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P21803

- FGFR2_MOUSE

UniProt

P21803 - FGFR2_MOUSE

Protein

Fibroblast growth factor receptor 2

Gene

Fgfr2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 150 (01 Oct 2014)
      Sequence version 4 (01 Nov 1997)
      Previous versions | rss
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    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 STAT1.4 Publications

    Catalytic activityi

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

    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 By similarity.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei517 – 5171ATPPROSITE-ProRule annotation
    Binding sitei571 – 5711ATPPROSITE-ProRule annotation
    Active sitei626 – 6261Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi487 – 4959ATPPROSITE-ProRule annotation
    Nucleotide bindingi565 – 5673ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. fibroblast growth factor-activated receptor activity Source: InterPro
    3. fibroblast growth factor binding Source: MGI
    4. heparin binding Source: UniProtKB-KW
    5. protein binding Source: IntAct

    GO - Biological processi

    1. angiogenesis Source: MGI
    2. apoptotic process Source: UniProtKB-KW
    3. axonogenesis Source: MGI
    4. bone development Source: MGI
    5. bone mineralization Source: MGI
    6. bone morphogenesis Source: MGI
    7. branch elongation involved in salivary gland morphogenesis Source: MGI
    8. branching involved in labyrinthine layer morphogenesis Source: MGI
    9. branching involved in prostate gland morphogenesis Source: MGI
    10. branching involved in salivary gland morphogenesis Source: MGI
    11. branching morphogenesis of a nerve Source: MGI
    12. bud elongation involved in lung branching Source: MGI
    13. cell-cell signaling Source: MGI
    14. cell fate commitment Source: MGI
    15. coronal suture morphogenesis Source: MGI
    16. digestive tract development Source: MGI
    17. embryonic cranial skeleton morphogenesis Source: InterPro
    18. embryonic digestive tract morphogenesis Source: MGI
    19. embryonic organ development Source: MGI
    20. embryonic organ morphogenesis Source: MGI
    21. embryonic pattern specification Source: MGI
    22. endodermal digestive tract morphogenesis Source: MGI
    23. epidermis morphogenesis Source: MGI
    24. epithelial cell differentiation Source: MGI
    25. epithelial cell proliferation Source: MGI
    26. epithelial cell proliferation involved in salivary gland morphogenesis Source: MGI
    27. epithelial tube branching involved in lung morphogenesis Source: MGI
    28. fibroblast growth factor receptor signaling pathway Source: MGI
    29. fibroblast growth factor receptor signaling pathway involved in hemopoiesis Source: UniProtKB
    30. fibroblast growth factor receptor signaling pathway involved in mammary gland specification Source: MGI
    31. fibroblast growth factor receptor signaling pathway involved in negative regulation of apoptotic process in bone marrow Source: UniProtKB
    32. fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development Source: UniProtKB
    33. fibroblast growth factor receptor signaling pathway involved in positive regulation of cell proliferation in bone marrow Source: UniProtKB
    34. gland morphogenesis Source: MGI
    35. hair follicle morphogenesis Source: MGI
    36. inner ear morphogenesis Source: MGI
    37. in utero embryonic development Source: MGI
    38. lacrimal gland development Source: MGI
    39. lateral sprouting from an epithelium Source: MGI
    40. lens fiber cell development Source: MGI
    41. limb bud formation Source: MGI
    42. lung alveolus development Source: MGI
    43. lung-associated mesenchyme development Source: MGI
    44. lung development Source: MGI
    45. lung lobe morphogenesis Source: MGI
    46. mammary gland bud formation Source: MGI
    47. membranous septum morphogenesis Source: MGI
    48. mesenchymal cell differentiation Source: MGI
    49. mesenchymal cell differentiation involved in lung development Source: MGI
    50. mesenchymal cell proliferation involved in lung development Source: MGI
    51. midbrain development Source: MGI
    52. morphogenesis of embryonic epithelium Source: MGI
    53. multicellular organism growth Source: MGI
    54. negative regulation of cell proliferation Source: MGI
    55. negative regulation of mitosis Source: MGI
    56. negative regulation of transcription from RNA polymerase II promoter Source: MGI
    57. neuromuscular junction development Source: MGI
    58. odontogenesis Source: MGI
    59. orbitofrontal cortex development Source: UniProtKB
    60. organ growth Source: MGI
    61. organ morphogenesis Source: MGI
    62. otic vesicle formation Source: MGI
    63. outflow tract septum morphogenesis Source: MGI
    64. positive regulation of canonical Wnt signaling pathway Source: MGI
    65. positive regulation of cardiac muscle cell proliferation Source: MGI
    66. positive regulation of cell cycle Source: UniProtKB
    67. positive regulation of cell division Source: MGI
    68. positive regulation of cell proliferation Source: UniProtKB
    69. positive regulation of epithelial cell proliferation Source: MGI
    70. positive regulation of epithelial cell proliferation involved in lung morphogenesis Source: MGI
    71. positive regulation of ERK1 and ERK2 cascade Source: MGI
    72. positive regulation of mesenchymal cell proliferation Source: MGI
    73. positive regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    74. positive regulation of Wnt signaling pathway Source: MGI
    75. post-embryonic development Source: MGI
    76. prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis Source: MGI
    77. prostate epithelial cord elongation Source: MGI
    78. prostate gland morphogenesis Source: MGI
    79. pyramidal neuron development Source: UniProtKB
    80. regulation of branching involved in prostate gland morphogenesis Source: MGI
    81. regulation of cell fate commitment Source: MGI
    82. regulation of cell proliferation Source: MGI
    83. regulation of epithelial cell proliferation Source: MGI
    84. regulation of ERK1 and ERK2 cascade Source: MGI
    85. regulation of fibroblast growth factor receptor signaling pathway Source: MGI
    86. regulation of morphogenesis of a branching structure Source: MGI
    87. regulation of multicellular organism growth Source: MGI
    88. regulation of smoothened signaling pathway Source: MGI
    89. regulation of smooth muscle cell differentiation Source: MGI
    90. reproductive structure development Source: MGI
    91. squamous basal epithelial stem cell differentiation involved in prostate gland acinus development Source: MGI
    92. synaptic vesicle transport Source: MGI
    93. ureteric bud development Source: MGI
    94. vasculogenesis involved in coronary vascular morphogenesis Source: DFLAT
    95. ventricular cardiac muscle tissue morphogenesis Source: MGI
    96. ventricular zone neuroblast division Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Heparin-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor receptor 2 (EC:2.7.10.1)
    Short name:
    FGFR-2
    Alternative name(s):
    Keratinocyte growth factor receptor
    Short name:
    KGFR
    CD_antigen: CD332
    Gene namesi
    Name:Fgfr2
    Synonyms:Bek, Ect1
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Unplaced

    Organism-specific databases

    MGIiMGI:95523. Fgfr2.

    Subcellular locationi

    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.By similarity

    GO - Cellular componenti

    1. cytoplasmic membrane-bounded vesicle Source: UniProtKB-SubCell
    2. excitatory synapse Source: UniProtKB
    3. extracellular region Source: MGI
    4. Golgi apparatus Source: UniProtKB-SubCell
    5. integral component of membrane Source: UniProtKB-KW
    6. nucleus Source: MGI
    7. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    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.4 Publications

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi769 – 7691Y → F: Abolishes phosphorylation of FRS2 and activation of MAP kinases. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2121Add
    BLAST
    Chaini22 – 821800Fibroblast growth factor receptor 2PRO_0000016784Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi62 ↔ 107PROSITE-ProRule annotation
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi123 – 1231N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi147 – 1471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi179 ↔ 231PROSITE-ProRule annotation
    Glycosylationi228 – 2281N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi241 – 2411N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi265 – 2651N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi278 ↔ 342PROSITE-ProRule annotation
    Glycosylationi297 – 2971N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi318 – 3181N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi331 – 3311N-linked (GlcNAc...)Sequence Analysis
    Modified residuei466 – 4661Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei586 – 5861Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei588 – 5881Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei656 – 6561Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei657 – 6571Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei769 – 7691Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    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.By similarity
    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.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.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiP21803.
    PRIDEiP21803.

    PTM databases

    PhosphoSiteiP21803.

    Expressioni

    Gene expression databases

    CleanExiMM_FGFR2.
    GenevestigatoriP21803.

    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. 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.By similarity

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ncam1P135952EBI-6286942,EBI-774943

    Protein-protein interaction databases

    BioGridi199657. 2 interactions.
    DIPiDIP-6038N.
    IntActiP21803. 2 interactions.

    Structurei

    Secondary structure

    1
    821
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi48 – 525
    Beta strandi58 – 614
    Beta strandi69 – 746
    Beta strandi77 – 793
    Beta strandi83 – 886
    Beta strandi91 – 944
    Helixi99 – 1013
    Beta strandi103 – 1108
    Beta strandi115 – 12410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4HWUX-ray2.90A/B45-127[»]
    ProteinModelPortaliP21803.
    SMRiP21803. Positions 47-363, 462-801.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini22 – 377356ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini399 – 821423CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei378 – 39821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 125101Ig-like C2-type 1Add
    BLAST
    Domaini154 – 24794Ig-like C2-type 2Add
    BLAST
    Domaini256 – 358103Ig-like C2-type 3Add
    BLAST
    Domaini481 – 770290Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni161 – 17818Heparin-bindingBy similarityAdd
    BLAST

    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 By similarity.By similarity

    Sequence similaritiesi

    Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.PROSITE-ProRule annotation
    Contains 1 protein kinase domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Immunoglobulin domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0515.
    HOGENOMiHOG000263410.
    HOVERGENiHBG000345.
    InParanoidiP21803.
    KOiK05093.
    PhylomeDBiP21803.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR028175. 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]
    PANTHERiPTHR24416:SF130. PTHR24416:SF130. 1 hit.
    PfamiPF07679. I-set. 3 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000628. FGFR. 1 hit.
    PRINTSiPR00109. TYRKINASE.
    SMARTiSM00408. IGc2. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view]
    SUPFAMiSSF56112. SSF56112. 1 hit.
    PROSITEiPS50835. IG_LIKE. 3 hits.
    PS00107. PROTEIN_KINASE_ATP. 1 hit.
    PS50011. PROTEIN_KINASE_DOM. 1 hit.
    PS00109. PROTEIN_KINASE_TYR. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform Long (identifier: P21803-1) [UniParc]FASTAAdd to Basket

    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

    MVSWGRFICL VLVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEAY    50
    VVAPGESLEL QCMLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR 100
    DSGLYACTAA RTVDSETWIF MVNVTDAISS GDDEDDTDSS EDVVSENRSN 150
    QRAPYWTNTE KMEKRLHACP AANTVKFRCP AGGNPTSTMR WLKNGKEFKQ 200
    EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CLVENEYGSI NHTYHLDVVE 250
    RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK 300
    NGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI 350
    SFHSAWLTVL PAPVREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVIFCRM 400
    KTTTKKPDFS SQPAVHKLTK RIPLRRQVTV SAESSSSMNS NTPLVRITTR 450
    LSSTADTPML AGVSEYELPE DPKWEFPRDK LTLGKPLGEG CFGQVVMAEA 500
    VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM IGKHKNIINL 550
    LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF 600
    KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD 650
    INNIDYYKKT TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG 700
    GSPYPGIPVE ELFKLLKEGH RMDKPTNCTN ELYMMMRDCW HAVPSQRPTF 750
    KQLVEDLDRI LTLTTNEEYL DLTQPLEQYS PSYPDTSSSC SSGDDSVFSP 800
    DPMPYEPCLP QYPHINGSVK T 821
    Length:821
    Mass (Da):91,984
    Last modified:November 1, 1997 - v4
    Checksum:iFCDB28ADD61F4414
    GO
    Isoform Short (identifier: P21803-2) [UniParc]FASTAAdd to Basket

    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

    Show »
    Length:707
    Mass (Da):79,531
    Checksum:iE57F5804B12F667C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti53 – 531A → V in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti55 – 562GE → RG in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti90 – 901E → R in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti119 – 1191I → Y in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti142 – 1432DV → R in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti169 – 1691C → V in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti169 – 1691C → V in AAA39377. (PubMed:1846048)Curated
    Sequence conflicti187 – 1871S → P in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti187 – 1871S → P in AAA39377. (PubMed:1846048)Curated
    Sequence conflicti214 – 2141W → R in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti229 – 2291Y → I in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti275 – 2751E → R in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti301 – 3011N → Y in CAA39083. (PubMed:1711190)Curated
    Sequence conflicti301 – 3011N → Y in AAA39377. (PubMed:1846048)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei37 – 371E → G in isoform Short. 1 PublicationVSP_002985
    Alternative sequencei38 – 152115Missing in isoform Short. 1 PublicationVSP_002986Add
    BLAST
    Alternative sequencei314 – 36148AAGVN…LTVLP → HSGINSSNAEVLALFNVTEM DAGEYICKVSNYIGQANQSA WLTVLPKQQ in isoform Short. 1 PublicationVSP_002987Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    PIRiA38429.
    A44142. TVMSBK.
    S17295.
    RefSeqiNP_034337.2. NM_010207.2.
    NP_963895.2. NM_201601.2.
    UniGeneiMm.16340.

    Genome annotation databases

    GeneIDi14183.
    KEGGimmu:14183.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    PIRi A38429.
    A44142. TVMSBK.
    S17295.
    RefSeqi NP_034337.2. NM_010207.2.
    NP_963895.2. NM_201601.2.
    UniGenei Mm.16340.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4HWU X-ray 2.90 A/B 45-127 [» ]
    ProteinModelPortali P21803.
    SMRi P21803. Positions 47-363, 462-801.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199657. 2 interactions.
    DIPi DIP-6038N.
    IntActi P21803. 2 interactions.

    Chemistry

    ChEMBLi CHEMBL2111391.

    PTM databases

    PhosphoSitei P21803.

    Proteomic databases

    PaxDbi P21803.
    PRIDEi P21803.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 14183.
    KEGGi mmu:14183.

    Organism-specific databases

    CTDi 2263.
    MGIi MGI:95523. Fgfr2.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000263410.
    HOVERGENi HBG000345.
    InParanoidi P21803.
    KOi K05093.
    PhylomeDBi P21803.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.

    Miscellaneous databases

    ChiTaRSi FGFR2. mouse.
    NextBioi 285386.
    PROi P21803.
    SOURCEi Search...

    Gene expression databases

    CleanExi MM_FGFR2.
    Genevestigatori P21803.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR028175. 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 ]
    PANTHERi PTHR24416:SF130. PTHR24416:SF130. 1 hit.
    Pfami PF07679. I-set. 3 hits.
    PF07714. Pkinase_Tyr. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000628. FGFR. 1 hit.
    PRINTSi PR00109. TYRKINASE.
    SMARTi SM00408. IGc2. 3 hits.
    SM00219. TyrKc. 1 hit.
    [Graphical view ]
    SUPFAMi SSF56112. SSF56112. 1 hit.
    PROSITEi 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 ]
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    Publicationsi

    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. 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.

    Entry informationi

    Entry nameiFGFR2_MOUSE
    AccessioniPrimary (citable) accession number: P21803
    Secondary accession number(s): O55141, Q00389, Q61342
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 1, 1991
    Last sequence update: November 1, 1997
    Last modified: October 1, 2014
    This is version 150 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3