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Q03364

- FGFR2_XENLA

UniProt

Q03364 - FGFR2_XENLA

Protein

Fibroblast growth factor receptor 2

Gene

fgfr2

Organism
Xenopus laevis (African clawed frog)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 112 (01 Oct 2014)
      Sequence version 1 (01 Jun 1994)
      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, 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 By similarity.By similarity

    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 sitei507 – 5071ATPPROSITE-ProRule annotation
    Binding sitei561 – 5611ATPPROSITE-ProRule annotation
    Active sitei616 – 6161Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi477 – 4859ATPPROSITE-ProRule annotation
    Nucleotide bindingi555 – 5573ATPPROSITE-ProRule annotation

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. fibroblast growth factor-activated receptor activity Source: InterPro

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. embryonic cranial skeleton morphogenesis Source: InterPro
    3. positive regulation of cell proliferation Source: InterPro

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Biological processi

    Apoptosis

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 6726.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor receptor 2 (EC:2.7.10.1)
    Short name:
    FGFR-2
    Gene namesi
    Name:fgfr2
    OrganismiXenopus laevis (African clawed frog)
    Taxonomic identifieri8355 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiAmphibiaBatrachiaAnuraPipoideaPipidaeXenopodinaeXenopusXenopus

    Organism-specific databases

    XenbaseiXB-GENE-1018301. 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. Golgi apparatus Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cytoplasmic vesicle, Golgi apparatus, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1414Add
    BLAST
    Chaini15 – 813799Fibroblast growth factor receptor 2PRO_0000016793Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi58 ↔ 103PROSITE-ProRule annotation
    Glycosylationi79 – 791N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi115 – 1151N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi170 ↔ 221PROSITE-ProRule annotation
    Glycosylationi231 – 2311N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi268 ↔ 332PROSITE-ProRule annotation
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi308 – 3081N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi321 – 3211N-linked (GlcNAc...)Sequence Analysis
    Modified residuei456 – 4561Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei576 – 5761Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei646 – 6461Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei647 – 6471Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei759 – 7591Phosphotyrosine; 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

    PRIDEiQ03364.

    Expressioni

    Tissue specificityi

    Expressed in the anterior neural plate in early neurula stage embryos. Later in development, the protein is also expressed in the eye anlagen, midbrain-hindbrain boundary and otic vesicle.

    Interactioni

    Subunit structurei

    Monomer. Homodimer after ligand binding By similarity.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ03364.
    SMRiQ03364. Positions 141-353, 458-755.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini18 – 367350ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini389 – 813425CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei368 – 38821HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini21 – 11797Ig-like C2-type 1Add
    BLAST
    Domaini145 – 23793Ig-like C2-type 2Add
    BLAST
    Domaini246 – 348103Ig-like C2-type 3Add
    BLAST
    Domaini471 – 760290Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni152 – 16918Heparin-bindingBy similarityAdd
    BLAST

    Domaini

    The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans.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

    HOVERGENiHBG000345.

    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. 2 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]

    Sequencei

    Sequence statusi: Complete.

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

    Q03364-1 [UniParc]FASTAAdd to Basket

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    MLLLALLAFL LVSRTIARPS YSMVDDTTPE PEEPPAKYQI SKADVFPVLP    50
    GEPLDLRCPL ADGPLVTWTK DGAKLEVNNR TLIVRTYLQI KESTTRDSGL 100
    YACSVLKNSH FFHVNVTEAS SSGDDEDDND GSEDFTNDNN NIRAPYWTNT 150
    EKMEKKLHAV SAANTVKLRC PAREPHPSNE WLKNGKEFKQ EHRIGGYKVR 200
    NQHWSLIMES VVPSDKGIYT CIVENEHGSI NHTYHLDVIE RSSHRPILQA 250
    GLPANTTAVV GGDAEFVCKV YSDAQPHIRW VRYIEKNGSR FGVDGLPYFK 300
    VLKAAGVNVT DEEIEVLYVR NVSFEDAGEY TCIAGNSIGI SQHSAWLTVH 350
    PAPVNPLEDN PVPYYMEIGI YSTGIFIIFC MVVVCVVCRM RQGAKKKKNF 400
    TGPPVHKLTK RIPLHRQVTV SADSSSSMNS TTPLVRITTR LLNSTDAMPL 450
    ANVSEYELPH DPMWEFSRDK LTLGKPLGEG CFGQVVMAEA LGIDKERPKE 500
    SVTVAVKMLK DNATEKDLAD LVSEMEMMKM IGKHKNIINL LGACTQGGTL 550
    YVIVEYAAKG NLRQYLRARR PLEMEYSFDV TRVPDEQMTF KDLVSCTYQI 600
    ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD VNNIDYYKKT 650
    SNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE 700
    ELFKLLKEGH RMDKPANCTN ELYMMMRDCW HAIPSHRPTF KQLVEDLDRI 750
    LTLTTNEEYL DLSAPLEQYS PSFPDSSCSA SSSSGDDSVF SPDPMPHDPC 800
    LPKFQHVNGV VKT 813
    Length:813
    Mass (Da):91,340
    Last modified:June 1, 1994 - v1
    Checksum:i815436569892A565
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65943 mRNA. Translation: CAA46758.1.
    PIRiA49123.
    UniGeneiXl.16135.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X65943 mRNA. Translation: CAA46758.1 .
    PIRi A49123.
    UniGenei Xl.16135.

    3D structure databases

    ProteinModelPortali Q03364.
    SMRi Q03364. Positions 141-353, 458-755.
    ModBasei Search...
    MobiDBi Search...

    Proteomic databases

    PRIDEi Q03364.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Organism-specific databases

    Xenbasei XB-GENE-1018301. fgfr2.

    Phylogenomic databases

    HOVERGENi HBG000345.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 6726.

    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. 2 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 ]
    ProtoNeti Search...

    Publicationsi

    1. "Spatially restricted expression of fibroblast growth factor receptor-2 during Xenopus development."
      Friesel R., Brown S.A.N.
      Development 116:1051-1058(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiFGFR2_XENLA
    AccessioniPrimary (citable) accession number: Q03364
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 1, 1994
    Last sequence update: June 1, 1994
    Last modified: October 1, 2014
    This is version 112 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3