P21802 (FGFR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	821 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, 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 process	Apoptosis
Cellular component	Cell membrane Cytoplasmic vesicle Golgi apparatus Membrane Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Craniosynostosis Disease mutation Ectodermal dysplasia Lacrimo-auriculo-dento-digital syndrome Mental retardation Proto-oncogene
Domain	Immunoglobulin domain Repeat Signal Transmembrane Transmembrane helix
Ligand	ATP-binding Heparin-binding Nucleotide-binding
Molecular function	Kinase Receptor Transferase Tyrosine-protein kinase
PTM	Disulfide bond Glycoprotein Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	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 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 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: Compara 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 pattern specification Inferred from sequence or structural similarity. Source: UniProtKB endodermal digestive tract morphogenesis Inferred from electronic annotation. Source: Compara epithelial cell proliferation involved in salivary gland morphogenesis Inferred from sequence or structural similarity. 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 hair follicle 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: Compara limb bud formation Inferred from sequence or structural similarity. Source: UniProtKB lung alveolus 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 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 midbrain development Inferred from sequence or structural similarity. Source: UniProtKB multicellular organism growth Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of cell proliferation Inferred from electronic annotation. Source: Compara negative regulation of mitosis Inferred from electronic annotation. Source: Compara 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: Compara odontogenesis Inferred from sequence or structural similarity. Source: UniProtKB organ growth 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 positive regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB positive regulation of canonical Wnt receptor 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 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 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 protein autophosphorylation Inferred from direct assay Ref.29. Source: UniProtKB pyramidal neuron development 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 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 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: Compara 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_component	Golgi 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 12493773PubMed 16597614. 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 to plasma membrane Inferred from direct assay Ref.29Ref.31. Source: UniProtKB nucleus Inferred from direct assay PubMed 16597614PubMed 17471512. Source: UniProtKB
Molecular_function	ATP 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
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
itself		2	EBI-1028658,EBI-1028658
FGF1	P03968	2	EBI-1028658,EBI-6358090	From a different organism.
FGF1	P05230	2	EBI-1028658,EBI-698068
FGF2	P09038	3	EBI-1028658,EBI-977447
FGF7	P21781	2	EBI-6354683,EBI-3937699
GRB2	P62993	5	EBI-1028658,EBI-401755

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Potential

Chain

22 – 821

800

Fibroblast growth factor receptor 2

PRO_0000016783

Regions

Topological domain

22 – 377

356

Extracellular Potential

Transmembrane

378 – 398

21

Helical; Potential

Topological domain

399 – 821

423

Cytoplasmic Potential

Domain

25 – 125

101

Ig-like C2-type 1

Domain

154 – 247

94

Ig-like C2-type 2

Domain

256 – 358

103

Ig-like C2-type 3

Domain

481 – 770

290

Protein kinase

Nucleotide binding

487 – 495

9

ATP

Nucleotide binding

565 – 567

3

ATP

Region

161 – 178

18

Heparin-binding

Sites

Active site

626

1

Proton acceptor Ref.50

Binding site

517

1

ATP

Binding site

571

1

ATP

Amino acid modifications

Modified residue

466

1

Phosphotyrosine; by autocatalysis Ref.35 Ref.50

Modified residue

586

1

Phosphotyrosine; by autocatalysis Ref.35 Ref.48 Ref.50

Modified residue

588

1

Phosphotyrosine; by autocatalysis Ref.35 Ref.50

Modified residue

656

1

Phosphotyrosine; by autocatalysis Ref.35 Ref.48 Ref.50

Modified residue

657

1

Phosphotyrosine; by autocatalysis Ref.35 Ref.48 Ref.50

Modified residue

769

1

Phosphotyrosine; by autocatalysis Ref.29 Ref.50

Glycosylation

83

1

N-linked (GlcNAc...) Potential

Glycosylation

123

1

N-linked (GlcNAc...) Potential

Glycosylation

228

1

N-linked (GlcNAc...) Potential

Glycosylation

241

1

N-linked (GlcNAc...) Potential

Glycosylation

265

1

N-linked (GlcNAc...) Potential

Glycosylation

297

1

N-linked (GlcNAc...) Potential

Glycosylation

318

1

N-linked (GlcNAc...) Potential

Glycosylation

331

1

N-linked (GlcNAc...) Potential

Disulfide bond

62 ↔ 107

By similarity

Disulfide bond

179 ↔ 231

Ref.47

Disulfide bond

278 ↔ 342

Ref.47

Natural variations

Alternative sequence

37 – 152

116

EPPTK…SNNKR → G in isoform 20.

VSP_019608

Alternative sequence

37 – 125

89

Missing in isoform 4, isoform 21 and isoform 22.

VSP_002964

Alternative sequence

250 – 361

112

Missing in isoform 23.

VSP_041914

Alternative sequence

250 – 254

5

ERSPH → GSQGL in isoform 14.

VSP_002965

Alternative sequence

255 – 821

567

Missing in isoform 14.

VSP_002966

Alternative sequence

313

1

K → KVTK in isoform 16.

VSP_002967

Alternative sequence

314 – 429

116

Missing in isoform 15.

VSP_002968

Alternative sequence

314 – 330

17

AAGVN…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 sequence

334 – 335

2

FE → 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 sequence

341 – 353

13

TCLAG…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 sequence

361

1

P → 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 sequence

362 – 365

4

APGR → GRRC in isoform 19.

VSP_002973

Alternative sequence

366 – 821

456

Missing in isoform 19.

VSP_002974

Alternative sequence

428 – 429

2

Missing in isoform 4, isoform 5, isoform 6, isoform 8, isoform 16 and isoform 18.

VSP_002975

Alternative sequence

429 – 430

2

Missing in isoform 20.

VSP_019609

Alternative sequence

761 – 821

61

LTLTT…GSVKT → PPNPSLMSIFRK in isoform 4.

VSP_002976

Alternative sequence

768 – 821

54

EYLDL…GSVKT → SFQSSLKSSSTGIPGWPPGS EVFSEVAFRGILNYDIERPI LCAGSKKIYDI in isoform 10.

VSP_002981

Alternative sequence

768 – 821

54

EYLDL…GSVKT → GRLPAWASQEKENSQTSLFA ISHVTLSSISKTRSSAKRDE KPGSSPHLALVRSQGLPQSV VP in isoform 11.

VSP_002982

Alternative sequence

768 – 821

54

EYLDL…GSVKT → PLS in isoform 12.

VSP_002983

Alternative sequence

768 – 821

54

Missing in isoform 13.

VSP_002977

Alternative sequence

768 – 821

54

EYLDL…GSVKT → I in isoform 2, isoform 8, isoform 17 and isoform 22.

VSP_002978

Alternative sequence

768 – 821

54

EYLDL…GSVKT → RYKLLPCPDKHNKRCKPEER GDLTEAGAAGSSRCVDSRKR VRQEKISTG in isoform 7.

VSP_002979

Alternative sequence

768 – 821

54

EYLDL…GSVKT → RILTLTTNENFQSTSGREGT EIHALQCLRSEVTPAISCES PLADTGSKVPN in isoform 9.

VSP_002980

Alternative sequence

769 – 821

53

YLDLS…GSVKT → EKKVSGAVDCHKPPCNPSHL PCVLAVDQ in isoform 21.

VSP_041915

Alternative sequence

778 – 821

44

QYSPS…GSVKT → PYSPCYPDPR in isoform 6.

VSP_002984

Natural variant

6

1

R → P. Ref.15
Corresponds to variant rs3750819 [ dbSNP | Ensembl ].

VAR_017258

Natural variant

57

1

S → L. Ref.84
Corresponds to variant rs56226109 [ dbSNP | Ensembl ].

VAR_042204

Natural variant

105

1

Y → C in CS. Ref.60 Ref.79

VAR_004112

Natural variant

172

1

A → F in PS; requires 2 nucleotide substitutions. Ref.79

VAR_017259

Natural variant

186

1

M → T. Ref.15 Ref.79 Ref.84
Corresponds to variant rs755793 [ dbSNP | Ensembl ].

VAR_017260

Natural variant

203

1

R → C in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.83 Ref.84

VAR_036380

Natural variant

252 – 253

2

SP → FS in PS.

VAR_004116

Natural variant

252

1

S → F in APRS; requires 2 nucleotide substitutions. Ref.65

VAR_004114

Natural variant

252

1

S → L in CS. Ref.65

VAR_004113

Natural variant

252

1

S → 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 variant

253

1

P → R in APRS; common mutation. Ref.21 Ref.45 Ref.57 Ref.67 Ref.69 Ref.79

VAR_004117

Natural variant

263

1

P → L in CS. Ref.75

VAR_017261

Natural variant

267

1

S → P in CS. Ref.79

VAR_004118

Natural variant

268

1

T → TG in CS. Ref.59

VAR_004119

Natural variant

272

1

G → V in an ovarian serous carcinoma sample; somatic mutation. Ref.84

VAR_042205

Natural variant

273

1

Missing in PS; type 2. Ref.74

VAR_017262

Natural variant

276

1

F → V in CS. Ref.68 Ref.75 Ref.79

VAR_004120

Natural variant

278

1

C → 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 variant

278

1

C → Y in CS. Ref.75

VAR_017263

Natural variant

281

1

Y → C in CS. Ref.78 Ref.79

VAR_017264

Natural variant

283

1

D → N in a lung squamous cell carcinoma sample; somatic mutation. Ref.84

VAR_042206

Natural variant

287 – 289

3

Missing in CS.

VAR_004122

Natural variant

288

1

I → S in CS. Ref.75

VAR_017265

Natural variant

289

1

Q → P in CS and JWS. Ref.24 Ref.59 Ref.75 Ref.78 Ref.79

VAR_004123

Natural variant

290

1

W → C in PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation. Ref.63 Ref.79 Ref.84

VAR_004124

Natural variant

290

1

W → G in CS. Ref.55

VAR_017266

Natural variant

290

1

W → R in CS.

VAR_004125

Natural variant

292

1

K → E in CS. Ref.66

VAR_004126

Natural variant

301

1

Y → C in CS. Ref.68

VAR_004127

Natural variant

314

1

A → S in craniosynostosis. Ref.68

VAR_004128

Natural variant

315

1

A → S in a non-syndromic craniosynostosis patient with abnormal intrauterine history; confers predisposition to craniosynostosis. Ref.76 Ref.79

VAR_017267

Natural variant

321

1

D → A in PS. Ref.56

VAR_004129

Natural variant

328

1

Y → C in CS. Ref.53

VAR_004130

Natural variant

331

1

N → I in CS. Ref.61

VAR_004131

Natural variant

337

1

A → ANA in CS.

VAR_004132

Natural variant

337

1

A → P in CS. Ref.67

VAR_017268

Natural variant

338

1

G → E in CS. Ref.60

VAR_004133

Natural variant

338

1

G → R in CS. Ref.24 Ref.67 Ref.79

VAR_015011

Natural variant

340

1

Y → C in PS. Ref.73 Ref.79

VAR_017269

Natural variant

340

1

Y → H in CS. Ref.52 Ref.79

VAR_004134

Natural variant

341

1

T → P in PS and CS. Ref.58 Ref.75 Ref.79

VAR_004135

Natural variant

342

1

C → F in CS. Ref.59 Ref.67 Ref.79

VAR_004136

Natural variant

342

1

C → G in PS. Ref.73

VAR_017270

Natural variant

342

1

C → 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 variant

342

1

C → 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 variant

342

1

C → W in CS. Ref.55 Ref.75 Ref.79

VAR_017271

Natural variant

342

1

C → Y in CS and PS. Ref.24 Ref.52 Ref.58 Ref.59 Ref.67 Ref.75 Ref.78 Ref.79

VAR_004139

Natural variant

344

1

A → G in CS and JWS. Ref.24 Ref.53

VAR_004140

Natural variant

344

1

A → P in CS and PS. Ref.59

VAR_004141

Natural variant

347

1

S → C in CS. Ref.53 Ref.79

VAR_004142

Natural variant

351

1

S → C in CS, PS and ABS2. Ref.60 Ref.70 Ref.77

VAR_004143

Natural variant

354

1

S → C in CS. Ref.24 Ref.52 Ref.55 Ref.75 Ref.79

VAR_004144

Natural variant

354

1

S → Y in CS. Ref.75

VAR_017272

Natural variant

356 – 358

3

Missing in CS.

VAR_004145

Natural variant

359

1

V → F in CS and PS. Ref.59 Ref.75

VAR_004146

Natural variant

362

1

A → S in CS. Ref.72

VAR_017273

Natural variant

372

1

S → C in BSTVS. Ref.62

VAR_017274

Natural variant

375

1

Y → C in PS and BSTVS. Ref.62 Ref.79 Ref.80

VAR_017275

Natural variant

381

1

Y → D in BBDS. Ref.85

VAR_067977

Natural variant

384

1

G → R in CS. Ref.60

VAR_004147

Natural variant

391

1

M → 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 variant

526

1

K → E in FSPC; constitutive kinase activity. Ref.48 Ref.81

VAR_023788

Natural variant

549

1

N → H in CS; constitutive kinase activity. Ref.48 Ref.79

VAR_017276

Natural variant

565

1

E → G in PS; constitutive kinase activity. Ref.48 Ref.79

VAR_017277

Natural variant

612

1

R → T in a lung adenocarcinoma sample; somatic mutation. Ref.84

VAR_046071

Natural variant

613

1

G → R. Ref.7 Ref.11

VAR_015012

Natural variant

628

1

A → T in LADDS; strongly reduced kinase activity. Ref.49 Ref.82

VAR_029884

Natural variant

641

1

K → R in PS; constitutive kinase activity. Ref.48 Ref.79

VAR_017278

Natural variant

648

1

A → T in LADDS. Ref.82

VAR_029885

Natural variant

649 – 650

2

RD → S in LADDS.

VAR_029886

Natural variant

659

1

K → N in craniosynostosis; constitutive kinase activity. Ref.48 Ref.79

VAR_017279

Natural variant

663

1

G → E in PS. Ref.79

VAR_017280

Natural variant

678

1

R → G in CS. Ref.79

VAR_017281

Experimental info

Mutagenesis

265

1

N → Q: Reduced N-glycosylation. Reduced expression at the cell surface. Ref.31

Mutagenesis

549

1

N → T: Constitutive kinase activity. Ref.48

Mutagenesis

565

1

E → A: Constitutive kinase activity. Ref.48

Mutagenesis

656 – 657

2

Missing: Loss of kinase activity.

Mutagenesis

769

1

Y → F: Increases fibroblast proliferation. Decreases phosphorylation of PLCG1 and FRS2. Decreases activation of MAP kinases. Ref.29 Ref.36

Sequence conflict

246

1

L → P in BAG57383. Ref.16

Sequence conflict

310

1

K → N in BAG57383. Ref.16

Isoform 16:

Sequence conflict

315

1

T → L in AAA61188. Ref.2

Secondary structure

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821

Helix Strand Turn

Details...

Beta strand

152 – 157

6

Turn

159 – 162

4

Beta strand

166 – 170

5

Beta strand

175 – 178

4

Beta strand

181 – 185

5

Beta strand

188 – 193

6

Helix

200 – 202

3

Beta strand

208 – 210

3

Helix

211 – 213

3

Beta strand

215 – 218

4

Helix

223 – 225

3

Beta strand

227 – 235

9

Beta strand

238 – 249

12

Beta strand

266 – 269

4

Beta strand

274 – 277

4

Beta strand

287 – 293

7

Beta strand

296 – 298

3

Beta strand

299 – 301

3

Beta strand

309 – 313

5

Beta strand

315 – 319

5

Turn

321 – 325

5

Beta strand

326 – 329

4

Helix

334 – 336

3

Beta strand

338 – 346

9

Beta strand

349 – 360

12

Helix

472 – 474

3

Helix

478 – 480

3

Beta strand

481 – 489

9

Beta strand

494 – 501

8

Beta strand

504 – 506

3

Beta strand

511 – 518

8

Helix

525 – 541

17

Beta strand

550 – 554

5

Beta strand

556 – 558

3

Beta strand

561 – 565

5

Beta strand

568 – 571

4

Helix

572 – 577

6

Helix

594 – 596

3

Helix

600 – 619

20

Helix

629 – 631

3

Beta strand

632 – 634

3

Turn

636 – 638

3

Beta strand

640 – 642

3

Turn

652 – 654

3

Turn

657 – 659

3

Beta strand

664 – 666

3

Helix

667 – 669

3

Helix

672 – 676

5

Helix

682 – 697

16

Helix

709 – 717

9

Beta strand

726 – 728

3

Helix

730 – 739

10

Helix

744 – 746

3

Helix

750 – 764

15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (BEK) (FGFR2IIIc) [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 6CD5001C960ED82F	FASTA	821	92,025
	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
	Isoform 2 (Short) [UniParc]. Checksum: 8D4734CBEA8E8C8F	FASTA	768	86,130
	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 RMDKPANCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEI
	Isoform 3 (BFR-1) (FGFR2IIIb) (KGFR) [UniParc]. Checksum: 288CF737673BA4AB	FASTA	822	92,118
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 780 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNEEY LDLSQPLEQY 790 800 810 820 SPSYPDTRSS CSSGDDSVFS PDPMPYEPCL PQYPHINGSV KT
	Isoform 4 (K-sam) [UniParc]. Checksum: D56050B4385A6635	FASTA	682	76,705
	10 20 30 40 50 60 MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEDAIS SGDDEDDTDG AEDFVSENSN 70 80 90 100 110 120 NKRAPYWTNT EKMEKRLHAV PAANTVKFRC PAGGNPMPTM RWLKNGKEFK QEHRIGGYKV 130 140 150 160 170 180 RNQHWSLIME SVVPSDKGNY TCVVENEYGS INHTYHLDVV ERSPHRPILQ AGLPANASTV 190 200 210 220 230 240 VGGDVEFVCK VYSDAQPHIQ WIKHVEKNGS KYGPDGLPYL KVLKHSGINS SNAEVLALFN 250 260 270 280 290 300 VTEADAGEYI CKVSNYIGQA NQSAWLTVLP KQQAPGREKE ITASPDYLEI AIYCIGVFLI 310 320 330 340 350 360 ACMVVTVILC RMKNTTKKPD FSSQPAVHKL TKRIPLRRQV SAESSSSMNS NTPLVRITTR 370 380 390 400 410 420 LSSTADTPML AGVSEYELPE DPKWEFPRDK LTLGKPLGEG CFGQVVMAEA VGIDKDKPKE 430 440 450 460 470 480 AVTVAVKMLK DDATEKDLSD LVSEMEMMKM IGKHKNIINL LGACTQDGPL YVIVEYASKG 490 500 510 520 530 540 NLREYLRARR PPGMEYSYDI NRVPEEQMTF KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR 550 560 570 580 590 600 NVLVTENNVM KIADFGLARD INNIDYYKKT TNGRLPVKWM APEALFDRVY THQSDVWSFG 610 620 630 640 650 660 VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH RMDKPANCTN ELYMMMRDCW HAVPSQRPTF 670 680 KQLVEDLDRI PPNPSLMSIF RK
	Isoform 5 (K-sam-I) (BEK) (IgIIIc) [UniParc]. Checksum: 4746938783A1D94F	FASTA	819	91,825
	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 RIPLRRQVSA ESSSSMNSNT PLVRITTRLS STADTPMLAG VSEYELPEDP KWEFPRDKLT 490 500 510 520 530 540 LGKPLGEGCF GQVVMAEAVG IDKDKPKEAV TVAVKMLKDD ATEKDLSDLV SEMEMMKMIG 550 560 570 580 590 600 KHKNIINLLG ACTQDGPLYV IVEYASKGNL REYLRARRPP GMEYSYDINR VPEEQMTFKD 610 620 630 640 650 660 LVSCTYQLAR GMEYLASQKC IHRDLAARNV LVTENNVMKI ADFGLARDIN NIDYYKKTTN 670 680 690 700 710 720 GRLPVKWMAP EALFDRVYTH QSDVWSFGVL MWEIFTLGGS PYPGIPVEEL FKLLKEGHRM 730 740 750 760 770 780 DKPANCTNEL YMMMRDCWHA VPSQRPTFKQ LVEDLDRILT LTTNEEYLDL SQPLEQYSPS 790 800 810 YPDTRSSCSS GDDSVFSPDP MPYEPCLPQY PHINGSVKT
	Isoform 6 (K-sam-IIC2) [UniParc]. Checksum: 042BF83F92CE97F5	FASTA	785	88,181
	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 RIPLRRQVSA ESSSSMNSNT PLVRITTRLS STADTPMLAG VSEYELPEDP KWEFPRDKLT 490 500 510 520 530 540 LGKPLGEGCF GQVVMAEAVG IDKDKPKEAV TVAVKMLKDD ATEKDLSDLV SEMEMMKMIG 550 560 570 580 590 600 KHKNIINLLG ACTQDGPLYV IVEYASKGNL REYLRARRPP GMEYSYDINR VPEEQMTFKD 610 620 630 640 650 660 LVSCTYQLAR GMEYLASQKC IHRDLAARNV LVTENNVMKI ADFGLARDIN NIDYYKKTTN 670 680 690 700 710 720 GRLPVKWMAP EALFDRVYTH QSDVWSFGVL MWEIFTLGGS PYPGIPVEEL FKLLKEGHRM 730 740 750 760 770 780 DKPANCTNEL YMMMRDCWHA VPSQRPTFKQ LVEDLDRILT LTTNEEYLDL SQPLEPYSPC YPDPR
	Isoform 7 (K-sam-IIO2) [UniParc]. Checksum: 46BA78E51DB700CD	FASTA	817	91,620
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 780 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNERY KLLPCPDKHN 790 800 810 KRCKPEERGD LTEAGAAGSS RCVDSRKRVR QEKISTG
	Isoform 8 (K-sam-IIC3) [UniParc]. Checksum: FE97A413B085D31E	FASTA	766	85,929
	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 RIPLRRQVSA ESSSSMNSNT PLVRITTRLS STADTPMLAG VSEYELPEDP KWEFPRDKLT 490 500 510 520 530 540 LGKPLGEGCF GQVVMAEAVG IDKDKPKEAV TVAVKMLKDD ATEKDLSDLV SEMEMMKMIG 550 560 570 580 590 600 KHKNIINLLG ACTQDGPLYV IVEYASKGNL REYLRARRPP GMEYSYDINR VPEEQMTFKD 610 620 630 640 650 660 LVSCTYQLAR GMEYLASQKC IHRDLAARNV LVTENNVMKI ADFGLARDIN NIDYYKKTTN 670 680 690 700 710 720 GRLPVKWMAP EALFDRVYTH QSDVWSFGVL MWEIFTLGGS PYPGIPVEEL FKLLKEGHRM 730 740 750 760 DKPANCTNEL YMMMRDCWHA VPSQRPTFKQ LVEDLDRILT LTTNEI
	Isoform 9 (K-sam-IIH1) [UniParc]. Checksum: C60FE09EC1BE0654	FASTA	819	91,566
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 780 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNERI LTLTTNENFQ 790 800 810 STSGREGTEI HALQCLRSEV TPAISCESPL ADTGSKVPN
	Isoform 10 (K-sam-IIH2) [UniParc]. Checksum: 467E9BAAD07C5463	FASTA	819	91,641
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 780 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNESF QSSLKSSSTG 790 800 810 IPGWPPGSEV FSEVAFRGIL NYDIERPILC AGSKKIYDI
	Isoform 11 (K-sam-IIH3) (K-sam-IIO4) [UniParc]. Checksum: E726FA4235995586	FASTA	830	92,733
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 780 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNEGR LPAWASQEKE 790 800 810 820 830 NSQTSLFAIS HVTLSSISKT RSSAKRDEKP GSSPHLALVR SQGLPQSVVP
	Isoform 12 (K-sam-IIO1) [UniParc]. Checksum: 881C475B4771CA5C	FASTA	771	86,407
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNEPL S
	Isoform 13 (K-sam-IIO3) [UniParc]. Checksum: BB4771CA5CBEEFAA	FASTA	768	86,110
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNE
	Isoform 14 (K-sam-IV) (Soluble KGFR) [UniParc]. Checksum: 1855113266C85F4F	FASTA	254	28,299
	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 NHTYHLDVVG SQGL
	Isoform 15 (K-sam-III) [UniParc]. Checksum: 590967DCBF5DA25D	FASTA	705	79,212
	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 VLKVSAESSS SMNSNTPLVR ITTRLSSTAD TPMLAGVSEY ELPEDPKWEF 370 380 390 400 410 420 PRDKLTLGKP LGEGCFGQVV MAEAVGIDKD KPKEAVTVAV KMLKDDATEK DLSDLVSEME 430 440 450 460 470 480 MMKMIGKHKN IINLLGACTQ DGPLYVIVEY ASKGNLREYL RARRPPGMEY SYDINRVPEE 490 500 510 520 530 540 QMTFKDLVSC TYQLARGMEY LASQKCIHRD LAARNVLVTE NNVMKIADFG LARDINNIDY 550 560 570 580 590 600 YKKTTNGRLP VKWMAPEALF DRVYTHQSDV WSFGVLMWEI FTLGGSPYPG IPVEELFKLL 610 620 630 640 650 660 KEGHRMDKPA NCTNELYMMM RDCWHAVPSQ RPTFKQLVED LDRILTLTTN EEYLDLSQPL 670 680 690 700 EQYSPSYPDT RSSCSSGDDS VFSPDPMPYE PCLPQYPHIN GSVKT
	Isoform 16 (TK14) [UniParc]. Checksum: 15D08A6D66AC4EA0	FASTA	822	92,153
	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 VLKVTKAAGV NTTDKEIEVL YIRNVTFEDA GEYTCLAGNS IGISFHSAWL 370 380 390 400 410 420 TVLPAPGREK EITASPDYLE IAIYCIGVFL IACMVVTVIL CRMKNTTKKP DFSSQPAVHK 430 440 450 460 470 480 LTKRIPLRRQ VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 770 780 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNEEY LDLSQPLEQY 790 800 810 820 SPSYPDTRSS CSSGDDSVFS PDPMPYEPCL PQYPHINGSV KT
	Isoform 17 [UniParc]. Checksum: 806B4771CA5CBEEF	FASTA	769	86,223
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVT VSAESSSSMN SNTPLVRITT RLSSTADTPM LAGVSEYELP EDPKWEFPRD 490 500 510 520 530 540 KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK EAVTVAVKML KDDATEKDLS DLVSEMEMMK 550 560 570 580 590 600 MIGKHKNIIN LLGACTQDGP LYVIVEYASK GNLREYLRAR RPPGMEYSYD INRVPEEQMT 610 620 630 640 650 660 FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA RNVLVTENNV MKIADFGLAR DINNIDYYKK 670 680 690 700 710 720 TTNGRLPVKW MAPEALFDRV YTHQSDVWSF GVLMWEIFTL GGSPYPGIPV EELFKLLKEG 730 740 750 760 HRMDKPANCT NELYMMMRDC WHAVPSQRPT FKQLVEDLDR ILTLTTNEI
	Isoform 18 (K-sam-IIC1) (KGFR) (IgIIIb) [UniParc]. Checksum: 806D62B2FF25AFF6	FASTA	820	91,918
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK 370 380 390 400 410 420 QQAPGREKEI TASPDYLEIA IYCIGVFLIA CMVVTVILCR MKNTTKKPDF SSQPAVHKLT 430 440 450 460 470 480 KRIPLRRQVS AESSSSMNSN TPLVRITTRL SSTADTPMLA GVSEYELPED PKWEFPRDKL 490 500 510 520 530 540 TLGKPLGEGC FGQVVMAEAV GIDKDKPKEA VTVAVKMLKD DATEKDLSDL VSEMEMMKMI 550 560 570 580 590 600 GKHKNIINLL GACTQDGPLY VIVEYASKGN LREYLRARRP PGMEYSYDIN RVPEEQMTFK 610 620 630 640 650 660 DLVSCTYQLA RGMEYLASQK CIHRDLAARN VLVTENNVMK IADFGLARDI NNIDYYKKTT 670 680 690 700 710 720 NGRLPVKWMA PEALFDRVYT HQSDVWSFGV LMWEIFTLGG SPYPGIPVEE LFKLLKEGHR 730 740 750 760 770 780 MDKPANCTNE LYMMMRDCWH AVPSQRPTFK QLVEDLDRIL TLTTNEEYLD LSQPLEQYSP 790 800 810 820 SYPDTRSSCS SGDDSVFSPD PMPYEPCLPQ YPHINGSVKT
	Isoform 19 (Soluble KGFR) [UniParc]. Checksum: C02708836203465F	FASTA	366	40,614
	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 VLKHSGINSS NAEVLALFNV TEADAGEYIC KVSNYIGQAN QSAWLTVLPK QQGRRC
	Isoform 20 [UniParc]. Checksum: 287F39DCF95B9312	FASTA	704	79,197
	10 20 30 40 50 60 MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEGAPY WTNTEKMEKR LHAVPAANTV 70 80 90 100 110 120 KFRCPAGGNP MPTMRWLKNG KEFKQEHRIG GYKVRNQHWS LIMESVVPSD KGNYTCVVEN 130 140 150 160 170 180 EYGSINHTYH LDVVERSPHR PILQAGLPAN ASTVVGGDVE FVCKVYSDAQ PHIQWIKHVE 190 200 210 220 230 240 KNGSKYGPDG LPYLKVLKAA GVNTTDKEIE VLYIRNVTFE DAGEYTCLAG NSIGISFHSA 250 260 270 280 290 300 WLTVLPAPGR EKEITASPDY LEIAIYCIGV FLIACMVVTV ILCRMKNTTK KPDFSSQPAV 310 320 330 340 350 360 HKLTKRIPLR RQVSAESSSS MNSNTPLVRI TTRLSSTADT PMLAGVSEYE LPEDPKWEFP 370 380 390 400 410 420 RDKLTLGKPL GEGCFGQVVM AEAVGIDKDK PKEAVTVAVK MLKDDATEKD LSDLVSEMEM 430 440 450 460 470 480 MKMIGKHKNI INLLGACTQD GPLYVIVEYA SKGNLREYLR ARRPPGMEYS YDINRVPEEQ 490 500 510 520 530 540 MTFKDLVSCT YQLARGMEYL ASQKCIHRDL AARNVLVTEN NVMKIADFGL ARDINNIDYY 550 560 570 580 590 600 KKTTNGRLPV KWMAPEALFD RVYTHQSDVW SFGVLMWEIF TLGGSPYPGI PVEELFKLLK 610 620 630 640 650 660 EGHRMDKPAN CTNELYMMMR DCWHAVPSQR PTFKQLVEDL DRILTLTTNE EYLDLSQPLE 670 680 690 700 QYSPSYPDTR SSCSSGDDSV FSPDPMPYEP CLPQYPHING SVKT
	Isoform 21 [UniParc]. Checksum: 01DF22CD5B50092A	FASTA	707	79,300
	10 20 30 40 50 60 MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEDAIS SGDDEDDTDG AEDFVSENSN 70 80 90 100 110 120 NKRAPYWTNT EKMEKRLHAV PAANTVKFRC PAGGNPMPTM RWLKNGKEFK QEHRIGGYKV 130 140 150 160 170 180 RNQHWSLIME SVVPSDKGNY TCVVENEYGS INHTYHLDVV ERSPHRPILQ AGLPANASTV 190 200 210 220 230 240 VGGDVEFVCK VYSDAQPHIQ WIKHVEKNGS KYGPDGLPYL KVLKAAGVNT TDKEIEVLYI 250 260 270 280 290 300 RNVTFEDAGE YTCLAGNSIG ISFHSAWLTV LPAPGREKEI TASPDYLEIA IYCIGVFLIA 310 320 330 340 350 360 CMVVTVILCR MKNTTKKPDF SSQPAVHKLT KRIPLRRQVT VSAESSSSMN SNTPLVRITT 370 380 390 400 410 420 RLSSTADTPM LAGVSEYELP EDPKWEFPRD KLTLGKPLGE GCFGQVVMAE AVGIDKDKPK 430 440 450 460 470 480 EAVTVAVKML KDDATEKDLS DLVSEMEMMK MIGKHKNIIN LLGACTQDGP LYVIVEYASK 490 500 510 520 530 540 GNLREYLRAR RPPGMEYSYD INRVPEEQMT FKDLVSCTYQ LARGMEYLAS QKCIHRDLAA 550 560 570 580 590 600 RNVLVTENNV MKIADFGLAR DINNIDYYKK TTNGRLPVKW MAPEALFDRV YTHQSDVWSF 610 620 630 640 650 660 GVLMWEIFTL GGSPYPGIPV EELFKLLKEG HRMDKPANCT NELYMMMRDC WHAVPSQRPT 670 680 690 700 FKQLVEDLDR ILTLTTNEEE KKVSGAVDCH KPPCNPSHLP CVLAVDQ
	Isoform 22 [UniParc]. Checksum: A6FF9BEBABCCE931	FASTA	680	76,423
	10 20 30 40 50 60 MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEDAIS SGDDEDDTDG AEDFVSENSN 70 80 90 100 110 120 NKRAPYWTNT EKMEKRLHAV PAANTVKFRC PAGGNPMPTM RWLKNGKEFK QEHRIGGYKV 130 140 150 160 170 180 RNQHWSLIME SVVPSDKGNY TCVVENEYGS INHTYHLDVV ERSPHRPILQ AGLPANASTV 190 200 210 220 230 240 VGGDVEFVCK VYSDAQPHIQ WIKHVEKNGS KYGPDGLPYL KVLKHSGINS SNAEVLALFN 250 260 270 280 290 300 VTEADAGEYI CKVSNYIGQA NQSAWLTVLP KQQAPGREKE ITASPDYLEI AIYCIGVFLI 310 320 330 340 350 360 ACMVVTVILC RMKNTTKKPD FSSQPAVHKL TKRIPLRRQV TVSAESSSSM NSNTPLVRIT 370 380 390 400 410 420 TRLSSTADTP MLAGVSEYEL PEDPKWEFPR DKLTLGKPLG EGCFGQVVMA EAVGIDKDKP 430 440 450 460 470 480 KEAVTVAVKM LKDDATEKDL SDLVSEMEMM KMIGKHKNII NLLGACTQDG PLYVIVEYAS 490 500 510 520 530 540 KGNLREYLRA RRPPGMEYSY DINRVPEEQM TFKDLVSCTY QLARGMEYLA SQKCIHRDLA 550 560 570 580 590 600 ARNVLVTENN VMKIADFGLA RDINNIDYYK KTTNGRLPVK WMAPEALFDR VYTHQSDVWS 610 620 630 640 650 660 FGVLMWEIFT LGGSPYPGIP VEELFKLLKE GHRMDKPANC TNELYMMMRD CWHAVPSQRP 670 680 TFKQLVEDLD RILTLTTNEI
	Isoform 23 [UniParc]. Checksum: 7F37AAB82F8B7A48	FASTA	709	79,833
	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 NHTYHLDVVA PGREKEITAS PDYLEIAIYC IGVFLIACMV VTVILCRMKN TTKKPDFSSQ 310 320 330 340 350 360 PAVHKLTKRI PLRRQVTVSA ESSSSMNSNT PLVRITTRLS STADTPMLAG VSEYELPEDP 370 380 390 400 410 420 KWEFPRDKLT LGKPLGEGCF GQVVMAEAVG IDKDKPKEAV TVAVKMLKDD ATEKDLSDLV 430 440 450 460 470 480 SEMEMMKMIG KHKNIINLLG ACTQDGPLYV IVEYASKGNL REYLRARRPP GMEYSYDINR 490 500 510 520 530 540 VPEEQMTFKD LVSCTYQLAR GMEYLASQKC IHRDLAARNV LVTENNVMKI ADFGLARDIN 550 560 570 580 590 600 NIDYYKKTTN GRLPVKWMAP EALFDRVYTH QSDVWSFGVL MWEIFTLGGS PYPGIPVEEL 610 620 630 640 650 660 FKLLKEGHRM DKPANCTNEL YMMMRDCWHA VPSQRPTFKQ LVEDLDRILT LTTNEEYLDL 670 680 690 700 SQPLEQYSPS YPDTRSSCSS GDDSVFSPDP MPYEPCLPQY PHINGSVKT

References

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[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. , 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. , 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, 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, 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. , 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. , 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. , 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.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

NIEHS-SNPs

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 , AF097341, AF097342, AF097343, AF097345, AF097346, AF097347, AF097348, AF097349, AF097350, AF097351, AF097352 Genomic DNA. Translation: AAD31560.1.
AF097353 , AF097341, AF097342, AF097344, AF097345, AF097346, AF097347, AF097348, AF097349, AF097350, AF097351, AF097352 Genomic DNA. Translation: AAD31561.1.
AF097340 , 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.

IPI

IPI00216602.
IPI00216603.
IPI00216604.
IPI00216605.
IPI00218416.
IPI00218417.
IPI00218418.
IPI00218419.
IPI00218420.
IPI00218421.
IPI00218422.
IPI00218423.
IPI00218424.
IPI00218425.
IPI00384713.
IPI00386650.
IPI00647907.
IPI00759837.
IPI00873362.
IPI00942110.

PIR

A35969.
TVHUF2. A42691.
A45081.
C42691.
S16236.

RefSeq

NP_000132.3. NM_000141.4.
NP_001138385.1. NM_001144913.1.
NP_001138386.1. NM_001144914.1.
NP_001138387.1. NM_001144915.1.
NP_001138388.1. NM_001144916.1.
NP_001138389.1. NM_001144917.1.
NP_001138390.1. NM_001144918.1.
NP_001138391.1. NM_001144919.1.
NP_075259.4. NM_022970.3.
NP_075418.1. NM_023029.2.

UniGene

Hs.533683.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1DJS	X-ray	2.40	A	153-362	[»]
1E0O	X-ray	2.80	B/D	148-366	[»]
1EV2	X-ray	2.20	E/F/G/H	147-366	[»]
1GJO	X-ray	2.40	A	456-768	[»]
1II4	X-ray	2.70	E/F/G/H	147-366	[»]
1IIL	X-ray	2.30	E/F/G/H	147-366	[»]
1NUN	X-ray	2.90	B	140-361	[»]
1OEC	X-ray	2.40	A	456-768	[»]
1WVZ	NMR	-	A	147-249	[»]
2FDB	X-ray	2.28	P/R	149-368	[»]
2PSQ	X-ray	2.40	A/B	413-768	[»]
2PVF	X-ray	1.80	A	458-778	[»]
			B	764-778	[»]
2PVY	X-ray	2.20	A/B/C/D	458-768	[»]
2PWL	X-ray	2.40	A/B	458-768	[»]
2PY3	X-ray	2.30	A/B	458-768	[»]
2PZ5	X-ray	2.40	A/B	458-768	[»]
2PZP	X-ray	2.40	A/B	458-768	[»]
2PZR	X-ray	3.00	A/B	458-768	[»]
2Q0B	X-ray	2.90	A/B	458-768	[»]
3B2T	X-ray	1.80	A/B	458-766	[»]
3CAF	X-ray	1.96	A	150-249	[»]
3CLY	X-ray	2.00	A	458-778	[»]
3CU1	X-ray	2.60	A/C	150-249	[»]
3DAR	X-ray	2.20	A/B	146-249	[»]
3EUU	X-ray	2.34	A/B	150-249	[»]
3OJ2	X-ray	2.20	C/D	140-361	[»]
3OJM	X-ray	2.10	B	140-361	[»]
3RI1	X-ray	2.10	A/B	458-768	[»]

ProteinModelPortal

P21802.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-3788N.

IntAct

P21802. 8 interactions.

MINT

MINT-118359.

Protein family/group databases

MEROPS

I43.001.

PTM databases

PhosphoSite

P21802.

Polymorphism databases

DMDM

120049.

Proteomic databases

PaxDb

P21802.

PRIDE

P21802.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000346997; ENSP00000263451; ENSG00000066468.
ENST00000351936; ENSP00000309878; ENSG00000066468.
ENST00000356226; ENSP00000348559; ENSG00000066468.
ENST00000357555; ENSP00000350166; ENSG00000066468.
ENST00000358487; ENSP00000351276; ENSG00000066468.
ENST00000359354; ENSP00000352309; ENSG00000066468.
ENST00000360144; ENSP00000353262; ENSG00000066468.
ENST00000369056; ENSP00000358052; ENSG00000066468.
ENST00000369058; ENSP00000358054; ENSG00000066468.
ENST00000369060; ENSP00000358056; ENSG00000066468.
ENST00000369061; ENSP00000358057; ENSG00000066468.
ENST00000457416; ENSP00000410294; ENSG00000066468.

GeneID

2263.

KEGG

hsa:2263.

UCSC

uc001lfg.4. human.
uc010qtl.2. human.
uc021pzw.1. human.
uc021pzy.1. human.
uc021qaa.1. human.

Organism-specific databases

CTD

2263.

GeneCards

GC10M123223.

HGNC

HGNC:3689. FGFR2.

HPA

CAB010886.
HPA035305.

MIM

101200. phenotype.
101600. phenotype.
123150. phenotype.
123500. phenotype.
123790. phenotype.
149730. phenotype.
176943. gene.
207410. phenotype.
609579. phenotype.
614592. phenotype.

neXtProt

NX_P21802.

Orphanet

263476. Antley-Bixler syndrome without genital anomaly or disorder of steroidogenesis.
87. Apert syndrome.
207. Crouzon disease.
1555. Cutis gyrata - acanthosis nigricans - craniosynostosis.
168624. Familial scaphocephaly syndrome, McGillivray type.
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.

PharmGKB

PA28128.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000263410.

HOVERGEN

HBG000345.

KO

K05093.

OMA

YEPCLPK.

OrthoDB

EOG4640BC.

Enzyme and pathway databases

BRENDA

2.7.10.1. 2681.

Pathway_Interaction_DB

fgf_pathway. FGF signaling pathway.

Reactome

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

Gene expression databases

ArrayExpress

P21802.

Bgee

P21802.

Genevestigator

P21802.

GermOnline

ENSG00000066468. Homo sapiens.

Family and domain databases

Gene3D

2.60.40.10. 3 hits.

InterPro

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

Pfam

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

PIRSF

PIRSF000628. FGFR. 1 hit.

PRINTS

PR00109. TYRKINASE.

SMART

SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]

SUPFAM

SSF56112. Kinase_like. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

BindingDB

P21802.

ChEMBL

CHEMBL4142.

DrugBank

DB00039. Palifermin.

EvolutionaryTrace

P21802.

GenomeRNAi

2263.

NextBio

9189.

SOURCE

Search...

Entry information

Entry name

FGFR2_HUMAN

Accession

Primary (citable) accession number: P21802
Secondary accession number(s): B4DFC2 , 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:	May 1, 2013
This is version 181 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

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