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Q03142

- FGFR4_MOUSE

UniProt

Q03142 - FGFR4_MOUSE

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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

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

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
Complete GO annotation...

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_230708. Phospholipase C-mediated cascade.
REACT_234357. FRS2-mediated cascade.
REACT_240139. PI3K Cascade.
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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini17 – 366350ExtracellularSequence AnalysisAdd
BLAST
Transmembranei367 – 38721HelicalSequence AnalysisAdd
BLAST
Topological domaini388 – 799412CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

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

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...)1 Publication
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...

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.
GeneTreeiENSGT00760000118923.
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

        10         20         30         40         50
MWLLLALLSI FQGTPALSLE ASEEMEQEPC LAPILEQQEQ VLTVALGQPV
60 70 80 90 100
RLCCGRTERG RHWYKEGSRL ASAGRVRGWR GRLEIASFLP EDAGRYLCLA
110 120 130 140 150
RGSMTVVHNL TLLMDDSLTS ISNDEDPKTL SSSSSGHVYP QQAPYWTHPQ
160 170 180 190 200
RMEKKLHAVP AGNTVKFRCP AAGNPMPTIH WLKDGQAFHG ENRIGGIRLR
210 220 230 240 250
HQHWSLVMES VVPSDRGTYT CLVENSLGSI RYSYLLDVLE RSPHRPILQA
260 270 280 290 300
GLPANTTAVV GSDVELLCKV YSDAQPHIQW LKHVVINGSS FGADGFPYVQ
310 320 330 340 350
VLKTTDINSS EVEVLYLRNV SAEDAGEYTC LAGNSIGLSY QSAWLTVLPE
360 370 380 390 400
EDLTWTTATP EARYTDIILY VSGSLVLLVL LLLAGVYHRQ VIRGHYSRQP
410 420 430 440 450
VTIQKLSRFP LARQFSLESR SSGKSSLSLV RGVRLSSSGP PLLTGLVNLD
460 470 480 490 500
LPLDPLWEFP RDRLVLGKPL GEGCFGQVVR AEAFGMDPSR PDQTSTVAVK
510 520 530 540 550
MLKDNASDKD LADLVSEMEV MKLIGRHKNI INLLGVCTQE GPLYVIVECA
560 570 580 590 600
AKGNLREFLR ARRPPGPDLS PDGPRSSEGP LSFPALVSCA YQVARGMQYL
610 620 630 640 650
ESRKCIHRDL AARNVLVTED DVMKIADFGL ARGVHHIDYY KKTSNGRLPV
660 670 680 690 700
KWMAPEALFD RVYTHQSDVW SFEILLWEIF TLGGSPYPGI PVEELFSLLR
710 720 730 740 750
EGHRMERPPN CPSELYGLMR ECWHAAPSQR PTFKQLVEAL DKVLLAVSEE
760 770 780 790
YLDLRLTFGP FSPSNGDASS TCSSSDSVFS HDPLPLEPSP FPFSDSQTT
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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

BindingDBi Q03142.
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 ENSGT00760000118923.
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_230708. Phospholipase C-mediated cascade.
REACT_234357. FRS2-mediated cascade.
REACT_240139. PI3K Cascade.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 151 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