Beta strandi302 – 304Combined sources3
Beta strandi324 – 326Combined sources3
Beta strandi335 – 345Combined sources11
Beta strandi348 – 357Combined sources10
Beta strandi369 – 372Combined sources4
Helixi374 – 398Combined sources25
Turni463 – 465Combined sources3
Helixi469 – 471Combined sources3
Beta strandi472 – 480Combined sources9
Beta strandi482 – 496Combined sources15
Beta strandi503 – 510Combined sources8
Helixi516 – 532Combined sources17
Beta strandi541 – 545Combined sources5
Beta strandi547 – 550Combined sources4
Beta strandi552 – 556Combined sources5
Helixi563 – 568Combined sources6
Helixi591 – 610Combined sources20
Helixi620 – 622Combined sources3
Beta strandi623 – 625Combined sources3
Beta strandi631 – 633Combined sources3
Beta strandi646 – 649Combined sources4
Helixi658 – 660Combined sources3
Helixi663 – 668Combined sources6
Helixi673 – 688Combined sources16
Helixi700 – 708Combined sources9
Helixi721 – 730Combined sources10
Helixi735 – 737Combined sources3
Helixi741 – 753Combined sources13

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RY7X-ray3.20B33-365[»]
2LZLNMR-A/B357-399[»]
4K33X-ray2.34A449-759[»]
ProteinModelPortaliP22607.
SMRiP22607.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP22607.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini24 – 126Ig-like C2-type 1Add BLAST103
Domaini151 – 244Ig-like C2-type 2Add BLAST94
Domaini253 – 355Ig-like C2-type 3Add BLAST103
Domaini472 – 761Protein kinasePROSITE-ProRule annotationAdd BLAST290

Domaini

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans.1 Publication

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation
Contains 1 protein kinase domain.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP22607.
KOiK05094.
OMAiSFDTCKP.
OrthoDBiEOG091G0CQZ.
PhylomeDBiP22607.
TreeFamiTF316307.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
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.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

Sequences (4)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 4 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P22607-1) [UniParc]FASTAAdd to basket
Also known as: IIIc

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
MGAPACALAL CVAVAIVAGA SSESLGTEQR VVGRAAEVPG PEPGQQEQLV
60 70 80 90 100
FGSGDAVELS CPPPGGGPMG PTVWVKDGTG LVPSERVLVG PQRLQVLNAS
110 120 130 140 150
HEDSGAYSCR QRLTQRVLCH FSVRVTDAPS SGDDEDGEDE AEDTGVDTGA
160 170 180 190 200
PYWTRPERMD KKLLAVPAAN TVRFRCPAAG NPTPSISWLK NGREFRGEHR
210 220 230 240 250
IGGIKLRHQQ WSLVMESVVP SDRGNYTCVV ENKFGSIRQT YTLDVLERSP
260 270 280 290 300
HRPILQAGLP ANQTAVLGSD VEFHCKVYSD AQPHIQWLKH VEVNGSKVGP
310 320 330 340 350
DGTPYVTVLK TAGANTTDKE LEVLSLHNVT FEDAGEYTCL AGNSIGFSHH
360 370 380 390 400
SAWLVVLPAE EELVEADEAG SVYAGILSYG VGFFLFILVV AAVTLCRLRS
410 420 430 440 450
PPKKGLGSPT VHKISRFPLK RQVSLESNAS MSSNTPLVRI ARLSSGEGPT
460 470 480 490 500
LANVSELELP ADPKWELSRA RLTLGKPLGE GCFGQVVMAE AIGIDKDRAA
510 520 530 540 550
KPVTVAVKML KDDATDKDLS DLVSEMEMMK MIGKHKNIIN LLGACTQGGP
560 570 580 590 600
LYVLVEYAAK GNLREFLRAR RPPGLDYSFD TCKPPEEQLT FKDLVSCAYQ
610 620 630 640 650
VARGMEYLAS QKCIHRDLAA RNVLVTEDNV MKIADFGLAR DVHNLDYYKK
660 670 680 690 700
TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLLWEIFTL GGSPYPGIPV
710 720 730 740 750
EELFKLLKEG HRMDKPANCT HDLYMIMREC WHAAPSQRPT FKQLVEDLDR
760 770 780 790 800
VLTVTSTDEY LDLSAPFEQY SPGGQDTPSS SSSGDDSVFA HDLLPPAPPS

SGGSRT
Length:806
Mass (Da):87,710
Last modified:August 1, 1991 - v1
Checksum:iBC5EA75EA46F447E
GO
Isoform 2 (identifier: P22607-2) [UniParc]FASTAAdd to basket
Also known as: IIIb

The sequence of this isoform differs from the canonical sequence as follows:
     311-358: TAGANTTDKE...HHSAWLVVLP → SWISESVEAD...FWLSVHGPRA

Show »
Length:808
Mass (Da):88,157
Checksum:iE08CE2C9FD56D8F9
GO
Isoform 3 (identifier: P22607-3) [UniParc]FASTAAdd to basket
Also known as: FGFR3deltaTM

The sequence of this isoform differs from the canonical sequence as follows:
     311-422: Missing.

Show »
Length:694
Mass (Da):75,696
Checksum:i4493C5990FD68964
GO
Isoform 4 (identifier: P22607-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     654-806: GRLPVKWMAP...APPSSGGSRT → LVLWGPALGD...DVKGHWSPTM

Note: No experimental confirmation available.
Show »
Length:791
Mass (Da):85,083
Checksum:iEA4EEB033A1433BB
GO

Sequence cautioni

The sequence BAD92678 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti395L → V in AAA58470 (PubMed:1664411).Curated1
Sequence conflicti421R → RQ in BAD92678 (Ref. 3) Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_02216765G → R.1 PublicationCorresponds to variant rs2305178dbSNPEnsembl.1
Natural variantiVAR_04220779T → S in a lung adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_042208228C → R in a colorectal adenocarcinoma sample; somatic mutation. 1 Publication1
Natural variantiVAR_004148248R → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1; severe and lethal; also found as somatic mutation in one patient with multiple myeloma; constitutive dimerization and kinase activation. 8 PublicationsCorresponds to variant rs121913482dbSNPEnsembl.1
Natural variantiVAR_004149249S → C in KERSEB, BLC, cervical cancer and TD1. 5 PublicationsCorresponds to variant rs121913483dbSNPEnsembl.1
Natural variantiVAR_004150250P → R in MNKS; also some individuals with autosomal dominant congenital sensorineural deafness without craniosynostosis. 4 PublicationsCorresponds to variant rs4647924dbSNPEnsembl.1
Natural variantiVAR_018388322E → K in colorectal cancer. 1 PublicationCorresponds to variant rs121913111dbSNPEnsembl.1
Natural variantiVAR_042209338T → M.1 Publication1
Natural variantiVAR_004151370G → C in KERSEB, BLC, keratinocytic non-epidermolytic nevus and TD1. 5 PublicationsCorresponds to variant rs121913479dbSNPEnsembl.1
Natural variantiVAR_004152371S → C in KERSEB and TD1. 2 PublicationsCorresponds to variant rs121913484dbSNPEnsembl.1
Natural variantiVAR_004153373Y → C in KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation. 5 PublicationsCorresponds to variant rs121913485dbSNPEnsembl.1
Natural variantiVAR_004154375G → C in ACH. 1 PublicationCorresponds to variant rs75790268dbSNPEnsembl.1
Natural variantiVAR_004155380G → R in keratinocytic non-epidermolytic nevus and ACH; very common mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 7 PublicationsCorresponds to variant rs28931614dbSNPEnsembl.1
Natural variantiVAR_022168384F → L.2 PublicationsCorresponds to variant rs17881656dbSNPEnsembl.1
Natural variantiVAR_004156391A → E in CAN. 2 PublicationsCorresponds to variant rs28931615dbSNPEnsembl.1
Natural variantiVAR_022169441A → T.1 PublicationCorresponds to variant rs17884368dbSNPEnsembl.1
Natural variantiVAR_029887513D → N in LADDS. 1 PublicationCorresponds to variant rs121913112dbSNPEnsembl.1
Natural variantiVAR_004157538I → V in hypochondroplasia. 1 PublicationCorresponds to variant rs80053154dbSNPEnsembl.1
Natural variantiVAR_004158540N → K in hypochondroplasia. 1 PublicationCorresponds to variant rs28933068dbSNPEnsembl.1
Natural variantiVAR_018389540N → S in hypochondroplasia; mild. 2 PublicationsCorresponds to variant rs77722678dbSNPEnsembl.1
Natural variantiVAR_004159540N → T in hypochondroplasia. 1 PublicationCorresponds to variant rs77722678dbSNPEnsembl.1
Natural variantiVAR_029108621R → H in CATSHLS. 1 PublicationCorresponds to variant rs121913113dbSNPEnsembl.1
Natural variantiVAR_042210646D → N.1 Publication1
Natural variantiVAR_004160650K → E in KERSEB, TD2, TGCT and BLC; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 12 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Natural variantiVAR_004161650K → M in KERSEB, ACH, TD1 and SADDAN; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. 6 PublicationsCorresponds to variant rs121913105dbSNPEnsembl.1
Natural variantiVAR_018390650K → Q in hypochondroplasia and BLC; in hypochondroplasia the form is milder than that seen in individuals with the K-540 or M-650 mutations; constitutively activated kinase. 3 PublicationsCorresponds to variant rs78311289dbSNPEnsembl.1
Natural variantiVAR_022170717A → T.1 PublicationCorresponds to variant rs17882190dbSNPEnsembl.1
Natural variantiVAR_022171726I → F.1 PublicationCorresponds to variant rs17880763dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_002989311 – 422Missing in isoform 3. 1 PublicationAdd BLAST112
Alternative sequenceiVSP_002988311 – 358TAGAN…LVVLP → SWISESVEADVRLRLANVSE RDGGEYLCRATNFIGVAEKA FWLSVHGPRA in isoform 2. 1 PublicationAdd BLAST48
Alternative sequenceiVSP_040945654 – 806GRLPV…GGSRT → LVLWGPALGDLHAGGLPVPR HPCGGALQAAEGGPPHGQAR QLHTRPVHDHAGVLACRALP EAHLQAAGGGPGPCPYRDVH RRVPGPVGAFRAVLPGWPGH PQLQLLRGRLRVCPRPAAPG PTQQWGLADVKGHWSPTM in isoform 4. 1 PublicationAdd BLAST153

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58051 mRNA. Translation: AAA52450.1.
AF245114 mRNA. Translation: AAF63380.1.
AB209441 mRNA. Translation: BAD92678.1. Different initiation.
AY768549 Genomic DNA. Translation: AAU89726.1.
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82564.1.
CH471131 Genomic DNA. Translation: EAW82565.1.
CH471131 Genomic DNA. Translation: EAW82566.1.
CH471131 Genomic DNA. Translation: EAW82567.1.
M64347 mRNA. Translation: AAA58470.1.
M59374 mRNA. Translation: AAA63209.1.
S76733 Genomic DNA. Translation: AAB33323.1.
X84939 mRNA. Translation: CAA59334.1.
U22410 Genomic DNA. Translation: AAA67781.1.
CCDSiCCDS3353.1. [P22607-1]
CCDS3354.1. [P22607-3]
CCDS54706.1. [P22607-2]
PIRiA38576. TVHUF3.
RefSeqiNP_000133.1. NM_000142.4. [P22607-1]
NP_001156685.1. NM_001163213.1. [P22607-2]
NP_075254.1. NM_022965.3. [P22607-3]
UniGeneiHs.1420.

Genome annotation databases

EnsembliENST00000260795; ENSP00000260795; ENSG00000068078. [P22607-1]
ENST00000340107; ENSP00000339824; ENSG00000068078. [P22607-2]
ENST00000352904; ENSP00000231803; ENSG00000068078. [P22607-3]
ENST00000412135; ENSP00000412903; ENSG00000068078. [P22607-3]
ENST00000440486; ENSP00000414914; ENSG00000068078. [P22607-1]
GeneIDi2261.
KEGGihsa:2261.
UCSCiuc003gdr.3. human. [P22607-1]

Keywords - Coding sequence diversityi

Alternative splicing, Chromosomal rearrangement, Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology
NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M58051 mRNA. Translation: AAA52450.1.
AF245114 mRNA. Translation: AAF63380.1.
AB209441 mRNA. Translation: BAD92678.1. Different initiation.
AY768549 Genomic DNA. Translation: AAU89726.1.
AC016773 Genomic DNA. No translation available.
CH471131 Genomic DNA. Translation: EAW82564.1.
CH471131 Genomic DNA. Translation: EAW82565.1.
CH471131 Genomic DNA. Translation: EAW82566.1.
CH471131 Genomic DNA. Translation: EAW82567.1.
M64347 mRNA. Translation: AAA58470.1.
M59374 mRNA. Translation: AAA63209.1.
S76733 Genomic DNA. Translation: AAB33323.1.
X84939 mRNA. Translation: CAA59334.1.
U22410 Genomic DNA. Translation: AAA67781.1.
CCDSiCCDS3353.1. [P22607-1]
CCDS3354.1. [P22607-3]
CCDS54706.1. [P22607-2]
PIRiA38576. TVHUF3.
RefSeqiNP_000133.1. NM_000142.4. [P22607-1]
NP_001156685.1. NM_001163213.1. [P22607-2]
NP_075254.1. NM_022965.3. [P22607-3]
UniGeneiHs.1420.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RY7X-ray3.20B33-365[»]
2LZLNMR-A/B357-399[»]
4K33X-ray2.34A449-759[»]
ProteinModelPortaliP22607.
SMRiP22607.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108552. 42 interactors.
DIPiDIP-4016N.
IntActiP22607. 27 interactors.
MINTiMINT-1034697.
STRINGi9606.ENSP00000339824.

Chemistry databases

BindingDBiP22607.
ChEMBLiCHEMBL2742.
DrugBankiDB09078. Lenvatinib.
DB09079. Nintedanib.
DB00039. Palifermin.
DB06589. Pazopanib.
DB08901. Ponatinib.
GuidetoPHARMACOLOGYi1810.

PTM databases

iPTMnetiP22607.
PhosphoSitePlusiP22607.

Polymorphism and mutation databases

BioMutaiFGFR3.
DMDMi120050.

Proteomic databases

PaxDbiP22607.
PeptideAtlasiP22607.
PRIDEiP22607.

Protocols and materials databases

DNASUi2261.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000260795; ENSP00000260795; ENSG00000068078. [P22607-1]
ENST00000340107; ENSP00000339824; ENSG00000068078. [P22607-2]
ENST00000352904; ENSP00000231803; ENSG00000068078. [P22607-3]
ENST00000412135; ENSP00000412903; ENSG00000068078. [P22607-3]
ENST00000440486; ENSP00000414914; ENSG00000068078. [P22607-1]
GeneIDi2261.
KEGGihsa:2261.
UCSCiuc003gdr.3. human. [P22607-1]

Organism-specific databases

CTDi2261.
DisGeNETi2261.
GeneCardsiFGFR3.
GeneReviewsiFGFR3.
HGNCiHGNC:3690. FGFR3.
HPAiCAB004231.
HPA067204.
MalaCardsiFGFR3.
MIMi100800. phenotype.
109800. phenotype.
134934. gene.
146000. phenotype.
149730. phenotype.
162900. phenotype.
182000. phenotype.
187600. phenotype.
187601. phenotype.
254500. phenotype.
273300. phenotype.
602849. phenotype.
603956. phenotype.
610474. phenotype.
612247. phenotype.
616482. phenotype.
neXtProtiNX_P22607.
OpenTargetsiENSG00000068078.
Orphaneti15. Achondroplasia.
85164. Camptodactyly - tall stature - scoliosis - hearing loss.
93262. Crouzon syndrome - acanthosis nigricans.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
429. Hypochondroplasia.
35099. Isolated brachycephaly.
35098. Isolated plagiocephaly.
2363. Lacrimoauriculodentodigital syndrome.
53271. Muenke syndrome.
794. Saethre-Chotzen syndrome.
85165. Severe achondroplasia - developmental delay - acanthosis nigricans.
1860. Thanatophoric dysplasia type 1.
93274. Thanatophoric dysplasia type 2.
PharmGKBiPA28129.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP22607.
KOiK05094.
OMAiSFDTCKP.
OrthoDBiEOG091G0CQZ.
PhylomeDBiP22607.
TreeFamiTF316307.

Enzyme and pathway databases

BioCyciZFISH:HS00929-MONOMER.
BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1839130. Signaling by activated point mutants of FGFR3.
R-HSA-190371. FGFR3b ligand binding and activation.
R-HSA-190372. FGFR3c ligand binding and activation.
R-HSA-2033514. FGFR3 mutant receptor activation.
R-HSA-2033515. t(4;14) translocations of FGFR3.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5654227. Phospholipase C-mediated cascade, FGFR3.
R-HSA-5654704. SHC-mediated cascade:FGFR3.
R-HSA-5654706. FRS-mediated FGFR3 signaling.
R-HSA-5654710. PI-3K cascade:FGFR3.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8853334. Signaling by FGFR3 fusions in cancer.
R-HSA-8853338. Signaling by FGFR3 point mutants in cancer.
SignaLinkiP22607.
SIGNORiP22607.

Miscellaneous databases

ChiTaRSiFGFR3. human.
EvolutionaryTraceiP22607.
GeneWikiiFibroblast_growth_factor_receptor_3.
GenomeRNAii2261.
PROiP22607.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000068078.
CleanExiHS_FGFR3.
ExpressionAtlasiP22607. baseline and differential.
GenevisibleiP22607. HS.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.