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Fibroblast growth factor receptor 4 (FGFR-4) (EC 2.7.10.1) (CD antigen CD334)

 FGFR4_HUMAN             Reviewed;         802 AA.
P22455; G3JVM2; G3JVM5; G3JVM7; G3JVM9; O43785; Q14309; Q71TW8;
Q8TDA0; Q96KE5;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
27-APR-2001, sequence version 2.
22-NOV-2017, entry version 198.
RecName: Full=Fibroblast growth factor receptor 4;
Short=FGFR-4;
EC=2.7.10.1;
AltName: CD_antigen=CD334;
Flags: Precursor;
Name=FGFR4; Synonyms=JTK2, TKF;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1709094;
Partanen J.M., Maekelae T.P., Eerola E., Korhonen J., Hirvonen H.,
Claesson-Welsh L., Alitalo K.;
"FGFR-4, a novel acidic fibroblast growth factor receptor with a
distinct expression pattern.";
EMBO J. 10:1347-1354(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION AS RECEPTOR FOR
FGF1 AND FGF2.
TISSUE=Mammary gland;
PubMed=7680645;
Ron D., Reich R., Chedid M., Lengel C., Cohen O.E., Chan A.M.,
Neufeld G., Miki T., Tronick S.R.;
"Fibroblast growth factor receptor 4 is a high affinity receptor for
both acidic and basic fibroblast growth factor but not for
keratinocyte growth factor.";
J. Biol. Chem. 268:5388-5394(1993).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-136, TISSUE
SPECIFICITY, AND SUBCELLULAR LOCATION.
TISSUE=Intestine;
PubMed=10631118; DOI=10.1006/bbrc.1999.2010;
Takaishi S., Sawada M., Morita Y., Seno H., Fukuzawa H., Chiba T.;
"Identification of a novel alternative splicing of human FGF receptor
4: soluble-form splice variant expressed in human gastrointestinal
epithelial cells.";
Biochem. Biophys. Res. Commun. 267:658-662(2000).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=9457674; DOI=10.1007/s003359900703;
Kostrzewa M., Muller U.;
"Genomic structure and complete sequence of the human FGFR4 gene.";
Mamm. Genome 9:131-135(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), SUBCELLULAR LOCATION (ISOFORM
3), INVOLVEMENT IN CANCER, AND VARIANT PC ARG-388.
TISSUE=Pituitary;
PubMed=11781352; DOI=10.1172/JCI14036;
Ezzat S., Zheng L., Zhu X.F., Wu G.E., Asa S.L.;
"Targeted expression of a human pituitary tumor-derived isoform of FGF
receptor-4 recapitulates pituitary tumorigenesis.";
J. Clin. Invest. 109:69-78(2002).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS ILE-10 AND LEU-136,
INVOLVEMENT IN CANCER, AND VARIANT PC ARG-388.
PubMed=21882254; DOI=10.1002/mc.20848;
Marshall A.D., van der Ent M.A., Grosveld G.C.;
"PAX3-FOXO1 and FGFR4 in alveolar rhabdomyosarcoma.";
Mol. Carcinog. 51:807-815(2012).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT LEU-136.
Lind D.L., Cox D.R.;
"Sequence variation in fibroblast growth factor receptors 3 and 4.";
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ILE-10; LEU-136 AND
ARG-388.
NIEHS SNPs program;
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-136.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Muscle;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 609-676.
TISSUE=Blood;
PubMed=2247464; DOI=10.1073/pnas.87.22.8913;
Partanen J., Maekelae T.P., Alitalo R., Lehvaeslaiho H., Alitalo K.;
"Putative tyrosine kinases expressed in K-562 human leukemia cells.";
Proc. Natl. Acad. Sci. U.S.A. 87:8913-8917(1990).
[13]
PROTEIN SEQUENCE OF 22-38.
PubMed=15340161; DOI=10.1110/ps.04682504;
Zhang Z., Henzel W.J.;
"Signal peptide prediction based on analysis of experimentally
verified cleavage sites.";
Protein Sci. 13:2819-2824(2004).
[14]
FUNCTION AS FGF1 RECEPTOR AND IN ACTIVATION OF SIGNALING VIA PLCG1 AND
PIK3R1, INTERACTION WITH PLCG1, PHOSPHORYLATION AT TYR-754, AND
MUTAGENESIS OF TYR-754.
PubMed=7518429;
Vainikka S., Joukov V., Wennstrom S., Bergman M., Pelicci P.G.,
Alitalo K.;
"Signal transduction by fibroblast growth factor receptor-4 (FGFR-4).
Comparison with FGFR-1.";
J. Biol. Chem. 269:18320-18326(1994).
[15]
INTERACTION WITH FGF1; FGF2; FGF4; FGF6; FGF8 AND FGF9, AND FUNCTION
IN CELL PROLIFERATION.
PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
Coulier F., Gao G., Goldfarb M.;
"Receptor specificity of the fibroblast growth factor family.";
J. Biol. Chem. 271:15292-15297(1996).
[16]
FUNCTION IN CELL DIFFERENTIATION, MUTAGENESIS OF LYS-503, CATALYTIC
ACTIVITY, AND IDENTIFICATION IN A COMPLEX WITH NCAM1; CDH2; PLCG1;
FRS2; SRC; SHC; GAP43 AND CTTN.
PubMed=11433297; DOI=10.1038/35083041;
Cavallaro U., Niedermeyer J., Fuxa M., Christofori G.;
"N-CAM modulates tumour-cell adhesion to matrix by inducing FGF-
receptor signalling.";
Nat. Cell Biol. 3:650-657(2001).
[17]
INVOLVEMENT IN CANCER.
PubMed=11830541;
Bange J., Prechtl D., Cheburkin Y., Specht K., Harbeck N., Schmitt M.,
Knyazeva T., Mueller S., Gaertner S., Sures I., Wang H., Imyanitov E.,
Haering H.U., Knayzev P., Iacobelli S., Hoefler H., Ullrich A.;
"Cancer progression and tumor cell motility are associated with the
FGFR4 Arg(388) allele.";
Cancer Res. 62:840-847(2002).
[18]
INTERACTION WITH FGF1; FGF17; FGF18; FGF19; FGF21 AND FGF23, AND
FUNCTION IN STIMULATION OF CELL PROLIFERATION.
PubMed=16597617; DOI=10.1074/jbc.M601252200;
Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M.,
Ornitz D.M.;
"Receptor specificity of the fibroblast growth factor family. The
complete mammalian FGF family.";
J. Biol. Chem. 281:15694-15700(2006).
[19]
INTERACTION WITH FGF19; FGF21 AND KLB, AND FUNCTION IN SIGNALING AND
IN REGULATION OF CYP7A1 AND BILE ACID SYNTHESIS.
PubMed=17623664; DOI=10.1074/jbc.M704165200;
Kurosu H., Choi M., Ogawa Y., Dickson A.S., Goetz R.,
Eliseenkova A.V., Mohammadi M., Rosenblatt K.P., Kliewer S.A.,
Kuro-o M.;
"Tissue-specific expression of betaKlotho and fibroblast growth factor
(FGF) receptor isoforms determines metabolic activity of FGF19 and
FGF21.";
J. Biol. Chem. 282:26687-26695(2007).
[20]
FUNCTION IN STAT1 PHOSPHORYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF
LYS-503, GLYCOSYLATION, AND PHOSPHORYLATION.
PubMed=17311277; DOI=10.1002/jcp.21014;
Citores L., Bai L., Sorensen V., Olsnes S.;
"Fibroblast growth factor receptor-induced phosphorylation of STAT1 at
the Golgi apparatus without translocation to the nucleus.";
J. Cell. Physiol. 212:148-156(2007).
[21]
INVOLVEMENT IN PC, AND VARIANT PC ARG-388.
PubMed=18756523; DOI=10.1002/ijc.23578;
Ma Z., Tsuchiya N., Yuasa T., Inoue T., Kumazawa T., Narita S.,
Horikawa Y., Tsuruta H., Obara T., Saito M., Satoh S., Ogawa O.,
Habuchi T.;
"Polymorphisms of fibroblast growth factor receptor 4 have association
with the development of prostate cancer and benign prostatic
hyperplasia and the progression of prostate cancer in a Japanese
population.";
Int. J. Cancer 123:2574-2579(2008).
[22]
CATALYTIC ACTIVITY, FUNCTION AS FGF1 RECEPTOR AND IN ACTIVATION OF
PLCG1; FRS2; MAPK1/ERK2 AND MAPK3/ERK1, ENZYME REGULATION,
UBIQUITINATION, AND SUBCELLULAR LOCATION.
PubMed=18480409; DOI=10.1091/mbc.E07-12-1219;
Haugsten E.M., Malecki J., Bjorklund S.M., Olsnes S., Wesche J.;
"Ubiquitination of fibroblast growth factor receptor 1 is required for
its intracellular sorting but not for its endocytosis.";
Mol. Biol. Cell 19:3390-3403(2008).
[23]
CATALYTIC ACTIVITY, FUNCTION AS FGF2 RECEPTOR AND IN STIMULATION OF
CELL PROLIFERATION, SUBCELLULAR LOCATION, INTERACTION WITH FGF2 AND
HIP1, PHOSPHORYLATION AT TYR-642 AND TYR-643, INVOLVEMENT IN PC, AND
CHARACTERIZATION OF VARIANT PC ARG-388.
PubMed=18670643; DOI=10.1593/neo.08450;
Wang J., Yu W., Cai Y., Ren C., Ittmann M.M.;
"Altered fibroblast growth factor receptor 4 stability promotes
prostate cancer progression.";
Neoplasia 10:847-856(2008).
[24]
INVOLVEMENT IN CANCER.
PubMed=20638838; DOI=10.1016/j.ejca.2010.06.017;
Xu W., Li Y., Wang X., Chen B., Wang Y., Liu S., Xu J., Zhao W.,
Wu J.;
"FGFR4 transmembrane domain polymorphism and cancer risk: a meta-
analysis including 8555 subjects.";
Eur. J. Cancer 46:3332-3338(2010).
[25]
FUNCTION IN FGF19 SIGNALING AND IN REGULATION OF BILE ACID SYNTHESIS
VIA CYP7A1, INTERACTION WITH FGF19; KL AND KLB, AUTOPHOSPHORYLATION,
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=20683963; DOI=10.1002/hep.23708;
Triantis V., Saeland E., Bijl N., Oude-Elferink R.P., Jansen P.L.;
"Glycosylation of fibroblast growth factor receptor 4 is a key
regulator of fibroblast growth factor 19-mediated down-regulation of
cytochrome P450 7A1.";
Hepatology 52:656-666(2010).
[26]
FUNCTION IN HEPATOCYTE PROLIFERATION AND FGF19 SIGNALING.
PubMed=20018895; DOI=10.1074/jbc.M109.068783;
Wu X., Ge H., Lemon B., Vonderfecht S., Weiszmann J., Hecht R.,
Gupte J., Hager T., Wang Z., Lindberg R., Li Y.;
"FGF19-induced hepatocyte proliferation is mediated through FGFR4
activation.";
J. Biol. Chem. 285:5165-5170(2010).
[27]
FUNCTION IN DOWN-REGULATION OF MMP14, AUTOPHOSPHORYLATION, AND
INTERACTION WITH MMP14.
PubMed=20798051; DOI=10.1073/pnas.0914459107;
Sugiyama N., Varjosalo M., Meller P., Lohi J., Chan K.M., Zhou Z.,
Alitalo K., Taipale J., Keski-Oja J., Lehti K.;
"FGF receptor-4 (FGFR4) polymorphism acts as an activity switch of a
membrane type 1 matrix metalloproteinase-FGFR4 complex.";
Proc. Natl. Acad. Sci. U.S.A. 107:15786-15791(2010).
[28]
INVOLVEMENT IN PC, AND VARIANT PC ARG-388.
PubMed=21349172; DOI=10.1186/1471-2407-11-84;
Xu B., Tong N., Chen S.Q., Hua L.X., Wang Z.J., Zhang Z.D., Chen M.;
"FGFR4 Gly388Arg polymorphism contributes to prostate cancer
development and progression: a meta-analysis of 2618 cases and 2305
controls.";
BMC Cancer 11:84-84(2011).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[30]
INVOLVEMENT IN CANCER.
PubMed=21412156; DOI=10.1097/CEJ.0b013e3283457274;
Frullanti E., Berking C., Harbeck N., Jezequel P., Haugen A.,
Mawrin C., Parise O. Jr., Sasaki H., Tsuchiya N., Dragani T.A.;
"Meta and pooled analyses of FGFR4 Gly388Arg polymorphism as a cancer
prognostic factor.";
Eur. J. Cancer Prev. 20:340-347(2011).
[31]
FUNCTION IN FGF19 SIGNALING, FUNCTION IN STIMULATION OF CELL
PROLIFERATION AND ACTIVATION OF MAPK1/ERK2 AND MAPK3/ERK1, AND
INTERACTION WITH FGF19; KLB AND SULFATED GLYCOSAMINOGLYCANS.
PubMed=21653700; DOI=10.1074/jbc.M111.251140;
Nakamura M., Uehara Y., Asada M., Honda E., Nagai N., Kimata K.,
Suzuki M., Imamura T.;
"Sulfated glycosaminoglycans are required for specific and sensitive
fibroblast growth factor (FGF) 19 signaling via FGF receptor 4 and
betaKlotho.";
J. Biol. Chem. 286:26418-26423(2011).
[32]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-573, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[34]
INTERACTION WITH STAT3, INVOLVEMENT IN CANCER, AND CHARACTERIZATION OF
VARIANT PC ARG-388.
PubMed=26675719; DOI=10.1038/nature16449;
Ulaganathan V.K., Sperl B., Rapp U.R., Ullrich A.;
"Germline variant FGFR4 p.G388R exposes a membrane-proximal STAT3
binding site.";
Nature 528:570-574(2015).
[35]
VARIANTS [LARGE SCALE ANALYSIS] ILE-10; LEU-136; ALA-179; SER-426;
ASN-516; MET-550; THR-712 AND ASN-772.
PubMed=17344846; DOI=10.1038/nature05610;
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
"Patterns of somatic mutation in human cancer genomes.";
Nature 446:153-158(2007).
[36]
REVIEW ON LIGAND SELECTIVITY AND SIGNALING.
PubMed=15863030; DOI=10.1016/j.cytogfr.2005.01.001;
Eswarakumar V.P., Lax I., Schlessinger J.;
"Cellular signaling by fibroblast growth factor receptors.";
Cytokine Growth Factor Rev. 16:139-149(2005).
[37]
REVIEW ON FUNCTION IN FGF SIGNALING.
PubMed=20094046; DOI=10.1038/nrc2780;
Turner N., Grose R.;
"Fibroblast growth factor signalling: from development to cancer.";
Nat. Rev. Cancer 10:116-129(2010).
[38]
CHARACTERIZATION OF VARIANT PC ARG-388, AND FUNCTION IN TUMOR CELL
INVASION.
PubMed=20876804; DOI=10.1158/0008-5472.CAN-10-1223;
Sugiyama N., Varjosalo M., Meller P., Lohi J., Hyytiainen M.,
Kilpinen S., Kallioniemi O., Ingvarsen S., Engelholm L.H., Taipale J.,
Alitalo K., Keski-Oja J., Lehti K.;
"Fibroblast growth factor receptor 4 regulates tumor invasion by
coupling fibroblast growth factor signaling to extracellular matrix
degradation.";
Cancer Res. 70:7851-7861(2010).
-!- 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. Mutations that
lead to constitutive kinase activation or impair normal FGFR4
inactivation lead to aberrant signaling.
{ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:16597617,
ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664,
ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:18670643,
ECO:0000269|PubMed:20018895, ECO:0000269|PubMed:20683963,
ECO:0000269|PubMed:20798051, ECO:0000269|PubMed:20876804,
ECO:0000269|PubMed:21653700, ECO:0000269|PubMed:7518429,
ECO:0000269|PubMed:7680645, ECO:0000269|PubMed:8663044}.
-!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
[protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
ProRule:PRU10028, ECO:0000269|PubMed:11433297,
ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:18480409,
ECO:0000269|PubMed:18670643}.
-!- 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.
{ECO:0000269|PubMed:18480409}.
-!- SUBUNIT: 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 (PubMed:11433297,
PubMed:16597617, PubMed:17623664, PubMed:18670643,
PubMed:20683963, PubMed:20798051, PubMed:21653700, PubMed:7518429,
PubMed:8663044). Interacts with STAT3 (PubMed:26675719).
{ECO:0000269|PubMed:11433297, ECO:0000269|PubMed:16597617,
ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18670643,
ECO:0000269|PubMed:20683963, ECO:0000269|PubMed:20798051,
ECO:0000269|PubMed:21653700, ECO:0000269|PubMed:26675719,
ECO:0000269|PubMed:7518429, ECO:0000269|PubMed:8663044}.
-!- INTERACTION:
P50281:MMP14; NbExp=6; IntAct=EBI-6256193, EBI-992788;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Endosome. Endoplasmic reticulum. Note=Internalized from
the cell membrane to recycling endosomes, and from there back to
the cell membrane.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm
{ECO:0000269|PubMed:11781352}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P22455-1; Sequence=Displayed;
Name=2; Synonyms=Soluble-form;
IsoId=P22455-2; Sequence=VSP_035108;
Name=3;
IsoId=P22455-3; Sequence=VSP_053542;
Note=Lacks a signal peptide. Constitutively phosphorylated.;
-!- TISSUE SPECIFICITY: Expressed in gastrointestinal epithelial
cells, pancreas, and gastric and pancreatic cancer cell lines.
{ECO:0000269|PubMed:10631118}.
-!- PTM: N-glycosylated. Full maturation of the glycan chains in the
Golgi is essential for high affinity interaction with FGF19.
-!- PTM: Ubiquitinated. Subject to proteasomal degradation when not
fully glycosylated. {ECO:0000269|PubMed:18480409}.
-!- PTM: 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. {ECO:0000269|PubMed:17311277,
ECO:0000269|PubMed:18670643, ECO:0000269|PubMed:7518429}.
-!- DISEASE: Prostate cancer (PC) [MIM:176807]: A malignancy
originating in tissues of the prostate. Most prostate cancers are
adenocarcinomas that develop in the acini of the prostatic ducts.
Other rare histopathologic types of prostate cancer that occur in
approximately 5% of patients include small cell carcinoma,
mucinous carcinoma, prostatic ductal carcinoma, transitional cell
carcinoma, squamous cell carcinoma, basal cell carcinoma, adenoid
cystic carcinoma (basaloid), signet-ring cell carcinoma and
neuroendocrine carcinoma. {ECO:0000269|PubMed:18670643,
ECO:0000269|PubMed:18756523, ECO:0000269|PubMed:20876804,
ECO:0000269|PubMed:21349172}. Note=The gene represented in this
entry is involved in disease pathogenesis. FGFR4 variant Arg-388
has been associated with prostate cancer as well as cancers of the
breast, colon, head and neck, larynx, lung, skin. Arg-388
predisposes cancer patients for accelerated disease progression
and is associated with poor prognosis.
{ECO:0000269|PubMed:11781352, ECO:0000269|PubMed:11830541,
ECO:0000269|PubMed:18670643, ECO:0000269|PubMed:18756523,
ECO:0000269|PubMed:20638838, ECO:0000269|PubMed:20876804,
ECO:0000269|PubMed:21349172, ECO:0000269|PubMed:21412156,
ECO:0000269|PubMed:21882254, ECO:0000269|PubMed:26675719}.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fibroblast growth factor receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgfr4/";
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FGFR4ID512ch5q35.html";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; X57205; CAA40490.1; -; mRNA.
EMBL; L03840; AAB59389.1; -; mRNA.
EMBL; AF202063; AAF27432.1; -; mRNA.
EMBL; Y13901; CAA74200.1; -; Genomic_DNA.
EMBL; AF359246; AAK51435.1; -; mRNA.
EMBL; JN007471; AEO19712.1; -; mRNA.
EMBL; JN007472; AEO19713.1; -; mRNA.
EMBL; JN007473; AEO19714.1; -; mRNA.
EMBL; JN007474; AEO19715.1; -; mRNA.
EMBL; JN007475; AEO19716.1; -; mRNA.
EMBL; JN007476; AEO19717.1; -; mRNA.
EMBL; JN007477; AEO19718.1; -; mRNA.
EMBL; JN007478; AEO19719.1; -; mRNA.
EMBL; JN007479; AEO19720.1; -; mRNA.
EMBL; JN007480; AEO19721.1; -; mRNA.
EMBL; JN007481; AEO19722.1; -; mRNA.
EMBL; JN007482; AEO19723.1; -; mRNA.
EMBL; AF487555; AAM13666.1; -; Genomic_DNA.
EMBL; EF571596; ABQ01235.1; -; Genomic_DNA.
EMBL; AC027314; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471195; EAW85036.1; -; Genomic_DNA.
EMBL; BC011847; AAH11847.1; -; mRNA.
EMBL; M59373; AAA63208.1; -; mRNA.
CCDS; CCDS4410.1; -. [P22455-1]
CCDS; CCDS4411.1; -. [P22455-2]
PIR; S15345; TVHUF4.
RefSeq; NP_001278909.1; NM_001291980.1.
RefSeq; NP_002002.3; NM_002011.4. [P22455-1]
RefSeq; NP_075252.2; NM_022963.3. [P22455-2]
RefSeq; NP_998812.1; NM_213647.2. [P22455-1]
RefSeq; XP_005265895.1; XM_005265838.3. [P22455-1]
UniGene; Hs.165950; -.
PDB; 1QCT; Model; -; B/E=36-353.
PDB; 4QQ5; X-ray; 2.20 A; A=445-753.
PDB; 4QQC; X-ray; 2.40 A; A=445-753.
PDB; 4QQJ; X-ray; 1.68 A; A=445-753.
PDB; 4QQT; X-ray; 1.50 A; A=445-753.
PDB; 4QRC; X-ray; 1.90 A; A=445-753.
PDB; 4R6V; X-ray; 2.35 A; A=445-753.
PDB; 4TYE; X-ray; 2.80 A; A=447-753.
PDB; 4TYG; X-ray; 2.40 A; A=447-753.
PDB; 4TYI; X-ray; 3.40 A; A=447-753.
PDB; 4TYJ; X-ray; 2.45 A; A=447-753.
PDB; 4UXQ; X-ray; 1.85 A; A=447-753.
PDB; 4XCU; X-ray; 1.71 A; A=449-751.
PDB; 5JKG; X-ray; 2.35 A; A=445-753.
PDBsum; 1QCT; -.
PDBsum; 4QQ5; -.
PDBsum; 4QQC; -.
PDBsum; 4QQJ; -.
PDBsum; 4QQT; -.
PDBsum; 4QRC; -.
PDBsum; 4R6V; -.
PDBsum; 4TYE; -.
PDBsum; 4TYG; -.
PDBsum; 4TYI; -.
PDBsum; 4TYJ; -.
PDBsum; 4UXQ; -.
PDBsum; 4XCU; -.
PDBsum; 5JKG; -.
ProteinModelPortal; P22455; -.
SMR; P22455; -.
BioGrid; 108555; 37.
CORUM; P22455; -.
DIP; DIP-5149N; -.
IntAct; P22455; 25.
STRING; 9606.ENSP00000292408; -.
BindingDB; P22455; -.
ChEMBL; CHEMBL3973; -.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB00039; Palifermin.
DrugBank; DB08901; Ponatinib.
GuidetoPHARMACOLOGY; 1811; -.
iPTMnet; P22455; -.
PhosphoSitePlus; P22455; -.
BioMuta; FGFR4; -.
DMDM; 13432140; -.
MaxQB; P22455; -.
PaxDb; P22455; -.
PeptideAtlas; P22455; -.
PRIDE; P22455; -.
DNASU; 2264; -.
Ensembl; ENST00000292408; ENSP00000292408; ENSG00000160867. [P22455-1]
Ensembl; ENST00000393637; ENSP00000377254; ENSG00000160867. [P22455-2]
Ensembl; ENST00000502906; ENSP00000424960; ENSG00000160867. [P22455-1]
GeneID; 2264; -.
KEGG; hsa:2264; -.
UCSC; uc003mfl.4; human. [P22455-1]
CTD; 2264; -.
DisGeNET; 2264; -.
EuPathDB; HostDB:ENSG00000160867.14; -.
GeneCards; FGFR4; -.
HGNC; HGNC:3691; FGFR4.
HPA; CAB005196; -.
HPA; HPA027273; -.
HPA; HPA027369; -.
HPA; HPA028251; -.
MalaCards; FGFR4; -.
MIM; 134935; gene.
MIM; 176807; phenotype.
neXtProt; NX_P22455; -.
OpenTargets; ENSG00000160867; -.
PharmGKB; PA28130; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; P22455; -.
KO; K05095; -.
OMA; THPQRME; -.
OrthoDB; EOG091G0CQZ; -.
PhylomeDB; P22455; -.
TreeFam; TF316307; -.
BRENDA; 2.7.10.1; 2681.
Reactome; R-HSA-109704; PI3K Cascade.
Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
Reactome; R-HSA-1307965; betaKlotho-mediated ligand binding.
Reactome; R-HSA-1839128; FGFR4 mutant receptor activation.
Reactome; R-HSA-190322; FGFR4 ligand binding and activation.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5654228; Phospholipase C-mediated cascade, FGFR4.
Reactome; R-HSA-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-HSA-5654719; SHC-mediated cascade:FGFR4.
Reactome; R-HSA-5654720; PI-3K cascade:FGFR4.
Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
Reactome; R-HSA-5655291; Signaling by FGFR4 in disease.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
SIGNOR; P22455; -.
ChiTaRS; FGFR4; human.
GeneWiki; Fibroblast_growth_factor_receptor_4; -.
GenomeRNAi; 2264; -.
PRO; PR:P22455; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000160867; -.
CleanEx; HS_FGFR4; -.
ExpressionAtlas; P22455; baseline and differential.
Genevisible; P22455; HS.
GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0030133; C:transport vesicle; IDA:UniProtKB.
GO; GO:0016303; F:1-phosphatidylinositol-3-kinase activity; TAS:Reactome.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0017134; F:fibroblast growth factor binding; IDA:UniProtKB.
GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; IDA:UniProtKB.
GO; GO:0008201; F:heparin binding; IDA:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; TAS:Reactome.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0055062; P:phosphate ion homeostasis; ISS:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0043085; P:positive regulation of catalytic activity; IMP:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000573; P:positive regulation of DNA biosynthetic process; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0010628; P:positive regulation of gene expression; IMP:UniProtKB.
GO; GO:0045862; P:positive regulation of proteolysis; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0070857; P:regulation of bile acid biosynthetic process; IMP:UniProtKB.
GO; GO:2000188; P:regulation of cholesterol homeostasis; ISS:UniProtKB.
GO; GO:0010715; P:regulation of extracellular matrix disassembly; IMP:UniProtKB.
GO; GO:0019216; P:regulation of lipid metabolic process; ISS:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR016248; FGF_rcpt_fam.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom_sf.
InterPro; IPR000719; Prot_kinase_dom.
InterPro; IPR017441; Protein_kinase_ATP_BS.
InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
InterPro; IPR008266; Tyr_kinase_AS.
InterPro; IPR020635; Tyr_kinase_cat_dom.
Pfam; PF07679; I-set; 1.
Pfam; PF07714; Pkinase_Tyr; 1.
PIRSF; PIRSF000628; FGFR; 1.
PRINTS; PR00109; TYRKINASE.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00219; TyrKc; 1.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF56112; SSF56112; 1.
PROSITE; PS50835; IG_LIKE; 2.
PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; ATP-binding; Cell membrane;
Complete proteome; Cytoplasm; Direct protein sequencing;
Disease mutation; Disulfide bond; Endoplasmic reticulum; Endosome;
Glycoprotein; Immunoglobulin domain; Kinase; Membrane;
Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor;
Reference proteome; Repeat; Secreted; Signal; Transferase;
Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
Ubl conjugation.
SIGNAL 1 21 {ECO:0000269|PubMed:15340161}.
CHAIN 22 802 Fibroblast growth factor receptor 4.
/FTId=PRO_0000016787.
TOPO_DOM 22 369 Extracellular. {ECO:0000255}.
TRANSMEM 370 390 Helical. {ECO:0000255}.
TOPO_DOM 391 802 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 118 Ig-like C2-type 1.
DOMAIN 152 240 Ig-like C2-type 2.
DOMAIN 249 349 Ig-like C2-type 3.
DOMAIN 467 755 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 473 481 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 612 612 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 503 503 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 573 573 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 642 642 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:18670643}.
MOD_RES 643 643 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:18670643}.
MOD_RES 754 754 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:7518429}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 258 258 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 290 290 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 322 322 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 57 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 172 224 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 271 333 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 1 210 Missing (in isoform 3).
{ECO:0000303|PubMed:11781352}.
/FTId=VSP_053542.
VAR_SEQ 353 416 EEDPTWTAAAPEARYTDIILYASGSLALAVLLLLAGLYRGQ
ALHGRHPRPPATVQKLSRFPLAR -> GTGRIPHLTCDSLT
PAGRTKSPTL (in isoform 2).
{ECO:0000303|PubMed:10631118}.
/FTId=VSP_035108.
VARIANT 10 10 V -> I (in dbSNP:rs1966265).
{ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21882254,
ECO:0000269|Ref.8}.
/FTId=VAR_029185.
VARIANT 136 136 P -> L (in dbSNP:rs376618).
{ECO:0000269|PubMed:10631118,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:21882254,
ECO:0000269|Ref.10, ECO:0000269|Ref.7,
ECO:0000269|Ref.8}.
/FTId=VAR_042211.
VARIANT 179 179 T -> A (in dbSNP:rs55675160).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042212.
VARIANT 388 388 G -> R (in PC; also found in other types
of cancer; associated with increased
disease susceptibility, accelerated
cancer progression and poor prognosis;
results in prolonged FGFR4 activity;
causes increased cell motility and tumor
cell invasion possibly due to increased
stability of the protease MMP14;
increased interaction with STAT3; results
in STAT3 phosphorylation and signaling
activation; dbSNP:rs351855).
{ECO:0000269|PubMed:11781352,
ECO:0000269|PubMed:18670643,
ECO:0000269|PubMed:18756523,
ECO:0000269|PubMed:20876804,
ECO:0000269|PubMed:21349172,
ECO:0000269|PubMed:21882254,
ECO:0000269|PubMed:26675719,
ECO:0000269|Ref.8}.
/FTId=VAR_014797.
VARIANT 426 426 G -> S (in dbSNP:rs55879131).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046102.
VARIANT 516 516 D -> N (in dbSNP:rs34158682).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042213.
VARIANT 529 529 R -> Q (in dbSNP:rs34284947).
/FTId=VAR_049720.
VARIANT 550 550 V -> M (in breast pleomorphic lobular
sample; somatic mutation;
dbSNP:rs774571806).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046103.
VARIANT 712 712 P -> T (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046104.
VARIANT 772 772 S -> N (in a lung neuroendocrine
carcinoma sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_046105.
MUTAGEN 503 503 K->R: Loss of kinase activity.
{ECO:0000269|PubMed:11433297,
ECO:0000269|PubMed:17311277}.
MUTAGEN 754 754 Y->F: Loss of interaction with PLCG1.
{ECO:0000269|PubMed:7518429}.
CONFLICT 121 121 L -> S (in Ref. 3; AAF27432).
{ECO:0000305}.
CONFLICT 194 194 E -> G (in Ref. 3; AAF27432).
{ECO:0000305}.
CONFLICT 297 297 D -> V (in Ref. 1; CAA40490).
{ECO:0000305}.
HELIX 445 448 {ECO:0000244|PDB:4QQ5}.
TURN 458 460 {ECO:0000244|PDB:4QQT}.
HELIX 464 466 {ECO:0000244|PDB:4QQT}.
STRAND 467 474 {ECO:0000244|PDB:4QQT}.
STRAND 480 487 {ECO:0000244|PDB:4QQT}.
STRAND 493 495 {ECO:0000244|PDB:5JKG}.
STRAND 497 504 {ECO:0000244|PDB:4QQT}.
HELIX 511 527 {ECO:0000244|PDB:4QQT}.
STRAND 536 540 {ECO:0000244|PDB:4QQT}.
STRAND 542 544 {ECO:0000244|PDB:4QQT}.
STRAND 547 551 {ECO:0000244|PDB:4QQT}.
HELIX 558 563 {ECO:0000244|PDB:4QQT}.
STRAND 572 574 {ECO:0000244|PDB:4TYE}.
HELIX 586 605 {ECO:0000244|PDB:4QQT}.
HELIX 615 617 {ECO:0000244|PDB:4QQT}.
STRAND 618 620 {ECO:0000244|PDB:4QQT}.
STRAND 626 628 {ECO:0000244|PDB:4QQT}.
TURN 631 635 {ECO:0000244|PDB:4XCU}.
HELIX 637 639 {ECO:0000244|PDB:4QQT}.
STRAND 642 644 {ECO:0000244|PDB:4UXQ}.
HELIX 652 655 {ECO:0000244|PDB:4QQT}.
HELIX 658 663 {ECO:0000244|PDB:4QQT}.
HELIX 668 683 {ECO:0000244|PDB:4QQT}.
STRAND 689 692 {ECO:0000244|PDB:4TYJ}.
HELIX 695 703 {ECO:0000244|PDB:4QQT}.
HELIX 716 725 {ECO:0000244|PDB:4QQT}.
HELIX 730 732 {ECO:0000244|PDB:4QQT}.
HELIX 736 748 {ECO:0000244|PDB:4QQT}.
SEQUENCE 802 AA; 87954 MW; B22B259831BB889F CRC64;
MRLLLALLGV LLSVPGPPVL SLEASEEVEL EPCLAPSLEQ QEQELTVALG QPVRLCCGRA
ERGGHWYKEG SRLAPAGRVR GWRGRLEIAS FLPEDAGRYL CLARGSMIVL QNLTLITGDS
LTSSNDDEDP KSHRDPSNRH SYPQQAPYWT HPQRMEKKLH AVPAGNTVKF RCPAAGNPTP
TIRWLKDGQA FHGENRIGGI RLRHQHWSLV MESVVPSDRG TYTCLVENAV GSIRYNYLLD
VLERSPHRPI LQAGLPANTT AVVGSDVELL CKVYSDAQPH IQWLKHIVIN GSSFGADGFP
YVQVLKTADI NSSEVEVLYL RNVSAEDAGE YTCLAGNSIG LSYQSAWLTV LPEEDPTWTA
AAPEARYTDI ILYASGSLAL AVLLLLAGLY RGQALHGRHP RPPATVQKLS RFPLARQFSL
ESGSSGKSSS SLVRGVRLSS SGPALLAGLV SLDLPLDPLW EFPRDRLVLG KPLGEGCFGQ
VVRAEAFGMD PARPDQASTV AVKMLKDNAS DKDLADLVSE MEVMKLIGRH KNIINLLGVC
TQEGPLYVIV ECAAKGNLRE FLRARRPPGP DLSPDGPRSS EGPLSFPVLV SCAYQVARGM
QYLESRKCIH RDLAARNVLV TEDNVMKIAD FGLARGVHHI DYYKKTSNGR LPVKWMAPEA
LFDRVYTHQS DVWSFGILLW EIFTLGGSPY PGIPVEELFS LLREGHRMDR PPHCPPELYG
LMRECWHAAP SQRPTFKQLV EALDKVLLAV SEEYLDLRLT FGPYSPSGGD ASSTCSSSDS
VFSHDPLPLG SSSFPFGSGV QT


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E0074h ELISA Basic fibroblast growth factor receptor 1,BFGFR,BFGFR,bFGF-R-1,CEK,FGFBR,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,FLG,FLT2,FLT-2,Fms-like tyrosine kinase 2,HBGFR,Homo sapiens,Human,N-sam 96T
U0074h CLIA Basic fibroblast growth factor receptor 1,BFGFR,BFGFR,bFGF-R-1,CEK,FGFBR,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,FLG,FLT2,FLT-2,Fms-like tyrosine kinase 2,HBGFR,Homo sapiens,Human,N-sam, 96T
U0074c CLIA Basic fibroblast growth factor receptor 1,bFGF-R-1,CEK1,Chicken,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,Gallus gallus,Tyrosine kinase receptor CEK1 96T
E0074c ELISA Basic fibroblast growth factor receptor 1,bFGF-R-1,CEK1,Chicken,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,Gallus gallus,Tyrosine kinase receptor CEK1 96T
E0074c ELISA kit Basic fibroblast growth factor receptor 1,bFGF-R-1,CEK1,Chicken,FGFR1,FGFR-1,Fibroblast growth factor receptor 1,Gallus gallus,Tyrosine kinase receptor CEK1 96T
orb61378 Vargatef Vargatef is an indolinone derivative that potently inhibits vascular endothelial growth factor receptor (VEGFR), platelet-derived growth factor receptor (PDGFR) and fibroblast growth factor r 25 mg
E0034m ELISA Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
E0034m ELISA kit Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
U0034m CLIA Fgf4,FGF-4,Fgf-4,Fibroblast growth factor 4,HBGF-4,Heparin-binding growth factor 4,Kfgf,K-fibroblast growth factor,Mouse,Mus musculus 96T
18-272-195176 FGFR2 - Rabbit polyclonal to FGFR2; EC 2.7.10.1; FGFR-2; Keratinocyte growth factor receptor 2; CD332 antigen Polyclonal 0.1 ml
18-272-195177 FGFR2 - Rabbit polyclonal to FGFR2; EC 2.7.10.1; FGFR-2; Keratinocyte growth factor receptor 2; CD332 antigen Polyclonal 0.05 ml
M10-045 FGF acidic, Host: E. coli, Species: Mouse, Synonyms: HBGF-1; aFGF; acidic fibroblast growth factor; fibroblast growth factor 1 (acidic); heparin-binding growth factor 1 50 ug
10-663-45195 Glycosylated Fibroblast Growth Factor-acidic Human - HBGF-1; Acidic fibroblast growth factor; aFGF; Beta-endothelial cell growth factor; ECGF-beta N_A 0.01 mg
10-663-45195 Glycosylated Fibroblast Growth Factor-acidic Human - HBGF-1; Acidic fibroblast growth factor; aFGF; Beta-endothelial cell growth factor; ECGF-beta N_A 1 mg
10-663-45195 Glycosylated Fibroblast Growth Factor-acidic Human - HBGF-1; Acidic fibroblast growth factor; aFGF; Beta-endothelial cell growth factor; ECGF-beta N_A 0.002 mg
M10-045 FGF acidic Mouse Host: E. coli HBGF-1; aFGF; acidic fibroblast growth factor; fibroblast growth factor 1 (acidic); heparin-binding growth factor 1 50
10-663-45129 Fibroblast Growth Factor-acidic (FGF-a) Human - HBGF-1; Acidic fibroblast growth factor; aFGF; Beta-endothelial cell growth factor; ECGF-beta N_A 1 mg


 

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