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Q03142

- FGFR4_MOUSE

UniProt

Q03142 - FGFR4_MOUSE

Protein

Fibroblast growth factor receptor 4

Gene

Fgfr4

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 149 (01 Oct 2014)
      Sequence version 3 (21 Mar 2006)
      Previous versions | rss
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    Functioni

    Tyrosine-protein kinase that acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration, and in regulation of lipid metabolism, bile acid biosynthesis, glucose uptake, vitamin D metabolism and phosphate homeostasis. Required for normal down-regulation of the expression of CYP7A1, the rate-limiting enzyme in bile acid synthesis, in response to FGF19. Phosphorylates PLCG1 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. Promotes SRC-dependent phosphorylation of the matrix protease MMP14 and its lysosomal degradation. FGFR4 signaling is down-regulated by receptor internalization and degradation; MMP14 promotes internalization and degradation of FGFR4. Plays a role in postnatal lung development. May be involved in the development of skeletal muscle cell lineages.5 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 sitei500 – 5001ATPPROSITE-ProRule annotation
    Active sitei609 – 6091Proton acceptorPROSITE-ProRule annotation

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi470 – 4789ATPPROSITE-ProRule annotation

    GO - Molecular functioni

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

    GO - Biological processi

    1. alveolar secondary septum development Source: MGI
    2. cell migration Source: UniProtKB
    3. fibroblast growth factor receptor signaling pathway Source: UniProtKB
    4. glucose homeostasis Source: UniProtKB
    5. lung development Source: MGI
    6. organ induction Source: MGI
    7. peptidyl-tyrosine phosphorylation Source: UniProtKB
    8. phosphate ion homeostasis Source: UniProtKB
    9. positive regulation of cell proliferation Source: UniProtKB
    10. positive regulation of DNA biosynthetic process Source: UniProtKB
    11. positive regulation of ERK1 and ERK2 cascade Source: UniProtKB
    12. positive regulation of metalloenzyme activity Source: UniProtKB
    13. positive regulation of proteolysis Source: UniProtKB
    14. protein autophosphorylation Source: UniProtKB
    15. regulation of bile acid biosynthetic process Source: UniProtKB
    16. regulation of cholesterol homeostasis Source: UniProtKB
    17. regulation of extracellular matrix disassembly Source: UniProtKB
    18. regulation of lipid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Kinase, Receptor, Transferase, Tyrosine-protein kinase

    Keywords - Ligandi

    ATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.10.1. 3474.
    ReactomeiREACT_196455. Signaling by FGFR mutants.
    REACT_196510. Signaling by FGFR4 mutants.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_199063. betaKlotho-mediated ligand binding.
    REACT_206694. FGFR4 ligand binding and activation.
    REACT_223993. PI-3K cascade.
    REACT_226341. PIP3 activates AKT signaling.
    REACT_94437. SHC-mediated cascade.

    Protein family/group databases

    MEROPSiI43.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Fibroblast growth factor receptor 4 (EC:2.7.10.1)
    Short name:
    FGFR-4
    Alternative name(s):
    Protein-tyrosine kinase receptor MPK-11
    CD_antigen: CD334
    Gene namesi
    Name:Fgfr4
    Synonyms:Fgfr-4, Mpk-11
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 13

    Organism-specific databases

    MGIiMGI:95525. Fgfr4.

    Subcellular locationi

    Cell membrane 1 Publication; Single-pass type I membrane protein 1 Publication. Endosome By similarity. Endoplasmic reticulum By similarity
    Note: Internalized from the cell membrane to recycling endosomes, and from there back to the cell membrane.By similarity

    GO - Cellular componenti

    1. cell-cell junction Source: Ensembl
    2. endoplasmic reticulum Source: UniProtKB
    3. endosome Source: UniProtKB-SubCell
    4. integral component of plasma membrane Source: UniProtKB
    5. nucleus Source: Ensembl

    Keywords - Cellular componenti

    Cell membrane, Endoplasmic reticulum, Endosome, Membrane

    Pathology & Biotechi

    Disruption phenotypei

    No visible phenotype. Mice display an elevated bile acid pool and elevated excretion of bile acids, due to loss of normal regulation of CYP7A1, the rate-limiting enzyme in bile acid synthesis. When on a normal diet, mice are prone to develop increased levels of white adipose tissue, hyperlipidemia, hypercholesterolemia, glucose intolerance and insulin resistance. Mice lacking both FGFR3 and FGFR4 display pronounced dwarfism, and while their lungs appear normal at birth, they are completely blocked in alveogenesis and do not form secondary septae to delimit alveoli. These mice also show elevated serum levels of 1,25-dihydroxyvitamin D3 and reduced serum phosphorus levels.5 Publications

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1616Sequence AnalysisAdd
    BLAST
    Chaini17 – 799783Fibroblast growth factor receptor 4PRO_0000016788Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 98PROSITE-ProRule annotation
    Glycosylationi109 – 1091N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi169 ↔ 221PROSITE-ProRule annotation
    Glycosylationi255 – 2551N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi268 ↔ 330PROSITE-ProRule annotation
    Glycosylationi287 – 2871N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi308 – 3081N-linked (GlcNAc...)2 Publications
    Glycosylationi319 – 3191N-linked (GlcNAc...)Sequence Analysis
    Modified residuei639 – 6391Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei640 – 6401Phosphotyrosine; by autocatalysisBy similarity
    Modified residuei751 – 7511Phosphotyrosine; by autocatalysisBy similarity

    Post-translational modificationi

    N-glycosylated. Isoform 1 and isoform 2 are glycosylated. Full maturation of the glycan chains in the Golgi is essential for high affinity interaction with FGF19 By similarity.By similarity
    Ubiquitinated. Subject to proteasomal degradation when not fully glycosylated By similarity.By similarity
    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. Isoform 1 and isoform 2 are phosphorylated on tyrosine residues By similarity.By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PaxDbiQ03142.
    PRIDEiQ03142.

    PTM databases

    PhosphoSiteiQ03142.

    Expressioni

    Tissue specificityi

    Isoform 1 and isoform 2 are expressed in lung and proliferating myoblasts and myotubes of primary myogenic cells (at protein level). Isoform 1 and isoform 2 are expressed in liver, muscle, spleen, heart, lung, kidney and in primary myogenic cells.2 Publications

    Developmental stagei

    Expressed in the developing gut endoderm, in myotomally derived skeletal muscle, the adrenal cortex, kidney and condensing cartilage.1 Publication

    Inductioni

    Isoform 1 and isoform 2 are up-regulated by estradiol during myogenic differentiation and down-regulated in fully developed myotubes.1 Publication

    Gene expression databases

    BgeeiQ03142.
    CleanExiMM_FGFR4.
    GenevestigatoriQ03142.

    Interactioni

    Subunit structurei

    Monomer. Homodimer after ligand binding. Interacts with FGF1, FGF2, FGF4, FGF6, FGF8, FGF9, FGF16, FGF17, FGF18, FGF19, FGF21 and FGF23 (in vitro). Binding affinity for FGF family members is enhanced by interactions between FGFs and heparan sulfate proteoglycans. Interacts with KLB; this strongly increases the affinity for FGF19 and FGF23. Affinity for FGF19 is strongly increased by KLB and sulfated glycosaminoglycans. KLB and KL both interact with the core-glycosylated FGFR4 in the endoplasmic reticulum and promote its degradation, so that only FGFR4 with fully mature N-glycans is expressed at the cell surface. Identified in a complex with NCAM1, CDH2, PLCG1, FRS2, SRC, SHC1, GAP43 and CTTN. Interacts with MMP14 and HIP1 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi199660. 2 interactions.
    DIPiDIP-58508N.

    Structurei

    3D structure databases

    ProteinModelPortaliQ03142.
    SMRiQ03142. Positions 18-352, 451-788.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini17 – 366350ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini388 – 799412CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei367 – 38721HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 11599Ig-like C2-type 1Add
    BLAST
    Domaini149 – 23789Ig-like C2-type 2Add
    BLAST
    Domaini246 – 346101Ig-like C2-type 3Add
    BLAST
    Domaini464 – 752289Protein kinasePROSITE-ProRule annotationAdd
    BLAST

    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.
    GeneTreeiENSGT00670000097694.
    HOGENOMiHOG000263410.
    HOVERGENiHBG000345.
    InParanoidiQ03142.
    KOiK05095.
    OrthoDBiEOG7NGQ9N.
    PhylomeDBiQ03142.
    TreeFamiTF316307.

    Family and domain databases

    Gene3Di2.60.40.10. 3 hits.
    InterProiIPR016248. 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]
    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. 2 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 1 (identifier: Q03142-1) [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

    MWLLLALLSI FQGTPALSLE ASEEMEQEPC LAPILEQQEQ VLTVALGQPV    50
    RLCCGRTERG RHWYKEGSRL ASAGRVRGWR GRLEIASFLP EDAGRYLCLA 100
    RGSMTVVHNL TLLMDDSLTS ISNDEDPKTL SSSSSGHVYP QQAPYWTHPQ 150
    RMEKKLHAVP AGNTVKFRCP AAGNPMPTIH WLKDGQAFHG ENRIGGIRLR 200
    HQHWSLVMES VVPSDRGTYT CLVENSLGSI RYSYLLDVLE RSPHRPILQA 250
    GLPANTTAVV GSDVELLCKV YSDAQPHIQW LKHVVINGSS FGADGFPYVQ 300
    VLKTTDINSS EVEVLYLRNV SAEDAGEYTC LAGNSIGLSY QSAWLTVLPE 350
    EDLTWTTATP EARYTDIILY VSGSLVLLVL LLLAGVYHRQ VIRGHYSRQP 400
    VTIQKLSRFP LARQFSLESR SSGKSSLSLV RGVRLSSSGP PLLTGLVNLD 450
    LPLDPLWEFP RDRLVLGKPL GEGCFGQVVR AEAFGMDPSR PDQTSTVAVK 500
    MLKDNASDKD LADLVSEMEV MKLIGRHKNI INLLGVCTQE GPLYVIVECA 550
    AKGNLREFLR ARRPPGPDLS PDGPRSSEGP LSFPALVSCA YQVARGMQYL 600
    ESRKCIHRDL AARNVLVTED DVMKIADFGL ARGVHHIDYY KKTSNGRLPV 650
    KWMAPEALFD RVYTHQSDVW SFEILLWEIF TLGGSPYPGI PVEELFSLLR 700
    EGHRMERPPN CPSELYGLMR ECWHAAPSQR PTFKQLVEAL DKVLLAVSEE 750
    YLDLRLTFGP FSPSNGDASS TCSSSDSVFS HDPLPLEPSP FPFSDSQTT 799
    Length:799
    Mass (Da):88,661
    Last modified:March 21, 2006 - v3
    Checksum:i799E17845CD4021E
    GO
    Isoform 2 (identifier: Q03142-2) [UniParc]FASTAAdd to Basket

    Also known as: Fgfr4 lacking exon 16, Fgfr4(-16)

    The sequence of this isoform differs from the canonical sequence as follows:
         670-715: Missing.

    Show »
    Length:753
    Mass (Da):83,335
    Checksum:i511687E06090ED01
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti172 – 1732AG → CR in CAA42551. (PubMed:1723680)Curated
    Sequence conflicti309 – 3091S → I in CAA42551. (PubMed:1723680)Curated
    Sequence conflicti313 – 3131E → Q in CAA42551. (PubMed:1723680)Curated
    Sequence conflicti474 – 4741C → CFGQVVRAEA in CAA42551. (PubMed:1723680)Curated
    Sequence conflicti673 – 6731E → G in ABD43187. (PubMed:18186042)Curated
    Sequence conflicti673 – 6731E → G in BAC39292. (PubMed:16141072)Curated
    Sequence conflicti673 – 6731E → G in AAH33313. (PubMed:15489334)Curated
    Sequence conflicti726 – 7261A → V in AAH33313. (PubMed:15489334)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei670 – 71546Missing in isoform 2. 1 PublicationVSP_017545Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59927 mRNA. Translation: CAA42551.1.
    DQ388428 mRNA. Translation: ABD43187.1.
    AY493377 mRNA. Translation: AAS72387.2.
    AK084850 mRNA. Translation: BAC39292.1.
    BC033313 mRNA. Translation: AAH33313.1.
    X57236 mRNA. Translation: CAA40512.1.
    CCDSiCCDS26540.1. [Q03142-1]
    PIRiS18209.
    RefSeqiNP_032037.2. NM_008011.2.
    UniGeneiMm.276715.

    Genome annotation databases

    EnsembliENSMUST00000005452; ENSMUSP00000005452; ENSMUSG00000005320.
    GeneIDi14186.
    KEGGimmu:14186.
    UCSCiuc007qqb.1. mouse. [Q03142-1]
    uc011yzq.1. mouse. [Q03142-2]

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X59927 mRNA. Translation: CAA42551.1 .
    DQ388428 mRNA. Translation: ABD43187.1 .
    AY493377 mRNA. Translation: AAS72387.2 .
    AK084850 mRNA. Translation: BAC39292.1 .
    BC033313 mRNA. Translation: AAH33313.1 .
    X57236 mRNA. Translation: CAA40512.1 .
    CCDSi CCDS26540.1. [Q03142-1 ]
    PIRi S18209.
    RefSeqi NP_032037.2. NM_008011.2.
    UniGenei Mm.276715.

    3D structure databases

    ProteinModelPortali Q03142.
    SMRi Q03142. Positions 18-352, 451-788.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 199660. 2 interactions.
    DIPi DIP-58508N.

    Chemistry

    ChEMBLi CHEMBL2111391.

    Protein family/group databases

    MEROPSi I43.001.

    PTM databases

    PhosphoSitei Q03142.

    Proteomic databases

    PaxDbi Q03142.
    PRIDEi Q03142.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000005452 ; ENSMUSP00000005452 ; ENSMUSG00000005320 .
    GeneIDi 14186.
    KEGGi mmu:14186.
    UCSCi uc007qqb.1. mouse. [Q03142-1 ]
    uc011yzq.1. mouse. [Q03142-2 ]

    Organism-specific databases

    CTDi 2264.
    MGIi MGI:95525. Fgfr4.

    Phylogenomic databases

    eggNOGi COG0515.
    GeneTreei ENSGT00670000097694.
    HOGENOMi HOG000263410.
    HOVERGENi HBG000345.
    InParanoidi Q03142.
    KOi K05095.
    OrthoDBi EOG7NGQ9N.
    PhylomeDBi Q03142.
    TreeFami TF316307.

    Enzyme and pathway databases

    BRENDAi 2.7.10.1. 3474.
    Reactomei REACT_196455. Signaling by FGFR mutants.
    REACT_196510. Signaling by FGFR4 mutants.
    REACT_196588. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_198525. Negative regulation of FGFR signaling.
    REACT_199063. betaKlotho-mediated ligand binding.
    REACT_206694. FGFR4 ligand binding and activation.
    REACT_223993. PI-3K cascade.
    REACT_226341. PIP3 activates AKT signaling.
    REACT_94437. SHC-mediated cascade.

    Miscellaneous databases

    NextBioi 285398.
    PROi Q03142.
    SOURCEi Search...

    Gene expression databases

    Bgeei Q03142.
    CleanExi MM_FGFR4.
    Genevestigatori Q03142.

    Family and domain databases

    Gene3Di 2.60.40.10. 3 hits.
    InterProi 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 ]
    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. 2 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. "FGFR-4, a new member of the fibroblast growth factor receptor family, expressed in the definitive endoderm and skeletal muscle lineages of the mouse."
      Stark K.L., McMahon J., McMahon A.P.
      Development 113:641-651(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: CD-1.
      Tissue: Fetal cerebellum.
    2. "FGFR4 and its novel splice form in myogenic cells: interplay of glycosylation and tyrosine phosphorylation."
      Kwiatkowski B.A., Kirillova I., Richard R.E., Israeli D., Yablonka-Reuveni Z.
      J. Cell. Physiol. 215:803-817(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PHOSPHORYLATION, GLYCOSYLATION, SUBCELLULAR LOCATION, INDUCTION, TISSUE SPECIFICITY.
      Strain: C57BL/6.
      Tissue: Myoblast.
    3. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: C57BL/6J.
      Tissue: Lung.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Strain: FVB/N.
      Tissue: Liver.
    5. "An Eph-related receptor protein tyrosine kinase gene segmentally expressed in the developing mouse hindbrain."
      Gilardi-Hebenstreit P., Nieto M.A., Frain M., Mattei M.-G., Chestier A., Wilkinson D.G., Charnay P.
      Oncogene 7:2499-2506(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 611-667 (ISOFORMS 1/2).
      Strain: C57BL/6.
      Tissue: Embryonic brain.
    6. "FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in the murine lung."
      Weinstein M., Xu X., Ohyama K., Deng C.X.
      Development 125:3615-3623(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    7. "Elevated cholesterol metabolism and bile acid synthesis in mice lacking membrane tyrosine kinase receptor FGFR4."
      Yu C., Wang F., Kan M., Jin C., Jones R.B., Weinstein M., Deng C.X., McKeehan W.L.
      J. Biol. Chem. 275:15482-15489(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN REGULATION OF CHOLESTEROL METABOLISM AND BILE ACID SYNTHESIS.
    8. "FGFR4 prevents hyperlipidemia and insulin resistance but underlies high-fat diet induced fatty liver."
      Huang X., Yang C., Luo Y., Jin C., Wang F., McKeehan W.L.
      Diabetes 56:2501-2510(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    9. Cited for: INTERACTION WITH KLB.
    10. "FGF15/FGFR4 integrates growth factor signaling with hepatic bile acid metabolism and insulin action."
      Shin D.J., Osborne T.F.
      J. Biol. Chem. 284:11110-11120(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION.
    11. "The mouse C2C12 myoblast cell surface N-linked glycoproteome: identification, glycosite occupancy, and membrane orientation."
      Gundry R.L., Raginski K., Tarasova Y., Tchernyshyov I., Bausch-Fluck D., Elliott S.T., Boheler K.R., Van Eyk J.E., Wollscheid B.
      Mol. Cell. Proteomics 8:2555-2569(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-308.
      Tissue: Myoblast.
    12. "Regulation of serum 1,25(OH)2Vitamin D3 levels by fibroblast growth factor 23 is mediated by FGF receptors 3 and 4."
      Gattineni J., Twombley K., Goetz R., Mohammadi M., Baum M.
      Am. J. Physiol. 301:F371-F377(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: DISRUPTION PHENOTYPE, FUNCTION IN VITAMIN D AND PHOSPHATE HOMEOSTASIS.

    Entry informationi

    Entry nameiFGFR4_MOUSE
    AccessioniPrimary (citable) accession number: Q03142
    Secondary accession number(s): Q27Q87
    , Q5J7D9, Q8C3V5, Q8CIB8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1994
    Last sequence update: March 21, 2006
    Last modified: October 1, 2014
    This is version 149 of the entry and version 3 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. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Human and mouse protein kinases
      Human and mouse protein kinases: classification and index
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3