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P22607 (FGFR3_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 189. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length806 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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. Secreted isoform 3 retains its capacity to bind FGF1 and FGF2 and hence may interfere with FGF signaling. Ref.2 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. Isoform 3 forms disulfide-linked dimers. Ref.2 Ref.11 Ref.12 Ref.16 Ref.17 Ref.18 Ref.21 Ref.25

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. Ref.2 Ref.12 Ref.17 Ref.18 Ref.19

Isoform 2: Cell membrane; Single-pass type I membrane protein By similarity Ref.2 Ref.12 Ref.17 Ref.18 Ref.19.

Isoform 3: Secreted Ref.2 Ref.12 Ref.17 Ref.18 Ref.19.

Isoform 4: Cell membrane; Single-pass type I membrane protein By similarity Ref.2 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 Ref.40

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.2 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.50 Ref.55 Ref.56 Ref.62

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.43 Ref.46 Ref.48

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 Ref.40

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.61

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.60

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.41 Ref.49 Ref.53

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.58

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.64

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 processApoptosis
   Cellular componentCell membrane
Cytoplasmic vesicle
Endoplasmic reticulum
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseCraniosynostosis
Deafness
Disease mutation
Dwarfism
Ectodermal dysplasia
Lacrimo-auriculo-dento-digital syndrome
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

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: Ensembl

axonogenesis involved in innervation

Inferred from electronic annotation. Source: Ensembl

bone maturation

Inferred from sequence or structural similarity PubMed 20582225. Source: BHF-UCL

bone mineralization

Inferred from sequence or structural similarity PubMed 20582225. Source: BHF-UCL

bone morphogenesis

Traceable author statement Ref.27. Source: UniProtKB

cell-cell signaling

Inferred from electronic annotation. Source: Ensembl

central nervous system myelination

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

endochondral bone growth

Traceable author statement Ref.27. Source: UniProtKB

endochondral ossification

Traceable author statement Ref.27. Source: UniProtKB

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

epithelial cell fate commitment

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor apoptotic signaling pathway

Inferred from mutant phenotype Ref.18. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from direct assay Ref.11. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

inner ear receptor cell differentiation

Inferred from electronic annotation. Source: Ensembl

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lens fiber cell development

Inferred from electronic annotation. Source: Ensembl

lens morphogenesis in camera-type eye

Inferred from electronic annotation. Source: Ensembl

morphogenesis of an epithelium

Inferred from electronic annotation. Source: Ensembl

negative regulation of astrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

negative regulation of mitosis

Inferred from electronic annotation. Source: Ensembl

negative regulation of smoothened signaling pathway

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.13. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype Ref.13. Source: UniProtKB

positive regulation of MAPK 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: Ensembl

positive regulation of canonical Wnt signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell differentiation

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

positive regulation of neuron apoptotic process

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

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

response to axon injury

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Traceable author statement PubMed 8601314. Source: ProtInc

somatic stem cell maintenance

Inferred from electronic annotation. Source: Ensembl

substantia nigra development

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell surface

Inferred from electronic annotation. Source: Ensembl

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

lysosome

Inferred from electronic annotation. Source: Ensembl

nucleus

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Traceable author statement. Source: Reactome

   Molecular_functionATP 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

protein binding

Inferred from physical interaction Ref.30PubMed 22939624. Source: IntAct

protein tyrosine kinase activity

Inferred from direct assay Ref.13. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

FGF1P052303EBI-348399,EBI-698068
HSP90AB1P082382EBI-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)

Also known as: FGFR3deltaTM;

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 806784Fibroblast growth factor receptor 3
PRO_0000016785

Regions

Topological domain23 – 375353Extracellular Potential
Transmembrane376 – 39621Helical; Potential
Topological domain397 – 806410Cytoplasmic Potential
Domain24 – 126103Ig-like C2-type 1
Domain151 – 24494Ig-like C2-type 2
Domain253 – 355103Ig-like C2-type 3
Domain472 – 761290Protein kinase
Nucleotide binding478 – 4869ATP By similarity

Sites

Active site6171Proton acceptor By similarity
Binding site5081ATP By similarity

Amino acid modifications

Modified residue6471Phosphotyrosine; by autocatalysis Probable
Modified residue6481Phosphotyrosine; by autocatalysis Probable
Modified residue7241Phosphotyrosine; by autocatalysis Ref.13
Modified residue7601Phosphotyrosine; by autocatalysis Ref.25
Glycosylation981N-linked (GlcNAc...) Potential
Glycosylation2251N-linked (GlcNAc...) Potential
Glycosylation2621N-linked (GlcNAc...) Potential
Glycosylation2941N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation3281N-linked (GlcNAc...) Potential
Disulfide bond61 ↔ 109 By similarity
Disulfide bond176 ↔ 228 By similarity
Disulfide bond275 ↔ 339 By similarity

Natural variations

Alternative sequence311 – 422112Missing in isoform 3.
VSP_002989
Alternative sequence311 – 35848TAGAN…LVVLP → SWISESVEADVRLRLANVSE RDGGEYLCRATNFIGVAEKA FWLSVHGPRA in isoform 2.
VSP_002988
Alternative sequence654 – 806153GRLPV…GGSRT → LVLWGPALGDLHAGGLPVPR HPCGGALQAAEGGPPHGQAR QLHTRPVHDHAGVLACRALP EAHLQAAGGGPGPCPYRDVH RRVPGPVGAFRAVLPGWPGH PQLQLLRGRLRVCPRPAAPG PTQQWGLADVKGHWSPTM in isoform 4.
VSP_040945
Natural variant651G → R. Ref.4
Corresponds to variant rs2305178 [ dbSNP | Ensembl ].
VAR_022167
Natural variant791T → S in a lung adenocarcinoma sample; somatic mutation. Ref.63
VAR_042207
Natural variant2281C → R in a colorectal adenocarcinoma sample; somatic mutation. Ref.63
VAR_042208
Natural variant2481R → 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.48 Ref.50 Ref.54 Ref.58 Ref.60
VAR_004148
Natural variant2491S → C in KERSEB, bladder cancer, cervical cancer and TD1. Ref.34 Ref.39 Ref.48 Ref.50 Ref.58
VAR_004149
Natural variant2501P → R in MNKS; also some individuals with autosomal dominant congenital sensorineural deafness without craniosynostosis. Ref.41 Ref.47 Ref.49 Ref.53
Corresponds to variant rs4647924 [ dbSNP | Ensembl ].
VAR_004150
Natural variant3221E → K in colorectal cancer. Ref.55
VAR_018388
Natural variant3381T → M. Ref.63
VAR_042209
Natural variant3701G → C in KERSEB, bladder cancer, keratinocytic non-epidermolytic nevus and TD1. Ref.39 Ref.43 Ref.50 Ref.58 Ref.60
VAR_004151
Natural variant3711S → C in KERSEB and TD1. Ref.35 Ref.58
VAR_004152
Natural variant3731Y → C in KERSEB and TD1; disulfide-linked dimer with constitutive kinase activation. Ref.19 Ref.39 Ref.42 Ref.48 Ref.58
VAR_004153
Natural variant3751G → C in ACH. Ref.33
VAR_004154
Natural variant3801G → 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.60
Corresponds to variant rs28931614 [ dbSNP | Ensembl ].
VAR_004155
Natural variant3841F → L. Ref.4 Ref.63
Corresponds to variant rs17881656 [ dbSNP | Ensembl ].
VAR_022168
Natural variant3911A → E in CAN. Ref.37 Ref.62
Corresponds to variant rs28931615 [ dbSNP | Ensembl ].
VAR_004156
Natural variant4411A → T. Ref.4
Corresponds to variant rs17884368 [ dbSNP | Ensembl ].
VAR_022169
Natural variant5131D → N in LADDS. Ref.61
VAR_029887
Natural variant5381I → V in hypochondroplasia. Ref.44
VAR_004157
Natural variant5401N → K in hypochondroplasia. Ref.36
Corresponds to variant rs28933068 [ dbSNP | Ensembl ].
VAR_004158
Natural variant5401N → S in hypochondroplasia; mild. Ref.52 Ref.57
VAR_018389
Natural variant5401N → T in hypochondroplasia. Ref.45
VAR_004159
Natural variant6211R → H in CATSHL syndrome. Ref.59
VAR_029108
Natural variant6461D → N. Ref.63
VAR_042210
Natural variant6501K → 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.40 Ref.42 Ref.50 Ref.58 Ref.63 Ref.64
VAR_004160
Natural variant6501K → M in KERSEB, ACH and TD1; constitutively activated kinase with impaired internalization and degradation, resulting in prolonged FGFR3 signaling. Ref.18 Ref.19 Ref.42 Ref.46 Ref.58
VAR_004161
Natural variant6501K → 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; constitutively activated kinase. Ref.40 Ref.51 Ref.56
VAR_018390
Natural variant7171A → T. Ref.4
Corresponds to variant rs17882190 [ dbSNP | Ensembl ].
VAR_022170
Natural variant7261I → F. Ref.4
Corresponds to variant rs17880763 [ dbSNP | Ensembl ].
VAR_022171

Experimental info

Mutagenesis5081K → A: Loss of kinase activity. Abolishes ubiquitination. Ref.14 Ref.17
Mutagenesis5771Y → F: Minor effect on kinase activity. Ref.13
Mutagenesis6501K → D: Constitutively activated kinase.
Mutagenesis6501K → L: Constitutively activated kinase.
Mutagenesis7241Y → F: Strongly reduced kinase activity. Strongly reduced mitogen activity. Ref.13
Mutagenesis7601Y → F: Minor effect on kinase activity. Ref.13
Mutagenesis7701Y → F: Minor effect on kinase activity. Increased mitogen activity. Ref.13
Sequence conflict3951L → V in AAA58470. Ref.7
Sequence conflict4211R → RQ in BAD92678. Ref.3

Secondary structure

.............................................................................. 806
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (IIIc) [UniParc].

Last modified August 1, 1991. Version 1.
Checksum: BC5EA75EA46F447E

FASTA80687,710
        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 

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Isoform 2 (IIIb) [UniParc].

Checksum: E08CE2C9FD56D8F9
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FASTA80888,157
Isoform 3 (FGFR3deltaTM) [UniParc].

Checksum: 4493C5990FD68964
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FASTA69475,696
Isoform 4 [UniParc].

Checksum: EA4EEB033A1433BB
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FASTA79185,083

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), FUNCTION, SUBUNIT, FGF1- AND FGF2-BINDING, SUBCELLULAR LOCATION, GLYCOSYLATION, DIMERIZATION.
Tissue: Squamous cell carcinoma.
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Profound ligand-independent kinase activation of fibroblast growth factor receptor 3 by the activation loop mutation responsible for a lethal skeletal dysplasia, thanatophoric dysplasia type II."
Webster M.K., D'Avis P.Y., Robertson S.C., Donoghue D.J.
Mol. Cell. Biol. 16:4081-4087(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION OF VARIANT TD2 GLU-650, CHARACTERIZATION OF VARIANT GLN-650, PHOSPHORYLATION AT TYR-647 AND TYR-648.
[41]"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. expand/collapse author list , 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.
[42]"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.
[43]"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.
[44]"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.
[45]"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.
[46]"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.
[47]"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.
[48]"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.
[49]"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.
[50]"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.
[51]"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.
[52]"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.
[53]"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.
[54]"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.
[55]"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.
[56]"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.
[57]"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.
[58]"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.
[59]"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.
[60]"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.
[61]"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. expand/collapse author list , Schlessinger J., van Bokhoven H., Wollnik B.
Nat. Genet. 38:414-417(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT LADDS ASN-513.
[62]"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.
[63]"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. expand/collapse author list , 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.
[64]"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.

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.
CCDSCCDS3353.1. [P22607-1]
CCDS3354.1. [P22607-3]
CCDS54706.1. [P22607-2]
PIRTVHUF3. A38576.
RefSeqNP_000133.1. NM_000142.4. [P22607-1]
NP_001156685.1. NM_001163213.1. [P22607-2]
NP_075254.1. NM_022965.3. [P22607-3]
UniGeneHs.1420.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1RY7X-ray3.20B33-365[»]
2LZLNMR-A/B357-399[»]
4K33X-ray2.34A449-759[»]
ProteinModelPortalP22607.
SMRP22607. Positions 45-399, 459-776.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108552. 34 interactions.
DIPDIP-4016N.
IntActP22607. 23 interactions.
MINTMINT-1034697.
STRING9606.ENSP00000260795.

Chemistry

BindingDBP22607.
ChEMBLCHEMBL2742.
DrugBankDB00039. Palifermin.
GuidetoPHARMACOLOGY1810.

PTM databases

PhosphoSiteP22607.

Polymorphism databases

DMDM120050.

Proteomic databases

PaxDbP22607.
PRIDEP22607.

Protocols and materials databases

DNASU2261.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000260795; ENSP00000260795; ENSG00000068078. [P22607-1]
ENST00000340107; ENSP00000339824; ENSG00000068078. [P22607-2]
ENST00000352904; ENSP00000231803; ENSG00000068078. [P22607-3]
ENST00000412135; ENSP00000412903; ENSG00000068078. [P22607-3]
ENST00000440486; ENSP00000414914; ENSG00000068078. [P22607-1]
GeneID2261.
KEGGhsa:2261.
UCSCuc003gdr.3. human. [P22607-1]
uc003gds.3. human. [P22607-3]
uc003gdu.2. human. [P22607-2]

Organism-specific databases

CTD2261.
GeneCardsGC04P001795.
GeneReviewsFGFR3.
HGNCHGNC:3690. FGFR3.
HPACAB004231.
MIM100800. 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.
neXtProtNX_P22607.
Orphanet15. Achondroplasia.
85164. Camptodactyly - tall stature - scoliosis - hearing loss.
93262. Crouzon syndrome - acanthosis nigricans.
1555. Cutis gyrata - acanthosis nigricans - craniosynostosis.
251579. Giant cell glioblastoma.
251576. Gliosarcoma.
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 dysplasia type 1.
93274. Thanatophoric dysplasia type 2.
PharmGKBPA28129.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000263410.
HOVERGENHBG000345.
KOK05094.
OMAVFTHDLL.
PhylomeDBP22607.
TreeFamTF316307.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP22607.

Gene expression databases

ArrayExpressP22607.
BgeeP22607.
CleanExHS_FGFR3.
GenevestigatorP22607.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028176. FGF_rcpt_3.
IPR016248. FGF_rcpt_fam.
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_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF128. PTHR24416:SF128. 1 hit.
PfamPF07679. I-set. 2 hits.
PF00047. ig. 1 hit.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00409. IG. 1 hit.
SM00408. IGc2. 2 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGFR3. human.
EvolutionaryTraceP22607.
GeneWikiFibroblast_growth_factor_receptor_3.
GenomeRNAi2261.
NextBio9179.
PROP22607.
SOURCESearch...

Entry information

Entry nameFGFR3_HUMAN
AccessionPrimary (citable) accession number: P22607
Secondary accession number(s): D3DVP9 expand/collapse secondary AC list , D3DVQ0, Q14308, Q16294, Q16608, Q59FL9
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1991
Last sequence update: August 1, 1991
Last modified: July 9, 2014
This is version 189 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries