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P21802 (FGFR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 195. 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 2

Short name=FGFR-2
EC=2.7.10.1
Alternative name(s):
K-sam
Short name=KGFR
Keratinocyte growth factor receptor
CD_antigen=CD332
Gene names
Name:FGFR2
Synonyms:BEK, KGFR, KSAM
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length821 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, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. 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. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.40 Ref.47

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.31 Ref.35 Ref.49 Ref.51

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 ARQ 523 and ARQ 069; these compounds maintain the kinase in an inactive conformation and inhibit autophosphorylation. Ref.48 Ref.51

Subunit structure

Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in vitro). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Isoform 1 has high affinity for FGF1 and FGF2, but low affinity for FGF7. Isoform 3 has high affinity for FGF1 and FGF7, and has much higher affinity for FGF7 than isoform 1 (in vitro). 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 PLCG1, GRB2 and PAK4. Ref.6 Ref.7 Ref.25 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.36 Ref.43 Ref.47 Ref.49

Subcellular location

Cell membrane; Single-pass type I membrane protein. Golgi apparatus. Cytoplasmic vesicle. Note: Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded. Ref.31 Ref.33 Ref.34 Ref.36

Isoform 1: Cell membrane; Single-pass type I membrane protein. Note: After ligand binding, the activated receptor is rapidly internalized and degraded. Ref.31 Ref.33 Ref.34 Ref.36

Isoform 3: Cell membrane; Single-pass type I membrane protein. Note: After ligand binding, the activated receptor is rapidly internalized and degraded. Ref.31 Ref.33 Ref.34 Ref.36

Isoform 14: Secreted Ref.31 Ref.33 Ref.34 Ref.36.

Isoform 19: Secreted Ref.31 Ref.33 Ref.34 Ref.36.

Domain

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Alternative splicing events affecting the third Ig-like domain are crucial for ligand selectivity. Ref.6 Ref.7 Ref.25

Post-translational modification

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on several tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Phosphorylation at Tyr-769 is essential for interaction with PLCG1. Ref.29 Ref.31 Ref.33 Ref.35 Ref.48 Ref.49 Ref.50 Ref.51

N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. Ref.31 Ref.33

Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome. Ref.28 Ref.31 Ref.38

Involvement in disease

Crouzon syndrome (CS) [MIM:123500]: An autosomal dominant syndrome characterized by craniosynostosis, hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.24 Ref.40 Ref.48 Ref.52 Ref.53 Ref.54 Ref.55 Ref.59 Ref.60 Ref.61 Ref.65 Ref.66 Ref.67 Ref.68 Ref.72 Ref.75 Ref.78 Ref.79

Jackson-Weiss syndrome (JWS) [MIM:123150]: An autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.53 Ref.55 Ref.59 Ref.64 Ref.67

Apert syndrome (APRS) [MIM:101200]: A syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.21 Ref.28 Ref.40 Ref.45 Ref.57 Ref.65 Ref.67 Ref.69 Ref.79

Pfeiffer syndrome (PS) [MIM:101600]: A syndrome characterized by the association of craniosynostosis, broad and deviated thumbs and big toes, and partial syndactyly of the fingers and toes. Three subtypes are known: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.31 Ref.40 Ref.48 Ref.56 Ref.58 Ref.59 Ref.63 Ref.65 Ref.70 Ref.71 Ref.73 Ref.74 Ref.75 Ref.79

Beare-Stevenson cutis gyrata syndrome (BSTVS) [MIM:123790]: An autosomal dominant disease characterized by craniofacial anomalies, particularly craniosynostosis, and ear defects, cutis gyrata, acanthosis nigricans, anogenital anomalies, skin tags, and prominent umbilical stump. The skin furrows have a corrugated appearance and are widespread. Cutis gyrata variably affects the scalp, forehead, face, preauricular area, neck, trunk, hands, and feet.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.62 Ref.80

Familial scaphocephaly syndrome (FSPC) [MIM:609579]: An autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.48 Ref.81

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.40 Ref.49 Ref.82

Antley-Bixler syndrome, without genital anomalies or disordered steroidogenesis (ABS2) [MIM:207410]: A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.77

Bent bone dysplasia syndrome (BBDS) [MIM:614592]: A perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.40 Ref.85

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 BAG57383.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell membrane
Cytoplasmic vesicle
Golgi apparatus
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCraniosynostosis
Disease mutation
Ectodermal dysplasia
Lacrimo-auriculo-dento-digital syndrome
Mental retardation
Proto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Heparin-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

angiogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axonogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

bone development

Inferred from sequence or structural similarity. Source: UniProtKB

bone mineralization

Inferred from sequence or structural similarity. Source: UniProtKB

bone morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branch elongation involved in salivary gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branching involved in labyrinthine layer morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branching involved in prostate gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branching involved in salivary gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

branching morphogenesis of a nerve

Inferred from sequence or structural similarity. Source: UniProtKB

bud elongation involved in lung branching

Inferred from sequence or structural similarity. Source: UniProtKB

cell fate commitment

Inferred from sequence or structural similarity. Source: UniProtKB

cell-cell signaling

Inferred from sequence or structural similarity. Source: UniProtKB

coronal suture morphogenesis

Inferred from electronic annotation. Source: Ensembl

digestive tract development

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic cranial skeleton morphogenesis

Inferred from mutant phenotype Ref.53Ref.52. Source: BHF-UCL

embryonic digestive tract morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic organ development

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic organ morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

embryonic pattern specification

Inferred from sequence or structural similarity. Source: UniProtKB

endodermal digestive tract morphogenesis

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

epidermis morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial cell proliferation involved in salivary gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

epithelial to mesenchymal transition

Inferred from electronic annotation. Source: Ensembl

fibroblast growth factor receptor signaling pathway

Inferred from direct assay Ref.29Ref.26. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in hemopoiesis

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in mammary gland specification

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in negative regulation of apoptotic process in bone marrow

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in positive regulation of cell proliferation in bone marrow

Inferred from sequence or structural similarity. Source: UniProtKB

gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

hair follicle morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

in utero embryonic development

Inferred from sequence or structural similarity. Source: UniProtKB

innate immune response

Traceable author statement. Source: Reactome

inner ear morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lacrimal gland development

Inferred from sequence or structural similarity. Source: UniProtKB

lateral sprouting from an epithelium

Inferred from sequence or structural similarity. Source: UniProtKB

lens fiber cell development

Inferred from electronic annotation. Source: Ensembl

limb bud formation

Inferred from sequence or structural similarity. Source: UniProtKB

lung alveolus development

Inferred from sequence or structural similarity. Source: UniProtKB

lung development

Inferred from sequence or structural similarity. Source: UniProtKB

lung lobe morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

lung-associated mesenchyme development

Inferred from sequence or structural similarity. Source: UniProtKB

mammary gland bud formation

Inferred from sequence or structural similarity. Source: UniProtKB

membranous septum morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

mesenchymal cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

mesenchymal cell differentiation involved in lung development

Inferred from sequence or structural similarity. Source: UniProtKB

mesenchymal cell proliferation involved in lung development

Inferred from sequence or structural similarity. Source: UniProtKB

mesodermal cell differentiation

Inferred from electronic annotation. Source: Ensembl

midbrain development

Inferred from sequence or structural similarity. Source: UniProtKB

morphogenesis of embryonic epithelium

Inferred from sequence or structural similarity. Source: UniProtKB

multicellular organism growth

Inferred from sequence or structural similarity. Source: UniProtKB

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 transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

neuromuscular junction development

Inferred from electronic annotation. Source: Ensembl

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

odontogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

orbitofrontal cortex development

Inferred from sequence or structural similarity. Source: UniProtKB

organ growth

Inferred from sequence or structural similarity. Source: UniProtKB

organ morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

otic vesicle formation

Inferred from sequence or structural similarity. Source: UniProtKB

outflow tract septum morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.29Ref.31. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement. Source: Reactome

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from mutant phenotype Ref.29. Source: UniProtKB

positive regulation of Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of canonical Wnt signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cardiac muscle cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell cycle

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell division

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from direct assay Ref.26. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of epithelial cell proliferation involved in lung morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of phospholipase activity

Inferred from mutant phenotype Ref.31. Source: UniProtKB

positive regulation of smooth muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

post-embryonic development

Inferred from sequence or structural similarity. Source: UniProtKB

prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

prostate epithelial cord elongation

Inferred from sequence or structural similarity. Source: UniProtKB

prostate gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.29. Source: UniProtKB

pyramidal neuron development

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of branching involved in prostate gland morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of cell fate commitment

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of fibroblast growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of morphogenesis of a branching structure

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of multicellular organism growth

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of osteoblast differentiation

Traceable author statement Ref.28. Source: UniProtKB

regulation of osteoblast proliferation

Traceable author statement Ref.28. Source: UniProtKB

regulation of smooth muscle cell differentiation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of smoothened signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

reproductive structure development

Inferred from sequence or structural similarity. Source: UniProtKB

skeletal system morphogenesis

Traceable author statement Ref.28. Source: UniProtKB

squamous basal epithelial stem cell differentiation involved in prostate gland acinus development

Inferred from sequence or structural similarity. Source: UniProtKB

synaptic vesicle transport

Inferred from electronic annotation. Source: Ensembl

ureteric bud development

Inferred from sequence or structural similarity. Source: UniProtKB

ventricular cardiac muscle tissue morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

ventricular zone neuroblast division

Inferred from sequence or structural similarity. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from direct assay PubMed 17471512. Source: UniProtKB

cell surface

Inferred from direct assay PubMed 16597614. Source: UniProtKB

cytoplasm

Inferred from direct assay PubMed 16597614PubMed 17471512. Source: UniProtKB

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

excitatory synapse

Inferred from sequence or structural similarity. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of membrane

Non-traceable author statement Ref.1. Source: UniProtKB

integral component of plasma membrane

Inferred from direct assay Ref.29Ref.31. Source: UniProtKB

intracellular membrane-bounded organelle

Inferred from direct assay. Source: HPA

membrane

Non-traceable author statement Ref.22. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 16597614PubMed 17471512. Source: UniProtKB

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.26. Source: UniProtKB

fibroblast growth factor-activated receptor activity

Inferred from direct assay Ref.29Ref.26. Source: UniProtKB

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

protein binding

Inferred from physical interaction Ref.44Ref.42Ref.43Ref.45Ref.7PubMed 22726438PubMed 23597563. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.31. Source: UniProtKB

protein tyrosine kinase activity

Non-traceable author statement Ref.1. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 23 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21802-1)

Also known as: BEK; FGFR2IIIc;

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: P21802-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 3 (identifier: P21802-3)

Also known as: BFR-1; FGFR2IIIb; KGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
Isoform 4 (identifier: P21802-4)

Also known as: K-sam;

The sequence of this isoform differs from the canonical sequence as follows:
     37-125: Missing.
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     428-429: Missing.
     761-821: LTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → PPNPSLMSIFRK
Isoform 5 (identifier: P21802-5)

Also known as: K-sam-I; BEK; IgIIIc;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
Isoform 6 (identifier: P21802-6)

Also known as: K-sam-IIC2;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     778-821: QYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → PYSPCYPDPR
Isoform 7 (identifier: P21802-7)

Also known as: K-sam-IIO2;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → RYKLLPCPDK...RVRQEKISTG
Isoform 8 (identifier: P21802-8)

Also known as: K-sam-IIC3;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 9 (identifier: P21802-9)

Also known as: K-sam-IIH1;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → RILTLTTNEN...LADTGSKVPN
Isoform 10 (identifier: P21802-10)

Also known as: K-sam-IIH2;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → SFQSSLKSSS...CAGSKKIYDI
Isoform 11 (identifier: P21802-11)

Also known as: K-sam-IIH3; K-sam-IIO4;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → GRLPAWASQE...SQGLPQSVVP
Isoform 12 (identifier: P21802-12)

Also known as: K-sam-IIO1;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → PLS
Isoform 13 (identifier: P21802-13)

Also known as: K-sam-IIO3;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: Missing.
Isoform 14 (identifier: P21802-14)

Also known as: K-sam-IV; Soluble KGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     250-254: ERSPH → GSQGL
     255-821: Missing.
Isoform 15 (identifier: P21802-15)

Also known as: K-sam-III;

The sequence of this isoform differs from the canonical sequence as follows:
     314-429: Missing.
Isoform 16 (identifier: P21802-16)

Also known as: TK14;

The sequence of this isoform differs from the canonical sequence as follows:
     313-313: K → KVTK
     428-429: Missing.
Isoform 17 (identifier: P21802-17)

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 18 (identifier: P21802-18)

Also known as: K-sam-IIC1; KGFR; IgIIIb;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     428-429: Missing.
Isoform 19 (identifier: P21802-19)

Also known as: Soluble KGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     362-365: APGR → GRRC
     366-821: Missing.
Isoform 20 (identifier: P21802-20)

The sequence of this isoform differs from the canonical sequence as follows:
     37-152: EPPTKYQISQ...FVSENSNNKR → G
     429-430: Missing.
Isoform 21 (identifier: P21802-21)

The sequence of this isoform differs from the canonical sequence as follows:
     37-125: Missing.
     769-821: YLDLSQPLEQ...YPHINGSVKT → EKKVSGAVDCHKPPCNPSHLPCVLAVDQ
Isoform 22 (identifier: P21802-22)

The sequence of this isoform differs from the canonical sequence as follows:
     37-125: Missing.
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 23 (identifier: P21802-23)

The sequence of this isoform differs from the canonical sequence as follows:
     250-361: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 821800Fibroblast growth factor receptor 2
PRO_0000016783

Regions

Topological domain22 – 377356Extracellular Potential
Transmembrane378 – 39821Helical; Potential
Topological domain399 – 821423Cytoplasmic Potential
Domain25 – 125101Ig-like C2-type 1
Domain154 – 24794Ig-like C2-type 2
Domain256 – 358103Ig-like C2-type 3
Domain481 – 770290Protein kinase
Nucleotide binding487 – 4959ATP
Nucleotide binding565 – 5673ATP
Region161 – 17818Heparin-binding

Sites

Active site6261Proton acceptor Ref.50
Binding site5171ATP
Binding site5711ATP

Amino acid modifications

Modified residue4661Phosphotyrosine; by autocatalysis Ref.35 Ref.50
Modified residue5861Phosphotyrosine; by autocatalysis Ref.35 Ref.48 Ref.50
Modified residue5881Phosphotyrosine; by autocatalysis Ref.35 Ref.50
Modified residue6561Phosphotyrosine; by autocatalysis Ref.35 Ref.48 Ref.50
Modified residue6571Phosphotyrosine; by autocatalysis Ref.35 Ref.48 Ref.50
Modified residue7691Phosphotyrosine; by autocatalysis Ref.29 Ref.50
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 107 By similarity
Disulfide bond179 ↔ 231 Ref.47
Disulfide bond278 ↔ 342 Ref.47

Natural variations

Alternative sequence37 – 152116EPPTK…SNNKR → G in isoform 20.
VSP_019608
Alternative sequence37 – 12589Missing in isoform 4, isoform 21 and isoform 22.
VSP_002964
Alternative sequence250 – 361112Missing in isoform 23.
VSP_041914
Alternative sequence250 – 2545ERSPH → GSQGL in isoform 14.
VSP_002965
Alternative sequence255 – 821567Missing in isoform 14.
VSP_002966
Alternative sequence3131K → KVTK in isoform 16.
VSP_002967
Alternative sequence314 – 429116Missing in isoform 15.
VSP_002968
Alternative sequence314 – 33017AAGVN…VLYIR → HSGINSSNAEVLALF in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18, isoform 19 and isoform 22.
VSP_002969
Alternative sequence334 – 3352FE → EA in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18, isoform 19 and isoform 22.
VSP_002970
Alternative sequence341 – 35313TCLAG…GISFH → ICKVSNYIGQANQ in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18, isoform 19 and isoform 22.
VSP_002971
Alternative sequence3611P → PKQQ in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18, isoform 19 and isoform 22.
VSP_002972
Alternative sequence362 – 3654APGR → GRRC in isoform 19.
VSP_002973
Alternative sequence366 – 821456Missing in isoform 19.
VSP_002974
Alternative sequence428 – 4292Missing in isoform 4, isoform 5, isoform 6, isoform 8, isoform 16 and isoform 18.
VSP_002975
Alternative sequence429 – 4302Missing in isoform 20.
VSP_019609
Alternative sequence761 – 82161LTLTT…GSVKT → PPNPSLMSIFRK in isoform 4.
VSP_002976
Alternative sequence768 – 82154EYLDL…GSVKT → SFQSSLKSSSTGIPGWPPGS EVFSEVAFRGILNYDIERPI LCAGSKKIYDI in isoform 10.
VSP_002981
Alternative sequence768 – 82154EYLDL…GSVKT → GRLPAWASQEKENSQTSLFA ISHVTLSSISKTRSSAKRDE KPGSSPHLALVRSQGLPQSV VP in isoform 11.
VSP_002982
Alternative sequence768 – 82154EYLDL…GSVKT → PLS in isoform 12.
VSP_002983
Alternative sequence768 – 82154Missing in isoform 13.
VSP_002977
Alternative sequence768 – 82154EYLDL…GSVKT → I in isoform 2, isoform 8, isoform 17 and isoform 22.
VSP_002978
Alternative sequence768 – 82154EYLDL…GSVKT → RYKLLPCPDKHNKRCKPEER GDLTEAGAAGSSRCVDSRKR VRQEKISTG in isoform 7.
VSP_002979
Alternative sequence768 – 82154EYLDL…GSVKT → RILTLTTNENFQSTSGREGT EIHALQCLRSEVTPAISCES PLADTGSKVPN in isoform 9.
VSP_002980
Alternative sequence769 – 82153YLDLS…GSVKT → EKKVSGAVDCHKPPCNPSHL PCVLAVDQ in isoform 21.
VSP_041915
Alternative sequence778 – 82144QYSPS…GSVKT → PYSPCYPDPR in isoform 6.
VSP_002984
Natural variant61R → P. Ref.15
Corresponds to variant rs3750819 [ dbSNP | Ensembl ].
VAR_017258
Natural variant571S → L. Ref.84
Corresponds to variant rs56226109 [ dbSNP | Ensembl ].
VAR_042204
Natural variant1051Y → C in CS. Ref.60 Ref.79
VAR_004112
Natural variant1721A → F in PS; requires 2 nucleotide substitutions. Ref.79
VAR_017259
Natural variant1861M → T. Ref.15 Ref.79 Ref.84
Corresponds to variant rs755793 [ dbSNP | Ensembl ].
VAR_017260
Natural variant2031R → C in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.83 Ref.84
VAR_036380
Natural variant252 – 2532SP → FS in PS.
VAR_004116
Natural variant2521S → F in APRS; requires 2 nucleotide substitutions. Ref.65
VAR_004114
Natural variant2521S → L in CS. Ref.65
VAR_004113
Natural variant2521S → W in APRS and PS; common mutation. Ref.21 Ref.28 Ref.45 Ref.57 Ref.67 Ref.69 Ref.71 Ref.79
VAR_004115
Natural variant2531P → R in APRS; common mutation. Ref.21 Ref.45 Ref.57 Ref.67 Ref.69 Ref.79
VAR_004117
Natural variant2631P → L in CS. Ref.75
VAR_017261
Natural variant2671S → P in CS. Ref.79
VAR_004118
Natural variant2681T → TG in CS. Ref.59
VAR_004119
Natural variant2721G → V in an ovarian serous carcinoma sample; somatic mutation. Ref.84
VAR_042205
Natural variant2731Missing in PS; type 2. Ref.74
VAR_017262
Natural variant2761F → V in CS. Ref.68 Ref.75 Ref.79
VAR_004120
Natural variant2781C → F in CS, JWS and PS; forms disulfide-linked dimers with constitutive kinase activity, is retained in an intracellular compartment and not detected at the cell surface. Ref.31 Ref.59 Ref.67 Ref.75 Ref.79
VAR_004121
Natural variant2781C → Y in CS. Ref.75
VAR_017263
Natural variant2811Y → C in CS. Ref.78 Ref.79
VAR_017264
Natural variant2831D → N in a lung squamous cell carcinoma sample; somatic mutation. Ref.84
VAR_042206
Natural variant287 – 2893Missing in CS.
VAR_004122
Natural variant2881I → S in CS. Ref.75
VAR_017265
Natural variant2891Q → P in CS and JWS. Ref.24 Ref.59 Ref.75 Ref.78 Ref.79
VAR_004123
Natural variant2901W → C in PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation. Ref.63 Ref.79 Ref.84
VAR_004124
Natural variant2901W → G in CS. Ref.55
VAR_017266
Natural variant2901W → R in CS.
VAR_004125
Natural variant2921K → E in CS. Ref.66
VAR_004126
Natural variant3011Y → C in CS. Ref.68
VAR_004127
Natural variant3141A → S in craniosynostosis. Ref.68
VAR_004128
Natural variant3151A → S in a non-syndromic craniosynostosis patient with abnormal intrauterine history; confers predisposition to craniosynostosis. Ref.76 Ref.79
VAR_017267
Natural variant3211D → A in PS. Ref.56
VAR_004129
Natural variant3281Y → C in CS. Ref.53
VAR_004130
Natural variant3311N → I in CS. Ref.61
VAR_004131
Natural variant3371A → ANA in CS.
VAR_004132
Natural variant3371A → P in CS. Ref.67
VAR_017268
Natural variant3381G → E in CS. Ref.60
VAR_004133
Natural variant3381G → R in CS. Ref.24 Ref.67 Ref.79
VAR_015011
Natural variant3401Y → C in PS. Ref.73 Ref.79
VAR_017269
Natural variant3401Y → H in CS. Ref.52 Ref.79
VAR_004134
Natural variant3411T → P in PS and CS. Ref.58 Ref.75 Ref.79
VAR_004135
Natural variant3421C → F in CS. Ref.59 Ref.67 Ref.79
VAR_004136
Natural variant3421C → G in PS. Ref.73
VAR_017270
Natural variant3421C → R in CS, JWS, PS and ABS2. Ref.52 Ref.55 Ref.58 Ref.59 Ref.67 Ref.75 Ref.77 Ref.78 Ref.79
VAR_004137
Natural variant3421C → S in CS, JWS, PS and ABS2. Ref.10 Ref.24 Ref.52 Ref.59 Ref.64 Ref.75 Ref.77 Ref.79
VAR_004138
Natural variant3421C → W in CS. Ref.55 Ref.75 Ref.79
VAR_017271
Natural variant3421C → Y in CS and PS. Ref.24 Ref.52 Ref.58 Ref.59 Ref.67 Ref.75 Ref.78 Ref.79
VAR_004139
Natural variant3441A → G in CS and JWS. Ref.24 Ref.53
VAR_004140
Natural variant3441A → P in CS and PS. Ref.59
VAR_004141
Natural variant3471S → C in CS. Ref.53 Ref.79
VAR_004142
Natural variant3511S → C in CS, PS and ABS2. Ref.60 Ref.70 Ref.77
VAR_004143
Natural variant3541S → C in CS. Ref.24 Ref.52 Ref.55 Ref.75 Ref.79
VAR_004144
Natural variant3541S → Y in CS. Ref.75
VAR_017272
Natural variant356 – 3583Missing in CS.
VAR_004145
Natural variant3591V → F in CS and PS. Ref.59 Ref.75
VAR_004146
Natural variant3621A → S in CS. Ref.72
VAR_017273
Natural variant3721S → C in BSTVS. Ref.62
VAR_017274
Natural variant3751Y → C in PS and BSTVS. Ref.62 Ref.79 Ref.80
VAR_017275
Natural variant3811Y → D in BBDS. Ref.85
VAR_067977
Natural variant3841G → R in CS. Ref.60
VAR_004147
Natural variant3911M → R in BBDS; the mutation selectively reduces plasma-membrane levels of the protein and markedly diminishes the receptor's responsiveness to extracellular FGF. Ref.85
VAR_067978
Natural variant5261K → E in FSPC; constitutive kinase activity. Ref.48 Ref.81
VAR_023788
Natural variant5491N → H in CS; constitutive kinase activity. Ref.48 Ref.79
VAR_017276
Natural variant5651E → G in PS; constitutive kinase activity. Ref.48 Ref.79
VAR_017277
Natural variant6121R → T in a lung adenocarcinoma sample; somatic mutation. Ref.84
VAR_046071
Natural variant6131G → R. Ref.7 Ref.11
VAR_015012
Natural variant6281A → T in LADDS; strongly reduced kinase activity. Ref.49 Ref.82
VAR_029884
Natural variant6411K → R in PS; constitutive kinase activity. Ref.48 Ref.79
VAR_017278
Natural variant6481A → T in LADDS. Ref.82
VAR_029885
Natural variant649 – 6502RD → S in LADDS.
VAR_029886
Natural variant6591K → N in craniosynostosis; constitutive kinase activity. Ref.48 Ref.79
VAR_017279
Natural variant6631G → E in PS. Ref.79
VAR_017280
Natural variant6781R → G in CS. Ref.79
VAR_017281

Experimental info

Mutagenesis2651N → Q: Reduced N-glycosylation. Reduced expression at the cell surface. Ref.31
Mutagenesis5491N → T: Constitutive kinase activity. Ref.48
Mutagenesis5651E → A: Constitutive kinase activity. Ref.48
Mutagenesis656 – 6572Missing: Loss of kinase activity.
Mutagenesis7691Y → F: Increases fibroblast proliferation. Decreases phosphorylation of PLCG1 and FRS2. Decreases activation of MAP kinases. Ref.29 Ref.36
Sequence conflict2461L → P in BAG57383. Ref.16
Sequence conflict3101K → N in BAG57383. Ref.16
Isoform 16:
Sequence conflict3151T → L in AAA61188. Ref.2

Secondary structure

........................................................................................................... 821
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BEK) (FGFR2IIIc) [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 6CD5001C960ED82F

FASTA82192,025
        10         20         30         40         50         60 
MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEVY VAAPGESLEV 

        70         80         90        100        110        120 
RCLLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAS RTVDSETWYF 

       130        140        150        160        170        180 
MVNVTDAISS GDDEDDTDGA EDFVSENSNN KRAPYWTNTE KMEKRLHAVP AANTVKFRCP 

       190        200        210        220        230        240 
AGGNPMPTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CVVENEYGSI 

       250        260        270        280        290        300 
NHTYHLDVVE RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK 

       310        320        330        340        350        360 
YGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI SFHSAWLTVL 

       370        380        390        400        410        420 
PAPGREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVILCRM KNTTKKPDFS SQPAVHKLTK 

       430        440        450        460        470        480 
RIPLRRQVTV SAESSSSMNS NTPLVRITTR LSSTADTPML AGVSEYELPE DPKWEFPRDK 

       490        500        510        520        530        540 
LTLGKPLGEG CFGQVVMAEA VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM 

       550        560        570        580        590        600 
IGKHKNIINL LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF 

       610        620        630        640        650        660 
KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD INNIDYYKKT 

       670        680        690        700        710        720 
TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH 

       730        740        750        760        770        780 
RMDKPANCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEEYL DLSQPLEQYS 

       790        800        810        820 
PSYPDTRSSC SSGDDSVFSP DPMPYEPCLP QYPHINGSVK T 

« Hide

Isoform 2 (Short) [UniParc].

Checksum: 8D4734CBEA8E8C8F
Show »

FASTA76886,130
Isoform 3 (BFR-1) (FGFR2IIIb) (KGFR) [UniParc].

Checksum: 288CF737673BA4AB
Show »

FASTA82292,118
Isoform 4 (K-sam) [UniParc].

Checksum: D56050B4385A6635
Show »

FASTA68276,705
Isoform 5 (K-sam-I) (BEK) (IgIIIc) [UniParc].

Checksum: 4746938783A1D94F
Show »

FASTA81991,825
Isoform 6 (K-sam-IIC2) [UniParc].

Checksum: 042BF83F92CE97F5
Show »

FASTA78588,181
Isoform 7 (K-sam-IIO2) [UniParc].

Checksum: 46BA78E51DB700CD
Show »

FASTA81791,620
Isoform 8 (K-sam-IIC3) [UniParc].

Checksum: FE97A413B085D31E
Show »

FASTA76685,929
Isoform 9 (K-sam-IIH1) [UniParc].

Checksum: C60FE09EC1BE0654
Show »

FASTA81991,566
Isoform 10 (K-sam-IIH2) [UniParc].

Checksum: 467E9BAAD07C5463
Show »

FASTA81991,641
Isoform 11 (K-sam-IIH3) (K-sam-IIO4) [UniParc].

Checksum: E726FA4235995586
Show »

FASTA83092,733
Isoform 12 (K-sam-IIO1) [UniParc].

Checksum: 881C475B4771CA5C
Show »

FASTA77186,407
Isoform 13 (K-sam-IIO3) [UniParc].

Checksum: BB4771CA5CBEEFAA
Show »

FASTA76886,110
Isoform 14 (K-sam-IV) (Soluble KGFR) [UniParc].

Checksum: 1855113266C85F4F
Show »

FASTA25428,299
Isoform 15 (K-sam-III) [UniParc].

Checksum: 590967DCBF5DA25D
Show »

FASTA70579,212
Isoform 16 (TK14) [UniParc].

Checksum: 15D08A6D66AC4EA0
Show »

FASTA82292,153
Isoform 17 [UniParc].

Checksum: 806B4771CA5CBEEF
Show »

FASTA76986,223
Isoform 18 (K-sam-IIC1) (KGFR) (IgIIIb) [UniParc].

Checksum: 806D62B2FF25AFF6
Show »

FASTA82091,918
Isoform 19 (Soluble KGFR) [UniParc].

Checksum: C02708836203465F
Show »

FASTA36640,614
Isoform 20 [UniParc].

Checksum: 287F39DCF95B9312
Show »

FASTA70479,197
Isoform 21 [UniParc].

Checksum: 01DF22CD5B50092A
Show »

FASTA70779,300
Isoform 22 [UniParc].

Checksum: A6FF9BEBABCCE931
Show »

FASTA68076,423
Isoform 23 [UniParc].

Checksum: 7F37AAB82F8B7A48
Show »

FASTA70979,833

References

« Hide 'large scale' references
[1]"Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors."
Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G., Ruta M., Burgess W.H., Jaye M., Schlessinger J.
EMBO J. 9:2685-2692(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Neonatal brain stem.
[2]"Related fibroblast growth factor receptor genes exist in the human genome."
Houssaint E., Blanquet P.R., Champion-Arnaud P., Gesnel M.-C., Torriglia A., Courtois Y., Breathnach R.
Proc. Natl. Acad. Sci. U.S.A. 87:8180-8184(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16).
[3]"Two cDNAs encoding novel human FGF receptor."
Seno M., Sasada R., Watanabe T., Ishimaru K., Igarashi K.
Biochim. Biophys. Acta 1089:244-246(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 17).
[4]"K-sam, an amplified gene in stomach cancer, is a member of the heparin-binding growth factor receptor genes."
Hattori Y., Odagiri H., Nakatani H., Miyagawa K., Naito K., Sakamoto H., Katoh O., Yoshida T., Sugimura T., Terada M.
Proc. Natl. Acad. Sci. U.S.A. 87:5983-5987(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Stomach cancer.
[5]"K-sam gene encodes secreted as well as transmembrane receptor tyrosine kinase."
Katoh M., Hattori Y., Sasaki H., Tanaka M., Sugano K., Yazaki Y., Sugimura T., Terada M.
Proc. Natl. Acad. Sci. U.S.A. 89:2960-2964(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 14 AND 15).
[6]"A novel form of fibroblast growth factor receptor 2. Alternative splicing of the third immunoglobulin-like domain confers ligand binding specificity."
Dell K.R., Williams L.T.
J. Biol. Chem. 267:21225-21229(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DOMAIN, SUBUNIT.
Tissue: Placenta.
[7]"Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene."
Miki T., Bottaro D.P., Fleming T.P., Smith C.L., Burgess W.H., Chan A.M.-L., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 89:246-250(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 19), SUBUNIT, DOMAIN, VARIANT ARG-613.
Tissue: Mammary gland.
[8]"Hepatocyte growth factor (HGF), keratinocyte growth factor (KGF), and their receptors in human breast cells and tissues: alternative receptors."
Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., Shay J.W.
Cell. Mol. Biol. Res. 40:337-350(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19).
Tissue: Cornea and Mammary gland.
[9]Erratum
Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., Shay J.W.
Cell. Mol. Biol. Res. 40:707-707(1994)
[10]Steinberger D., Mueller U.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CS SER-342.
Tissue: Blood.
[11]"Deletion of the carboxyl-terminal exons of K-sam/FGFR2 by short homology-mediated recombination, generating preferential expression of specific messenger RNAs."
Ueda T., Sasaki H., Kuwahara Y., Nezu M., Shibuya T., Sakamoto H., Ishii H., Yanagihara K., Mafune K., Makuuchi M., Terada M.
Cancer Res. 59:6080-6086(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 9; 10; 11; 12 AND 13), VARIANT ARG-613.
[12]"Fibroblast growth factor receptor 2 (FGFR2): genomic sequence and variations."
Ingersoll R.G., Paznekas W.A., Tran A.K., Scott A.F., Jiang G., Jabs E.W.
Cytogenet. Cell Genet. 94:121-126(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 5; 6; 8; 14 AND 18).
[13]"Sequence and polymorphisms in fibroblast growth factor receptor 2 (FGFR2) gene in humans."
Lind D.L., Cox D.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
[14]"Identification of a novel variant of FGFR2."
Jang J.
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 23).
[15]NIEHS SNPs program
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-6 AND THR-186.
[16]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 21).
Tissue: Cerebellum.
[17]"The DNA sequence and comparative analysis of human chromosome 10."
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J. expand/collapse author list , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[18]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 20).
Tissue: Brain.
[19]"Paternal origin of FGFR2 mutations in sporadic cases of Crouzon syndrome and Pfeiffer syndrome."
Glaser R.L., Jiang W., Boyadjiev S.A., Tran A.K., Zachary A.A., Van Maldergem L., Johnson D., Walsh S., Oldridge M., Wall S.A., Wilkie A.O.M., Jabs E.W.
Am. J. Hum. Genet. 66:768-777(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-427.
[20]"Genomic organization of the human fibroblast growth factor receptor 2 (FGFR2) gene and comparative analysis of the human FGFR gene family."
Zhang Y., Gorry M.C., Post J.C., Ehrlich G.D.
Gene 230:69-79(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209; 212-767 AND 771-821 (ISOFORMS 5; 14 AND 18).
[21]"Analysis of phenotypic features and FGFR2 mutations in Apert syndrome."
Park W.-J., Theda C., Maestri N.E., Meyers G.A., Fryburg J.S., Dufresne C., Cohen M.M. Jr., Jabs E.W.
Am. J. Hum. Genet. 57:321-328(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-313, VARIANTS APRS TRP-252 AND ARG-253.
[22]"Nucleotide sequences at intron 6 and exon 7 junction of fibroblast growth factor receptor 2 and rapid mutational analysis in Apert syndrome."
Wada C., Ishigaki M., Toyo-oka Y., Yamabe H., Ohnuki Y., Takada F., Yamazaki Y., Ohtani H.
Rinsho Byori 44:435-438(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-259.
[23]"Exclusive paternal origin of new mutations in Apert syndrome."
Moloney D.M., Slaney S.F., Oldridge M., Wall S.A., Sahlin P., Stenman G., Wilkie A.O.M.
Nat. Genet. 13:48-53(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-318.
[24]"Crouzon syndrome: mutations in two spliceoforms of FGFR2 and a common point mutation shared with Jackson-Weiss syndrome."
Gorry M.C., Preston R.A., White G.J., Zhang Y., Singhal V.K., Losken H.W., Parker M.G., Nwokoro N.A., Post J.C., Ehrlich G.D.
Hum. Mol. Genet. 4:1387-1390(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-361, VARIANTS CS PRO-289; ARG-338; SER-342; TYR-342; GLY-344 AND CYS-354.
[25]"Asparagine-344 is a key residue for ligand binding in keratinocyte growth factor receptor."
Gray T.E., Eisenstein M., Yayon A., Givol D.
Biochemistry 35:15640-15645(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION (ISOFORM 3), SUBUNIT, DOMAIN.
[26]"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; FGF3; FGF4; FGF6; FGF7 AND FGF9, FUNCTION IN CELL PROLIFERATION.
[27]"p21-activated protein kinase 4 (PAK4) interacts with the keratinocyte growth factor receptor and participates in keratinocyte growth factor-mediated inhibition of oxidant-induced cell death."
Lu Y., Pan Z.-Z., Devaux Y., Ray P.
J. Biol. Chem. 278:10374-10380(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PAK4; REGULATION OF CELL PROLIFERATION AND APOPTOSIS, INTERACTION WITH GRB2 AND PAK4.
[28]"Cbl-mediated degradation of Lyn and Fyn induced by constitutive fibroblast growth factor receptor-2 activation supports osteoblast differentiation."
Kaabeche K., Lemonnier J., Le Mee S., Caverzasio J., Marie P.J.
J. Biol. Chem. 279:36259-36267(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN OSTEOBLAST DIFFERENTIATION AND IN PHOSPHORYLATION OF CBL, INTERACTION WITH CBL, UBIQUITINATION, CHARACTERIZATION OF VARIANT APRS TRP-252.
[29]"Tyrosine 769 of the keratinocyte growth factor receptor is required for receptor signaling but not endocytosis."
Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R.
Biochem. Biophys. Res. Commun. 327:523-532(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION AND ACTIVATION OF SIGNALING PATHWAYS, MUTAGENESIS OF TYR-769, PHOSPHORYLATION AT TYR-769, INTERACTION WITH PLCG1.
[30]"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; FGF7; FGF8; FGF9; FGF10; FGF19; FGF21; FGF22 AND FGF23, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
[31]"Intracellular retention, degradation, and signaling of glycosylation-deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F."
Hatch N.E., Hudson M., Seto M.L., Cunningham M.L., Bothwell M.
J. Biol. Chem. 281:27292-27305(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF PLCG1 (ISOFORM 1), CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH PLCG1, SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-265 AND 656-TYR-TYR-657, UBIQUITINATION, CHARACTERIZATION OF VARIANT PS PHE-278.
[32]"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, FUNCTION IN PHOSPHORYLATION OF FRS2 AND ACTIVATION OF MAP KINASES.
[33]"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, SUBCELLULAR LOCATION, PHOSPHORYLATION.
[34]"FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt signaling and osteoblast survival."
Dufour C., Guenou H., Kaabeche K., Bouvard D., Sanjay A., Marie P.J.
Bone 42:1032-1039(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION.
[35]"Novel phosphotyrosine targets of FGFR2IIIb signaling."
Luo Y., Yang C., Jin C., Xie R., Wang F., McKeehan W.L.
Cell. Signal. 21:1370-1378(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS FGF7 RECEPTOR AND IN PHOSPHORYLATION OF PLCG1 AND FRS2, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-466; TYR-586; TYR-588; TYR-656 AND TYR-657, IDENTIFICATION BY MASS SPECTROMETRY.
[36]"Aberrant receptor internalization and enhanced FRS2-dependent signaling contribute to the transforming activity of the fibroblast growth factor receptor 2 IIIb C3 isoform."
Cha J.Y., Maddileti S., Mitin N., Harden T.K., Der C.J.
J. Biol. Chem. 284:6227-6240(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN FIBROBLAST PROLIFERATION; ACTIVATION OF MAP KINASES AND PHOSPHORYLATION OF PLCG1 AND FRS2, INTERACTION WITH PLCG1 AND FRS2, SUBCELLULAR LOCATION, MUTAGENESIS OF TYR-769.
[37]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[38]"The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic differentiation in human mesenchymal stromal cells in part by decreased Cbl-mediated platelet-derived growth factor receptor alpha and fibroblast growth factor receptor 2 ubiquitination."
Severe N., Miraoui H., Marie P.J.
J. Biol. Chem. 286:24443-24450(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, UBIQUITINATION.
[39]"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 LIGAND SPECIFICITY, ALTERNATIVE SPLICING, SIGNALING.
[40]"FGFR2 abnormalities underlie a spectrum of bone, skin, and cancer pathologies."
Katoh M.
J. Invest. Dermatol. 129:1861-1867(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON LIGAND SPECIFICITY, ALTERNATIVE SPLICING, SIGNALING, ROLE IN DISEASE.
[41]"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.
[42]"Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."
Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.
Cell 101:413-424(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 147-366 IN COMPLEX WITH FGF2.
[43]"Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin."
Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.
Nature 407:1029-1034(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 148-366 IN COMPLEX WITH FGF1 AND HEPARIN, INTERACTION WITH FGF1 AND HEPARIN.
[44]"Structural interactions of fibroblast growth factor receptor with its ligands."
Stauber D.J., DiGabriele A.D., Hendrickson W.A.
Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 147-362 IN COMPLEX WITH FGF1.
[45]"Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome."
Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-366 OF VARIANTS APRS TRP-252 AND ARG-253 IN COMPLEX WITH FGF2.
[46]"Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors."
Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D., Aaronson S.A., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-371 IN COMPLEX WITH FGF10.
[47]"Structural basis by which alternative splicing modulates the organizer activity of FGF8 in the brain."
Olsen S.K., Li J.Y.H., Bromleigh C., Eliseenkova A.V., Ibrahimi O.A., Lao Z., Zhang F., Linhardt R.J., Joyner A.L., Mohammadi M.
Genes Dev. 20:185-198(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 149-368 IN COMPLEX WITH FGF8, FUNCTION AS FGF8 RECEPTOR, INTERACTION WITH FGF8, DISULFIDE BONDS.
[48]"A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases."
Chen H., Ma J., Li W., Eliseenkova A.V., Xu C., Neubert T.A., Miller W.T., Mohammadi M.
Mol. Cell 27:717-730(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP ANALOG; PEPTIDE SUBSTRATE AND MAGNESIUM, ENZYME REGULATION, PHOSPHORYLATION AT TYR-586; TYR-656 AND TYR-657, MUTAGENESIS OF ASN-549 AND GLU-565, CHARACTERIZATION OF VARIANT FSPC GLU-526, CHARACTERIZATION OF VARIANT CS HIS-549, CHARACTERIZATION OF VARIANTS PS GLY-565 AND ARG-641, CHARACTERIZATION OF VARIANT CRANIOSYNOSTOSIS ASN-659.
[49]"Structural basis for reduced FGFR2 activity in LADD syndrome: Implications for FGFR autoinhibition and activation."
Lew E.D., Bae J.H., Rohmann E., Wollnik B., Schlessinger J.
Proc. Natl. Acad. Sci. U.S.A. 104:19802-19807(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-766 OF VARIANT LADDS THR-628 IN COMPLEX WITH ATP ANALOG, CATALYTIC ACTIVITY, SUBUNIT, AUTOPHOSPHORYLATION.
[50]"A crystallographic snapshot of tyrosine trans-phosphorylation in action."
Chen H., Xu C.F., Ma J., Eliseenkova A.V., Li W., Pollock P.M., Pitteloud N., Miller W.T., Neubert T.A., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 105:19660-19665(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP, ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-466; TYR-586; TYR-588; TYR-656; TYR-657 AND TYR-769.
[51]"A novel mode of protein kinase inhibition exploiting hydrophobic motifs of autoinhibited kinases: discovery of ATP-independent inhibitors of fibroblast growth factor receptor."
Eathiraj S., Palma R., Hirschi M., Volckova E., Nakuci E., Castro J., Chen C.R., Chan T.C., France D.S., Ashwell M.A.
J. Biol. Chem. 286:20677-20687(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 458-768 IN COMPLEX WITH INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, ENZYME REGULATION.
[52]"Mutations in the fibroblast growth factor receptor 2 gene cause Crouzon syndrome."
Reardon W., Winter R.M., Rutland P., Pulleyn L.J., Jones B.M., Malcolm S.
Nat. Genet. 8:98-103(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS HIS-340; ARG-342; SER-342; TYR-342 AND CYS-354.
[53]"Jackson-Weiss and Crouzon syndromes are allelic with mutations in fibroblast growth factor receptor 2."
Jabs E.W., Li X., Scott A.F., Meyers G.A., Chen W., Eccles M., Mao J., Charnas L.R., Jackson C.E., Jaye M.
Nat. Genet. 8:275-279(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS CYS-328 AND CYS-347, VARIANT JWS GLY-344.
[54]"Mutations in the third immunoglobulin domain of the fibroblast growth factor receptor-2 gene in Crouzon syndrome."
Oldridge M., Wilkie A.O.M., Slaney S.F., Poole M.D., Pulleyn L.J., Rutland P., Hockley A.D., Wake M.J.C., Goldin J.H., Winter R.M., Reardon W., Malcolm S.
Hum. Mol. Genet. 4:1077-1082(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS.
[55]"Novel FGFR2 mutations in Crouzon and Jackson-Weiss syndromes show allelic heterogeneity and phenotypic variability."
Park W.-J., Meyers G.A., Li X., Theda C., Day D., Orlow S.J., Jones M.C., Jabs E.W.
Hum. Mol. Genet. 4:1229-1233(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS GLY-290; TRP-342 AND CYS-354, VARIANT JWS ARG-342.
[56]"FGFR2 mutations in Pfeiffer syndrome."
Lajeunie E., Wei M.H., Bonaventure J., Munnich A., le Merrer M., Renier D.
Nat. Genet. 9:108-108(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PS ALA-321.
[57]"Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome."
Wilkie A.O.M., Slaney S.F., Oldridge M., Poole M.D., Ashworth G.J., Hockley A.D., Hayward R.D., David D.J., Pulleyn L.J., Rutland P., Malcolm S., Winter R.M., Reardon W.
Nat. Genet. 9:165-172(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APRS TRP-252 AND ARG-253.
[58]"Identical mutations in the FGFR2 gene cause both Pfeiffer and Crouzon syndrome phenotypes."
Rutland P., Pulleyn L.J., Reardon W., Baraister M., Hayward R., Jones B.M., Malcolm S., Winter R.M., Oldridge M., Slaney S.F., Poole M.D., Wilkie A.O.M.
Nat. Genet. 9:173-176(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PS PRO-341; ARG-342 AND TYR-342.
[59]"FGFR2 exon IIIa and IIIc mutations in Crouzon, Jackson-Weiss, and Pfeiffer syndromes: evidence for missense changes, insertions, and a deletion due to alternative RNA splicing."
Meyers G.A., Day D., Goldberg R., Daentl D.L., Przylepa K.A., Abrams L.J., Graham J.M. Jr., Feingold M., Moeschler J.B., Rawnsley E., Scott A.F., Jabs E.W.
Am. J. Hum. Genet. 58:491-498(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS GLY-268 INS; PHE-342 AND TYR-342, VARIANTS PS PHE-278; ARG-342; SER-342; PRO-344 AND PHE-359, VARIANT JWS PRO-289.
[60]"Spectrum of craniosynostosis phenotypes associated with novel mutations at the fibroblast growth factor receptor 2 locus."
Pulleyn L.J., Reardon W., Wilkes D., Rutland P., Jones B.M., Hayward R., Hall C.M., Brueton L., Chun N., Lammer E., Malcolm S., Winter R.M.
Eur. J. Hum. Genet. 4:283-291(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS CYS-105; GLU-338; CYS-351 AND ARG-384.
[61]"Crouzon syndrome: previously unrecognized deletion, duplication, and point mutation within FGFR2 gene."
Steinberger D., Mulliken J.B., Mueller U.
Hum. Mutat. 8:386-390(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS ILE-331; ASN-ALA-337 INS AND 356-TRP--THR-358 DEL.
[62]"Fibroblast growth factor receptor 2 mutations in Beare-Stevenson cutis gyrata syndrome."
Przylepa K.A., Paznekas W.A., Zhang M., Golabi M., Bias W., Bamshad M.J., Carey J.C., Hall B.D., Stevenson R., Orlow S.J., Cohen M.M. Jr., Jabs E.W.
Nat. Genet. 13:492-494(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BSTVS CYS-372 AND CYS-375.
[63]"Trp290Cys mutation in exon IIIa of the fibroblast growth factor receptor 2 (FGFR2) gene is associated with Pfeiffer syndrome."
Tartaglia M., Valeri S., Velardi F., di Rocco C., Battaglia P.A.
Hum. Genet. 99:602-606(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PS CYS-290.
[64]"Jackson-Weiss syndrome: identification of two novel FGFR2 missense mutations shared with Crouzon and Pfeiffer craniosynostotic disorders."
Tartaglia M., Di Rocco C., Lajeunie E., Valeri S., Velardi F., Battaglia P.A.
Hum. Genet. 101:47-50(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT JWS SER-342.
[65]"Genotype-phenotype correlation for nucleotide substitutions in the IgII-IgIII linker of FGFR2."
Oldridge M., Lunt P.W., Zackai E.H., McDonald-Mcginn D.M., Muenke M., Moloney D.M., Twigg S.R.F., Heath J.K., Howard T.D., Hoganson G., Gagnon D.M., Jabs E.W., Wilkie A.O.M.
Hum. Mol. Genet. 6:137-143(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CS LEU-252, VARIANT APRS PHE-252, VARIANT PS 252-PHE-SER-253.
[66]"A novel mutation (a886g) in exon 5 of FGFR2 in members of a family with Crouzon phenotype and plagiocephaly."
Steinberger D., Collmann H., Schmalenberger B., Mueller U.
J. Med. Genet. 34:420-422(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CS GLU-292.
[67]"Description of a new mutation and characterization of FGFR1, FGFR2, and FGFR3 mutations among Brazilian patients with syndromic craniosynostoses."
Passos-Bueno M.R., Sertie A.L., Richieri-Costa A., Alonso L.G., Zatz M., Alonso N., Brunoni D., Ribeiro S.F.M.
Am. J. Med. Genet. 78:237-241(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS PHE-278; PRO-337; ARG-338; ARG-342; PHE-342 AND TYR-342, VARIANTS APRS TRP-252 AND ARG-253, VARIANT JWS PHE-278.
[68]"The mutations in FGFR2-associated craniosynostoses are clustered in five structural elements of immunoglobulin-like domain III of the receptor."
Steinberger D., Vriend G., Mulliken J.B., Mueller U.
Hum. Genet. 102:145-150(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS VAL-276 AND CYS-301, VARIANT CRANIOSYNOSTOSIS SER-314.
[69]"Two common mutations 934C to G and 937C to G of fibroblast growth factor receptor 2 (FGFR2) gene in Chinese patients with Apert syndrome."
Tsai F.-J., Hwu W.-L., Lin S.-P., Chang J.-G., Wang T.-R., Tsai C.-H.
Hum. Mutat. Suppl. 1:S18-S19(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS APRS TRP-252 AND ARG-253.
[70]"Pfeiffer's syndrome resulting from an S351C mutation in the fibroblast growth factor receptor-2 gene."
Mathijssen I.M., Vaandrager J.M., Hoogeboom A.J., Hesseling-Janssen A.L.W., van den Ouweland A.M.W.
J. Craniofac. Surg. 9:207-209(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PS CYS-351.
[71]"Presence of the Apert canonical S252W FGFR2 mutation in a patient without severe syndactyly."
Passos-Bueno M.R., Richieri-Costa A., Sertie A.L., Kneppers A.
J. Med. Genet. 35:677-679(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PS TRP-252.
[72]"A novel FGFR2 gene mutation in Crouzon syndrome associated with apparent nonpenetrance."
Everett E.T., Britto D.A., Ward R.E., Hartsfield J.K. Jr.
Cleft Palate Craniofac. J. 36:533-541(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT CS SER-362.
[73]"Analysis of the mutational spectrum of the FGFR2 gene in Pfeiffer syndrome."
Cornejo-Roldan L.R., Roessler E., Muenke M.
Hum. Genet. 104:425-431(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS PS CYS-340 AND GLY-342.
[74]"Pfeiffer syndrome type 2 associated with a single amino acid deletion in the FGFR2 gene."
Priolo M., Lerone M., Baffico M., Baldi M., Ravazzolo R., Cama A., Capra V., Silengo M.
Clin. Genet. 58:81-83(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PS ASP-273 DEL.
[75]"Clustering of FGFR2 gene mutations in patients with Pfeiffer and Crouzon syndromes (FGFR2-associated craniosynostoses)."
Kress W., Collmann H., Buesse M., Halliger-Keller B., Mueller C.R.
Cytogenet. Cell Genet. 91:134-137(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS/PS ARG-342 AND TYR-342, VARIANTS CS LEU-263; VAL-276; PHE-278; TYR-278; SER-288; PRO-289; PRO-341; TRP-342; CYS-354; TYR-354 AND PHE-359, VARIANT PS SER-342.
[76]"A novel mutation, Ala315Ser, in FGFR2: a gene-environment interaction leading to craniosynostosis?"
Johnson D., Wall S.A., Mann S., Wilkie A.O.M.
Eur. J. Hum. Genet. 8:571-577(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT SER-315.
[77]"Evidence for digenic inheritance in some cases of Antley-Bixler syndrome?"
Reardon W., Smith A., Honour J.W., Hindmarsh P., Das D., Rumsby G., Nelson I., Malcolm S., Ades L., Sillence D., Kumar D., DeLozier-Blanchet C., McKee S., Kelly T., McKeehan W.L., Baraitser M., Winter R.M.
J. Med. Genet. 37:26-32(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS ABS2 ARG-342; SER-342 AND CYS-351.
[78]"Mutation analysis of Crouzon syndrome and identification of one novel mutation in Taiwanese patients."
Tsai F.-J., Yang C.-F., Wu J.-Y., Tsai C.-H., Lee C.-C.
Pediatr. Int. 43:263-266(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS CYS-281; PRO-289; ARG-342 AND TYR-342.
[79]"Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis."
Kan S.-H., Elanko N., Johnson D., Cornejo-Roldan L.R., Cook J., Reich E.W., Tomkins S., Verloes A., Twigg S.R.F., Rannan-Eliya S., McDonald-McGinn D.M., Zackai E.H., Wall S.A., Muenke M., Wilkie A.O.M.
Am. J. Hum. Genet. 70:472-486(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS CS CYS-105; PRO-267; VAL-276; CYS-281; PRO-289; ARG-338; HIS-340; PHE-342; TRP-342; CYS-347; CYS-354; HIS-549 AND GLY-678, VARIANTS PS PHE-172; 252-PHE-SER-253; CYS-290; CYS-340; PRO-341; ARG-342; SER-342; CYS-375; GLY-565; ARG-641 AND GLU-663, VARIANTS APRS TRP-252 AND ARG-253, VARIANTS CS/PS PHE-278 AND TYR-342, VARIANT CRANIOSYNOSTOSIS ASN-659, VARIANTS THR-186 AND SER-315.
[80]"Mutation in the FGFR2 gene in a Taiwanese patient with Beare-Stevenson cutis gyrata syndrome."
Wang T.-J., Huang C.-B., Tsai F.-J., Wu J.-Y., Lai R.-B., Hsiao M.
Clin. Genet. 61:218-221(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT BSTVS CYS-375.
[81]"Familial scaphocephaly syndrome caused by a novel mutation in the FGFR2 tyrosine kinase domain."
McGillivray G., Savarirayan R., Cox T.C., Stojkoski C., McNeil R., Bankier A., Bateman J.F., Roscioli T., Gardner R.J.M., Lamande S.R.
J. Med. Genet. 42:656-662(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT FSPC GLU-526.
[82]"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: VARIANTS LADDS THR-628; THR-648 AND 649-ARG-ASP-650 DELINS SER.
[83]"The consensus coding sequences of human breast and colorectal cancers."
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V. expand/collapse author list , Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.
Science 314:268-274(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-203.
[84]"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] LEU-57; THR-186; CYS-203; VAL-272; ASN-283; CYS-290 AND THR-612.
[85]"Bent bone dysplasia-FGFR2 type, a distinct skeletal disorder, has deficient canonical FGF signaling."
Merrill A.E., Sarukhanov A., Krejci P., Idoni B., Camacho N., Estrada K.D., Lyons K.M., Deixler H., Robinson H., Chitayat D., Curry C.J., Lachman R.S., Wilcox W.R., Krakow D.
Am. J. Hum. Genet. 90:550-557(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS BBDS ASP-381 AND ARG-391, CHARACTERIZATION OF VARIANT BBDS ARG-391.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52832 mRNA. Translation: CAA37014.1.
M55614 mRNA. Translation: AAA61188.1.
X56191 mRNA. Translation: CAA39654.1.
M35718 mRNA. Translation: AAA36152.1.
M87770 mRNA. Translation: AAA59470.1.
M87771 mRNA. Translation: AAA59471.1.
M87772 mRNA. Translation: AAA59472.1.
M97193 mRNA. Translation: AAA52449.1.
U11814 mRNA. Translation: AAA68514.1.
M80634 mRNA. Translation: AAA36147.1.
Z71929 mRNA. Translation: CAA96492.1.
AB030073 mRNA. Translation: BAA89296.1.
AB030074 mRNA. Translation: BAA89297.1.
AB030075 mRNA. Translation: BAA89298.1.
AB030076 mRNA. Translation: BAA89299.1.
AB030077 mRNA. Translation: BAA89300.1.
AB030078 mRNA. Translation: BAA89301.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94205.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94206.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94207.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94208.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94209.1.
AF487553 Genomic DNA. Translation: AAM74056.1.
AB084153 mRNA. Translation: BAC45037.1.
DQ493927 Genomic DNA. Translation: ABE96832.1.
AK294026 mRNA. Translation: BAG57383.1. Different initiation.
AC009988 Genomic DNA. No translation available.
BC039243 mRNA. Translation: AAH39243.2.
AF169399 Genomic DNA. Translation: AAF43273.1.
AF169399 Genomic DNA. Translation: AAF43274.1.
AF097353 expand/collapse EMBL AC list , AF097341, AF097342, AF097343, AF097345, AF097346, AF097347, AF097348, AF097349, AF097350, AF097351, AF097352 Genomic DNA. Translation: AAD31560.1.
AF097353 expand/collapse EMBL AC list , AF097341, AF097342, AF097344, AF097345, AF097346, AF097347, AF097348, AF097349, AF097350, AF097351, AF097352 Genomic DNA. Translation: AAD31561.1.
AF097340 expand/collapse EMBL AC list , AF097337, AF097338, AF097339 Genomic DNA. Translation: AAD31562.1.
AF097354 Genomic DNA. Translation: AAD31565.1.
AF097341 Genomic DNA. Translation: AAD31567.1.
S82438 Genomic DNA. Translation: AAD14392.1.
Y17131 Genomic DNA. Translation: CAA76643.1.
L49237 Genomic DNA. Translation: AAC41933.1.
L49242 Genomic DNA. Translation: AAC41934.1.
L49238 Genomic DNA. Translation: AAC41935.1.
L49239 Genomic DNA. Translation: AAC41936.1.
L49240 Genomic DNA. Translation: AAC41937.1.
L49241 Genomic DNA. Translation: AAC41938.1.
CCDSCCDS31298.1. [P21802-1]
CCDS44485.1. [P21802-20]
CCDS44486.1. [P21802-23]
CCDS44487.1. [P21802-15]
CCDS44488.1. [P21802-22]
CCDS44489.1. [P21802-17]
CCDS53584.1. [P21802-21]
CCDS7620.2. [P21802-3]
PIRA35969.
TVHUF2. A42691.
A45081.
C42691.
S16236.
RefSeqNP_000132.3. NM_000141.4. [P21802-1]
NP_001138385.1. NM_001144913.1. [P21802-17]
NP_001138386.1. NM_001144914.1. [P21802-23]
NP_001138387.1. NM_001144915.1. [P21802-21]
NP_001138388.1. NM_001144916.1.
NP_001138389.1. NM_001144917.1. [P21802-15]
NP_001138390.1. NM_001144918.1. [P21802-20]
NP_001138391.1. NM_001144919.1. [P21802-22]
NP_075259.4. NM_022970.3. [P21802-3]
NP_075418.1. NM_023029.2.
UniGeneHs.533683.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJSX-ray2.40A32-362[»]
1E0OX-ray2.80B/D148-366[»]
1EV2X-ray2.20E/F/G/H147-366[»]
1GJOX-ray2.40A456-768[»]
1II4X-ray2.70E/F/G/H147-366[»]
1IILX-ray2.30E/F/G/H147-366[»]
1NUNX-ray2.90B140-368[»]
1OECX-ray2.40A456-768[»]
1WVZNMR-A147-249[»]
2FDBX-ray2.28P/R149-368[»]
2PSQX-ray2.40A/B413-768[»]
2PVFX-ray1.80A458-778[»]
B764-778[»]
2PVYX-ray2.20A/B/C/D458-768[»]
2PWLX-ray2.40A/B458-768[»]
2PY3X-ray2.30A/B458-768[»]
2PZ5X-ray2.40A/B458-768[»]
2PZPX-ray2.40A/B458-768[»]
2PZRX-ray3.00A/B458-768[»]
2Q0BX-ray2.90A/B458-768[»]
3B2TX-ray1.80A/B458-766[»]
3CAFX-ray1.96A150-249[»]
3CLYX-ray2.00A458-778[»]
3CU1X-ray2.60A/C150-249[»]
3DARX-ray2.20A/B146-249[»]
3EUUX-ray2.34A/B150-249[»]
3OJ2X-ray2.20C/D140-313[»]
3OJMX-ray2.10B140-313[»]
3RI1X-ray2.10A/B458-768[»]
4J23X-ray3.88A147-366[»]
4J95X-ray2.38A/B/C/D458-768[»]
4J96X-ray2.30A/B458-768[»]
4J97X-ray2.55A/B/C/D458-768[»]
4J98X-ray2.31A/B458-768[»]
4J99X-ray1.85A/B/C/D458-768[»]
ProteinModelPortalP21802.
SMRP21802. Positions 5-364, 462-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108554. 21 interactions.
DIPDIP-3788N.
IntActP21802. 10 interactions.
MINTMINT-118359.

Chemistry

BindingDBP21802.
ChEMBLCHEMBL4142.
DrugBankDB00039. Palifermin.
GuidetoPHARMACOLOGY1809.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteP21802.

Polymorphism databases

DMDM120049.

Proteomic databases

MaxQBP21802.
PaxDbP21802.
PRIDEP21802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000346997; ENSP00000263451; ENSG00000066468. [P21802-5]
ENST00000351936; ENSP00000309878; ENSG00000066468. [P21802-6]
ENST00000356226; ENSP00000348559; ENSG00000066468. [P21802-20]
ENST00000357555; ENSP00000350166; ENSG00000066468. [P21802-21]
ENST00000358487; ENSP00000351276; ENSG00000066468. [P21802-1]
ENST00000359354; ENSP00000352309; ENSG00000066468. [P21802-14]
ENST00000360144; ENSP00000353262; ENSG00000066468. [P21802-22]
ENST00000369056; ENSP00000358052; ENSG00000066468. [P21802-17]
ENST00000369058; ENSP00000358054; ENSG00000066468. [P21802-13]
ENST00000369060; ENSP00000358056; ENSG00000066468. [P21802-15]
ENST00000369061; ENSP00000358057; ENSG00000066468. [P21802-23]
ENST00000457416; ENSP00000410294; ENSG00000066468. [P21802-3]
GeneID2263.
KEGGhsa:2263.
UCSCuc001lfg.4. human. [P21802-20]
uc001lfn.5. human. [P21802-1]
uc010qtl.2. human. [P21802-15]
uc021pzv.1. human. [P21802-23]
uc021pzx.1. human. [P21802-21]
uc021pzy.1. human. [P21802-3]
uc021qaa.1. human. [P21802-17]
uc021qab.1. human. [P21802-22]
uc021qac.1. human. [P21802-4]

Organism-specific databases

CTD2263.
GeneCardsGC10M123223.
GeneReviewsFGFR2.
HGNCHGNC:3689. FGFR2.
HPACAB010886.
HPA035305.
HPA056562.
MIM101200. phenotype.
101600. phenotype.
123150. phenotype.
123500. phenotype.
123790. phenotype.
149730. phenotype.
176943. gene.
207410. phenotype.
609579. phenotype.
614592. phenotype.
neXtProtNX_P21802.
Orphanet83. Antley-Bixler syndrome.
87. Apert syndrome.
207. Crouzon disease.
1555. Cutis gyrata - acanthosis nigricans - craniosynostosis.
168624. Familial scaphocephaly syndrome, McGillivray type.
313855. FGFR2-related bent bone dysplasia.
1540. Jackson-Weiss syndrome.
2363. Lacrimo-auriculo-dento-digital syndrome.
93258. Pfeiffer syndrome type 1.
93259. Pfeiffer syndrome type 2.
93260. Pfeiffer syndrome type 3.
794. Saethre-Chotzen syndrome.
PharmGKBPA28128.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000263410.
HOVERGENHBG000345.
KOK05093.
OMALELRCQL.
OrthoDBEOG7NGQ9N.
PhylomeDBP21802.
TreeFamTF316307.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP21802.

Gene expression databases

ArrayExpressP21802.
BgeeP21802.
GenevestigatorP21802.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028175. FGF_rcpt_2.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF130. PTHR24416:SF130. 1 hit.
PfamPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 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

EvolutionaryTraceP21802.
GeneWikiFibroblast_growth_factor_receptor_2.
GenomeRNAi2263.
NextBio9189.
PROP21802.
SOURCESearch...

Entry information

Entry nameFGFR2_HUMAN
AccessionPrimary (citable) accession number: P21802
Secondary accession number(s): B4DFC2 expand/collapse secondary AC list , E7EVR6, E9PCR0, P18443, Q01742, Q12922, Q14300, Q14301, Q14302, Q14303, Q14304, Q14305, Q14672, Q14718, Q14719, Q1KHY5, Q86YI4, Q8IXC7, Q96KL9, Q96KM0, Q96KM1, Q96KM2, Q9NZU2, Q9NZU3, Q9UD01, Q9UD02, Q9UIH3, Q9UIH4, Q9UIH5, Q9UIH6, Q9UIH7, Q9UIH8, Q9UM87, Q9UMC6, Q9UNS7, Q9UQH7, Q9UQH8, Q9UQH9, Q9UQI0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 195 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 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human cell differentiation molecules

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