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FGFR4 (fibroblast growth factor receptor 4)

Written2012-05Alberto Peláez-García, Rodrigo Barderas, J Ignacio Casal
Functional Proteomics Laboratory, Centro de Investigaciones Biologicas (CIB-CSIC), 28040 Madrid, Spain (APG, JIC); Departamento Bioquimica y Biologia Molecular I, Universidad Complutense de Madrid, 28040 Madrid, Spain (RB)

(Note : for Links provided by Atlas : click)


Alias (NCBI)CD334
HGNC Alias symbJTK2
LocusID (NCBI) 2264
Atlas_Id 512
Location 5q35.2  [Link to chromosome band 5q35]
Location_base_pair Starts at 177086915 and ends at 177098144 bp from pter ( according to GRCh38/hg38-Dec_2013)  [Mapping FGFR4.png]
Fusion genes
(updated 2017)
Data from Atlas, Mitelman, Cosmic Fusion, Fusion Cancer, TCGA fusion databases with official HUGO symbols (see references in chromosomal bands)
FGFR4 (5q35.2)::ABL1 (9q34.12)FGFR4 (5q35.2)::MALAT1 (11q13.1)


  FGFR4 comprises an extracellular domain, a transmembrane domain, and an intracellular domain. FGFR4 alternative splicing has been described, with up to 18 different transcripts ranging from 552 to 3559 bp, (evidence of 11 transcripts at protein level ranging from 87 to 1030 aminoacids).
Description The DNA was cloned in 1991 (Partanen et al., 1991).
18.9 Kb; 18 exons.
Transcription 3.1 Kb mRNA; alternative splicing gives rise to 18 transcripts with evidence of 11 transcripts at protein level.


  Analysis of the expression of FGFR4 in SW480 colorectal cancer cells by Confocal Microscopy. FGFR4 was detected in plasma membrane, cytoplasm and nucleus. The 4',6-diamidino-2-phenylindole (DAPI) was used to detect the nucleus of the cells in blue. Representative micrographs show FGFR4 in green and F-actin (TRITC-phalloidin) in red.
Description The canonical sequence possesses 802 amino acids, 120 kDa, contains a signal peptide 1-17 amino acids, an extracellular domain with 3 Ig-like loops, a transmembrane domain with 26 amino acids and an intracellular domain with tyrosine kinase activity.
Transcripts lacking the intracellular domain and transmembrane domain are secreted.
Expression FGFR4 is expressed in a tissue-specific manner during embryogenesis and displays unique affinity for certain FGF ligands (FGF1, FGF2, FGF4, FGF6, FGF8, FGF9, FGF16, FGF17, FGF18 and FGF19). FGFR4 function is not essential during embryogenesis and adult life (Weinstein et al., 1998), though it may be involved in several metabolic pathways (Gutierrez et al., 2006; Yu et al., 2000).
Evidence of FGFR4 expression has been described at: adrenal cortex, adrenal gland, bile duct, cervix, cornea, corneal endothelial cell, corneal epithelial cell, heart, hepatocyte, intestine, islets of langerhans, kidney, lamina propria, liver, lung, lymph node, mammary gland, muscle, muscularis mucosa, ovary, pituitary gland, renal tubular epithelium, retina, skin, spleen, stomach, sublingual gland, ureter, urothelium and uterus (
Localisation Plasma membrane, but also some FGF-FGFR complexed are endocytosed and develop its function directly in the cytosol or nucleus.
FGFR4 isoform 2 may be secreted.
Function FGF receptor with tyrosine-protein kinase activity acts as cell-surface receptor for fibroblast growth factors and plays a role in the regulation of cell proliferation, differentiation and migration.
Binding of fibroblast growth factors produces receptor dimerization, autophosphorilation and signal transduction. FGFR4 binds mainly FGF19.
There are evidences that FGFR4 function may not necessarily require FGF ligand: i) heparin in the absence of FGF produced the activation of FGFR4 (Gao and Goldfarb, 1995), ii) FGFR4 was found to function in a complex with N-CAM independently of FGF (Cavallaro et al., 2001), and iii) the detection of N-linked glycosylation on an overexpressed extracellular domain of human FGFR4 suggested that the function of this receptor might also be regulated by glycosylation, similar to what occurs with other FGFRs (Tuominen et al., 2001).
A key regulator of the FGFR4 pathway is its co-receptor klotho-beta (KLB), a 130 kDa transmembrane protein that exhibits a more restricted expression profile in adipose, liver and pancreas tissues. KLB and FGFR4 are both expressed at high levels in mature hepatocytes, where KLB stabilizes FGF19-FGFR4 binding to regulate production of cholesterol 7a-hydroxylase (CYP7A1) and hepatocyte proliferation (Kurosu et al., 2007; Lin et al., 2007; Wu et al., 2010).
It has also been identified that FGFR4 is part of a complex with MT1-MMP, where MT1-MMP and FGFR4 are regulated in an opposite direction depending on the tumor progression and the presence of FGFR4 SNP Gly388Arg (Hotary et al., 2000; Lehti et al., 2000; Okada et al., 1995; Sugiyama et al., 2010). This SNP changes Gly388Arg in the predicted FGFR4 transmembrane domain, resulting in enhanced stability of the activated receptor (Ingvarsen et al., 2008). Both FGFR4-R388 and FGFR4-G388 form a complex with MT1-MMP and induced MT1-MMP tyrosil phosphorylation, but they had opposite effects on MT1-MMP levels. FGFR4-R388 stabilizes MT1-MMP, whereas FGFR4-G388 down-regulates MT1-MMP. The Y573F point mutation blocks MT1-MMP tyrosyl phosphorylation increasing cell-membrane MT1-MMP (Ingvarsen et al., 2008).
  FGFR4 related pathways are mostly related to an enhanced proliferation, cell survival and cell migration in cancer.
Homology Other fibroblast growth factor receptors (FGFR1, FGFR2 and FGFR3).
Homology with other tyrosin-protein kinase family members through its tyrosin-protein kinase domain.


  Mutational spectrum of the human FGFR4 gene. Red labels represent somatic mutations occurring in different cancers. Black labels represent germinal mutations.
Germinal In the FGFR4 gene transcript from a mammary carcinoma cell line, a G-to-A transition was discovered that resulted in the substitution of glycine by arginine at position 388 in the transmembrane domain of the receptor (Bange et al., 2002). The arg388 allele was also found in cell lines derived from a variety of other tumor types as well as in the germline of cancer patients and healthy individuals. Analysis of 3 geographically separated groups indicated that it occurs in approximately 50% of humans. Moreover, the FGFR4 arg388 allele was associated with early metastasis and advanced tumor-node metastasis stage in 82 colon cancer patients.
The results support that FGFR4 arg388 allele represents an innocuous determinant in healthy individuals but predisposes cancer patients for significantly accelerated disease progression.
Somatic FGFR4 was significantly overexpressed in rhabdomyosarcoma tumors of high metastatic potential. Higher FGFR4 expression was associated to a lower rate of survival (Taylor et al., 2009).
Six missense mutations were observed in the FGFR4 tyrosine kinase domain among 7 of 94 (7.5%) primary rhabdomyosarcomas, and none of these substitutions were found in normal controls. Comparison with the available genomic data suggested that the mutations were somatic. Four of the mutations affected residues Asn535 and Val550 and were predicted to be activating mutations that would alter conformational dynamics during phosphorylation in the case of Asn535 substitutions and ATP binding in the case of Val550 substitutions.
Using human and mouse rhabdomyosarcoma cell lines, it was found that two of these mutations, Asn535Lys (N535K) and Val550Glu (V550E), increased autophosphorylation, Stat3 signaling, cell growth, tumor proliferation and metastatic potential when injected into nude mice (Taylor et al., 2009). These mutants differentiated mouse NIH3T3 cells to an enhanced metastatic phenotype.
Ruhe et al. discovered the Y367C mutation in the FGFR4 gene by a comprehensive analysis of the tyrosine kinase gene family in cancer cell lines (Ruhe et al., 2007). This mutation occurred in the MDA-MB453 breast cancer cell line.
Cloning and ectopic expression of the FGFR4 Y367C mutant in HEK293 cells revealed high pERK levels and enhanced cell proliferation (Roidl et al., 2010).
Based on these findings, it has been proposed that FGFR4 may be a driver gene of tumour growth.

Implicated in

Entity Various cancers
Note Gly388Arg polymorphism
Disease Gly388Arg polymorphism seems to be associated to poor prognosis and cancer aggressiveness in different cancers but no with predisposition to any cancer as it has been described prostate, breast, gastric and skin cancer (see in paragraphs below).
Prognosis Gly388Arg seems to be associated to a worst prognosis and aggressiveness in different cancers. The SNP might be mainly associated with increased risks of breast and prostate cancer, and contributes to susceptibility to cancer, especially in Asians (Xu et al., 2010).
Entity Prostate cancer
Disease It has been described a significant association between FGFR4 polymorphism and prostate cancer using a total of 2618 cases and 2305 controls. FGFR4 contributes to susceptibility to prostate cancer (Liwei et al., 2011).
FGFR4 polymorphism results in an increased stability and activation of the receptor, resulting in an association of prostate cancer patients to clinical progression (Wang et al., 2008).
Entity Melanoma
Disease FGFR4 Arg388 polymorphism was detected in 83 out of 185 (45%) melanoma patients and was significantly associated to tumour thickness and the nodular melanoma subtype. Moreover, the analysis of 137 melanoma tissues by immunohistochemistry showed that 45% of the specimens expressed FGFR4 at different levels and correlated with pTNM tumour stages, metastases, number of primary tumors and survival (Streit et al., 2006).
In another independent study with 218 samples from melanoma, 285 squamous cell carcinoma, 300 basal cell carcinoma and 870 controls, it was observed no association between the presence of the SNP and predisposition to develop skin cancer.
Entity Hepatocellular carcinoma
Note FGF19 and its receptor FGFR4 are co-expressed in human liver, lung and colon tumors and in several colon cancer cell lines.
Prognosis The presence of the SNP in cancer patients in a population of 58 cases (29% heterozygous and 24% homozygous) and 88 controls (43% heterozygous and 27% homozygous) was associated with a poor prognosis in hepatocellular carcinoma patients. Moreover, overexpression of FGFR4 was also observed in 33% of cancer patients (Ho et al., 2009).
Oncogenesis A specific antibody directed against FGF19 abolished signaling mediated through FGFR4 in vitro, resulting in an inhibition of tumor xenografts in vivo and preventing hepatocellular carcinomas in FGF19 transgenic mice.
The targeting of FGF19 by antibodies that disrupt FGF19-FGFR4 interaction could be beneficial for colon, liver and lung cancer patients whose tumors co-express FGF19 and FGFR4 (Desnoyers et al., 2008).
Entity Breast cancer
Disease Approximately 40% and 10% of breast cancer patients present the Gly388Arg polymorphism in heterozygous or homozygous, respectively; without significant differences in the presence of the SNP between control and case specimens. FGFR4 expression levels do not correlate with the presence of the SNP (Thussbas et al., 2006).
Gly388Arg polymorphism is not associated with initiation of breast cancer but has been suggested that could be a marker for increased tumor aggressiveness in advanced breast cancer (Bange et al., 2002; Jezequel et al., 2004; Thussbas et al., 2006).
Entity Gastric cancer
Note FGFR4 expression abundance by immunohistochemistry was intermediate or high in 41% and 38% of gastric cancer tissue samples.
Disease The SNP is present in 50% of gastric cancer patients in either heterozygous or homozygous. It was found a significant association between Gly388Arg and gastric cancer patient survival, suggesting that FGFR4 Arg388 genotype might be a marker of gastric cancer progression (Ye et al., 2010; Ye et al., 2011).
Oncogenesis FGFR4 expression was associated to lymph node status and survival decreased with an increased in FGFR4 expression.
Knockdown of FGFR4 expression produced a decrease in proliferation by increasing the apoptosis rate of gastric cancer cell lines in vitro (Ye et al., 2011).
Entity Rhabdomyosarcomas
Note Rhabdomyosarcoma is a cancer that takes place in the childhood and is originated from skeletal muscle.
Oncogenesis FGFR4 is highly overexpressed in RMS samples at mRNA and protein level in comparison to pediatric tumors and normal tissue (Taylor et al., 2009). FGFR4 overexpression has been linked to advanced-stage cancer and poor survival (Baird et al., 2005; Taylor et al., 2009). FGFR4 silencing in the RH30 alveolar RMS human cell line produced a significant reduction in tumor growth and lung metastases when xenotransplanted in mice (Taylor et al., 2009).
Entity Colorectal cancer
Note FGFR4 is overexpressed in low- and high-metastatic CRC cell lines, with higher expression at late CRC stages (Barderas et al., 2012).
FGFR4 is a tumor-associated antigen of autoantibodies in colorectal cancer patients; it might serve for the diagnosis of colorectal cancer at early stages in combination with other tumor-associated antigens (Babel et al., 2009; Barderas et al., 2012).
Entity Pancreatic cancer
Oncogenesis FGFR4 is overexpressed in 50-70% of pancreatic cancer cell lines and pancreatic carcinomas (Motoda et al., 2011; Shah et al., 2002).
FGFR4 is significantly increased in high-grade pancreatic intraepithelial neoplasia and pancreatic ductal adenocarcinoma, where FGFR4 stimulation by FGF19 increased cell adhesion to extracellular matrix and decreased cell migration.


Identification of tumor-associated autoantigens for the diagnosis of colorectal cancer in serum using high density protein microarrays.
Babel I, Barderas R, Diaz-Uriarte R, Martinez-Torrecuadrada JL, Sanchez-Carbayo M, Casal JI.
Mol Cell Proteomics. 2009 Oct;8(10):2382-95. Epub 2009 Jul 28.
PMID 19638618
Gene expression profiling of human sarcomas: insights into sarcoma biology.
Baird K, Davis S, Antonescu CR, Harper UL, Walker RL, Chen Y, Glatfelter AA, Duray PH, Meltzer PS.
Cancer Res. 2005 Oct 15;65(20):9226-35.
PMID 16230383
Cancer progression and tumor cell motility are associated with the FGFR4 Arg(388) allele.
Bange J, Prechtl D, Cheburkin Y, Specht K, Harbeck N, Schmitt M, Knyazeva T, Muller S, Gartner S, Sures I, Wang H, Imyanitov E, Haring HU, Knayzev P, Iacobelli S, Hofler H, Ullrich A.
Cancer Res. 2002 Feb 1;62(3):840-7.
PMID 11830541
An optimized predictor panel for colorectal cancer diagnosis based on the combination of tumor-associated antigens obtained from protein and phage microarrays.
Barderas R, Babel I, Diaz-Uriarte R, Moreno V, Suarez A, Bonilla F, Villar-Vazquez R, Capella G, Casal JI.
J Proteomics. 2012 Aug 3;75(15):4647-55. Epub 2012 Mar 18.
PMID 22465712
N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-receptor signalling.
Cavallaro U, Niedermeyer J, Fuxa M, Christofori G.
Nat Cell Biol. 2001 Jul;3(7):650-7.
PMID 11433297
Targeting FGF19 inhibits tumor growth in colon cancer xenograft and FGF19 transgenic hepatocellular carcinoma models.
Desnoyers LR, Pai R, Ferrando RE, Hotzel K, Le T, Ross J, Carano R, D'Souza A, Qing J, Mohtashemi I, Ashkenazi A, French DM.
Oncogene. 2008 Jan 3;27(1):85-97. Epub 2007 Jun 25.
PMID 17599042
Heparin can activate a receptor tyrosine kinase.
Gao G, Goldfarb M.
EMBO J. 1995 May 15;14(10):2183-90.
PMID 7774576
Bile acids decrease hepatic paraoxonase 1 expression and plasma high-density lipoprotein levels via FXR-mediated signaling of FGFR4.
Gutierrez A, Ratliff EP, Andres AM, Huang X, McKeehan WL, Davis RA.
Arterioscler Thromb Vasc Biol. 2006 Feb;26(2):301-6. Epub 2005 Nov 10.
PMID 16284190
Fibroblast growth factor receptor 4 regulates proliferation, anti-apoptosis and alpha-fetoprotein secretion during hepatocellular carcinoma progression and represents a potential target for therapeutic intervention.
Ho HK, Pok S, Streit S, Ruhe JE, Hart S, Lim KS, Loo HL, Aung MO, Lim SG, Ullrich A.
J Hepatol. 2009 Jan;50(1):118-27. Epub 2008 Oct 12.
PMID 19008009
Regulation of cell invasion and morphogenesis in a three-dimensional type I collagen matrix by membrane-type matrix metalloproteinases 1, 2, and 3.
Hotary K, Allen E, Punturieri A, Yana I, Weiss SJ.
J Cell Biol. 2000 Jun 12;149(6):1309-23.
PMID 10851027
Dimerization of endogenous MT1-MMP is a regulatory step in the activation of the 72-kDa gelatinase MMP-2 on fibroblasts and fibrosarcoma cells.
Ingvarsen S, Madsen DH, Hillig T, Lund LR, Holmbeck K, Behrendt N, Engelholm LH.
Biol Chem. 2008 Jul;389(7):943-53.
PMID 18627313
G388R mutation of the FGFR4 gene is not relevant to breast cancer prognosis.
Jezequel P, Campion L, Joalland MP, Millour M, Dravet F, Classe JM, Delecroix V, Deporte R, Fumoleau P, Ricolleau G.
Br J Cancer. 2004 Jan 12;90(1):189-93.
PMID 14710228
Tissue-specific expression of betaKlotho and fibroblast growth factor (FGF) receptor isoforms determines metabolic activity of FGF19 and FGF21.
Kurosu H, Choi M, Ogawa Y, Dickson AS, Goetz R, Eliseenkova AV, Mohammadi M, Rosenblatt KP, Kliewer SA, Kuro-o M.
J Biol Chem. 2007 Sep 14;282(37):26687-95. Epub 2007 Jul 10.
PMID 17623664
Regulation of membrane-type-1 matrix metalloproteinase activity by its cytoplasmic domain.
Lehti K, Valtanen H, Wickstrom SA, Lohi J, Keski-Oja J.
J Biol Chem. 2000 May 19;275(20):15006-13.
PMID 10748199
Liver-specific activities of FGF19 require Klotho beta.
Lin BC, Wang M, Blackmore C, Desnoyers LR.
J Biol Chem. 2007 Sep 14;282(37):27277-84. Epub 2007 Jul 11.
PMID 17627937
Association between fibroblast growth factor receptor-4 gene polymorphism and risk of prostate cancer: a meta-analysis.
Liwei L, Chunyu L, Jie L, Ruifa H.
Urol Int. 2011;87(2):159-64. Epub 2011 May 28.
PMID 21625079
Overexpression of fibroblast growth factor receptor 4 in high-grade pancreatic intraepithelial neoplasia and pancreatic ductal adenocarcinoma.
Motoda N, Matsuda Y, Onda M, Ishiwata T, Uchida E, Naito Z.
Int J Oncol. 2011 Jan;38(1):133-43.
PMID 21109934
Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in stromal cells of human colon, breast, and head and neck carcinomas.
Okada A, Bellocq JP, Rouyer N, Chenard MP, Rio MC, Chambon P, Basset P.
Proc Natl Acad Sci U S A. 1995 Mar 28;92(7):2730-4.
PMID 7708715
FGFR-4, a novel acidic fibroblast growth factor receptor with a distinct expression pattern.
Partanen J, Makela TP, Eerola E, Korhonen J, Hirvonen H, Claesson-Welsh L, Alitalo K.
EMBO J. 1991 Jun;10(6):1347-54.
PMID 1709094
The FGFR4 Y367C mutant is a dominant oncogene in MDA-MB453 breast cancer cells.
Roidl A, Foo P, Wong W, Mann C, Bechtold S, Berger HJ, Streit S, Ruhe JE, Hart S, Ullrich A, Ho HK.
Oncogene. 2010 Mar 11;29(10):1543-52. Epub 2009 Nov 30.
PMID 19946327
Genetic alterations in the tyrosine kinase transcriptome of human cancer cell lines.
Ruhe JE, Streit S, Hart S, Wong CH, Specht K, Knyazev P, Knyazeva T, Tay LS, Loo HL, Foo P, Wong W, Pok S, Lim SJ, Ong H, Luo M, Ho HK, Peng K, Lee TC, Bezler M, Mann C, Gaertner S, Hoefler H, Iacobelli S, Peter S, Tay A, Brenner S, Venkatesh B, Ullrich A.
Cancer Res. 2007 Dec 1;67(23):11368-76.
PMID 18056464
FGFR4 overexpression in pancreatic cancer is mediated by an intronic enhancer activated by HNF1alpha.
Shah RN, Ibbitt JC, Alitalo K, Hurst HC.
Oncogene. 2002 Nov 28;21(54):8251-61.
PMID 12447688
FGFR4 Arg388 allele correlates with tumour thickness and FGFR4 protein expression with survival of melanoma patients.
Streit S, Mestel DS, Schmidt M, Ullrich A, Berking C.
Br J Cancer. 2006 Jun 19;94(12):1879-86. Epub 2006 May 23.
PMID 16721364
Fibroblast growth factor receptor 4 regulates tumor invasion by coupling fibroblast growth factor signaling to extracellular matrix degradation.
Sugiyama N, Varjosalo M, Meller P, Lohi J, Hyytiainen M, Kilpinen S, Kallioniemi O, Ingvarsen S, Engelholm LH, Taipale J, Alitalo K, Keski-Oja J, Lehti K.
Cancer Res. 2010 Oct 15;70(20):7851-61. Epub 2010 Sep 28.
PMID 20876804
Identification of FGFR4-activating mutations in human rhabdomyosarcomas that promote metastasis in xenotransplanted models.
Taylor JG 6th, Cheuk AT, Tsang PS, Chung JY, Song YK, Desai K, Yu Y, Chen QR, Shah K, Youngblood V, Fang J, Kim SY, Yeung C, Helman LJ, Mendoza A, Ngo V, Staudt LM, Wei JS, Khanna C, Catchpoole D, Qualman SJ, Hewitt SM, Merlino G, Chanock SJ, Khan J.
J Clin Invest. 2009 Nov;119(11):3395-407. doi: 10.1172/JCI39703. Epub 2009 Oct 5.
PMID 19809159
FGFR4 Arg388 allele is associated with resistance to adjuvant therapy in primary breast cancer.
Thussbas C, Nahrig J, Streit S, Bange J, Kriner M, Kates R, Ulm K, Kiechle M, Hoefler H, Ullrich A, Harbeck N.
J Clin Oncol. 2006 Aug 10;24(23):3747-55. Epub 2006 Jul 5.
PMID 16822847
Expression and glycosylation studies of human FGF receptor 4.
Tuominen H, Heikinheimo P, Loo BM, Kataja K, Oker-Blom C, Uutela M, Jalkanen M, Goldman A.
Protein Expr Purif. 2001 Mar;21(2):275-85.
PMID 11237689
Altered fibroblast growth factor receptor 4 stability promotes prostate cancer progression.
Wang J, Yu W, Cai Y, Ren C, Ittmann MM.
Neoplasia. 2008 Aug;10(8):847-56.
PMID 18670643
FGFR-3 and FGFR-4 function cooperatively to direct alveogenesis in the murine lung.
Weinstein M, Xu X, Ohyama K, Deng CX.
Development. 1998 Sep;125(18):3615-23.
PMID 9716527
FGF19-induced hepatocyte proliferation is mediated through FGFR4 activation.
Wu X, Ge H, Lemon B, Vonderfecht S, Weiszmann J, Hecht R, Gupte J, Hager T, Wang Z, Lindberg R, Li Y.
J Biol Chem. 2010 Feb 19;285(8):5165-70. Epub 2009 Dec 15.
PMID 20018895
FGFR4 transmembrane domain polymorphism and cancer risk: a meta-analysis including 8555 subjects.
Xu W, Li Y, Wang X, Chen B, Wang Y, Liu S, Xu J, Zhao W, Wu J.
Eur J Cancer. 2010 Dec;46(18):3332-8. Epub 2010 Jul 16.
PMID 20638838
The fibroblast growth factor receptor-4 Arg388 allele is associated with gastric cancer progression.
Ye Y, Shi Y, Zhou Y, Du C, Wang C, Zhan H, Zheng B, Cao X, Sun MH, Fu H.
Ann Surg Oncol. 2010 Dec;17(12):3354-61. Epub 2010 Sep 16.
PMID 20844967
Fibroblast growth factor receptor 4 regulates proliferation and antiapoptosis during gastric cancer progression.
Ye YW, Zhou Y, Yuan L, Wang CM, Du CY, Zhou XY, Zheng BQ, Cao X, Sun MH, Fu H, Shi YQ.
Cancer. 2011 Dec 1;117(23):5304-13. doi: 10.1002/cncr.26207. Epub 2011 May 12.
PMID 21567388
Elevated cholesterol metabolism and bile acid synthesis in mice lacking membrane tyrosine kinase receptor FGFR4.
Yu C, Wang F, Kan M, Jin C, Jones RB, Weinstein M, Deng CX, McKeehan WL.
J Biol Chem. 2000 May 19;275(20):15482-9.
PMID 10809780


This paper should be referenced as such :
Pelaez-Garcia, A ; Barderas, R ; Casal, JI
FGFR4 (fibroblast growth factor receptor 4)
Atlas Genet Cytogenet Oncol Haematol. 2012;16(11):802-808.
Free journal version : [ pdf ]   [ DOI ]

External links

HGNC (Hugo)FGFR4   3691
Entrez_Gene (NCBI)FGFR4    fibroblast growth factor receptor 4
AliasesCD334; JTK2; TKF
GeneCards (Weizmann)FGFR4
Ensembl hg19 (Hinxton)ENSG00000160867 [Gene_View]
Ensembl hg38 (Hinxton)ENSG00000160867 [Gene_View]  ENSG00000160867 [Sequence]  chr5:177086915-177098144 [Contig_View]  FGFR4 [Vega]
ICGC DataPortalENSG00000160867
TCGA cBioPortalFGFR4
Genatlas (Paris)FGFR4
SOURCE (Princeton)FGFR4
Genetics Home Reference (NIH)FGFR4
Genomic and cartography
GoldenPath hg38 (UCSC)FGFR4  -     chr5:177086915-177098144 +  5q35.2   [Description]    (hg38-Dec_2013)
GoldenPath hg19 (UCSC)FGFR4  -     5q35.2   [Description]    (hg19-Feb_2009)
GoldenPathFGFR4 - 5q35.2 [CytoView hg19]  FGFR4 - 5q35.2 [CytoView hg38]
Genome Data Viewer NCBIFGFR4 [Mapview hg19]  
Gene and transcription
Genbank (Entrez)AB209631 AF202063 AF359241 AF359246 AK225280
RefSeq transcript (Entrez)NM_001291980 NM_001354984 NM_002011 NM_022963 NM_213647
Consensus coding sequences : CCDS (NCBI)FGFR4
Gene ExpressionFGFR4 [ NCBI-GEO ]   FGFR4 [ EBI - ARRAY_EXPRESS ]   FGFR4 [ SEEK ]   FGFR4 [ MEM ]
Gene Expression Viewer (FireBrowse)FGFR4 [ Firebrowse - Broad ]
GenevisibleExpression of FGFR4 in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)2264
GTEX Portal (Tissue expression)FGFR4
Human Protein AtlasENSG00000160867-FGFR4 [pathology]   [cell]   [tissue]
Protein : pattern, domain, 3D structure
Domain families : Pfam (Sanger)
Domain families : Pfam (NCBI)
Conserved Domain (NCBI)FGFR4
Human Protein Atlas [tissue]ENSG00000160867-FGFR4 [tissue]
Protein Interaction databases
Ontologies - Pathways
PubMed240 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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