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P18460

- FGFR3_CHICK

UniProt

P18460 - FGFR3_CHICK

Protein

Fibroblast growth factor receptor 3

Gene

FGFR3

Organism
Gallus gallus (Chicken)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 122 (01 Oct 2014)
      Sequence version 1 (01 Nov 1990)
      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 and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required for normal skeleton development. Regulates both osteogenesis and postnatal bone mineralization by osteoblasts. Promotes apoptosis in chondrocytes, but can also promote cancer cell proliferation. Phosphorylates PLCG1, CBL and FRS2. 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 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 sitei502 – 5021ATPPROSITE-ProRule annotation
    Active sitei611 – 6111Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi472 – 4809ATPPROSITE-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. positive regulation of cell proliferation Source: InterPro
    3. skeletal system development 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. 1306.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor receptor 3 (EC:2.7.10.1)
    Short name:
    FGFR-3
    Alternative name(s):
    Tyrosine kinase receptor CEK2
    Gene namesi
    Name:FGFR3
    Synonyms:CEK2
    OrganismiGallus gallus (Chicken)
    Taxonomic identifieri9031 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeGallus
    ProteomesiUP000000539: Unplaced

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. plasma membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Membrane

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 806787Fibroblast growth factor receptor 3PRO_0000016790Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi61 ↔ 107PROSITE-ProRule annotation
    Glycosylationi83 – 831N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi118 – 1181N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi170 ↔ 222PROSITE-ProRule annotation
    Glycosylationi219 – 2191N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi256 – 2561N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi269 ↔ 333PROSITE-ProRule annotation
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi309 – 3091N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi322 – 3221N-linked (GlcNAc...)Sequence Analysis
    Modified residuei641 – 6411Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei642 – 6421Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei718 – 7181Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei754 – 7541Phosphotyrosine; 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

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein

    Proteomic databases

    PaxDbiP18460.

    Interactioni

    Subunit structurei

    Monomer. Homodimer after ligand binding By similarity.By similarity

    Protein-protein interaction databases

    STRINGi9031.ENSGALP00000001710.

    Structurei

    3D structure databases

    ProteinModelPortaliP18460.
    SMRiP18460. Positions 145-355, 453-750.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini20 – 364345ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini390 – 806417CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei365 – 38925HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini24 – 124101Ig-like C2-type 1Add
    BLAST
    Domaini150 – 23889Ig-like C2-type 2Add
    BLAST
    Domaini247 – 349103Ig-like C2-type 3Add
    BLAST
    Domaini466 – 755290Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi131 – 14111Asp/Glu-rich (highly acidic)Add
    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

    eggNOGiCOG0515.
    HOGENOMiHOG000263410.
    HOVERGENiHBG000345.
    InParanoidiP18460.
    KOiK05094.
    PhylomeDBiP18460.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR028176. FGF_rcpt_3.
    IPR016248. FGF_rcpt_fam.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR013151. Immunoglobulin.
    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:SF128. PTHR24416:SF128. 1 hit.
    PfamiPF07679. I-set. 2 hits.
    PF00047. ig. 1 hit.
    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.

    P18460-1 [UniParc]FASTAAdd to Basket

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    MRAAWGSVWC LCLAAAVGAL PAARRRGAER SGGQAAEYLR SETAFLEELV    50
    FGSGDTIELS CNTQSSSVSV FWFKDGIGIA PSNRTHIGQK LLKIINVSYD 100
    DSGLYSCKPR HSNEVLGNFT VRVTDSPSSG DDEDDDDESE DTGVPFWTRP 150
    DKMEKKLLAV PAANTVRFRC PAGGNPTPTI YWLKNGKEFK GEHRIGGIKL 200
    RHQQWSLVME SVVPSDRGNY TCVVENKYGN IRHTYQLDVL ERSPHRPILQ 250
    AGLPANQTVV VGSNVEFHCK VYSDAQPHIQ WLKHVEVNGS KYGPDGTPYV 300
    TVLKTAGVNT TDKELEILYL RNVTFEDAGE YTCLAGNSIG FSHHSAWLTV 350
    LPAEELMEMD DSGSVYAGIL SYGTGLVLFI LVLVIVIICR MKMPNKKAMN 400
    TTTVQKVSKF PLKRQQVSLE SNSSMNSNTP LVRITRLSSS DGPMLANVSE 450
    LELPPDPKWE LARSRLTLGK PLGEGCFGQV VMAEAIGIDK DKPNKAITVA 500
    VKMLKDDATD KDLSDLVSEM EMMKMIGKHK NIINLLGACT QDGPLYVLVE 550
    YASKGNLREY LRARRPPGMD YSFDTCKLPE EQLTFKDLVS CAYQVARGME 600
    YLASQKCIHR DLAARNVLVT EDNVMKIADF GLARDVHNID YYKKTTNGRL 650
    PVKWMAPEAL FDRVYTHQSD VWSFGVLLWE IFTLGGSPYP GIPVEELFKL 700
    LKEGHRMDKP ANCTHDLYMI MRECWHAVPS QRPTFKQLVE DLDRVLTMTS 750
    TDEYLDLSVP FEQYSPAGQD THSTCSSGDD SVFAHDLLPD EPCLPKHVPC 800
    NGVIRT 806
    Length:806
    Mass (Da):89,730
    Last modified:November 1, 1990 - v1
    Checksum:iB38B3C6D5F2314B6
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35195 mRNA. Translation: AAA48664.1.
    PIRiA35963.
    RefSeqiNP_990840.2. NM_205509.2.
    UniGeneiGga.14066.

    Genome annotation databases

    GeneIDi396515.
    KEGGigga:396515.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M35195 mRNA. Translation: AAA48664.1 .
    PIRi A35963.
    RefSeqi NP_990840.2. NM_205509.2.
    UniGenei Gga.14066.

    3D structure databases

    ProteinModelPortali P18460.
    SMRi P18460. Positions 145-355, 453-750.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 9031.ENSGALP00000001710.

    Proteomic databases

    PaxDbi P18460.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 396515.
    KEGGi gga:396515.

    Organism-specific databases

    CTDi 2261.

    Phylogenomic databases

    eggNOGi COG0515.
    HOGENOMi HOG000263410.
    HOVERGENi HBG000345.
    InParanoidi P18460.
    KOi K05094.
    PhylomeDBi P18460.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 1306.

    Miscellaneous databases

    NextBioi 20816552.
    PROi P18460.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi IPR028176. FGF_rcpt_3.
    IPR016248. FGF_rcpt_fam.
    IPR007110. Ig-like_dom.
    IPR013783. Ig-like_fold.
    IPR013098. Ig_I-set.
    IPR003598. Ig_sub2.
    IPR013151. Immunoglobulin.
    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:SF128. PTHR24416:SF128. 1 hit.
    Pfami PF07679. I-set. 2 hits.
    PF00047. ig. 1 hit.
    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. "A distinctive family of embryonic protein-tyrosine kinase receptors."
      Pasquale E.B.
      Proc. Natl. Acad. Sci. U.S.A. 87:5812-5816(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiFGFR3_CHICK
    AccessioniPrimary (citable) accession number: P18460
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1990
    Last sequence update: November 1, 1990
    Last modified: October 1, 2014
    This is version 122 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3