FGFR3
entrez
2261
canonical
uniprot
P22607
canonical
ensembl
ENSG00000068078
resolver
ensp
ENSP00000231803
resolver
ensp
ENSP00000339824
resolver
ensp
ENSP00000414914
resolver
ensp
ENSP00000420533
resolver
ensp
ENSP00000571284
resolver
ensp
ENSP00000571285
resolver
ensp
ENSP00000581529
resolver
ensp
ENSP00000581532
resolver
ensp
ENSP00000625462
resolver
ensp
ENSP00000625463
resolver
enst
ENST00000481110
resolver
genesymbol
FGFR3
resolver
genesymbol_syn
JTK4
resolver
hgnc
HGNC:3690
resolver
uniprot
D3DVP9
resolver
uniprot
D3DVQ0
resolver
uniprot
F8W9L4
resolver
uniprot
Q0IJ44
resolver
uniprot
Q14308
resolver
uniprot
Q16294
resolver
uniprot
Q16608
resolver
uniprot
Q59FL9
resolver
uniprot
X5D2G8
resolver
uniprot_entry
F8W9L4_HUMAN
resolver
uniprot_entry
FGFR3_HUMAN
resolver
uniprot_entry
Q0IJ44_HUMAN
resolver
uniprot_entry
X5D2G8_HUMAN
resolver
uniprot_sec
D3DVP9
resolver
uniprot_sec
D3DVQ0
resolver
uniprot_sec
Q14308
resolver
uniprot_sec
Q16294
resolver
uniprot_sec
Q16608
resolver
uniprot_sec
Q59FL9
resolver
activity_regulation
ACTIVITY REGULATION: 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. {ECO:0000269|PubMed:14732692, ECO:0000269|PubMed:17145761, ECO:0000269|PubMed:17509076}.
uniprot
proteins
amino_acid_sequence
MGAPACALALCVAVAIVAGASSESLGTEQRVVGRAAEVPGPEPGQQEQLVFGSGDAVELSCPPPGGGPMGPTVWVKDGTGLVPSERVLVGPQRLQVLNASHEDSGAYSCRQRLTQRVLCHFSVRVTDAPSSGDDEDGEDEAEDTGVDTGAPYWTRPERMDKKLLAVPAANTVRFRCPAAGNPTPSISWLKNGREFRGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKFGSIRQTYTLDVLERSPHRPILQAGLPANQTAVLGSDVEFHCKVYSDAQPHIQWLKHVEVNGSKVGPDGTPYVTVLKTAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHSAWLVVLPAEEELVEADEAGSVYAGILSYGVGFFLFILVVAAVTLCRLRSPPKKGLGSPTVHKISRFPLKRQVSLESNASMSSNTPLVRIARLSSGEGPTLANVSELELPADPKWELSRARLTLGKPLGEGCFGQVVMAEAIGIDKDRAAKPVTVAVKMLKDDATDKDLSDLVSEMEMMKMIGKHKNIINLLGACTQGGPLYVLVEYAAKGNLREFLRARRPPGLDYSFDTCKPPEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVTEDNVMKIADFGLARDVHNLDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAPSQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQDTPSSSSSGDDSVFAHDLLPPAPPSSGGSRT
uniprot
proteins
disease_involvement
DISEASE: Achondroplasia (ACH) [MIM:100800]: A 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. ACH is an autosomal dominant disease. {ECO:0000269|PubMed:10611230, ECO:0000269|PubMed:12297284, ECO:0000269|PubMed:7758520, ECO:0000269|PubMed:7847369, ECO:0000269|PubMed:8078586, ECO:0000269|PubMed:8599935}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Crouzon syndrome with acanthosis nigricans (CAN) [MIM:612247]: Classic 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. {ECO:0000269|PubMed:17935505, ECO:0000269|PubMed:7493034}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thanatophoric dysplasia 1 (TD1) [MIM:187600]: A neonatal lethal skeletal dysplasia. Affected individuals manifest severe shortening of the limbs with macrocephaly, narrow thorax, short ribs, and curved femurs. {ECO:0000269|PubMed:10360402, ECO:0000269|PubMed:10671061, ECO:0000269|PubMed:7773297, ECO:0000269|PubMed:8589699, ECO:0000269|PubMed:8845844, ECO:0000269|PubMed:9790257}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Thanatophoric dysplasia 2 (TD2) [MIM:187601]: A 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. {ECO:0000269|PubMed:12297284, ECO:0000269|PubMed:7773297, ECO:0000269|PubMed:8754806}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hypochondroplasia (HCH) [MIM:146000]: Autosomal dominant disease and is characterized by disproportionate short stature. It resembles achondroplasia, but with a less severe phenotype. {ECO:0000269|PubMed:10215410, ECO:0000269|PubMed:10777366, ECO:0000269|PubMed:11055896, ECO:0000269|PubMed:12707965, ECO:0000269|PubMed:7670477, ECO:0000269|PubMed:9452043}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bladder cancer (BLC) [MIM:109800]: A 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. {ECO:0000269|PubMed:10471491, ECO:0000269|PubMed:11314002}. Note=Disease susceptibility is associated with variants affecting the gene represented in this entry. Somatic mutations can constitutively activate FGFR3.; DISEASE: Cervical cancer (CERCA) [MIM:603956]: A 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. {ECO:0000269|PubMed:10471491}. Note=The gene represented in this entry is involved in disease pathogenesis.; DISEASE: Camptodactyly, tall stature, and hearing loss syndrome (CATSHLS) [MIM:610474]: An 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 intellectual disability, 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. {ECO:0000269|PubMed:17033969}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Multiple myeloma (MM) [MIM:254500]: A 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. {ECO:0000269|PubMed:11529856, ECO:0000269|PubMed:9207791}. Note=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: Lacrimo-auriculo-dento-digital syndrome 2 (LADD2) [MIM:620192]: A form of lacrimo-auriculo-dento-digital syndrome, an autosomal dominant disease 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. {ECO:0000269|PubMed:16501574}. Note=The disease may be caused by variants affecting the gene represented in this entry.; DISEASE: Keratinocytic non-epidermolytic nevus (KNEN) [MIM:162900]: Epidermal 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. {ECO:0000269|PubMed:16841094}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Muenke syndrome (MNKS) [MIM:602849]: A 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, intellectual disability and respiratory insufficiency. {ECO:0000269|PubMed:11746040, ECO:0000269|PubMed:9042914, ECO:0000269|PubMed:9950359}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Keratosis, seborrheic (KERSEB) [MIM:182000]: A 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. {ECO:0000269|PubMed:15772091}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A 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. {ECO:0000269|PubMed:19855393}. Note=The gene represented in this entry may be involved in disease pathogenesis.; DISEASE: Achondroplasia, severe, with developmental delay and acanthosis nigricans (SADDAN) [MIM:616482]: A 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. {ECO:0000269|PubMed:10053006}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a 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. {ECO:0000269|PubMed:10611230, ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:11703096, ECO:0000269|PubMed:14534538, ECO:0000269|PubMed:16410555, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17145761, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:17561467, ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:19286672, ECO:0000269|PubMed:8663044}.
uniprot
proteins
mass_dalton
87710
uniprot
proteins
mutagenesis
MUTAGEN 508; /note="K->A: Loss of kinase activity. Abolishes ubiquitination."; /evidence="ECO:0000269|PubMed:12297284, ECO:0000269|PubMed:16410555"; MUTAGEN 577; /note="Y->F: Minor effect on kinase activity."; /evidence="ECO:0000269|PubMed:11294897"; MUTAGEN 650; /note="K->D: Constitutively activated kinase."; MUTAGEN 650; /note="K->L: Constitutively activated kinase."; MUTAGEN 724; /note="Y->F: Strongly reduced kinase activity. Strongly reduced mitogen activity."; /evidence="ECO:0000269|PubMed:11294897"; MUTAGEN 760; /note="Y->F: Minor effect on kinase activity."; /evidence="ECO:0000269|PubMed:11294897"; MUTAGEN 770; /note="Y->F: Minor effect on kinase activity. Increased mitogen activity."; /evidence="ECO:0000269|PubMed:11294897
uniprot
proteins
post_translational_modification
PTM: 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. {ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:19286672}.; PTM: Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation. {ECO:0000269|PubMed:12297284, ECO:0000269|PubMed:17509076}.; PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. {ECO:0000269|PubMed:11703096, ECO:0000269|PubMed:16410555, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17509076}.
uniprot
proteins
protein_family
Fibroblast growth factor receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10053006
uniprot
proteins
pubmed
10215410
uniprot
proteins
pubmed
10360402
uniprot
proteins
pubmed
10471491
uniprot
proteins
pubmed
10611230
uniprot
proteins
pubmed
10671061
uniprot
proteins
pubmed
10777366
uniprot
proteins
pubmed
11055896
uniprot
proteins
pubmed
11294897
uniprot
proteins
pubmed
11314002
uniprot
proteins
pubmed
11325814
uniprot
proteins
pubmed
11529856
uniprot
proteins
pubmed
11703096
uniprot
proteins
pubmed
11746040
uniprot
proteins
pubmed
12297284
uniprot
proteins
pubmed
12707965
uniprot
proteins
pubmed
14534538
uniprot
proteins
pubmed
14732692
uniprot
proteins
pubmed
15748888
uniprot
proteins
pubmed
15772091
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
15863030
uniprot
proteins
pubmed
16410555
uniprot
proteins
pubmed
16501574
uniprot
proteins
pubmed
16597617
uniprot
proteins
pubmed
1664411
uniprot
proteins
pubmed
16841094
uniprot
proteins
pubmed
17033969
uniprot
proteins
pubmed
17145761
uniprot
proteins
pubmed
17311277
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17509076
uniprot
proteins
pubmed
17561467
uniprot
proteins
pubmed
17623664
uniprot
proteins
pubmed
17935505
uniprot
proteins
pubmed
1847508
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
19066716
uniprot
proteins
pubmed
19088846
uniprot
proteins
pubmed
19286672
uniprot
proteins
pubmed
19855393
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
2247464
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
7493034
uniprot
proteins
pubmed
7495869
uniprot
proteins
pubmed
7670477
uniprot
proteins
pubmed
7758520
uniprot
proteins
pubmed
7773297
uniprot
proteins
pubmed
7847369
uniprot
proteins
pubmed
7923141
uniprot
proteins
pubmed
8078586
uniprot
proteins
pubmed
8589699
uniprot
proteins
pubmed
8599935
uniprot
proteins
pubmed
8663044
uniprot
proteins
pubmed
8754806
uniprot
proteins
pubmed
8845844
uniprot
proteins
pubmed
9042914
uniprot
proteins
pubmed
9207791
uniprot
proteins
pubmed
9452043
uniprot
proteins
pubmed
9525367
uniprot
proteins
pubmed
9790257
uniprot
proteins
pubmed
9950359
uniprot
proteins
sequence_length
806
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle. Endoplasmic reticulum. Note=The activated receptor is rapidly internalized and degraded. Detected in intracellular vesicles after internalization of the autophosphorylated receptor.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted.; SUBCELLULAR LOCATION: [Isoform 4]: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 376..396; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins