P22607 (FGFR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fibroblast growth factor receptor 3
Short name=FGFR-3
EC=2.7.10.1

Alternative name(s):
CD_antigen=CD333

Gene names

Name:	FGFR3
Synonyms:	JTK4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	806 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.17 Ref.18 Ref.19 Ref.20 Ref.22 Ref.23 Ref.25
Catalytic activity	ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.14 Ref.20
Enzyme 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. Ref.19 Ref.20 Ref.30
Subunit structure	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. Ref.11 Ref.12 Ref.16 Ref.17 Ref.18 Ref.21 Ref.25
Subcellular location	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. Ref.12 Ref.17 Ref.18 Ref.19
Tissue specificity	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. Ref.7
Domain	The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Ref.30
Post-translational modification	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. Ref.12 Ref.13 Ref.14 Ref.15 Ref.17 Ref.18 Ref.22 Ref.25 Ubiquitinated. Is rapidly ubiquitinated after ligand binding and autophosphorylation, leading to receptor internalization and degradation. Subject to both proteasomal and lysosomal degradation. Ref.12 Ref.14 Ref.19 N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. Ref.17 Ref.19 Ref.22
Involvement in 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.12 Ref.14 Ref.31 Ref.32 Ref.33 Ref.38 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.37 Ref.49 Ref.54 Ref.55 Ref.61 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34 Ref.35 Ref.39 Ref.42 Ref.45 Ref.47 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.14 Ref.35 Hypochondroplasia (HCH) [MIM:146000]: Autosomal dominant disease and is characterized by disproportionate short stature. It resembles achondroplasia, but with a less severe phenotype. Note: The disease is caused by mutations affecting the gene represented in this entry. 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Somatic mutations can constitutively activate FGFR3. 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. Note: The gene represented in this entry is involved in disease pathogenesis. Camptodactyly tall stature and hearing loss syndrome (CATSHL syndrome) [MIM:610474]: 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. Note: The disease is caused by mutations affecting the gene represented in this entry. 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. 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. Lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]: An 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.60 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.59 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, mental retardation and respiratory insufficiency. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.48 Ref.52 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. Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.57 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. Note: The gene represented in this entry may be involved in disease pathogenesis. Ref.63
Sequence similarities	Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily. Contains 3 Ig-like C2-type (immunoglobulin-like) domains. Contains 1 protein kinase domain.
Sequence caution	The sequence BAD92678.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Apoptosis
Cellular component	Cell membrane Cytoplasmic vesicle Endoplasmic reticulum Membrane
Coding sequence diversity	Alternative splicing Chromosomal rearrangement Polymorphism
Disease	Craniosynostosis Deafness Disease mutation Dwarfism Ectodermal dysplasia Lacrimo-auriculo-dento-digital syndrome
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	JAK-STAT cascade Traceable author statement PubMed 10918587. Source: ProtInc MAPK cascade Traceable author statement PubMed 10918587. Source: ProtInc alveolar secondary septum development Inferred from electronic annotation. Source: Compara apoptotic process Inferred from electronic annotation. Source: UniProtKB-KW axonogenesis involved in innervation Inferred from electronic annotation. Source: Compara bone maturation Inferred from sequence or structural similarity PubMed 20582225. Source: BHF-UCL central nervous system myelination Inferred from electronic annotation. Source: Compara chondrocyte differentiation Traceable author statement Ref.27. Source: UniProtKB chondrocyte proliferation Traceable author statement Ref.27. Source: UniProtKB cochlea development Inferred from electronic annotation. Source: Compara digestive tract morphogenesis Inferred from electronic annotation. Source: Compara endochondral bone growth Traceable author statement Ref.27. Source: UniProtKB endochondral ossification Traceable author statement Ref.27. Source: UniProtKB epithelial cell fate commitment Inferred from electronic annotation. Source: Compara inner ear receptor cell differentiation Inferred from electronic annotation. Source: Compara insulin receptor signaling pathway Traceable author statement. Source: Reactome lens fiber cell development Inferred from electronic annotation. Source: Compara lens morphogenesis in camera-type eye Inferred from electronic annotation. Source: Compara morphogenesis of an epithelium Inferred from electronic annotation. Source: Compara negative regulation of apoptotic process Inferred from electronic annotation. Source: Compara negative regulation of astrocyte differentiation Inferred from electronic annotation. Source: Compara negative regulation of developmental growth Inferred from sequence or structural similarity PubMed 20582225. Source: BHF-UCL negative regulation of epithelial cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of mitosis Inferred from electronic annotation. Source: Compara negative regulation of smoothened signaling pathway Inferred from electronic annotation. Source: Compara negative regulation of transcription from RNA polymerase II promoter Inferred from electronic annotation. Source: Compara peptidyl-tyrosine phosphorylation Inferred from direct assay Ref.13. Source: UniProtKB positive regulation of ERK1 and ERK2 cascade Inferred from mutant phenotype Ref.13. Source: UniProtKB positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of apoptotic process Inferred from electronic annotation. Source: Compara positive regulation of canonical Wnt receptor signaling pathway Inferred from electronic annotation. Source: Compara positive regulation of cell differentiation Inferred from electronic annotation. Source: Compara positive regulation of cell proliferation Inferred from mutant phenotype Ref.13Ref.11. Source: UniProtKB positive regulation of endothelial cell proliferation Inferred from electronic annotation. Source: Compara positive regulation of phosphatidylinositol 3-kinase activity Inferred from mutant phenotype Ref.13. Source: UniProtKB positive regulation of phospholipase activity Inferred from mutant phenotype Ref.18. Source: UniProtKB positive regulation of protein ubiquitination Inferred from electronic annotation. Source: Compara positive regulation of tyrosine phosphorylation of Stat1 protein Inferred from mutant phenotype Ref.13Ref.18. Source: UniProtKB positive regulation of tyrosine phosphorylation of Stat3 protein Inferred from mutant phenotype Ref.13. Source: UniProtKB protein autophosphorylation Inferred from direct assay Ref.13. Source: UniProtKB regulation of apoptotic process Inferred from mutant phenotype Ref.18. Source: UniProtKB response to axon injury Inferred from electronic annotation. Source: Compara somatic stem cell maintenance Inferred from electronic annotation. Source: Compara substantia nigra development Inferred from electronic annotation. Source: Compara
Cellular_component	cytoplasmic membrane-bounded vesicle Inferred from electronic annotation. Source: UniProtKB-SubCell endoplasmic reticulum Inferred from electronic annotation. Source: UniProtKB-SubCell integral to plasma membrane Inferred from direct assay Ref.11. Source: UniProtKB internal side of plasma membrane Inferred from electronic annotation. Source: Compara lysosome Inferred from electronic annotation. Source: Compara perinuclear region of cytoplasm Inferred from electronic annotation. Source: Compara
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW fibroblast growth factor binding Inferred from direct assay Ref.11. Source: UniProtKB fibroblast growth factor-activated receptor activity Inferred from mutant phenotype Ref.11. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
FGF1	P05230	3	EBI-348399,EBI-698068
HSP90AB1	P08238	2	EBI-348399,EBI-352572

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P22607-1)

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.

Isoform 2 (identifier: P22607-2)

Also known as: IIIb;

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

Isoform 3 (identifier: P22607-3)

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

Isoform 4 (identifier: P22607-4)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 22

22

Chain

23 – 806

784

Fibroblast growth factor receptor 3

PRO_0000016785

Regions

Topological domain

23 – 375

353

Extracellular Potential

Transmembrane

376 – 396

21

Helical; Potential

Topological domain

397 – 806

410

Cytoplasmic Potential

Domain

24 – 126

103

Ig-like C2-type 1

Domain

151 – 244

94

Ig-like C2-type 2

Domain

253 – 355

103

Ig-like C2-type 3

Domain

472 – 761

290

Protein kinase

Nucleotide binding

478 – 486

9

ATP By similarity

Sites

Active site

617

1

Proton acceptor By similarity

Binding site

508

1

ATP By similarity

Amino acid modifications

Modified residue

647

1

Phosphotyrosine; by autocatalysis

Modified residue

648

1

Phosphotyrosine; by autocatalysis

Modified residue

724

1

Phosphotyrosine; by autocatalysis Ref.13

Modified residue

760

1

Phosphotyrosine; by autocatalysis Ref.25

Glycosylation

98

1

N-linked (GlcNAc...) Potential

Glycosylation

225

1

N-linked (GlcNAc...) Potential

Glycosylation

262

1

N-linked (GlcNAc...) Potential

Glycosylation

294

1

N-linked (GlcNAc...) Potential

Glycosylation

315

1

N-linked (GlcNAc...) Potential

Glycosylation

328

1

N-linked (GlcNAc...) Potential

Disulfide bond

61 ↔ 109

By similarity

Disulfide bond

176 ↔ 228

By similarity

Disulfide bond

275 ↔ 339

By similarity

Natural variations

Alternative sequence

311 – 422

112

Missing in isoform 3.

VSP_002989

Alternative sequence

311 – 358

48

TAGAN…LVVLP → SWISESVEADVRLRLANVSE RDGGEYLCRATNFIGVAEKA FWLSVHGPRA in isoform 2.

VSP_002988

Alternative sequence

654 – 806

153

GRLPV…GGSRT → LVLWGPALGDLHAGGLPVPR HPCGGALQAAEGGPPHGQAR QLHTRPVHDHAGVLACRALP EAHLQAAGGGPGPCPYRDVH RRVPGPVGAFRAVLPGWPGH PQLQLLRGRLRVCPRPAAPG PTQQWGLADVKGHWSPTM in isoform 4.

VSP_040945

Natural variant

65

1

G → R. Ref.4
Corresponds to variant rs2305178 [ dbSNP | Ensembl ].

VAR_022167

Natural variant

79

1

T → S in a lung adenocarcinoma sample; somatic mutation. Ref.62

VAR_042207

Natural variant

228

1

C → R in a colorectal adenocarcinoma sample; somatic mutation. Ref.62

VAR_042208

Natural variant

248

1

R → C in KERSEB, bladder cancer, 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. Ref.19 Ref.35 Ref.39 Ref.47 Ref.49 Ref.53 Ref.57 Ref.59

VAR_004148

Natural variant

249

1

S → C in KERSEB, bladder cancer, cervical cancer and TD1. Ref.34 Ref.39 Ref.47 Ref.49 Ref.57

VAR_004149

Natural variant

250

1

P → R in MNKS; also some individuals with autosomal dominant congenital sensorineural deafness without craniosynostosis. Ref.40 Ref.46 Ref.48 Ref.52
Corresponds to variant rs4647924 [ dbSNP | Ensembl ].

VAR_004150

Natural variant

322

1

E → K in colorectal cancer. Ref.54

VAR_018388

Natural variant

338

1

T → M. Ref.62

VAR_042209

Natural variant

370

1

G → C in KERSEB, bladder cancer, keratinocytic non-epidermolytic nevus and TD1. Ref.39 Ref.42 Ref.49 Ref.57 Ref.59

VAR_004151

Natural variant

371

1

S → C in KERSEB and TD1. Ref.35 Ref.57

VAR_004152

Natural variant

373

1

Y → C in KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation. Ref.19 Ref.39 Ref.41 Ref.47 Ref.57

VAR_004153

Natural variant

375

1

G → C in ACH. Ref.33

VAR_004154

Natural variant

380

1

G → R in keratinocytic non-epidermolytic nevus and ACH; very common mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. Ref.12 Ref.14 Ref.18 Ref.31 Ref.32 Ref.38 Ref.59
Corresponds to variant rs28931614 [ dbSNP | Ensembl ].

VAR_004155

Natural variant

384

1

F → L. Ref.4 Ref.62
Corresponds to variant rs17881656 [ dbSNP | Ensembl ].

VAR_022168

Natural variant

391

1

A → E in CAN. Ref.37 Ref.61
Corresponds to variant rs28931615 [ dbSNP | Ensembl ].

VAR_004156

Natural variant

441

1

A → T. Ref.4
Corresponds to variant rs17884368 [ dbSNP | Ensembl ].

VAR_022169

Natural variant

513

1

D → N in LADDS. Ref.60

VAR_029887

Natural variant

538

1

I → V in hypochondroplasia. Ref.43

VAR_004157

Natural variant

540

1

N → K in hypochondroplasia. Ref.36
Corresponds to variant rs28933068 [ dbSNP | Ensembl ].

VAR_004158

Natural variant

540

1

N → S in hypochondroplasia; mild. Ref.51 Ref.56

VAR_018389

Natural variant

540

1

N → T in hypochondroplasia. Ref.44

VAR_004159

Natural variant

621

1

R → H in CATSHL syndrome. Ref.58

VAR_029108

Natural variant

646

1

D → N. Ref.62

VAR_042210

Natural variant

650

1

K → E in KERSEB, TD2, TGCT and bladder cancer samples; bladder transitional cell carcinoma; somatic mutation; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. Ref.13 Ref.14 Ref.15 Ref.18 Ref.20 Ref.35 Ref.41 Ref.49 Ref.57 Ref.62 Ref.63

VAR_004160

Natural variant

650

1

K → M in KERSEB, ACH and TD1; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. Ref.18 Ref.19 Ref.41 Ref.45 Ref.57

VAR_004161

Natural variant

650

1

K → Q in hypochondroplasia and bladder cancer; in hypochondroplasia the form is milder than that seen in individuals with the K-540 or M-650 mutations. Ref.50 Ref.55

VAR_018390

Natural variant

717

1

A → T. Ref.4
Corresponds to variant rs17882190 [ dbSNP | Ensembl ].

VAR_022170

Natural variant

726

1

I → F. Ref.4
Corresponds to variant rs17880763 [ dbSNP | Ensembl ].

VAR_022171

Experimental info

Mutagenesis

508

1

K → A: Loss of kinase activity. Abolishes ubiquitination. Ref.14 Ref.17

Mutagenesis

577

1

Y → F: Minor effect on kinase activity. Ref.13

Mutagenesis

724

1

Y → F: Strongly reduced kinase activity. Strongly reduced mitogen activity. Ref.13

Mutagenesis

760

1

Y → F: Minor effect on kinase activity. Ref.13

Mutagenesis

770

1

Y → F: Minor effect on kinase activity. Increased mitogen activity. Ref.13

Sequence conflict

395

1

L → V in AAA58470. Ref.7

Sequence conflict

421

1

R → RQ in BAD92678. Ref.3

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

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.

.

.

.

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.

.

.

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806

Helix Strand Turn

Details...

Beta strand

163 – 167

5

Beta strand

172 – 175

4

Beta strand

185 – 187

3

Turn

208 – 211

4

Beta strand

212 – 215

4

Helix

220 – 222

3

Beta strand

226 – 232

7

Beta strand

235 – 246

12

Beta strand

263 – 268

6

Beta strand

271 – 273

3

Beta strand

283 – 289

7

Helix

293 – 295

3

Beta strand

302 – 304

3

Beta strand

324 – 326

3

Beta strand

335 – 345

11

Beta strand

348 – 357

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (IIIc) [UniParc]. Last modified August 1, 1991. Version 1. Checksum: BC5EA75EA46F447E	FASTA	806	87,710
	10 20 30 40 50 60 MGAPACALAL CVAVAIVAGA SSESLGTEQR VVGRAAEVPG PEPGQQEQLV FGSGDAVELS 70 80 90 100 110 120 CPPPGGGPMG PTVWVKDGTG LVPSERVLVG PQRLQVLNAS HEDSGAYSCR QRLTQRVLCH 130 140 150 160 170 180 FSVRVTDAPS SGDDEDGEDE AEDTGVDTGA PYWTRPERMD KKLLAVPAAN TVRFRCPAAG 190 200 210 220 230 240 NPTPSISWLK NGREFRGEHR IGGIKLRHQQ WSLVMESVVP SDRGNYTCVV ENKFGSIRQT 250 260 270 280 290 300 YTLDVLERSP HRPILQAGLP ANQTAVLGSD VEFHCKVYSD AQPHIQWLKH VEVNGSKVGP 310 320 330 340 350 360 DGTPYVTVLK TAGANTTDKE LEVLSLHNVT FEDAGEYTCL AGNSIGFSHH SAWLVVLPAE 370 380 390 400 410 420 EELVEADEAG SVYAGILSYG VGFFLFILVV AAVTLCRLRS PPKKGLGSPT VHKISRFPLK 430 440 450 460 470 480 RQVSLESNAS MSSNTPLVRI ARLSSGEGPT LANVSELELP ADPKWELSRA RLTLGKPLGE 490 500 510 520 530 540 GCFGQVVMAE AIGIDKDRAA KPVTVAVKML KDDATDKDLS DLVSEMEMMK MIGKHKNIIN 550 560 570 580 590 600 LLGACTQGGP LYVLVEYAAK GNLREFLRAR RPPGLDYSFD TCKPPEEQLT FKDLVSCAYQ 610 620 630 640 650 660 VARGMEYLAS QKCIHRDLAA RNVLVTEDNV MKIADFGLAR DVHNLDYYKK TTNGRLPVKW 670 680 690 700 710 720 MAPEALFDRV YTHQSDVWSF GVLLWEIFTL GGSPYPGIPV EELFKLLKEG HRMDKPANCT 730 740 750 760 770 780 HDLYMIMREC WHAAPSQRPT FKQLVEDLDR VLTVTSTDEY LDLSAPFEQY SPGGQDTPSS 790 800 SSSGDDSVFA HDLLPPAPPS SGGSRT
	Isoform 2 (IIIb) [UniParc]. Checksum: E08CE2C9FD56D8F9	FASTA	808	88,157
	10 20 30 40 50 60 MGAPACALAL CVAVAIVAGA SSESLGTEQR VVGRAAEVPG PEPGQQEQLV FGSGDAVELS 70 80 90 100 110 120 CPPPGGGPMG PTVWVKDGTG LVPSERVLVG PQRLQVLNAS HEDSGAYSCR QRLTQRVLCH 130 140 150 160 170 180 FSVRVTDAPS SGDDEDGEDE AEDTGVDTGA PYWTRPERMD KKLLAVPAAN TVRFRCPAAG 190 200 210 220 230 240 NPTPSISWLK NGREFRGEHR IGGIKLRHQQ WSLVMESVVP SDRGNYTCVV ENKFGSIRQT 250 260 270 280 290 300 YTLDVLERSP HRPILQAGLP ANQTAVLGSD VEFHCKVYSD AQPHIQWLKH VEVNGSKVGP 310 320 330 340 350 360 DGTPYVTVLK SWISESVEAD VRLRLANVSE RDGGEYLCRA TNFIGVAEKA FWLSVHGPRA 370 380 390 400 410 420 AEEELVEADE AGSVYAGILS YGVGFFLFIL VVAAVTLCRL RSPPKKGLGS PTVHKISRFP 430 440 450 460 470 480 LKRQVSLESN ASMSSNTPLV RIARLSSGEG PTLANVSELE LPADPKWELS RARLTLGKPL 490 500 510 520 530 540 GEGCFGQVVM AEAIGIDKDR AAKPVTVAVK MLKDDATDKD LSDLVSEMEM MKMIGKHKNI 550 560 570 580 590 600 INLLGACTQG GPLYVLVEYA AKGNLREFLR ARRPPGLDYS FDTCKPPEEQ LTFKDLVSCA 610 620 630 640 650 660 YQVARGMEYL ASQKCIHRDL AARNVLVTED NVMKIADFGL ARDVHNLDYY KKTTNGRLPV 670 680 690 700 710 720 KWMAPEALFD RVYTHQSDVW SFGVLLWEIF TLGGSPYPGI PVEELFKLLK EGHRMDKPAN 730 740 750 760 770 780 CTHDLYMIMR ECWHAAPSQR PTFKQLVEDL DRVLTVTSTD EYLDLSAPFE QYSPGGQDTP 790 800 SSSSSGDDSV FAHDLLPPAP PSSGGSRT
	Isoform 3 [UniParc]. Checksum: 4493C5990FD68964	FASTA	694	75,696
	10 20 30 40 50 60 MGAPACALAL CVAVAIVAGA SSESLGTEQR VVGRAAEVPG PEPGQQEQLV FGSGDAVELS 70 80 90 100 110 120 CPPPGGGPMG PTVWVKDGTG LVPSERVLVG PQRLQVLNAS HEDSGAYSCR QRLTQRVLCH 130 140 150 160 170 180 FSVRVTDAPS SGDDEDGEDE AEDTGVDTGA PYWTRPERMD KKLLAVPAAN TVRFRCPAAG 190 200 210 220 230 240 NPTPSISWLK NGREFRGEHR IGGIKLRHQQ WSLVMESVVP SDRGNYTCVV ENKFGSIRQT 250 260 270 280 290 300 YTLDVLERSP HRPILQAGLP ANQTAVLGSD VEFHCKVYSD AQPHIQWLKH VEVNGSKVGP 310 320 330 340 350 360 DGTPYVTVLK VSLESNASMS SNTPLVRIAR LSSGEGPTLA NVSELELPAD PKWELSRARL 370 380 390 400 410 420 TLGKPLGEGC FGQVVMAEAI GIDKDRAAKP VTVAVKMLKD DATDKDLSDL VSEMEMMKMI 430 440 450 460 470 480 GKHKNIINLL GACTQGGPLY VLVEYAAKGN LREFLRARRP PGLDYSFDTC KPPEEQLTFK 490 500 510 520 530 540 DLVSCAYQVA RGMEYLASQK CIHRDLAARN VLVTEDNVMK IADFGLARDV HNLDYYKKTT 550 560 570 580 590 600 NGRLPVKWMA PEALFDRVYT HQSDVWSFGV LLWEIFTLGG SPYPGIPVEE LFKLLKEGHR 610 620 630 640 650 660 MDKPANCTHD LYMIMRECWH AAPSQRPTFK QLVEDLDRVL TVTSTDEYLD LSAPFEQYSP 670 680 690 GGQDTPSSSS SGDDSVFAHD LLPPAPPSSG GSRT
	Isoform 4 [UniParc]. Checksum: EA4EEB033A1433BB	FASTA	791	85,083
	10 20 30 40 50 60 MGAPACALAL CVAVAIVAGA SSESLGTEQR VVGRAAEVPG PEPGQQEQLV FGSGDAVELS 70 80 90 100 110 120 CPPPGGGPMG PTVWVKDGTG LVPSERVLVG PQRLQVLNAS HEDSGAYSCR QRLTQRVLCH 130 140 150 160 170 180 FSVRVTDAPS SGDDEDGEDE AEDTGVDTGA PYWTRPERMD KKLLAVPAAN TVRFRCPAAG 190 200 210 220 230 240 NPTPSISWLK NGREFRGEHR IGGIKLRHQQ WSLVMESVVP SDRGNYTCVV ENKFGSIRQT 250 260 270 280 290 300 YTLDVLERSP HRPILQAGLP ANQTAVLGSD VEFHCKVYSD AQPHIQWLKH VEVNGSKVGP 310 320 330 340 350 360 DGTPYVTVLK TAGANTTDKE LEVLSLHNVT FEDAGEYTCL AGNSIGFSHH SAWLVVLPAE 370 380 390 400 410 420 EELVEADEAG SVYAGILSYG VGFFLFILVV AAVTLCRLRS PPKKGLGSPT VHKISRFPLK 430 440 450 460 470 480 RQVSLESNAS MSSNTPLVRI ARLSSGEGPT LANVSELELP ADPKWELSRA RLTLGKPLGE 490 500 510 520 530 540 GCFGQVVMAE AIGIDKDRAA KPVTVAVKML KDDATDKDLS DLVSEMEMMK MIGKHKNIIN 550 560 570 580 590 600 LLGACTQGGP LYVLVEYAAK GNLREFLRAR RPPGLDYSFD TCKPPEEQLT FKDLVSCAYQ 610 620 630 640 650 660 VARGMEYLAS QKCIHRDLAA RNVLVTEDNV MKIADFGLAR DVHNLDYYKK TTNLVLWGPA 670 680 690 700 710 720 LGDLHAGGLP VPRHPCGGAL QAAEGGPPHG QARQLHTRPV HDHAGVLACR ALPEAHLQAA 730 740 750 760 770 780 GGGPGPCPYR DVHRRVPGPV GAFRAVLPGW PGHPQLQLLR GRLRVCPRPA APGPTQQWGL 790 ADVKGHWSPT M

References

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[1]	"Isolation of an additional member of the fibroblast growth factor receptor family, FGFR-3." Keegan K., Johnson D.E., Williams L.T., Hayman M.J. Proc. Natl. Acad. Sci. U.S.A. 88:1095-1099(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]	"Fibroblast growth factor receptor 3 lacking the Ig IIIb and transmembrane domains secreted from human squamous cell carcinoma DJM-1 binds to FGFs." Terada M., Shimizu A., Sato N., Miyakaze S.I., Katayama H., Kurokawa-Seo M. Mol. Cell Biol. Res. Commun. 4:365-373(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[3]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). Tissue: Brain.
[4]	NIEHS SNPs program Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ARG-65; LEU-384; THR-441; THR-717 AND PHE-726.
[5]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"A gene encoding a fibroblast growth factor receptor isolated from the Huntington disease gene region of human chromosome 4." Thompson L.M., Plummer S., Schalling M., Altherr M.R., Gusella J.F., Housman D.E., Wasmuth J.J. Genomics 11:1133-1142(1991) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 76-806 (ISOFORM 1), TISSUE SPECIFICITY. Tissue: Fetal brain.
[8]	"Putative tyrosine kinases expressed in K-562 human leukemia cells." Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K. Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 614-681.
[9]	"Identification of a novel variant form of fibroblast growth factor receptor 3 (FGFR3 IIIb) in human colonic epithelium." Murgue B., Tsunekawa S., Rosenberg I., deBeaumont M., Podolsky D.K. Cancer Res. 54:5206-5211(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-358 (ISOFORM 2). Tissue: Colon tumor.
[10]	"The choice between alternative IIIb and IIIc exons of the FGFR-3 gene is not strictly tissue-specific." Scotet E., Houssaint E. Biochim. Biophys. Acta 1264:238-242(1995) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 311-358 (ISOFORM 2). Tissue: Keratinocyte.
[11]	"Receptor specificity of the fibroblast growth factor family." Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M. J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1; FGF2; FGF4; FGF8 AND FGF9, FUNCTION IN CELL PROLIFERATION.
[12]	"The transmembrane mutation G380R in fibroblast growth factor receptor 3 uncouples ligand-mediated receptor activation from down-regulation." Monsonego-Ornan E., Adar R., Feferman T., Segev O., Yayon A. Mol. Cell. Biol. 20:516-522(2000) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS FGF9 RECEPTOR IN CHONDROCYTES AND IN ACTIVATION OF SIGNALING PATHWAYS, SUBUNIT, SUBCELLULAR LOCATION, DEGRADATION, AUTOPHOSPHORYLATION, CHARACTERIZATION OF VARIANT ACH ARG-380.
[13]	"Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation." Hart K.C., Robertson S.C., Donoghue D.J. Mol. Biol. Cell 12:931-942(2001) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN STIMULATION OF CELL PROLIFERATION; PHOSPHORYLATION OF PIK3R1; PTPN11/SHP2; STAT1; STAT3 AND MAP KINASES, PHOSPHORYLATION AT TYR-724, MUTAGENESIS OF TYR-577; TYR-724; TYR-760 AND TYR-770, CHARACTERIZATION OF VARIANT GLU-650.
[14]	"FGF receptors ubiquitylation: dependence on tyrosine kinase activity and role in downregulation." Monsonego-Ornan E., Adar R., Rom E., Yayon A. FEBS Lett. 528:83-89(2002) [PubMed] [Europe PMC] [Abstract] Cited for: UBIQUITINATION, PHOSPHORYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF LYS-508, CHARACTERIZATION OF VARIANT ACH ARG-380, CHARACTERIZATION OF VARIANT TD2 GLU-650.
[15]	"The phosphotyrosine phosphatase SHP2 is a critical mediator of transformation induced by the oncogenic fibroblast growth factor receptor 3." Agazie Y.M., Movilla N., Ischenko I., Hayman M.J. Oncogene 22:6909-6918(2003) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION AS PROTO-ONCOGENE IN ACTIVATION OF SIGNALING AND CELL PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF FRS2, CHARACTERIZATION OF VARIANT GLU-650, AUTOPHOSPHORYLATION.
[16]	"Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family." Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M. J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF1; FGF8; FGF9; FGF17; FGF18; FGF19 AND FGF20, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
[17]	"Suppressors of cytokine signaling (SOCS) 1 and SOCS3 interact with and modulate fibroblast growth factor receptor signaling." Ben-Zvi T., Yayon A., Gertler A., Monsonego-Ornan E. J. Cell Sci. 119:380-387(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH SOCS1 AND SOCS3, FUNCTION IN ACTIVATION OF STAT1 AND MAP KINASES, GLYCOSYLATION, PHOSPHORYLATION, MUTAGENESIS OF LYS-508, SUBCELLULAR LOCATION.
[18]	"Sustained phosphorylation of mutated FGFR3 is a crucial feature of genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell line via PLCgamma-activated STAT1." Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y., Tanaka H. Bone 41:273-281(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN REGULATION OF CHONDROCYTE PROLIFERATION AND IN ACTIVATION OF PLCG1 AND STAT1, INTERACTION WITH FHF1 AND HEPARIN, SUBCELLULAR LOCATION, PHOSPHORYLATION, CHARACTERIZATION OF VARIANTS ARG-380; GLU-650 AND MET-650.
[19]	"The localization of FGFR3 mutations causing thanatophoric dysplasia type I differentially affects phosphorylation, processing and ubiquitylation of the receptor." Bonaventure J., Horne W.C., Baron R. FEBS J. 274:3078-3093(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF CBL, UBIQUITINATION, GLYCOSYLATION, SUBCELLULAR LOCATION, ENZYME REGULATION, CHARACTERIZATION OF VARIANTS CYS-248; CYS-373 AND MET-650.
[20]	"Bisindolylmaleimide I suppresses fibroblast growth factor-mediated activation of Erk MAP kinase in chondrocytes by preventing Shp2 association with the Frs2 and Gab1 adaptor proteins." Krejci P., Masri B., Salazar L., Farrington-Rock C., Prats H., Thompson L.M., Wilcox W.R. J. Biol. Chem. 282:2929-2936(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2, CHARACTERIZATION OF VARIANT GLU-650, ENZYME REGULATION, CATALYTIC ACTIVITY.
[21]	"Tissue-specific expression of betaKlotho and fibroblast growth factor (FGF) receptor isoforms determines metabolic activity of FGF19 and FGF21." Kurosu H., Choi M., Ogawa Y., Dickson A.S., Goetz R., Eliseenkova A.V., Mohammadi M., Rosenblatt K.P., Kliewer S.A., Kuro-o M. J. Biol. Chem. 282:26687-26695(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH FGF19; FGF21 AND KLB.
[22]	"Fibroblast growth factor receptor-induced phosphorylation of STAT1 at the Golgi apparatus without translocation to the nucleus." Citores L., Bai L., Sorensen V., Olsnes S. J. Cell. Physiol. 212:148-156(2007) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN STAT1 PHOSPHORYLATION, GLYCOSYLATION, PHOSPHORYLATION.
[23]	"Analysis of STAT1 activation by six FGFR3 mutants associated with skeletal dysplasia undermines dominant role of STAT1 in FGFR3 signaling in cartilage." Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A., Thompson L.M., Bryja V., Kozubik A., Wilcox W.R. PLoS ONE 3:E3961-E3961(2008) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN ACTIVATION OF STAT1; STAT5; MAPK1/ERK2; MAPK3/ERK1 AND THE MAP KINASE SIGNALING PATHWAY.
[24]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[25]	"A novel interaction between fibroblast growth factor receptor 3 and the p85 subunit of phosphoinositide 3-kinase: activation-dependent regulation of ERK by p85 in multiple myeloma cells." Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D., Wilcox W.R., Thompson L.M. Hum. Mol. Genet. 18:1951-1961(2009) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PIK3R1 AND PLCG1, PHOSPHORYLATION AT TYR-760.
[26]	"Cellular signaling by fibroblast growth factor receptors." Eswarakumar V.P., Lax I., Schlessinger J. Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION; ALTERNATIVE SPLICING; SIGNALING AND ROLE IN DISEASE.
[27]	"Cell responses to FGFR3 signalling: growth, differentiation and apoptosis." L'Hote C.G., Knowles M.A. Exp. Cell Res. 304:417-431(2005) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION; LIGANDS; SIGNALING; ALTERNATIVE SPLICING; DOMAIN; ROLE IN DISEASE; UBIQUITINATION AND DEGRADATION.
[28]	"FGFR3-related dwarfism and cell signaling." Harada D., Yamanaka Y., Ueda K., Tanaka H., Seino Y. J. Bone Miner. Metab. 27:9-15(2009) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON ROLE IN SKELETON DEVELOPMENT AND DISEASE.
[29]	"Fibroblast growth factor signalling: from development to cancer." Turner N., Grose R. Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION IN FGF SIGNALING.
[30]	"Insights into the molecular basis for fibroblast growth factor receptor autoinhibition and ligand-binding promiscuity." Olsen S.K., Ibrahimi O.A., Raucci A., Zhang F., Eliseenkova A.V., Yayon A., Basilico C., Linhardt R.J., Schlessinger J., Mohammadi M. Proc. Natl. Acad. Sci. U.S.A. 101:935-940(2004) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-365 IN COMPLEX WITH FGF1, ENZYME REGULATION, DOMAIN.
[31]	"Mutations in the gene encoding fibroblast growth factor receptor-3 in achondroplasia." Rousseau F., Bonaventure J., Legeai-Mallet L., Pelet A., Rozet J.-M., Maroteaux P., le Merrer M., Munnich A. Nature 371:252-254(1994) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACH ARG-380.
[32]	"Achondroplasia is defined by recurrent G380R mutations of FGFR3." Bellus G.A., Hefferon T.W., de Luna R.I., Hecht J.T., Horton W.A., Machado M., Kaitila I., McIntosh I., Francomano C.A. Am. J. Hum. Genet. 56:368-373(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACH ARG-380.
[33]	"A glycine 375-to-cysteine substitution in the transmembrane domain of the fibroblast growth factor receptor-3 in a newborn with achondroplasia." Superti-Furga A., Eich G., Bucher H.U., Wisser J., Giedion A., Gitzelmann R., Steinmann B. Eur. J. Pediatr. 154:215-219(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ACH CYS-375.
[34]	"Another mutation that results in the substitution of an unpaired cysteine residue in the extracellular domain of FGFR3 in thanatophoric dysplasia type I." Tavormina P.L., Rimoin D.L., Cohn D.H., Zhu Y.-Z., Shiang R., Wasmuth J.J. Hum. Mol. Genet. 4:2175-2177(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TD1 CYS-249.
[35]	"Thanatophoric dysplasia (types I and II) caused by distinct mutations in fibroblast growth factor receptor 3." Tavormina P.L., Shiang R., Thompson L.M., Zhu Y.-Z., Wilkin D.J., Lachman R.S., Wilcox W.R., Rimoin D.L., Cohn D.H., Wasmuth J.J. Nat. Genet. 9:321-328(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TD1 CYS-248 AND CYS-371, VARIANT TD2 GLU-650.
[36]	"A recurrent mutation in the tyrosine kinase domain of fibroblast growth factor receptor 3 causes hypochondroplasia." Bellus G.A., McIntosh I., Smith E.A., Aylsworth A.S., Kaitila I., Horton W.A., Greenhaw G.A., Hecht J.T., Francomano C.A. Nat. Genet. 10:357-359(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROPLASIA LYS-540.
[37]	"Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in Crouzon syndrome with acanthosis nigricans." Meyers G.A., Orlow S.J., Munro I.R., Przylepa K.A., Jabs E.W. Nat. Genet. 11:462-464(1995) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CAN GLU-391.
[38]	"Constitutive activation of fibroblast growth factor receptor 3 by the transmembrane domain point mutation found in achondroplasia." Webster M.K., Donoghue D.J. EMBO J. 15:520-527(1996) [PubMed] [Europe PMC] [Abstract] Cited for: CHARACTERIZATION OF VARIANT ACH ARG-380.
[39]	"Missense FGFR3 mutations create cysteine residues in thanatophoric dwarfism type I (TD1)." Rousseau F., el Ghouzzi V., Delezoide A.-L., Legeai-Mallet L., le Merrer M., Munnich A., Bonaventure J. Hum. Mol. Genet. 5:509-512(1996) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TD1 CYS-248; CYS-249; CYS-370 AND CYS-373.
[40]	"A unique point mutation in the fibroblast growth factor receptor 3 gene (FGFR3) defines a new craniosynostosis syndrome." Muenke M., Gripp K.W., McDonald-Mcginn D.M., Gaudenz K., Whitaker L.A., Bartlett S.P., Markowitz R.I., Robin N.H., Nwokoro N., Mulvihill J.J., Losken H.W., Mulliken J.B., Guttmacher A.E., Wilroy R.S., Clarke L.A., Hollway G., Ades L.C., Haan E.A. , Mulley J.C., Cohen M.M. Jr., Bellus G.A., Francomano C.A., Moloney D.M., Wall S.A., Wilkie A.O.M., Zackai E.H. Am. J. Hum. Genet. 60:555-564(1997) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MNKS ARG-250.
[41]	"Frequent translocation t(4;14)(p16.3;q32.3) in multiple myeloma is associated with increased expression and activating mutations of fibroblast growth factor receptor 3." Chesi M., Nardini E., Brents L.A., Schroeck E., Ried T., Kuehl W.M., Bergsagel P.L. Nat. Genet. 16:260-264(1997) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MULTIPLE MYELOMA, VARIANTS CYS-373; GLU-650 AND MET-650.
[42]	"G370C mutation in the FGFR3 gene in a Japanese patient with thanatophoric dysplasia." Katsumata N., Kuno T., Miyazaki S., Mikami S., Nagashima-Miyokawa A., Nimura A., Horikawa R., Tanaka T. Endocr. J. 45:S171-S174(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TD1 CYS-370.
[43]	"A novel missense mutation Ile538Val in the fibroblast growth factor receptor 3 in hypochondroplasia." Grigelioniene G., Hagenaes L., Ekloef O., Neumeyer L., Haereid P.E., Anvret M. Hum. Mutat. 11:333-333(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROPLASIA VAL-538.
[44]	"Asn540Thr substitution in the fibroblast growth factor receptor 3 tyrosine kinase domain causing hypochondroplasia." Deutz-Terlouw P.P., Losekoot M., Aalfs C.M., Hennekam R.C.M., Bakker E. Hum. Mutat. Suppl. 1:S62-S65(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROPLASIA THR-540.
[45]	"Lys650Met substitution in the tyrosine kinase domain of the fibroblast growth factor receptor gene causes thanatophoric dysplasia type I." Kitoh H., Brodie S.G., Kupke K.G., Lachman R.S., Wilcox W.R. Hum. Mutat. 12:362-363(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TD1 MET-650.
[46]	"Deafness due to Pro250Arg mutation of FGFR3." Hollway G.E., Suthers G.K., Battese K.M., Turner A.M., David D.J., Mulley J.C. Lancet 351:877-878(1998) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT ARG-250.
[47]	"Platyspondylic lethal skeletal dysplasia, San Diego type, is caused by FGFR3 mutations." Brodie S.G., Kitoh H., Lachman R.S., Nolasco L.M., Mekikian P.B., Wilcox W.R. Am. J. Med. Genet. 84:476-480(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS TD1 CYS-248; CYS-249 AND CYS-373.
[48]	"Sex related expressivity of the phenotype in coronal craniosynostosis caused by the recurrent P250R FGFR3 mutation." Lajeunie E., El Ghouzzi V., Le Merrer M., Munnich A., Bonaventure J., Renier D. J. Med. Genet. 36:9-13(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MNKS ARG-250.
[49]	"Frequent activating mutations of FGFR3 in human bladder and cervix carcinomas." Cappellen D., De Oliveira C., Ricol D., Gil Diez de Medina S., Bourdin J., Sastre-Garau X., Chopin D., Thiery J.P., Radvanyi F. Nat. Genet. 23:18-20(1999) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS BLADDER AND CERVIX CANCERS CYS-248; CYS-249; CYS-370 AND GLU-650.
[50]	"Distinct missense mutations of the FGFR3 Lys650 codon modulate receptor kinase activation and the severity of the skeletal dysplasia phenotype." Bellus G.A., Spector E.B., Speiser P.W., Weaver C.A., Garber A.T., Bryke C.R., Israel J., Rosengren S.S., Webster M.K., Donoghue D.J., Francomano C.A. Am. J. Hum. Genet. 67:1411-1421(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROPLASIA GLN-650.
[51]	"Clinical and radiographic features of a family with hypochondroplasia owing to a novel asn540ser mutation in the fibroblast growth factor receptor 3 gene." Mortier G., Nuytinck L., Craen M., Renard J.-P., Leroy J.G., De Paepe A. J. Med. Genet. 37:220-224(2000) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROPLASIA SER-540.
[52]	"Syndrome of coronal craniosynostosis, Klippel-Feil anomaly, and sprengel shoulder with and without Pro250Arg mutation in the FGFR3 gene." Lowry R.B., Jabs E.W., Graham G.E., Gerritsen J., Fleming J. Am. J. Med. Genet. 104:112-119(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT MNKS ARG-250.
[53]	"Analysis of FGFR3 gene mutations in multiple myeloma patients with t(4;14)." Intini D., Baldini L., Fabris S., Lombardi L., Ciceri G., Maiolo A.T., Neri A. Br. J. Haematol. 114:362-364(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN MULTIPLE MYELOMA, VARIANT CYS-248.
[54]	"Mutations in fibroblast growth factor receptor 2 and fibroblast growth factor receptor 3 genes associated with human gastric and colorectal cancers." Jang J.-H., Shin K.-H., Park J.-G. Cancer Res. 61:3541-3543(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT COLORECTAL CANCER LYS-322.
[55]	"Loss of heterozygosity at 4p16.3 and mutation of FGFR3 in transitional cell carcinoma." Sibley K., Cuthbert-Heavens D., Knowles M.A. Oncogene 20:686-691(2001) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT BLADDER CANCER GLN-650.
[56]	"Hypochondroplasia and stature within normal limits: another family with an Asn540-to-Ser mutation in the fibroblast growth factor receptor 3 gene." Thauvin-Robinet C., Faivre L., Lewin P., De Monleon J.-V., Francois C., Huet F., Couailler J.-F., Campos-Xavier A.B., Bonaventure J., Le Merrer M. Am. J. Med. Genet. A 119:81-84(2003) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT HYPOCHONDROPLASIA SER-540.
[57]	"Activating mutations of the tyrosine kinase receptor FGFR3 are associated with benign skin tumors in mice and humans." Logie A., Dunois-Larde C., Rosty C., Levrel O., Blanche M., Ribeiro A., Gasc J.-M., Jorcano J., Werner S., Sastre-Garau X., Thiery J.P., Radvanyi F. Hum. Mol. Genet. 14:1153-1160(2005) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS KERSEB CYS-248; CYS-249; CYS-370; CYS-371; CYS-373; GLU-650 AND MET-650.
[58]	"A novel mutation in FGFR3 causes camptodactyly, tall stature, and hearing loss (CATSHL) syndrome." Toydemir R.M., Brassington A.E., Bayrak-Toydemir P., Krakowiak P.A., Jorde L.B., Whitby F.G., Longo N., Viskochil D.H., Carey J.C., Bamshad M.J. Am. J. Hum. Genet. 79:935-941(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CATSHL SYNDROME HIS-621.
[59]	"Mosaicism of activating FGFR3 mutations in human skin causes epidermal nevi." Hafner C., van Oers J.M.M., Vogt T., Landthaler M., Stoehr R., Blaszyk H., Hofstaedter F., Zwarthoff E.C., Hartmann A. J. Clin. Invest. 116:2201-2207(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS KNEN CYS-248; CYS-370 AND ARG-380.
[60]	"Mutations in different components of FGF signaling in LADD syndrome." Rohmann E., Brunner H.G., Kayserili H., Uyguner O., Nuernberg G., Lew E.D., Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M., Leroy J.G., Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J., Yueksel-Apak M., Nuernberg P., Kubisch C. , Schlessinger J., van Bokhoven H., Wollnik B. Nat. Genet. 38:414-417(2006) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT LADDS ASN-513.
[61]	"Crouzon with acanthosis nigricans. Further delineation of the syndrome." Arnaud-Lopez L., Fragoso R., Mantilla-Capacho J., Barros-Nunez P. Clin. Genet. 72:405-410(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT CAN GLU-391.
[62]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-79; ARG-228; MET-338; LEU-384; ASN-646 AND GLU-650.
[63]	"Activating mutations in FGFR3 and HRAS reveal a shared genetic origin for congenital disorders and testicular tumors." Goriely A., Hansen R.M., Taylor I.B., Olesen I.A., Jacobsen G.K., McGowan S.J., Pfeifer S.P., McVean G.A., Rajpert-De Meyts E., Wilkie A.O. Nat. Genet. 41:1247-1252(2009) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANT TGCT GLU-650.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00027174.
IPI00220253.
IPI00220254.
IPI01013721.

PIR

TVHUF3. A38576.

RefSeq

NP_000133.1. NM_000142.4.
NP_001156685.1. NM_001163213.1.
NP_075254.1. NM_022965.3.

UniGene

Hs.1420.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1RY7	X-ray	3.20	B	33-365	[»]

ProteinModelPortal

P22607.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-4016N.

IntAct

P22607. 22 interactions.

MINT

MINT-1034697.

STRING

9606.ENSP00000260795.

PTM databases

PhosphoSite

P22607.

Polymorphism databases

DMDM

120050.

Proteomic databases

PaxDb

P22607.

PRIDE

P22607.

Protocols and materials databases

DNASU

2261.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000260795; ENSP00000260795; ENSG00000068078.
ENST00000340107; ENSP00000339824; ENSG00000068078.
ENST00000352904; ENSP00000231803; ENSG00000068078.
ENST00000412135; ENSP00000412903; ENSG00000068078.
ENST00000440486; ENSP00000414914; ENSG00000068078.

GeneID

2261.

KEGG

hsa:2261.

UCSC

uc003gdr.3. human.
uc003gds.3. human.
uc003gdu.2. human.

Organism-specific databases

CTD

2261.

GeneCards

GC04P001795.

HGNC

HGNC:3690. FGFR3.

HPA

CAB004231.

MIM

100800. 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.

neXtProt

NX_P22607.

Orphanet

15. Achondroplasia.
85164. Camptodactyly - tall stature - scoliosis - hearing loss.
93262. Crouzon syndrome - acanthosis nigricans.
1555. Cutis gyrata - acanthosis nigricans - craniosynostosis.
429. Hypochondroplasia.
35099. Isolated brachycephaly.
2343. Isolated cloverleaf skull syndrome.
35098. Isolated plagiocephaly.
2363. Lacrimo-auriculo-dento-digital syndrome.
53271. Muenke syndrome.
794. Saethre-Chotzen syndrome.
85165. Severe achondroplasia - developmental delay - acanthosis nigricans.
1860. Thanatophoric dwarfism type I.
93274. Thanatophoric dwarfism type II.

PharmGKB

PA28129.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000263410.

HOVERGEN

HBG000345.

KO

K05094.

OMA

VFTHDLL.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.

Reactome

REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.

Gene expression databases

ArrayExpress

P22607.

Bgee

P22607.

CleanEx

HS_FGFR3.

Genevestigator

P22607.

GermOnline

ENSG00000068078. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013151. Immunoglobulin.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
IPR016248. Tyr_kinase_fibroblast_GF_rcpt.
[Graphical view]

Pfam

PF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]

PIRSF

PIRSF000628. FGFR. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00409. IG. 1 hit.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

PS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P22607.

ChEMBL

CHEMBL2742.

ChiTaRS

FGFR3. human.

DrugBank

DB00039. Palifermin.

EvolutionaryTrace

P22607.

GenomeRNAi

2261.

NextBio

9179.

SOURCE

Search...

Entry information

Entry name

FGFR3_HUMAN

Accession

Primary (citable) accession number: P22607
Secondary accession number(s): D3DVP9 , D3DVQ0, Q14308, Q16294, Q16608, Q59FL9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1991
Last sequence update:	August 1, 1991
Last modified:	May 1, 2013
This is version 176 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.