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Q03142 (FGFR4_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 147. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fibroblast growth factor receptor 4

Short name=FGFR-4
EC=2.7.10.1
Alternative name(s):
Protein-tyrosine kinase receptor MPK-11
CD_antigen=CD334
Gene names
Name:Fgfr4
Synonyms:Fgfr-4, Mpk-11
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length799 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8 Ref.10 Ref.12

Catalytic activity

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

Enzyme regulation

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.

Subunit structure

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. Ref.9

Subcellular location

Cell membrane; Single-pass type I membrane protein. 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. Ref.2

Tissue specificity

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. Ref.1 Ref.2

Developmental stage

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

Induction

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

Post-translational modification

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. Ref.2

Ubiquitinated. Subject to proteasomal degradation when not fully glycosylated By similarity. Ref.2

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. Ref.2

Disruption phenotype

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. Ref.6 Ref.7 Ref.8 Ref.10 Ref.12

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Endoplasmic reticulum
Endosome
Membrane
   Coding sequence diversityAlternative splicing
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processalveolar secondary septum development

Inferred from genetic interaction Ref.6. Source: MGI

cell migration

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

glucose homeostasis

Inferred from mutant phenotype Ref.8. Source: UniProtKB

lung development

Inferred from mutant phenotype PubMed 15576401. Source: MGI

organ induction

Inferred from mutant phenotype PubMed 15576401. Source: MGI

peptidyl-tyrosine phosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

phosphate ion homeostasis

Inferred from mutant phenotype Ref.12. Source: UniProtKB

positive regulation of DNA biosynthetic process

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of ERK1 and ERK2 cascade

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of cell proliferation

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of metalloenzyme activity

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of proteolysis

Inferred from sequence or structural similarity. Source: UniProtKB

protein autophosphorylation

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of bile acid biosynthetic process

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of cholesterol homeostasis

Inferred from mutant phenotype Ref.7. Source: UniProtKB

regulation of extracellular matrix disassembly

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of lipid metabolic process

Inferred from mutant phenotype Ref.8. Source: UniProtKB

   Cellular_componentcell-cell junction

Inferred from electronic annotation. Source: Ensembl

endoplasmic reticulum

Inferred from sequence or structural similarity. Source: UniProtKB

endosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral component of plasma membrane

Inferred from sequence or structural similarity. Source: UniProtKB

nucleus

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fibroblast growth factor binding

Inferred from sequence or structural similarity. Source: UniProtKB

fibroblast growth factor-activated receptor activity

Inferred from sequence or structural similarity. Source: UniProtKB

heparin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 16436388. Source: MGI

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q03142-1)

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.
Isoform 2 (identifier: Q03142-2)

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

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1616 Potential
Chain17 – 799783Fibroblast growth factor receptor 4
PRO_0000016788

Regions

Topological domain17 – 366350Extracellular Potential
Transmembrane367 – 38721Helical; Potential
Topological domain388 – 799412Cytoplasmic Potential
Domain17 – 11599Ig-like C2-type 1
Domain149 – 23789Ig-like C2-type 2
Domain246 – 346101Ig-like C2-type 3
Domain464 – 752289Protein kinase
Nucleotide binding470 – 4789ATP By similarity

Sites

Active site6091Proton acceptor By similarity
Binding site5001ATP By similarity

Amino acid modifications

Modified residue6391Phosphotyrosine; by autocatalysis By similarity
Modified residue6401Phosphotyrosine; by autocatalysis By similarity
Modified residue7511Phosphotyrosine; by autocatalysis By similarity
Glycosylation1091N-linked (GlcNAc...) Potential
Glycosylation2551N-linked (GlcNAc...) Potential
Glycosylation2871N-linked (GlcNAc...) Potential
Glycosylation3081N-linked (GlcNAc...) Ref.11
Glycosylation3191N-linked (GlcNAc...) Potential
Disulfide bond54 ↔ 98 By similarity
Disulfide bond169 ↔ 221 By similarity
Disulfide bond268 ↔ 330 By similarity

Natural variations

Alternative sequence670 – 71546Missing in isoform 2.
VSP_017545

Experimental info

Sequence conflict172 – 1732AG → CR in CAA42551. Ref.1
Sequence conflict3091S → I in CAA42551. Ref.1
Sequence conflict3131E → Q in CAA42551. Ref.1
Sequence conflict4741C → CFGQVVRAEA in CAA42551. Ref.1
Sequence conflict6731E → G in ABD43187. Ref.2
Sequence conflict6731E → G in BAC39292. Ref.3
Sequence conflict6731E → G in AAH33313. Ref.4
Sequence conflict7261A → V in AAH33313. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 21, 2006. Version 3.
Checksum: 799E17845CD4021E

FASTA79988,661
        10         20         30         40         50         60 
MWLLLALLSI FQGTPALSLE ASEEMEQEPC LAPILEQQEQ VLTVALGQPV RLCCGRTERG 

        70         80         90        100        110        120 
RHWYKEGSRL ASAGRVRGWR GRLEIASFLP EDAGRYLCLA RGSMTVVHNL TLLMDDSLTS 

       130        140        150        160        170        180 
ISNDEDPKTL SSSSSGHVYP QQAPYWTHPQ RMEKKLHAVP AGNTVKFRCP AAGNPMPTIH 

       190        200        210        220        230        240 
WLKDGQAFHG ENRIGGIRLR HQHWSLVMES VVPSDRGTYT CLVENSLGSI RYSYLLDVLE 

       250        260        270        280        290        300 
RSPHRPILQA GLPANTTAVV GSDVELLCKV YSDAQPHIQW LKHVVINGSS FGADGFPYVQ 

       310        320        330        340        350        360 
VLKTTDINSS EVEVLYLRNV SAEDAGEYTC LAGNSIGLSY QSAWLTVLPE EDLTWTTATP 

       370        380        390        400        410        420 
EARYTDIILY VSGSLVLLVL LLLAGVYHRQ VIRGHYSRQP VTIQKLSRFP LARQFSLESR 

       430        440        450        460        470        480 
SSGKSSLSLV RGVRLSSSGP PLLTGLVNLD LPLDPLWEFP RDRLVLGKPL GEGCFGQVVR 

       490        500        510        520        530        540 
AEAFGMDPSR PDQTSTVAVK MLKDNASDKD LADLVSEMEV MKLIGRHKNI INLLGVCTQE 

       550        560        570        580        590        600 
GPLYVIVECA AKGNLREFLR ARRPPGPDLS PDGPRSSEGP LSFPALVSCA YQVARGMQYL 

       610        620        630        640        650        660 
ESRKCIHRDL AARNVLVTED DVMKIADFGL ARGVHHIDYY KKTSNGRLPV KWMAPEALFD 

       670        680        690        700        710        720 
RVYTHQSDVW SFEILLWEIF TLGGSPYPGI PVEELFSLLR EGHRMERPPN CPSELYGLMR 

       730        740        750        760        770        780 
ECWHAAPSQR PTFKQLVEAL DKVLLAVSEE YLDLRLTFGP FSPSNGDASS TCSSSDSVFS 

       790 
HDPLPLEPSP FPFSDSQTT 

« Hide

Isoform 2 (Fgfr4 lacking exon 16) (Fgfr4(-16)) [UniParc].

Checksum: 511687E06090ED01
Show »

FASTA75383,335

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"BetaKlotho is required for metabolic activity of fibroblast growth factor 21."
Ogawa Y., Kurosu H., Yamamoto M., Nandi A., Rosenblatt K.P., Goetz R., Eliseenkova A.V., Mohammadi M., Kuro-o M.
Proc. Natl. Acad. Sci. U.S.A. 104:7432-7437(2007) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS26540.1. [Q03142-1]
PIRS18209.
RefSeqNP_032037.2. NM_008011.2.
UniGeneMm.276715.

3D structure databases

ProteinModelPortalQ03142.
SMRQ03142. Positions 18-352, 451-788.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid199660. 2 interactions.
DIPDIP-58508N.

Chemistry

ChEMBLCHEMBL2111391.

Protein family/group databases

MEROPSI43.001.

PTM databases

PhosphoSiteQ03142.

Proteomic databases

PaxDbQ03142.
PRIDEQ03142.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000005452; ENSMUSP00000005452; ENSMUSG00000005320.
GeneID14186.
KEGGmmu:14186.
UCSCuc007qqb.1. mouse. [Q03142-1]
uc011yzq.1. mouse. [Q03142-2]

Organism-specific databases

CTD2264.
MGIMGI:95525. Fgfr4.

Phylogenomic databases

eggNOGCOG0515.
GeneTreeENSGT00670000097694.
HOGENOMHOG000263410.
HOVERGENHBG000345.
InParanoidQ03142.
KOK05095.
OrthoDBEOG7NGQ9N.
PhylomeDBQ03142.
TreeFamTF316307.

Enzyme and pathway databases

BRENDA2.7.10.1. 3474.

Gene expression databases

BgeeQ03142.
CleanExMM_FGFR4.
GenevestigatorQ03142.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR016248. 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]
PfamPF07679. I-set. 2 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 2 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio285398.
PROQ03142.
SOURCESearch...

Entry information

Entry nameFGFR4_MOUSE
AccessionPrimary (citable) accession number: Q03142
Secondary accession number(s): Q27Q87 expand/collapse secondary AC list , Q5J7D9, Q8C3V5, Q8CIB8
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: March 21, 2006
Last modified: July 9, 2014
This is version 147 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot