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Protein

Fibroblast growth factor receptor 2

Gene

FGFR2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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 STAT1.13 Publications

Catalytic activityi

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.PROSITE-ProRule annotation4 Publications

Enzyme regulationi

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.2 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei517ATPPROSITE-ProRule annotation1 Publication1
Binding sitei571ATPPROSITE-ProRule annotation1 Publication1
Active sitei626Proton acceptorPROSITE-ProRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi487 – 495ATPPROSITE-ProRule annotation1 Publication9
Nucleotide bindingi565 – 567ATPPROSITE-ProRule annotation1 Publication3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHeparin-binding, Kinase, Receptor, Transferase, Tyrosine-protein kinase
Biological processApoptosis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.10.1. 2681.
ReactomeiR-HSA-109704. PI3K Cascade.
R-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-190375. FGFR2c ligand binding and activation.
R-HSA-190377. FGFR2b ligand binding and activation.
R-HSA-2023837. Signaling by FGFR2 amplification mutants.
R-HSA-2033519. Activated point mutants of FGFR2.
R-HSA-2219530. Constitutive Signaling by Aberrant PI3K in Cancer.
R-HSA-5654221. Phospholipase C-mediated cascade, FGFR2.
R-HSA-5654695. PI-3K cascade:FGFR2.
R-HSA-5654699. SHC-mediated cascade:FGFR2.
R-HSA-5654700. FRS-mediated FGFR2 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5655253. Signaling by FGFR2 in disease.
R-HSA-5673001. RAF/MAP kinase cascade.
R-HSA-6811558. PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
R-HSA-8851708. Signaling by FGFR2 IIIa TM.
R-HSA-8853333. Signaling by FGFR2 fusions.
SignaLinkiP21802.
SIGNORiP21802.

Names & Taxonomyi

Protein namesi
Recommended name:
Fibroblast growth factor receptor 2 (EC:2.7.10.14 Publications)
Short name:
FGFR-2
Alternative name(s):
K-sam
Short name:
KGFR
Keratinocyte growth factor receptor
CD_antigen: CD332
Gene namesi
Name:FGFR2
Synonyms:BEK, KGFR, KSAM
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

EuPathDBiHostDB:ENSG00000066468.20.
HGNCiHGNC:3689. FGFR2.
MIMi176943. gene.
neXtProtiNX_P21802.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini22 – 377ExtracellularSequence analysisAdd BLAST356
Transmembranei378 – 398HelicalSequence analysisAdd BLAST21
Topological domaini399 – 821CytoplasmicSequence analysisAdd BLAST423

Keywords - Cellular componenti

Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane, Secreted

Pathology & Biotechi

Involvement in diseasei

Crouzon syndrome (CS)18 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant syndrome characterized by craniosynostosis, hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.
See also OMIM:123500
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004112105Y → C in CS. 2 Publications1
Natural variantiVAR_004113252S → L in CS. 1 PublicationCorresponds to variant dbSNP:rs79184941Ensembl.1
Natural variantiVAR_017261263P → L in CS. 1 PublicationCorresponds to variant dbSNP:rs779326224Ensembl.1
Natural variantiVAR_004118267S → P in CS. 1 PublicationCorresponds to variant dbSNP:rs121918505Ensembl.1
Natural variantiVAR_004119268T → TG in CS. 1 Publication1
Natural variantiVAR_004120276F → V in CS. 3 PublicationsCorresponds to variant dbSNP:rs1057519036Ensembl.1
Natural variantiVAR_004121278C → 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. 5 PublicationsCorresponds to variant dbSNP:rs776587763Ensembl.1
Natural variantiVAR_017263278C → Y in CS. 1 Publication1
Natural variantiVAR_017264281Y → C in CS. 2 PublicationsCorresponds to variant dbSNP:rs1057519038Ensembl.1
Natural variantiVAR_004122287 – 289Missing in CS. 3
Natural variantiVAR_017265288I → S in CS. 1 Publication1
Natural variantiVAR_017266290W → G in CS. 1 PublicationCorresponds to variant dbSNP:rs121918501Ensembl.1
Natural variantiVAR_004125290W → R in CS. Corresponds to variant dbSNP:rs121918501Ensembl.1
Natural variantiVAR_004126292K → E in CS. 1 PublicationCorresponds to variant dbSNP:rs121918500Ensembl.1
Natural variantiVAR_004127301Y → C in CS. 1 Publication1
Natural variantiVAR_004130328Y → C in CS. 1 PublicationCorresponds to variant dbSNP:rs121918493Ensembl.1
Natural variantiVAR_004131331N → I in CS. 1 Publication1
Natural variantiVAR_004132337A → ANA in CS. 1
Natural variantiVAR_017268337A → P in CS. 1 PublicationCorresponds to variant dbSNP:rs387906676Ensembl.1
Natural variantiVAR_004133338G → E in CS. 1 PublicationCorresponds to variant dbSNP:rs1057519044Ensembl.1
Natural variantiVAR_015011338G → R in CS. 3 PublicationsCorresponds to variant dbSNP:rs1057519043Ensembl.1
Natural variantiVAR_004134340Y → H in CS. 2 PublicationsCorresponds to variant dbSNP:rs121918489Ensembl.1
Natural variantiVAR_004136342C → F in CS. 3 PublicationsCorresponds to variant dbSNP:rs121918487Ensembl.1
Natural variantiVAR_004137342C → R in CS, JWS, PS and ABS2. 9 PublicationsCorresponds to variant dbSNP:rs121918488Ensembl.1
Natural variantiVAR_004138342C → S in CS, JWS, PS and ABS2. 8 PublicationsCorresponds to variant dbSNP:rs121918488Ensembl.1
Natural variantiVAR_017271342C → W in CS. 3 PublicationsCorresponds to variant dbSNP:rs121918496Ensembl.1
Natural variantiVAR_004142347S → C in CS. 2 PublicationsCorresponds to variant dbSNP:rs121918494Ensembl.1
Natural variantiVAR_004143351S → C in CS, PS and ABS2. 3 PublicationsCorresponds to variant dbSNP:rs121918502Ensembl.1
Natural variantiVAR_004144354S → C in CS. 5 PublicationsCorresponds to variant dbSNP:rs121918490Ensembl.1
Natural variantiVAR_017272354S → Y in CS. 1 Publication1
Natural variantiVAR_004145356 – 358Missing in CS. 1 Publication3
Natural variantiVAR_017273362A → S in CS. 1 Publication1
Natural variantiVAR_004147384G → R in CS. 1 Publication1
Natural variantiVAR_017276549N → H in CS; constitutive kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs1057519045Ensembl.1
Natural variantiVAR_017281678R → G in CS. 1 Publication1
Jackson-Weiss syndrome (JWS)5 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.
See also OMIM:123150
Apert syndrome (APRS)8 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:101200
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_004114252S → F in APRS; requires 2 nucleotide substitutions. 1 PublicationCorresponds to variant dbSNP:rs121918498Ensembl.1
Natural variantiVAR_004117253P → R in APRS; common mutation. 5 PublicationsCorresponds to variant dbSNP:rs77543610Ensembl.1
Pfeiffer syndrome (PS)13 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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).
See also OMIM:101600
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017259172A → F in PS; requires 2 nucleotide substitutions. 1 Publication1
Natural variantiVAR_004116252 – 253SP → FS in PS. Corresponds to variant dbSNP:rs281865420Ensembl.2
Natural variantiVAR_017262273Missing in PS; type 2. 1 Publication1
Natural variantiVAR_004124290W → C in PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation. 3 PublicationsCorresponds to variant dbSNP:rs121918499Ensembl.1
Natural variantiVAR_004129321D → A in PS. 1 PublicationCorresponds to variant dbSNP:rs121918510Ensembl.1
Natural variantiVAR_017269340Y → C in PS. 2 Publications1
Natural variantiVAR_017270342C → G in PS. 1 PublicationCorresponds to variant dbSNP:rs121918488Ensembl.1
Natural variantiVAR_017277565E → G in PS; constitutive kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs121918506Ensembl.1
Natural variantiVAR_017278641K → R in PS; constitutive kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs1057519047Ensembl.1
Natural variantiVAR_017280663G → E in PS. 1 Publication1
Beare-Stevenson cutis gyrata syndrome (BSTVS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:123790
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_017274372S → C in BSTVS. 1 PublicationCorresponds to variant dbSNP:rs121913477Ensembl.1
Familial scaphocephaly syndrome (FSPC)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:609579
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_023788526K → E in FSPC; constitutive kinase activity. 2 PublicationsCorresponds to variant dbSNP:rs121918507Ensembl.1
Lacrimo-auriculo-dento-digital syndrome (LADDS)2 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn 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.
See also OMIM:149730
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_029884628A → T in LADDS; strongly reduced kinase activity. 1 PublicationCorresponds to variant dbSNP:rs121918509Ensembl.1
Natural variantiVAR_029885648A → T in LADDS. 1 PublicationCorresponds to variant dbSNP:rs121918508Ensembl.1
Natural variantiVAR_029886649 – 650RD → S in LADDS. 1 Publication2
Antley-Bixler syndrome, without genital anomalies or disordered steroidogenesis (ABS2)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:207410
Bent bone dysplasia syndrome (BBDS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA 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.
See also OMIM:614592
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067977381Y → D in BBDS. 1 PublicationCorresponds to variant dbSNP:rs387906678Ensembl.1
Natural variantiVAR_067978391M → R in BBDS; the mutation selectively reduces plasma-membrane levels of the protein and markedly diminishes the receptor's responsiveness to extracellular FGF. 1 PublicationCorresponds to variant dbSNP:rs387906677Ensembl.1
Saethre-Chotzen syndrome (SCS)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionA craniosynostosis syndrome characterized by coronal synostosis, brachycephaly, low frontal hairline, facial asymmetry, hypertelorism, broad halluces, and clinodactyly.
See also OMIM:101400
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_075856269 – 270Missing in SCS. 1 Publication2

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi265N → Q: Reduced N-glycosylation. Reduced expression at the cell surface. 1 Publication1
Mutagenesisi549N → T: Constitutive kinase activity. 1 Publication1
Mutagenesisi565E → A: Constitutive kinase activity. 1 Publication1
Mutagenesisi656 – 657Missing : Loss of kinase activity. 1 Publication2
Mutagenesisi769Y → F: Increases fibroblast proliferation. Decreases phosphorylation of PLCG1 and FRS2. Decreases activation of MAP kinases. 2 Publications1

Keywords - Diseasei

Craniosynostosis, Disease mutation, Ectodermal dysplasia, Lacrimo-auriculo-dento-digital syndrome, Mental retardation, Proto-oncogene

Organism-specific databases

DisGeNETi2263.
GeneReviewsiFGFR2.
MalaCardsiFGFR2.
MIMi101200. phenotype.
101400. phenotype.
101600. phenotype.
123150. phenotype.
123500. phenotype.
123790. phenotype.
149730. phenotype.
207410. phenotype.
609579. phenotype.
614592. phenotype.
OpenTargetsiENSG00000066468.
Orphaneti83. Antley-Bixler syndrome.
87. Apert syndrome.
207. Crouzon disease.
1555. Cutis gyrata - acanthosis nigricans - craniosynostosis.
168624. Familial scaphocephaly syndrome, McGillivray type.
313855. FGFR2-related bent bone dysplasia.
1540. Jackson-Weiss syndrome.
2363. Lacrimoauriculodentodigital syndrome.
93258. Pfeiffer syndrome type 1.
93259. Pfeiffer syndrome type 2.
93260. Pfeiffer syndrome type 3.
794. Saethre-Chotzen syndrome.
PharmGKBiPA28128.

Chemistry databases

ChEMBLiCHEMBL4142.
DrugBankiDB02491. 4-[4-(1-Amino-1-Methylethyl)Phenyl]-5-Chloro-N-[4-(2-Morpholin-4-Ylethyl)Phenyl]Pyrimidin-2-Amine.
DB09078. Lenvatinib.
DB09079. Nintedanib.
DB00039. Palifermin.
DB08901. Ponatinib.
DB08896. Regorafenib.
DB02058. SU4984.
DB01041. Thalidomide.
GuidetoPHARMACOLOGYi1809.

Polymorphism and mutation databases

BioMutaiFGFR2.
DMDMi120049.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 21Sequence analysisAdd BLAST21
ChainiPRO_000001678322 – 821Fibroblast growth factor receptor 2Add BLAST800

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi62 ↔ 107PROSITE-ProRule annotation
Glycosylationi83N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi123N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi179 ↔ 231PROSITE-ProRule annotation1 Publication
Glycosylationi228N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi241N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi265N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi278 ↔ 342PROSITE-ProRule annotation1 Publication
Glycosylationi297N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi318N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi331N-linked (GlcNAc...) asparagineSequence analysis1
Modified residuei466Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei586Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei588Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei656Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei657Phosphotyrosine; by autocatalysis3 Publications1
Modified residuei769Phosphotyrosine; by autocatalysis2 Publications1
Modified residuei780PhosphoserineCombined sources1

Post-translational modificationi

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 PLCG1.2 Publications
N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus.2 Publications
Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome.3 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP21802.
PeptideAtlasiP21802.
PRIDEiP21802.
TopDownProteomicsiP21802-8. [P21802-8]

PTM databases

iPTMnetiP21802.
PhosphoSitePlusiP21802.

Expressioni

Gene expression databases

BgeeiENSG00000066468.
ExpressionAtlasiP21802. baseline and differential.
GenevisibleiP21802. HS.

Organism-specific databases

HPAiCAB010886.
HPA035305.
HPA056562.

Interactioni

Subunit structurei

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. Interacts with FLRT2 (By similarity).By similarity21 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • fibroblast growth factor binding Source: UniProtKB
  • identical protein binding Source: IntAct
  • protein homodimerization activity Source: UniProtKB
  • Ras guanyl-nucleotide exchange factor activity Source: Reactome

Protein-protein interaction databases

BioGridi108554. 89 interactors.
CORUMiP21802.
DIPiDIP-3788N.
IntActiP21802. 30 interactors.
MINTiMINT-118359.
STRINGi9606.ENSP00000410294.

Chemistry databases

BindingDBiP21802.

Structurei

Secondary structure

1821
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi152 – 157Combined sources6
Turni159 – 162Combined sources4
Beta strandi166 – 170Combined sources5
Beta strandi175 – 178Combined sources4
Beta strandi181 – 185Combined sources5
Beta strandi188 – 193Combined sources6
Helixi200 – 202Combined sources3
Beta strandi203 – 205Combined sources3
Beta strandi208 – 210Combined sources3
Helixi211 – 213Combined sources3
Beta strandi215 – 218Combined sources4
Helixi223 – 225Combined sources3
Beta strandi227 – 235Combined sources9
Beta strandi238 – 249Combined sources12
Beta strandi266 – 269Combined sources4
Beta strandi274 – 277Combined sources4
Beta strandi287 – 293Combined sources7
Beta strandi296 – 298Combined sources3
Beta strandi299 – 301Combined sources3
Beta strandi303 – 305Combined sources3
Beta strandi309 – 314Combined sources6
Beta strandi315 – 319Combined sources5
Helixi321 – 323Combined sources3
Beta strandi324 – 327Combined sources4
Helixi334 – 336Combined sources3
Beta strandi338 – 346Combined sources9
Beta strandi349 – 360Combined sources12
Turni463 – 465Combined sources3
Turni472 – 474Combined sources3
Helixi478 – 480Combined sources3
Beta strandi481 – 489Combined sources9
Beta strandi494 – 500Combined sources7
Beta strandi504 – 506Combined sources3
Beta strandi513 – 518Combined sources6
Helixi525 – 541Combined sources17
Beta strandi550 – 554Combined sources5
Beta strandi556 – 558Combined sources3
Beta strandi561 – 565Combined sources5
Beta strandi568 – 571Combined sources4
Helixi572 – 577Combined sources6
Turni585 – 588Combined sources4
Helixi594 – 596Combined sources3
Helixi600 – 619Combined sources20
Helixi629 – 631Combined sources3
Beta strandi632 – 634Combined sources3
Turni636 – 638Combined sources3
Beta strandi640 – 642Combined sources3
Helixi645 – 647Combined sources3
Turni652 – 654Combined sources3
Beta strandi655 – 658Combined sources4
Turni659 – 662Combined sources4
Beta strandi664 – 666Combined sources3
Helixi667 – 669Combined sources3
Helixi672 – 677Combined sources6
Helixi682 – 697Combined sources16
Helixi709 – 718Combined sources10
Beta strandi726 – 728Combined sources3
Helixi730 – 739Combined sources10
Helixi744 – 746Combined sources3
Helixi750 – 764Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1DJSX-ray2.40A153-362[»]
1E0OX-ray2.80B/D148-366[»]
1EV2X-ray2.20E/F/G/H147-366[»]
1GJOX-ray2.40A456-768[»]
1II4X-ray2.70E/F/G/H147-366[»]
1IILX-ray2.30E/F/G/H147-366[»]
1NUNX-ray2.90B140-368[»]
1OECX-ray2.40A456-768[»]
1WVZNMR-A147-249[»]
2FDBX-ray2.28P/R149-368[»]
2PSQX-ray2.40A/B413-768[»]
2PVFX-ray1.80A458-778[»]
B764-778[»]
2PVYX-ray2.20A/B/C/D458-768[»]
2PWLX-ray2.40A/B458-768[»]
2PY3X-ray2.30A/B458-768[»]
2PZ5X-ray2.40A/B458-768[»]
2PZPX-ray2.40A/B458-768[»]
2PZRX-ray3.00A/B458-768[»]
2Q0BX-ray2.90A/B458-768[»]
3B2TX-ray1.80A/B458-766[»]
3CAFX-ray1.96A150-249[»]
3CLYX-ray2.00A458-778[»]
3CU1X-ray2.60A/C150-249[»]
3DARX-ray2.20A/B146-249[»]
3EUUX-ray2.34A/B150-249[»]
3OJ2X-ray2.20C/D140-313[»]
3OJMX-ray2.10B140-313[»]
3RI1X-ray2.10A/B458-768[»]
4J23X-ray3.88A147-366[»]
4J95X-ray2.38A/B/C/D458-768[»]
4J96X-ray2.30A/B458-768[»]
4J97X-ray2.55A/B/C/D458-768[»]
4J98X-ray2.31A/B458-768[»]
4J99X-ray1.85A/B/C/D458-768[»]
4WV1X-ray2.36C/F153-251[»]
5EG3X-ray2.61A458-778[»]
5UGLX-ray1.86A/B458-768[»]
5UGXX-ray2.35A/B458-768[»]
5UHNX-ray2.91A/B458-768[»]
5UI0X-ray2.05A/B458-768[»]
ProteinModelPortaliP21802.
SMRiP21802.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP21802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini25 – 125Ig-like C2-type 1Add BLAST101
Domaini154 – 247Ig-like C2-type 2Add BLAST94
Domaini256 – 358Ig-like C2-type 3Add BLAST103
Domaini481 – 770Protein kinasePROSITE-ProRule annotationAdd BLAST290

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni161 – 178Heparin-bindingAdd BLAST18

Domaini

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.3 Publications

Sequence similaritiesi

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation

Keywords - Domaini

Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG0200. Eukaryota.
COG0515. LUCA.
GeneTreeiENSGT00760000118923.
HOGENOMiHOG000263410.
HOVERGENiHBG000345.
InParanoidiP21802.
KOiK05093.
OrthoDBiEOG091G0CQZ.
PhylomeDBiP21802.
TreeFamiTF316307.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiView protein in InterPro
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR036179. Ig-like_dom_sf.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom_sf.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
PfamiView protein in Pfam
PF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
PIRSFiPIRSF000628. FGFR. 1 hit.
PRINTSiPR00109. TYRKINASE.
SMARTiView protein in SMART
SM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF56112. SSF56112. 1 hit.
PROSITEiView protein in PROSITE
PS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.

Sequences (23)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 23 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P21802-1) [UniParc]FASTAAdd to basket
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.

« Hide

        10         20         30         40         50
MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEVY
60 70 80 90 100
VAAPGESLEV RCLLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR
110 120 130 140 150
DSGLYACTAS RTVDSETWYF MVNVTDAISS GDDEDDTDGA EDFVSENSNN
160 170 180 190 200
KRAPYWTNTE KMEKRLHAVP AANTVKFRCP AGGNPMPTMR WLKNGKEFKQ
210 220 230 240 250
EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CVVENEYGSI NHTYHLDVVE
260 270 280 290 300
RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK
310 320 330 340 350
YGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI
360 370 380 390 400
SFHSAWLTVL PAPGREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVILCRM
410 420 430 440 450
KNTTKKPDFS SQPAVHKLTK RIPLRRQVTV SAESSSSMNS NTPLVRITTR
460 470 480 490 500
LSSTADTPML AGVSEYELPE DPKWEFPRDK LTLGKPLGEG CFGQVVMAEA
510 520 530 540 550
VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM IGKHKNIINL
560 570 580 590 600
LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF
610 620 630 640 650
KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD
660 670 680 690 700
INNIDYYKKT TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG
710 720 730 740 750
GSPYPGIPVE ELFKLLKEGH RMDKPANCTN ELYMMMRDCW HAVPSQRPTF
760 770 780 790 800
KQLVEDLDRI LTLTTNEEYL DLSQPLEQYS PSYPDTRSSC SSGDDSVFSP
810 820
DPMPYEPCLP QYPHINGSVK T
Length:821
Mass (Da):92,025
Last modified:May 1, 1991 - v1
Checksum:i6CD5001C960ED82F
GO
Isoform 2 (identifier: P21802-2) [UniParc]FASTAAdd to basket
Also known as: Short

The sequence of this isoform differs from the canonical sequence as follows:
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I

Show »
Length:768
Mass (Da):86,130
Checksum:i8D4734CBEA8E8C8F
GO
Isoform 3 (identifier: P21802-3) [UniParc]FASTAAdd to basket
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

Show »
Length:822
Mass (Da):92,118
Checksum:i288CF737673BA4AB
GO
Isoform 4 (identifier: P21802-4) [UniParc]FASTAAdd to basket
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

Show »
Length:682
Mass (Da):76,705
Checksum:iD56050B4385A6635
GO
Isoform 5 (identifier: P21802-5) [UniParc]FASTAAdd to basket
Also known as: K-sam-I, BEK, IgIIIc

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.

Show »
Length:819
Mass (Da):91,825
Checksum:i4746938783A1D94F
GO
Isoform 6 (identifier: P21802-6) [UniParc]FASTAAdd to basket
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

Show »
Length:785
Mass (Da):88,181
Checksum:i042BF83F92CE97F5
GO
Isoform 7 (identifier: P21802-7) [UniParc]FASTAAdd to basket
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

Show »
Length:817
Mass (Da):91,620
Checksum:i46BA78E51DB700CD
GO
Isoform 8 (identifier: P21802-8) [UniParc]FASTAAdd to basket
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

Show »
Length:766
Mass (Da):85,929
Checksum:iFE97A413B085D31E
GO
Isoform 9 (identifier: P21802-9) [UniParc]FASTAAdd to basket
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

Show »
Length:819
Mass (Da):91,566
Checksum:iC60FE09EC1BE0654
GO
Isoform 10 (identifier: P21802-10) [UniParc]FASTAAdd to basket
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

Show »
Length:819
Mass (Da):91,641
Checksum:i467E9BAAD07C5463
GO
Isoform 11 (identifier: P21802-11) [UniParc]FASTAAdd to basket
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

Show »
Length:830
Mass (Da):92,733
Checksum:iE726FA4235995586
GO
Isoform 12 (identifier: P21802-12) [UniParc]FASTAAdd to basket
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

Show »
Length:771
Mass (Da):86,407
Checksum:i881C475B4771CA5C
GO
Isoform 13 (identifier: P21802-13) [UniParc]FASTAAdd to basket
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.

Show »
Length:768
Mass (Da):86,110
Checksum:iBB4771CA5CBEEFAA
GO
Isoform 14 (identifier: P21802-14) [UniParc]FASTAAdd to basket
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.

Show »
Length:254
Mass (Da):28,299
Checksum:i1855113266C85F4F
GO
Isoform 15 (identifier: P21802-15) [UniParc]FASTAAdd to basket
Also known as: K-sam-III

The sequence of this isoform differs from the canonical sequence as follows:
     314-429: Missing.

Show »
Length:705
Mass (Da):79,212
Checksum:i590967DCBF5DA25D
GO
Isoform 16 (identifier: P21802-16) [UniParc]FASTAAdd to basket
Also known as: TK14

The sequence of this isoform differs from the canonical sequence as follows:
     313-313: K → KVTK
     428-429: Missing.

Show »
Length:822
Mass (Da):92,153
Checksum:i15D08A6D66AC4EA0
GO
Isoform 17 (identifier: P21802-17) [UniParc]FASTAAdd to basket

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

Show »
Length:769
Mass (Da):86,223
Checksum:i806B4771CA5CBEEF