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P21803 (FGFR2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 148. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor receptor 2

Short name=FGFR-2
EC=2.7.10.1
Alternative name(s):
Keratinocyte growth factor receptor
Short name=KGFR
CD_antigen=CD332
Gene names
Name:Fgfr2
Synonyms:Bek, Ect1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. Ref.6 Ref.7 Ref.11 Ref.13

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

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 By similarity.

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. 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 By similarity. Ref.7 Ref.13

Subcellular location

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

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 By similarity.

Post-translational modification

Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer By similarity. Ref.13

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

Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome By similarity.

Disruption phenotype

Embryonic lethality shortly after implantation, due to trophoblast defects, absence of a functional placenta, failure of limb bud formation, plus defects in lung branching and heart development. Ref.8 Ref.9 Ref.10 Ref.12

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.

Ontologies

Keywords
   Biological processApoptosis
   Cellular componentCell membrane
Cytoplasmic vesicle
Golgi apparatus
Membrane
   Coding sequence diversityAlternative splicing
   DiseaseProto-oncogene
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Heparin-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from genetic interaction PubMed 16778080. Source: MGI

apoptotic process

Inferred from electronic annotation. Source: UniProtKB-KW

axonogenesis

Inferred from mutant phenotype PubMed 17951031. Source: MGI

bone development

Inferred from mutant phenotype PubMed 16989802. Source: MGI

bone mineralization

Inferred from mutant phenotype PubMed 12756187. Source: MGI

bone morphogenesis

Inferred from mutant phenotype Ref.10. Source: MGI

branch elongation involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 15972105. Source: MGI

branching involved in labyrinthine layer morphogenesis

Inferred from mutant phenotype Ref.8. Source: MGI

branching involved in prostate gland morphogenesis

Inferred from mutant phenotype PubMed 12666202PubMed 17215304. Source: MGI

branching involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 11731698. Source: MGI

branching morphogenesis of a nerve

Inferred from mutant phenotype PubMed 17951031. Source: MGI

bud elongation involved in lung branching

Inferred from mutant phenotype PubMed 16989802. Source: MGI

cell fate commitment

Inferred from direct assay PubMed 15509736. Source: MGI

cell-cell signaling

Inferred from mutant phenotype PubMed 15199404. Source: MGI

coronal suture morphogenesis

Inferred from mutant phenotype PubMed 19389359. Source: MGI

digestive tract development

Inferred from mutant phenotype PubMed 15234214. Source: MGI

embryonic cranial skeleton morphogenesis

Inferred from electronic annotation. Source: InterPro

embryonic digestive tract morphogenesis

Inferred from mutant phenotype PubMed 16618415PubMed 21550054. Source: MGI

embryonic organ development

Inferred from mutant phenotype Ref.8. Source: MGI

embryonic organ morphogenesis

Inferred from mutant phenotype PubMed 15843416. Source: MGI

embryonic pattern specification

Inferred from mutant phenotype PubMed 16618415. Source: MGI

endodermal digestive tract morphogenesis

Inferred from mutant phenotype PubMed 21550054. Source: MGI

epidermis morphogenesis

Inferred from mutant phenotype PubMed 14530295. Source: MGI

epithelial cell differentiation

Inferred from mutant phenotype PubMed 16618415. Source: MGI

epithelial cell proliferation

Inferred from mutant phenotype PubMed 11312155PubMed 15843416. Source: MGI

epithelial cell proliferation involved in salivary gland morphogenesis

Inferred from mutant phenotype PubMed 15972105. Source: MGI

fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype Ref.8. Source: MGI

fibroblast growth factor receptor signaling pathway involved in hemopoiesis

Inferred from mutant phenotype PubMed 20345253. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in mammary gland specification

Inferred from mutant phenotype PubMed 16720875. Source: MGI

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

Inferred from mutant phenotype PubMed 20345253. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

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

Inferred from mutant phenotype PubMed 20345253. Source: UniProtKB

gland morphogenesis

Inferred from mutant phenotype PubMed 17202188. Source: MGI

hair follicle morphogenesis

Inferred from mutant phenotype PubMed 14530295. Source: MGI

in utero embryonic development

Inferred from mutant phenotype Ref.8. Source: MGI

inner ear morphogenesis

Inferred from mutant phenotype PubMed 10934262. Source: MGI

lacrimal gland development

Inferred from mutant phenotype PubMed 10821755. Source: MGI

lateral sprouting from an epithelium

Inferred from mutant phenotype PubMed 12666202. Source: MGI

lens fiber cell development

Inferred from mutant phenotype PubMed 23136392. Source: MGI

limb bud formation

Inferred from mutant phenotype Ref.10Ref.8. Source: MGI

lung alveolus development

Inferred from mutant phenotype PubMed 16989802. Source: MGI

lung development

Inferred from mutant phenotype Ref.10. Source: MGI

lung lobe morphogenesis

Inferred from mutant phenotype PubMed 16989802. Source: MGI

lung-associated mesenchyme development

Inferred from mutant phenotype PubMed 16989802. Source: MGI

mammary gland bud formation

Inferred from mutant phenotype PubMed 11782400. Source: MGI

membranous septum morphogenesis

Inferred from mutant phenotype PubMed 16687131. Source: MGI

mesenchymal cell differentiation

Inferred from genetic interaction PubMed 16442091. Source: MGI

mesenchymal cell differentiation involved in lung development

Inferred from genetic interaction PubMed 16989802. Source: MGI

mesenchymal cell proliferation involved in lung development

Inferred from mutant phenotype PubMed 16989802. Source: MGI

midbrain development

Inferred from genetic interaction PubMed 17687036. Source: MGI

morphogenesis of embryonic epithelium

Inferred from mutant phenotype PubMed 15843416. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 16989802. Source: MGI

negative regulation of cell proliferation

Inferred from genetic interaction PubMed 18455718. Source: MGI

negative regulation of mitosis

Inferred from genetic interaction PubMed 18455718. Source: MGI

negative regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 16989802. Source: MGI

neuromuscular junction development

Inferred from mutant phenotype PubMed 17418794. Source: MGI

odontogenesis

Inferred from mutant phenotype PubMed 17951031. Source: MGI

orbitofrontal cortex development

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

organ growth

Inferred from mutant phenotype PubMed 16618415. Source: MGI

organ morphogenesis

Inferred from mutant phenotype PubMed 12666202. Source: MGI

otic vesicle formation

Inferred from mutant phenotype Ref.8. Source: MGI

outflow tract septum morphogenesis

Inferred from mutant phenotype PubMed 16687131. Source: MGI

positive regulation of ERK1 and ERK2 cascade

Inferred from genetic interaction PubMed 17202188. Source: MGI

positive regulation of Wnt signaling pathway

Inferred from mutant phenotype PubMed 16989802. Source: MGI

positive regulation of canonical Wnt signaling pathway

Inferred from mutant phenotype PubMed 16720875. Source: MGI

positive regulation of cardiac muscle cell proliferation

Inferred from genetic interaction PubMed 15621532. Source: MGI

positive regulation of cell cycle

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

positive regulation of cell division

Inferred from mutant phenotype PubMed 14530295. Source: MGI

positive regulation of cell proliferation

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

positive regulation of epithelial cell proliferation

Inferred from genetic interaction PubMed 15972105. Source: MGI

positive regulation of epithelial cell proliferation involved in lung morphogenesis

Inferred from mutant phenotype PubMed 16989802. Source: MGI

positive regulation of mesenchymal cell proliferation

Inferred from genetic interaction PubMed 16540513. Source: MGI

positive regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

post-embryonic development

Inferred from mutant phenotype PubMed 16989802. Source: MGI

prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis

Inferred from mutant phenotype PubMed 17215304. Source: MGI

prostate epithelial cord elongation

Inferred from mutant phenotype PubMed 17215304. Source: MGI

prostate gland morphogenesis

Inferred from mutant phenotype PubMed 18184727. Source: MGI

pyramidal neuron development

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

regulation of ERK1 and ERK2 cascade

Inferred from mutant phenotype PubMed 16989802. Source: MGI

regulation of branching involved in prostate gland morphogenesis

Inferred from mutant phenotype PubMed 17202188. Source: MGI

regulation of cell fate commitment

Inferred from mutant phenotype PubMed 16989802. Source: MGI

regulation of cell proliferation

Inferred from mutant phenotype PubMed 12756187. Source: MGI

regulation of epithelial cell proliferation

Inferred from mutant phenotype PubMed 17215304PubMed 18184727. Source: MGI

regulation of fibroblast growth factor receptor signaling pathway

Inferred from mutant phenotype PubMed 16989802. Source: MGI

regulation of morphogenesis of a branching structure

Inferred from mutant phenotype PubMed 17202188. Source: MGI

regulation of multicellular organism growth

Inferred from mutant phenotype Ref.8. Source: MGI

regulation of smooth muscle cell differentiation

Inferred from mutant phenotype PubMed 16989802. Source: MGI

regulation of smoothened signaling pathway

Inferred from mutant phenotype PubMed 16618415. Source: MGI

reproductive structure development

Inferred from mutant phenotype PubMed 12666202. Source: MGI

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

Inferred from mutant phenotype PubMed 17215304. Source: MGI

synaptic vesicle transport

Inferred from mutant phenotype PubMed 17418794. Source: MGI

ureteric bud development

Inferred from genetic interaction PubMed 16442091. Source: MGI

vasculogenesis involved in coronary vascular morphogenesis

Traceable author statement PubMed 20299672. Source: DFLAT

ventricular cardiac muscle tissue morphogenesis

Inferred from mutant phenotype PubMed 16687131. Source: MGI

ventricular zone neuroblast division

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

   Cellular_componentGolgi apparatus

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

excitatory synapse

Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB

extracellular region

Traceable author statement PubMed 12024206. Source: MGI

integral component of membrane

Inferred from electronic annotation. Source: UniProtKB-KW

nucleus

Inferred from direct assay PubMed 15229180PubMed 15944199. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fibroblast growth factor binding

Inferred from direct assay Ref.8. Source: MGI

fibroblast growth factor-activated receptor activity

Inferred from electronic annotation. Source: InterPro

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ncam1P135952EBI-6286942,EBI-774943

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform Long (identifier: P21803-1)

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 Short (identifier: P21803-2)

The sequence of this isoform differs from the canonical sequence as follows:
     37-37: E → G
     38-152: Missing.
     314-361: AAGVNTTDKE...FHSAWLTVLP → HSGINSSNAE...AWLTVLPKQQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121
Chain22 – 821800Fibroblast growth factor receptor 2
PRO_0000016784

Regions

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

Sites

Active site6261Proton acceptor By similarity
Binding site5171ATP By similarity
Binding site5711ATP By similarity

Amino acid modifications

Modified residue4661Phosphotyrosine; by autocatalysis By similarity
Modified residue5861Phosphotyrosine; by autocatalysis By similarity
Modified residue5881Phosphotyrosine; by autocatalysis By similarity
Modified residue6561Phosphotyrosine; by autocatalysis By similarity
Modified residue6571Phosphotyrosine; by autocatalysis By similarity
Modified residue7691Phosphotyrosine; by autocatalysis By similarity
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation1471N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 107 By similarity
Disulfide bond179 ↔ 231 By similarity
Disulfide bond278 ↔ 342 By similarity

Natural variations

Alternative sequence371E → G in isoform Short.
VSP_002985
Alternative sequence38 – 152115Missing in isoform Short.
VSP_002986
Alternative sequence314 – 36148AAGVN…LTVLP → HSGINSSNAEVLALFNVTEM DAGEYICKVSNYIGQANQSA WLTVLPKQQ in isoform Short.
VSP_002987

Experimental info

Mutagenesis7691Y → F: Abolishes phosphorylation of FRS2 and activation of MAP kinases. Ref.13
Sequence conflict531A → V in CAA39083. Ref.1
Sequence conflict55 – 562GE → RG in CAA39083. Ref.1
Sequence conflict901E → R in CAA39083. Ref.1
Sequence conflict1191I → Y in CAA39083. Ref.1
Sequence conflict142 – 1432DV → R in CAA39083. Ref.1
Sequence conflict1691C → V in CAA39083. Ref.1
Sequence conflict1691C → V in AAA39377. Ref.2
Sequence conflict1871S → P in CAA39083. Ref.1
Sequence conflict1871S → P in AAA39377. Ref.2
Sequence conflict2141W → R in CAA39083. Ref.1
Sequence conflict2291Y → I in CAA39083. Ref.1
Sequence conflict2751E → R in CAA39083. Ref.1
Sequence conflict3011N → Y in CAA39083. Ref.1
Sequence conflict3011N → Y in AAA39377. Ref.2

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform Long [UniParc].

Last modified November 1, 1997. Version 4.
Checksum: FCDB28ADD61F4414

FASTA82191,984
        10         20         30         40         50         60 
MVSWGRFICL VLVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEAY VVAPGESLEL 

        70         80         90        100        110        120 
QCMLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAA RTVDSETWIF 

       130        140        150        160        170        180 
MVNVTDAISS GDDEDDTDSS EDVVSENRSN QRAPYWTNTE KMEKRLHACP AANTVKFRCP 

       190        200        210        220        230        240 
AGGNPTSTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CLVENEYGSI 

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

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

       370        380        390        400        410        420 
PAPVREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVIFCRM KTTTKKPDFS 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 
RMDKPTNCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEEYL DLTQPLEQYS 

       790        800        810        820 
PSYPDTSSSC SSGDDSVFSP DPMPYEPCLP QYPHINGSVK T 

« Hide

Isoform Short [UniParc].

Checksum: E57F5804B12F667C
Show »

FASTA70779,531

References

[1]"PCR-based identification of new receptors: molecular cloning of a receptor for fibroblast growth factors."
Raz V., Kelman Z., Avivi A., Neufeld G., Givol D., Yarden Y.
Oncogene 6:753-760(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Strain: BALB/c.
Tissue: Brain.
[2]"Expression cDNA cloning of the KGF receptor by creation of a transforming autocrine loop."
Miki T., Fleming T.P., Bottaro D.P., Rubin J.S., Ron D., Aaronson S.A.
Science 251:72-75(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM SHORT).
[3]"Characterization of the murine BEK fibroblast growth factor (FGF) receptor: activation by three members of the FGF family and requirement for heparin."
Mansukhani A., Dell'Era P., Moscatelli D., Kornbluth S., Hanafusa H., Basilico C.
Proc. Natl. Acad. Sci. U.S.A. 89:3305-3309(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
Tissue: Brain and Liver.
[4]"Conserved use of a non-canonical 5' splice site (/GA) in alternative splicing by fibroblast growth factor receptors 1, 2 and 3."
Twigg S.R.F., Burns H.D., Oldridge M., Heath J.K., Wilkie A.O.M.
Hum. Mol. Genet. 7:685-691(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM LONG).
[5]"Novel tyrosine kinase identified by phosphotyrosine antibody screening of cDNA libraries."
Kornbluth S., Paulson K.E., Hanafusa H.
Mol. Cell. Biol. 8:5541-5544(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 477-821.
Tissue: Liver.
[6]"Developmental localization of the splicing alternatives of fibroblast growth factor receptor-2 (FGFR2)."
Orr-Urtreger A., Bedford M.T., Burakova T., Arman E., Zimmer Y., Yayon A., Givol D., Lonai P.
Dev. Biol. 158:475-486(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[7]"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.
[8]"Fibroblast growth factor receptor 2 (FGFR2)-mediated reciprocal regulation loop between FGF8 and FGF10 is essential for limb induction."
Xu X., Weinstein M., Li C., Naski M., Cohen R.I., Ornitz D.M., Leder P., Deng C.
Development 125:753-765(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[9]"Targeted disruption of fibroblast growth factor (FGF) receptor 2 suggests a role for FGF signaling in pregastrulation mammalian development."
Arman E., Haffner-Krausz R., Chen Y., Heath J.K., Lonai P.
Proc. Natl. Acad. Sci. U.S.A. 95:5082-5087(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[10]"Fgfr2 is required for limb outgrowth and lung-branching morphogenesis."
Arman E., Haffner-Krausz R., Gorivodsky M., Lonai P.
Proc. Natl. Acad. Sci. U.S.A. 96:11895-11899(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[11]"Signaling by fibroblast growth factors (FGF) and fibroblast growth factor receptor 2 (FGFR2)-activating mutations blocks mineralization and induces apoptosis in osteoblasts."
Mansukhani A., Bellosta P., Sahni M., Basilico C.
J. Cell Biol. 149:1297-1308(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[12]"The IIIc alternative of Fgfr2 is a positive regulator of bone formation."
Eswarakumar V.P., Monsonego-Ornan E., Pines M., Antonopoulou I., Morriss-Kay G.M., Lonai P.
Development 129:3783-3793(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[13]"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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X55441 mRNA. Translation: CAA39083.1.
M63503 mRNA. Translation: AAA39377.1.
M86441 mRNA. Translation: AAA37286.1.
Y16152 Genomic DNA. Translation: CAA76098.1.
Y16167 Genomic DNA. Translation: CAA76099.1.
M23362 mRNA. Translation: AAA37285.1.
PIRA38429.
TVMSBK. A44142.
S17295.
RefSeqNP_034337.2. NM_010207.2.
NP_963895.2. NM_201601.2.
UniGeneMm.16340.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4HWUX-ray2.90A/B45-127[»]
ProteinModelPortalP21803.
SMRP21803. Positions 47-363, 462-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199657. 2 interactions.
DIPDIP-6038N.
IntActP21803. 2 interactions.

Chemistry

ChEMBLCHEMBL2111391.

PTM databases

PhosphoSiteP21803.

Proteomic databases

PaxDbP21803.
PRIDEP21803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID14183.
KEGGmmu:14183.

Organism-specific databases

CTD2263.
MGIMGI:95523. Fgfr2.

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000263410.
HOVERGENHBG000345.
InParanoidP21803.
KOK05093.
PhylomeDBP21803.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

CleanExMM_FGFR2.
GenevestigatorP21803.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028175. FGF_rcpt_2.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF130. PTHR24416:SF130. 1 hit.
PfamPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGFR2. mouse.
NextBio285386.
PROP21803.
SOURCESearch...

Entry information

Entry nameFGFR2_MOUSE
AccessionPrimary (citable) accession number: P21803
Secondary accession number(s): O55141, Q00389, Q61342
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: November 1, 1997
Last modified: April 16, 2014
This is version 148 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot