P21803 (FGFR2_MOUSE) 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):
Keratinocyte growth factor receptor
Short name=KGFR
CD_antigen=CD332

Gene names

Name:	Fgfr2
Synonyms:	Bek, Ect1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

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.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 process	Apoptosis
Cellular component	Cell membrane Cytoplasmic vesicle Golgi apparatus Membrane
Coding sequence diversity	Alternative splicing
Disease	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 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 mineralization Inferred from mutant phenotype PubMed 12756187. 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 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 coronal suture morphogenesis Inferred from mutant phenotype PubMed 19389359. Source: MGI embryonic digestive tract morphogenesis Inferred from mutant phenotype PubMed 16618415PubMed 21550054. 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 epithelial cell proliferation involved in salivary gland morphogenesis Inferred from mutant phenotype PubMed 15972105. 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 hair follicle morphogenesis Inferred from mutant phenotype PubMed 14530295. 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 genetic interaction PubMed 18455718. 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 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 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 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 organ growth Inferred from mutant phenotype PubMed 16618415. 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 canonical Wnt receptor 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 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 pyramidal neuron development Inferred from mutant phenotype PubMed 20410112. Source: UniProtKB 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 fibroblast growth factor receptor signaling pathway Inferred from mutant phenotype PubMed 16989802. 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 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_component	Golgi 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 to 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_function	ATP 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...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 21

21

Chain

22 – 821

800

Fibroblast growth factor receptor 2

PRO_0000016784

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 By similarity

Nucleotide binding

565 – 567

3

ATP By similarity

Region

161 – 178

18

Heparin-binding By similarity

Sites

Active site

626

1

Proton acceptor By similarity

Binding site

517

1

ATP By similarity

Binding site

571

1

ATP By similarity

Amino acid modifications

Modified residue

466

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

586

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

588

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

656

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

657

1

Phosphotyrosine; by autocatalysis By similarity

Modified residue

769

1

Phosphotyrosine; by autocatalysis By similarity

Glycosylation

83

1

N-linked (GlcNAc...) Potential

Glycosylation

123

1

N-linked (GlcNAc...) Potential

Glycosylation

147

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

By similarity

Disulfide bond

278 ↔ 342

By similarity

Natural variations

Alternative sequence

37

1

E → G in isoform Short.

VSP_002985

Alternative sequence

38 – 152

115

Missing in isoform Short.

VSP_002986

Alternative sequence

314 – 361

48

AAGVN…LTVLP → HSGINSSNAEVLALFNVTEM DAGEYICKVSNYIGQANQSA WLTVLPKQQ in isoform Short.

VSP_002987

Experimental info

Mutagenesis

769

1

Y → F: Abolishes phosphorylation of FRS2 and activation of MAP kinases. Ref.13

Sequence conflict

53

1

A → V in CAA39083. Ref.1

Sequence conflict

55 – 56

2

GE → RG in CAA39083. Ref.1

Sequence conflict

90

1

E → R in CAA39083. Ref.1

Sequence conflict

119

1

I → Y in CAA39083. Ref.1

Sequence conflict

142 – 143

2

DV → R in CAA39083. Ref.1

Sequence conflict

169

1

C → V in CAA39083. Ref.1

Sequence conflict

169

1

C → V in AAA39377. Ref.2

Sequence conflict

187

1

S → P in CAA39083. Ref.1

Sequence conflict

187

1

S → P in AAA39377. Ref.2

Sequence conflict

214

1

W → R in CAA39083. Ref.1

Sequence conflict

229

1

Y → I in CAA39083. Ref.1

Sequence conflict

275

1

E → R in CAA39083. Ref.1

Sequence conflict

301

1

N → Y in CAA39083. Ref.1

Sequence conflict

301

1

N → Y in AAA39377. Ref.2

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

821

Helix Strand Turn

Details...

Beta strand

48 – 52

5

Beta strand

58 – 61

4

Beta strand

69 – 74

6

Beta strand

77 – 79

3

Beta strand

83 – 88

6

Beta strand

91 – 94

4

Helix

99 – 101

3

Beta strand

103 – 110

8

Beta strand

115 – 124

10

Sequences

	Sequence		Length	Mass (Da)
	Isoform Long [UniParc]. Last modified November 1, 1997. Version 4. Checksum: FCDB28ADD61F4414	FASTA	821	91,984
	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
	Isoform Short [UniParc]. Checksum: E57F5804B12F667C	FASTA	707	79,531
	10 20 30 40 50 60 MVSWGRFICL VLVTMATLSL ARPSFSLVED TTLEPEGAPY WTNTEKMEKR LHACPAANTV 70 80 90 100 110 120 KFRCPAGGNP TSTMRWLKNG KEFKQEHRIG GYKVRNQHWS LIMESVVPSD KGNYTCLVEN 130 140 150 160 170 180 EYGSINHTYH LDVVERSPHR PILQAGLPAN ASTVVGGDVE FVCKVYSDAQ PHIQWIKHVE 190 200 210 220 230 240 KNGSKNGPDG LPYLKVLKHS GINSSNAEVL ALFNVTEMDA GEYICKVSNY IGQANQSAWL 250 260 270 280 290 300 TVLPKQQAPV REKEITASPD YLEIAIYCIG VFLIACMVVT VIFCRMKTTT KKPDFSSQPA 310 320 330 340 350 360 VHKLTKRIPL RRQVTVSAES SSSMNSNTPL VRITTRLSST ADTPMLAGVS EYELPEDPKW 370 380 390 400 410 420 EFPRDKLTLG KPLGEGCFGQ VVMAEAVGID KDKPKEAVTV AVKMLKDDAT EKDLSDLVSE 430 440 450 460 470 480 MEMMKMIGKH KNIINLLGAC TQDGPLYVIV EYASKGNLRE YLRARRPPGM EYSYDINRVP 490 500 510 520 530 540 EEQMTFKDLV SCTYQLARGM EYLASQKCIH RDLAARNVLV TENNVMKIAD FGLARDINNI 550 560 570 580 590 600 DYYKKTTNGR LPVKWMAPEA LFDRVYTHQS DVWSFGVLMW EIFTLGGSPY PGIPVEELFK 610 620 630 640 650 660 LLKEGHRMDK PTNCTNELYM MMRDCWHAVP SQRPTFKQLV EDLDRILTLT TNEEYLDLTQ 670 680 690 700 PLEQYSPSYP DTSSSCSSGD DSVFSPDPMP YEPCLPQYPH INGSVKT

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.

IPI

IPI00128462.
IPI00989007.

PIR

A38429.
TVMSBK. A44142.
S17295.

RefSeq

NP_034337.2. NM_010207.2.
NP_963895.2. NM_201601.2.

UniGene

Mm.16340.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
4HWU	X-ray	2.90	A/B	45-127	[»]

ProteinModelPortal

P21803.

SMR

P21803. Positions 47-363, 467-806.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-6038N.

IntAct

P21803. 1 interaction.

PTM databases

PhosphoSite

P21803.

Proteomic databases

PaxDb

P21803.

PRIDE

P21803.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

GeneID

14183.

KEGG

mmu:14183.

Organism-specific databases

CTD

2263.

MGI

MGI:95523. Fgfr2.

Phylogenomic databases

eggNOG

COG0515.

HOGENOM

HOG000263410.

HOVERGEN

HBG000345.

InParanoid

P21803.

KO

K05093.

Enzyme and pathway databases

BRENDA

2.7.10.1. 3474.

Gene expression databases

CleanEx

MM_FGFR2.

Genevestigator

P21803.

GermOnline

ENSMUSG00000030849. Mus musculus.

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. 3 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

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Other

ChEMBL

CHEMBL3648.

ChiTaRS

FGFR2. mouse.

NextBio

285386.

SOURCE

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Entry information

Entry name

FGFR2_MOUSE

Accession

Primary (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:	May 1, 2013
This is version 139 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program