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Fibroblast growth factor receptor 3 (FGFR-3) (EC 2.7.10.1) (CD antigen CD333)

 FGFR3_HUMAN             Reviewed;         806 AA.
P22607; D3DVP9; D3DVQ0; Q14308; Q16294; Q16608; Q59FL9;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
27-SEP-2017, entry version 222.
RecName: Full=Fibroblast growth factor receptor 3;
Short=FGFR-3;
EC=2.7.10.1;
AltName: CD_antigen=CD333;
Flags: Precursor;
Name=FGFR3; Synonyms=JTK4;
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=1847508; DOI=10.1073/pnas.88.4.1095;
Keegan K., Johnson D.E., Williams L.T., Hayman M.J.;
"Isolation of an additional member of the fibroblast growth factor
receptor family, FGFR-3.";
Proc. Natl. Acad. Sci. U.S.A. 88:1095-1099(1991).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBUNIT, FGF1- AND
FGF2-BINDING, SUBCELLULAR LOCATION, GLYCOSYLATION, AND DIMERIZATION.
TISSUE=Squamous cell carcinoma;
PubMed=11703096; DOI=10.1006/mcbr.2001.0306;
Terada M., Shimizu A., Sato N., Miyakaze S.I., Katayama H.,
Kurokawa-Seo M.;
"Fibroblast growth factor receptor 3 lacking the Ig IIIb and
transmembrane domains secreted from human squamous cell carcinoma DJM-
1 binds to FGFs.";
Mol. Cell Biol. Res. Commun. 4:365-373(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ARG-65; LEU-384;
THR-441; THR-717 AND PHE-726.
NIEHS SNPs program;
Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] OF 76-806 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Fetal brain;
PubMed=1664411; DOI=10.1016/0888-7543(91)90041-C;
Thompson L.M., Plummer S., Schalling M., Altherr M.R., Gusella J.F.,
Housman D.E., Wasmuth J.J.;
"A gene encoding a fibroblast growth factor receptor isolated from the
Huntington disease gene region of human chromosome 4.";
Genomics 11:1133-1142(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 614-681.
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).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 311-358 (ISOFORM 2).
TISSUE=Colon tumor;
PubMed=7923141;
Murgue B., Tsunekawa S., Rosenberg I., deBeaumont M., Podolsky D.K.;
"Identification of a novel variant form of fibroblast growth factor
receptor 3 (FGFR3 IIIb) in human colonic epithelium.";
Cancer Res. 54:5206-5211(1994).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 311-358 (ISOFORM 2).
TISSUE=Keratinocyte;
PubMed=7495869; DOI=10.1016/0167-4781(95)00156-B;
Scotet E., Houssaint E.;
"The choice between alternative IIIb and IIIc exons of the FGFR-3 gene
is not strictly tissue-specific.";
Biochim. Biophys. Acta 1264:238-242(1995).
[11]
INTERACTION WITH FGF1; FGF2; FGF4; 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).
[12]
INVOLVEMENT IN SADDAN, VARIANT SADDAN MET-650, AND CHARACTERIZATION OF
VARIANT SADDAN MET-650.
PubMed=10053006; DOI=10.1086/302275;
Tavormina P.L., Bellus G.A., Webster M.K., Bamshad M.J., Fraley A.E.,
McIntosh I., Szabo J., Jiang W., Jabs E.W., Wilcox W.R., Wasmuth J.J.,
Donoghue D.J., Thompson L.M., Francomano C.A.;
"A novel skeletal dysplasia with developmental delay and acanthosis
nigricans is caused by a Lys650Met mutation in the fibroblast growth
factor receptor 3 gene.";
Am. J. Hum. Genet. 64:722-731(1999).
[13]
FUNCTION AS FGF9 RECEPTOR IN CHONDROCYTES AND IN ACTIVATION OF
SIGNALING PATHWAYS, SUBUNIT, SUBCELLULAR LOCATION, DEGRADATION,
AUTOPHOSPHORYLATION, AND CHARACTERIZATION OF VARIANT ACH ARG-380.
PubMed=10611230; DOI=10.1128/MCB.20.2.516-522.2000;
Monsonego-Ornan E., Adar R., Feferman T., Segev O., Yayon A.;
"The transmembrane mutation G380R in fibroblast growth factor receptor
3 uncouples ligand-mediated receptor activation from down-
regulation.";
Mol. Cell. Biol. 20:516-522(2000).
[14]
FUNCTION IN STIMULATION OF CELL PROLIFERATION; PHOSPHORYLATION OF
PIK3R1; PTPN11/SHP2; STAT1; STAT3 AND MAP KINASES, PHOSPHORYLATION AT
TYR-724, MUTAGENESIS OF TYR-577; TYR-724; TYR-760 AND TYR-770, AND
CHARACTERIZATION OF VARIANT GLU-650.
PubMed=11294897; DOI=10.1091/mbc.12.4.931;
Hart K.C., Robertson S.C., Donoghue D.J.;
"Identification of tyrosine residues in constitutively activated
fibroblast growth factor receptor 3 involved in mitogenesis, Stat
activation, and phosphatidylinositol 3-kinase activation.";
Mol. Biol. Cell 12:931-942(2001).
[15]
UBIQUITINATION, PHOSPHORYLATION, CATALYTIC ACTIVITY, MUTAGENESIS OF
LYS-508, CHARACTERIZATION OF VARIANT ACH ARG-380, AND CHARACTERIZATION
OF VARIANT TD2 GLU-650.
PubMed=12297284; DOI=10.1016/S0014-5793(02)03255-6;
Monsonego-Ornan E., Adar R., Rom E., Yayon A.;
"FGF receptors ubiquitylation: dependence on tyrosine kinase activity
and role in downregulation.";
FEBS Lett. 528:83-89(2002).
[16]
FUNCTION AS PROTO-ONCOGENE IN ACTIVATION OF SIGNALING AND CELL
PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF FRS2, CHARACTERIZATION
OF VARIANT GLU-650, AND AUTOPHOSPHORYLATION.
PubMed=14534538; DOI=10.1038/sj.onc.1206798;
Agazie Y.M., Movilla N., Ischenko I., Hayman M.J.;
"The phosphotyrosine phosphatase SHP2 is a critical mediator of
transformation induced by the oncogenic fibroblast growth factor
receptor 3.";
Oncogene 22:6909-6918(2003).
[17]
INTERACTION WITH FGF1; FGF8; FGF9; FGF17; FGF18; FGF19 AND FGF20, 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).
[18]
INTERACTION WITH SOCS1 AND SOCS3, FUNCTION IN ACTIVATION OF STAT1 AND
MAP KINASES, GLYCOSYLATION, PHOSPHORYLATION, MUTAGENESIS OF LYS-508,
AND SUBCELLULAR LOCATION.
PubMed=16410555; DOI=10.1242/jcs.02740;
Ben-Zvi T., Yayon A., Gertler A., Monsonego-Ornan E.;
"Suppressors of cytokine signaling (SOCS) 1 and SOCS3 interact with
and modulate fibroblast growth factor receptor signaling.";
J. Cell Sci. 119:380-387(2006).
[19]
FUNCTION IN REGULATION OF CHONDROCYTE PROLIFERATION AND IN ACTIVATION
OF PLCG1 AND STAT1, INTERACTION WITH FHF1 AND HEPARIN, SUBCELLULAR
LOCATION, PHOSPHORYLATION, AND CHARACTERIZATION OF VARIANTS ARG-380;
GLU-650 AND MET-650.
PubMed=17561467; DOI=10.1016/j.bone.2006.11.030;
Harada D., Yamanaka Y., Ueda K., Nishimura R., Morishima T., Seino Y.,
Tanaka H.;
"Sustained phosphorylation of mutated FGFR3 is a crucial feature of
genetic dwarfism and induces apoptosis in the ATDC5 chondrogenic cell
line via PLCgamma-activated STAT1.";
Bone 41:273-281(2007).
[20]
FUNCTION IN PHOSPHORYLATION OF CBL, UBIQUITINATION, GLYCOSYLATION,
SUBCELLULAR LOCATION, ENZYME REGULATION, AND CHARACTERIZATION OF
VARIANTS CYS-248; CYS-373 AND MET-650.
PubMed=17509076; DOI=10.1111/j.1742-4658.2007.05835.x;
Bonaventure J., Horne W.C., Baron R.;
"The localization of FGFR3 mutations causing thanatophoric dysplasia
type I differentially affects phosphorylation, processing and
ubiquitylation of the receptor.";
FEBS J. 274:3078-3093(2007).
[21]
FUNCTION IN PHOSPHORYLATION OF FRS2, CHARACTERIZATION OF VARIANT
GLU-650, ENZYME REGULATION, AND CATALYTIC ACTIVITY.
PubMed=17145761; DOI=10.1074/jbc.M606144200;
Krejci P., Masri B., Salazar L., Farrington-Rock C., Prats H.,
Thompson L.M., Wilcox W.R.;
"Bisindolylmaleimide I suppresses fibroblast growth factor-mediated
activation of Erk MAP kinase in chondrocytes by preventing Shp2
association with the Frs2 and Gab1 adaptor proteins.";
J. Biol. Chem. 282:2929-2936(2007).
[22]
INTERACTION WITH FGF19; FGF21 AND KLB.
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).
[23]
FUNCTION IN STAT1 PHOSPHORYLATION, 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).
[24]
FUNCTION IN ACTIVATION OF STAT1; STAT5; MAPK1/ERK2; MAPK3/ERK1 AND THE
MAP KINASE SIGNALING PATHWAY.
PubMed=19088846; DOI=10.1371/journal.pone.0003961;
Krejci P., Salazar L., Kashiwada T.A., Chlebova K., Salasova A.,
Thompson L.M., Bryja V., Kozubik A., Wilcox W.R.;
"Analysis of STAT1 activation by six FGFR3 mutants associated with
skeletal dysplasia undermines dominant role of STAT1 in FGFR3
signaling in cartilage.";
PLoS ONE 3:E3961-E3961(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[26]
FUNCTION, INTERACTION WITH PIK3R1 AND PLCG1, AND PHOSPHORYLATION AT
TYR-760.
PubMed=19286672; DOI=10.1093/hmg/ddp116;
Salazar L., Kashiwada T., Krejci P., Muchowski P., Donoghue D.,
Wilcox W.R., Thompson L.M.;
"A novel interaction between fibroblast growth factor receptor 3 and
the p85 subunit of phosphoinositide 3-kinase: activation-dependent
regulation of ERK by p85 in multiple myeloma cells.";
Hum. Mol. Genet. 18:1951-1961(2009).
[27]
REVIEW ON FUNCTION; ALTERNATIVE SPLICING; SIGNALING AND ROLE IN
DISEASE.
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).
[28]
REVIEW ON FUNCTION; LIGANDS; SIGNALING; ALTERNATIVE SPLICING; DOMAIN;
ROLE IN DISEASE; UBIQUITINATION AND DEGRADATION.
PubMed=15748888; DOI=10.1016/j.yexcr.2004.11.012;
L'Hote C.G., Knowles M.A.;
"Cell responses to FGFR3 signalling: growth, differentiation and
apoptosis.";
Exp. Cell Res. 304:417-431(2005).
[29]
REVIEW ON ROLE IN SKELETON DEVELOPMENT AND DISEASE.
PubMed=19066716; DOI=10.1007/s00774-008-0009-7;
Harada D., Yamanaka Y., Ueda K., Tanaka H., Seino Y.;
"FGFR3-related dwarfism and cell signaling.";
J. Bone Miner. Metab. 27:9-15(2009).
[30]
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).
[31]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
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).
[32]
X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 32-365 IN COMPLEX WITH FGF1,
ENZYME REGULATION, AND DOMAIN.
PubMed=14732692; DOI=10.1073/pnas.0307287101;
Olsen S.K., Ibrahimi O.A., Raucci A., Zhang F., Eliseenkova A.V.,
Yayon A., Basilico C., Linhardt R.J., Schlessinger J., Mohammadi M.;
"Insights into the molecular basis for fibroblast growth factor
receptor autoinhibition and ligand-binding promiscuity.";
Proc. Natl. Acad. Sci. U.S.A. 101:935-940(2004).
[33]
VARIANT ACH ARG-380.
PubMed=8078586; DOI=10.1038/371252a0;
Rousseau F., Bonaventure J., Legeai-Mallet L., Pelet A., Rozet J.-M.,
Maroteaux P., le Merrer M., Munnich A.;
"Mutations in the gene encoding fibroblast growth factor receptor-3 in
achondroplasia.";
Nature 371:252-254(1994).
[34]
VARIANT ACH ARG-380.
PubMed=7847369;
Bellus G.A., Hefferon T.W., de Luna R.I., Hecht J.T., Horton W.A.,
Machado M., Kaitila I., McIntosh I., Francomano C.A.;
"Achondroplasia is defined by recurrent G380R mutations of FGFR3.";
Am. J. Hum. Genet. 56:368-373(1995).
[35]
VARIANT ACH CYS-375.
PubMed=7758520; DOI=10.1007/BF01954274;
Superti-Furga A., Eich G., Bucher H.U., Wisser J., Giedion A.,
Gitzelmann R., Steinmann B.;
"A glycine 375-to-cysteine substitution in the transmembrane domain of
the fibroblast growth factor receptor-3 in a newborn with
achondroplasia.";
Eur. J. Pediatr. 154:215-219(1995).
[36]
VARIANT TD1 CYS-249.
PubMed=8589699; DOI=10.1093/hmg/4.11.2175;
Tavormina P.L., Rimoin D.L., Cohn D.H., Zhu Y.-Z., Shiang R.,
Wasmuth J.J.;
"Another mutation that results in the substitution of an unpaired
cysteine residue in the extracellular domain of FGFR3 in thanatophoric
dysplasia type I.";
Hum. Mol. Genet. 4:2175-2177(1995).
[37]
VARIANTS TD1 CYS-248 AND CYS-371, AND VARIANT TD2 GLU-650.
PubMed=7773297; DOI=10.1038/ng0395-321;
Tavormina P.L., Shiang R., Thompson L.M., Zhu Y.-Z., Wilkin D.J.,
Lachman R.S., Wilcox W.R., Rimoin D.L., Cohn D.H., Wasmuth J.J.;
"Thanatophoric dysplasia (types I and II) caused by distinct mutations
in fibroblast growth factor receptor 3.";
Nat. Genet. 9:321-328(1995).
[38]
VARIANT HYPOCHONDROPLASIA LYS-540.
PubMed=7670477; DOI=10.1038/ng0795-357;
Bellus G.A., McIntosh I., Smith E.A., Aylsworth A.S., Kaitila I.,
Horton W.A., Greenhaw G.A., Hecht J.T., Francomano C.A.;
"A recurrent mutation in the tyrosine kinase domain of fibroblast
growth factor receptor 3 causes hypochondroplasia.";
Nat. Genet. 10:357-359(1995).
[39]
VARIANT CAN GLU-391.
PubMed=7493034; DOI=10.1038/ng1295-462;
Meyers G.A., Orlow S.J., Munro I.R., Przylepa K.A., Jabs E.W.;
"Fibroblast growth factor receptor 3 (FGFR3) transmembrane mutation in
Crouzon syndrome with acanthosis nigricans.";
Nat. Genet. 11:462-464(1995).
[40]
CHARACTERIZATION OF VARIANT ACH ARG-380.
PubMed=8599935;
Webster M.K., Donoghue D.J.;
"Constitutive activation of fibroblast growth factor receptor 3 by the
transmembrane domain point mutation found in achondroplasia.";
EMBO J. 15:520-527(1996).
[41]
VARIANTS TD1 CYS-248; CYS-249; CYS-370 AND CYS-373.
PubMed=8845844; DOI=10.1093/hmg/5.4.509;
Rousseau F., el Ghouzzi V., Delezoide A.-L., Legeai-Mallet L.,
le Merrer M., Munnich A., Bonaventure J.;
"Missense FGFR3 mutations create cysteine residues in thanatophoric
dwarfism type I (TD1).";
Hum. Mol. Genet. 5:509-512(1996).
[42]
CHARACTERIZATION OF VARIANT TD2 GLU-650, CHARACTERIZATION OF VARIANT
GLN-650, AND PHOSPHORYLATION AT TYR-647 AND TYR-648.
PubMed=8754806; DOI=10.1128/MCB.16.8.4081;
Webster M.K., D'Avis P.Y., Robertson S.C., Donoghue D.J.;
"Profound ligand-independent kinase activation of fibroblast growth
factor receptor 3 by the activation loop mutation responsible for a
lethal skeletal dysplasia, thanatophoric dysplasia type II.";
Mol. Cell. Biol. 16:4081-4087(1996).
[43]
VARIANT MNKS ARG-250.
PubMed=9042914;
Muenke M., Gripp K.W., McDonald-Mcginn D.M., Gaudenz K.,
Whitaker L.A., Bartlett S.P., Markowitz R.I., Robin N.H., Nwokoro N.,
Mulvihill J.J., Losken H.W., Mulliken J.B., Guttmacher A.E.,
Wilroy R.S., Clarke L.A., Hollway G., Ades L.C., Haan E.A.,
Mulley J.C., Cohen M.M. Jr., Bellus G.A., Francomano C.A.,
Moloney D.M., Wall S.A., Wilkie A.O.M., Zackai E.H.;
"A unique point mutation in the fibroblast growth factor receptor 3
gene (FGFR3) defines a new craniosynostosis syndrome.";
Am. J. Hum. Genet. 60:555-564(1997).
[44]
INVOLVEMENT IN MULTIPLE MYELOMA, AND VARIANTS CYS-373; GLU-650 AND
MET-650.
PubMed=9207791; DOI=10.1038/ng0797-260;
Chesi M., Nardini E., Brents L.A., Schroeck E., Ried T., Kuehl W.M.,
Bergsagel P.L.;
"Frequent translocation t(4;14)(p16.3;q32.3) in multiple myeloma is
associated with increased expression and activating mutations of
fibroblast growth factor receptor 3.";
Nat. Genet. 16:260-264(1997).
[45]
VARIANT TD1 CYS-370.
PubMed=9790257; DOI=10.1507/endocrj.45.Suppl_S171;
Katsumata N., Kuno T., Miyazaki S., Mikami S., Nagashima-Miyokawa A.,
Nimura A., Horikawa R., Tanaka T.;
"G370C mutation in the FGFR3 gene in a Japanese patient with
thanatophoric dysplasia.";
Endocr. J. 45:S171-S174(1998).
[46]
VARIANT HYPOCHONDROPLASIA VAL-538.
PubMed=10215410;
DOI=10.1002/(SICI)1098-1004(1998)11:4<333::AID-HUMU17>3.0.CO;2-J;
Grigelioniene G., Hagenaes L., Ekloef O., Neumeyer L., Haereid P.E.,
Anvret M.;
"A novel missense mutation Ile538Val in the fibroblast growth factor
receptor 3 in hypochondroplasia.";
Hum. Mutat. 11:333-333(1998).
[47]
VARIANT HYPOCHONDROPLASIA THR-540.
PubMed=9452043;
Deutz-Terlouw P.P., Losekoot M., Aalfs C.M., Hennekam R.C.M.,
Bakker E.;
"Asn540Thr substitution in the fibroblast growth factor receptor 3
tyrosine kinase domain causing hypochondroplasia.";
Hum. Mutat. Suppl. 1:S62-S65(1998).
[48]
VARIANT TD1 MET-650.
PubMed=10671061;
Kitoh H., Brodie S.G., Kupke K.G., Lachman R.S., Wilcox W.R.;
"Lys650Met substitution in the tyrosine kinase domain of the
fibroblast growth factor receptor gene causes thanatophoric dysplasia
type I.";
Hum. Mutat. 12:362-363(1998).
[49]
VARIANT ARG-250.
PubMed=9525367; DOI=10.1016/S0140-6736(98)24012-8;
Hollway G.E., Suthers G.K., Battese K.M., Turner A.M., David D.J.,
Mulley J.C.;
"Deafness due to Pro250Arg mutation of FGFR3.";
Lancet 351:877-878(1998).
[50]
VARIANTS TD1 CYS-248; CYS-249 AND CYS-373.
PubMed=10360402;
DOI=10.1002/(SICI)1096-8628(19990611)84:5<476::AID-AJMG12>3.3.CO;2-O;
Brodie S.G., Kitoh H., Lachman R.S., Nolasco L.M., Mekikian P.B.,
Wilcox W.R.;
"Platyspondylic lethal skeletal dysplasia, San Diego type, is caused
by FGFR3 mutations.";
Am. J. Med. Genet. 84:476-480(1999).
[51]
VARIANT MNKS ARG-250.
PubMed=9950359;
Lajeunie E., El Ghouzzi V., Le Merrer M., Munnich A., Bonaventure J.,
Renier D.;
"Sex related expressivity of the phenotype in coronal craniosynostosis
caused by the recurrent P250R FGFR3 mutation.";
J. Med. Genet. 36:9-13(1999).
[52]
VARIANTS BLC CYS-248; CYS-249; CYS-370 AND GLU-650, AND VARIANTS CERCA
CYS-248; CYS-249; CYS-370 AND GLU-650.
PubMed=10471491; DOI=10.1038/12615;
Cappellen D., De Oliveira C., Ricol D., Gil Diez de Medina S.,
Bourdin J., Sastre-Garau X., Chopin D., Thiery J.P., Radvanyi F.;
"Frequent activating mutations of FGFR3 in human bladder and cervix
carcinomas.";
Nat. Genet. 23:18-20(1999).
[53]
VARIANT HYPOCHONDROPLASIA GLN-650.
PubMed=11055896; DOI=10.1086/316892;
Bellus G.A., Spector E.B., Speiser P.W., Weaver C.A., Garber A.T.,
Bryke C.R., Israel J., Rosengren S.S., Webster M.K., Donoghue D.J.,
Francomano C.A.;
"Distinct missense mutations of the FGFR3 Lys650 codon modulate
receptor kinase activation and the severity of the skeletal dysplasia
phenotype.";
Am. J. Hum. Genet. 67:1411-1421(2000).
[54]
VARIANT HYPOCHONDROPLASIA SER-540.
PubMed=10777366; DOI=10.1136/jmg.37.3.220;
Mortier G., Nuytinck L., Craen M., Renard J.-P., Leroy J.G.,
De Paepe A.;
"Clinical and radiographic features of a family with hypochondroplasia
owing to a novel asn540ser mutation in the fibroblast growth factor
receptor 3 gene.";
J. Med. Genet. 37:220-224(2000).
[55]
VARIANT MNKS ARG-250.
PubMed=11746040; DOI=10.1002/ajmg.10049;
Lowry R.B., Jabs E.W., Graham G.E., Gerritsen J., Fleming J.;
"Syndrome of coronal craniosynostosis, Klippel-Feil anomaly, and
sprengel shoulder with and without Pro250Arg mutation in the FGFR3
gene.";
Am. J. Med. Genet. 104:112-119(2001).
[56]
INVOLVEMENT IN MULTIPLE MYELOMA, AND VARIANT CYS-248.
PubMed=11529856; DOI=10.1046/j.1365-2141.2001.02957.x;
Intini D., Baldini L., Fabris S., Lombardi L., Ciceri G., Maiolo A.T.,
Neri A.;
"Analysis of FGFR3 gene mutations in multiple myeloma patients with
t(4;14).";
Br. J. Haematol. 114:362-364(2001).
[57]
VARIANT COLORECTAL CANCER LYS-322.
PubMed=11325814;
Jang J.-H., Shin K.-H., Park J.-G.;
"Mutations in fibroblast growth factor receptor 2 and fibroblast
growth factor receptor 3 genes associated with human gastric and
colorectal cancers.";
Cancer Res. 61:3541-3543(2001).
[58]
VARIANT BLC CANCER GLN-650.
PubMed=11314002; DOI=10.1038/sj.onc.1204110;
Sibley K., Cuthbert-Heavens D., Knowles M.A.;
"Loss of heterozygosity at 4p16.3 and mutation of FGFR3 in
transitional cell carcinoma.";
Oncogene 20:686-691(2001).
[59]
VARIANT HYPOCHONDROPLASIA SER-540.
PubMed=12707965; DOI=10.1002/ajmg.a.10238;
Thauvin-Robinet C., Faivre L., Lewin P., De Monleon J.-V.,
Francois C., Huet F., Couailler J.-F., Campos-Xavier A.B.,
Bonaventure J., Le Merrer M.;
"Hypochondroplasia and stature within normal limits: another family
with an Asn540-to-Ser mutation in the fibroblast growth factor
receptor 3 gene.";
Am. J. Med. Genet. A 119:81-84(2003).
[60]
VARIANTS KERSEB CYS-248; CYS-249; CYS-370; CYS-371; CYS-373; GLU-650
AND MET-650.
PubMed=15772091; DOI=10.1093/hmg/ddi127;
Logie A., Dunois-Larde C., Rosty C., Levrel O., Blanche M.,
Ribeiro A., Gasc J.-M., Jorcano J., Werner S., Sastre-Garau X.,
Thiery J.P., Radvanyi F.;
"Activating mutations of the tyrosine kinase receptor FGFR3 are
associated with benign skin tumors in mice and humans.";
Hum. Mol. Genet. 14:1153-1160(2005).
[61]
VARIANT CATSHLS HIS-621.
PubMed=17033969; DOI=10.1086/508433;
Toydemir R.M., Brassington A.E., Bayrak-Toydemir P., Krakowiak P.A.,
Jorde L.B., Whitby F.G., Longo N., Viskochil D.H., Carey J.C.,
Bamshad M.J.;
"A novel mutation in FGFR3 causes camptodactyly, tall stature, and
hearing loss (CATSHL) syndrome.";
Am. J. Hum. Genet. 79:935-941(2006).
[62]
VARIANTS KNEN CYS-248; CYS-370 AND ARG-380.
PubMed=16841094; DOI=10.1172/JCI28163;
Hafner C., van Oers J.M.M., Vogt T., Landthaler M., Stoehr R.,
Blaszyk H., Hofstaedter F., Zwarthoff E.C., Hartmann A.;
"Mosaicism of activating FGFR3 mutations in human skin causes
epidermal nevi.";
J. Clin. Invest. 116:2201-2207(2006).
[63]
VARIANT LADDS ASN-513.
PubMed=16501574; DOI=10.1038/ng1757;
Rohmann E., Brunner H.G., Kayserili H., Uyguner O., Nuernberg G.,
Lew E.D., Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M.,
Leroy J.G., Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J.,
Yueksel-Apak M., Nuernberg P., Kubisch C., Schlessinger J.,
van Bokhoven H., Wollnik B.;
"Mutations in different components of FGF signaling in LADD
syndrome.";
Nat. Genet. 38:414-417(2006).
[64]
VARIANT CAN GLU-391.
PubMed=17935505; DOI=10.1111/j.1399-0004.2007.00884.x;
Arnaud-Lopez L., Fragoso R., Mantilla-Capacho J., Barros-Nunez P.;
"Crouzon with acanthosis nigricans. Further delineation of the
syndrome.";
Clin. Genet. 72:405-410(2007).
[65]
VARIANTS [LARGE SCALE ANALYSIS] SER-79; ARG-228; MET-338; LEU-384;
ASN-646 AND GLU-650.
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).
[66]
VARIANT TGCT GLU-650.
PubMed=19855393; DOI=10.1038/ng.470;
Goriely A., Hansen R.M., Taylor I.B., Olesen I.A., Jacobsen G.K.,
McGowan S.J., Pfeifer S.P., McVean G.A., Rajpert-De Meyts E.,
Wilkie A.O.;
"Activating mutations in FGFR3 and HRAS reveal a shared genetic origin
for congenital disorders and testicular tumors.";
Nat. Genet. 41:1247-1252(2009).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for fibroblast growth factors and plays an essential role
in the regulation of cell proliferation, differentiation and
apoptosis. Plays an essential role in the regulation of
chondrocyte differentiation, proliferation and apoptosis, and is
required for normal skeleton development. Regulates both
osteogenesis and postnatal bone mineralization by osteoblasts.
Promotes apoptosis in chondrocytes, but can also promote cancer
cell proliferation. Required for normal development of the inner
ear. Phosphorylates PLCG1, CBL 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. Plays a role in the regulation of vitamin D metabolism.
Mutations that lead to constitutive kinase activation or impair
normal FGFR3 maturation, internalization and degradation lead to
aberrant signaling. Over-expressed or constitutively activated
FGFR3 promotes activation of PTPN11/SHP2, STAT1, STAT5A and
STAT5B. Secreted isoform 3 retains its capacity to bind FGF1 and
FGF2 and hence may interfere with FGF signaling.
{ECO:0000269|PubMed:10611230, ECO:0000269|PubMed:11294897,
ECO:0000269|PubMed:11703096, ECO:0000269|PubMed:14534538,
ECO:0000269|PubMed:16410555, ECO:0000269|PubMed:16597617,
ECO:0000269|PubMed:17145761, ECO:0000269|PubMed:17311277,
ECO:0000269|PubMed:17509076, ECO:0000269|PubMed:17561467,
ECO:0000269|PubMed:19088846, ECO:0000269|PubMed:19286672,
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:12297284,
ECO:0000269|PubMed:17145761}.
-!- 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. Inhibited
by SU5402. {ECO:0000269|PubMed:14732692,
ECO:0000269|PubMed:17145761, ECO:0000269|PubMed:17509076}.
-!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts with
FGF1, FGF2, FGF4, FGF6; FGF8, FGF9, FGF10, FGF17, FGF18, FGF19,
FGF20 and FGF23 (in vitro). Interacts with KLB. Affinity for
fibroblast growth factors (FGFs) is increased by heparan sulfate
glycosaminoglycans that function as coreceptors. Likewise, KLB
increases the affinity for FGF19 and FGF21. Interacts with PIK3R1,
PLCG1, SOCS1 and SOCS3. Isoform 3 forms disulfide-linked dimers.
{ECO:0000269|PubMed:10611230, ECO:0000269|PubMed:11703096,
ECO:0000269|PubMed:14732692, ECO:0000269|PubMed:16410555,
ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17561467,
ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:19286672,
ECO:0000269|PubMed:8663044}.
-!- INTERACTION:
P05230:FGF1; NbExp=3; IntAct=EBI-348399, EBI-698068;
P08238:HSP90AB1; NbExp=2; IntAct=EBI-348399, EBI-352572;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
membrane protein. Cytoplasmic vesicle. Endoplasmic reticulum.
Note=The activated receptor is rapidly internalized and degraded.
Detected in intracellular vesicles after internalization of the
autophosphorylated receptor.
-!- SUBCELLULAR LOCATION: Isoform 2: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 4: Cell membrane {ECO:0000250};
Single-pass type I membrane protein {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=IIIc;
IsoId=P22607-1; Sequence=Displayed;
Name=2; Synonyms=IIIb;
IsoId=P22607-2; Sequence=VSP_002988;
Name=3; Synonyms=FGFR3deltaTM;
IsoId=P22607-3; Sequence=VSP_002989;
Name=4;
IsoId=P22607-4; Sequence=VSP_040945;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in brain, kidney and testis. Very
low or no expression in spleen, heart, and muscle. In 20- to 22-
week old fetuses it is expressed at high level in kidney, lung,
small intestine and brain, and to a lower degree in spleen, liver,
and muscle. Isoform 2 is detected in epithelial cells. Isoform 1
is not detected in epithelial cells. Isoform 1 and isoform 2 are
detected in fibroblastic cells. {ECO:0000269|PubMed:1664411}.
-!- DOMAIN: The second and third Ig-like domains directly interact
with fibroblast growth factors (FGF) and heparan sulfate
proteoglycans. {ECO:0000269|PubMed:14732692}.
-!- 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. Phosphorylation at Tyr-724 is essential for
stimulation of cell proliferation and activation of PIK3R1, STAT1
and MAP kinase signaling. Phosphorylation at Tyr-760 is required
for interaction with PIK3R1 and PLCG1.
{ECO:0000269|PubMed:11294897, ECO:0000269|PubMed:19286672}.
-!- PTM: Ubiquitinated. Is rapidly ubiquitinated after ligand binding
and autophosphorylation, leading to receptor internalization and
degradation. Subject to both proteasomal and lysosomal
degradation. {ECO:0000269|PubMed:12297284,
ECO:0000269|PubMed:17509076}.
-!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan
chains undergo further maturation to an Endo H-resistant form in
the Golgi apparatus. {ECO:0000269|PubMed:11703096,
ECO:0000269|PubMed:16410555, ECO:0000269|PubMed:17311277,
ECO:0000269|PubMed:17509076}.
-!- DISEASE: Achondroplasia (ACH) [MIM:100800]: A frequent form of
short-limb dwarfism. It is characterized by a long, narrow trunk,
short extremities, particularly in the proximal (rhizomelic)
segments, a large head with frontal bossing, hypoplasia of the
midface and a trident configuration of the hands.
{ECO:0000269|PubMed:10611230, ECO:0000269|PubMed:12297284,
ECO:0000269|PubMed:7758520, ECO:0000269|PubMed:7847369,
ECO:0000269|PubMed:8078586, ECO:0000269|PubMed:8599935}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Crouzon syndrome with acanthosis nigricans (CAN)
[MIM:612247]: Classic Crouzon disease which is caused by mutations
in the FGFR2 gene is characterized by craniosynostosis (premature
fusion of the skull sutures), and facial hypoplasia. Crouzon
syndrome with acanthosis nigricans (a skin disorder characterized
by pigmentation anomalies), CAN, is considered to be an
independent disorder from classic Crouzon syndrome. CAN is
characterized by additional more severe physical manifestation,
such as Chiari malformation, hydrocephalus, and atresia or
stenosis of the choanas, and is caused by a specific mutation
(Ala-391 to Glu) in the transmembrane domain of FGFR3. It is
proposed to have an autosomal dominant mode of inheritance.
{ECO:0000269|PubMed:17935505, ECO:0000269|PubMed:7493034}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Thanatophoric dysplasia 1 (TD1) [MIM:187600]: A neonatal
lethal skeletal dysplasia. Affected individuals manifest severe
shortening of the limbs with macrocephaly, narrow thorax, short
ribs, and curved femurs. {ECO:0000269|PubMed:10360402,
ECO:0000269|PubMed:10671061, ECO:0000269|PubMed:7773297,
ECO:0000269|PubMed:8589699, ECO:0000269|PubMed:8845844,
ECO:0000269|PubMed:9790257}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Thanatophoric dysplasia 2 (TD2) [MIM:187601]: A neonatal
lethal skeletal dysplasia causing severe shortening of the limbs,
narrow thorax and short ribs. Patients with thanatophoric
dysplasia type 2 have straight femurs and cloverleaf skull.
{ECO:0000269|PubMed:12297284, ECO:0000269|PubMed:7773297,
ECO:0000269|PubMed:8754806}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hypochondroplasia (HCH) [MIM:146000]: Autosomal dominant
disease and is characterized by disproportionate short stature. It
resembles achondroplasia, but with a less severe phenotype.
{ECO:0000269|PubMed:10215410, ECO:0000269|PubMed:10777366,
ECO:0000269|PubMed:11055896, ECO:0000269|PubMed:12707965,
ECO:0000269|PubMed:7670477, ECO:0000269|PubMed:9452043}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Bladder cancer (BLC) [MIM:109800]: A malignancy
originating in tissues of the urinary bladder. It often presents
with multiple tumors appearing at different times and at different
sites in the bladder. Most bladder cancers are transitional cell
carcinomas that begin in cells that normally make up the inner
lining of the bladder. Other types of bladder cancer include
squamous cell carcinoma (cancer that begins in thin, flat cells)
and adenocarcinoma (cancer that begins in cells that make and
release mucus and other fluids). Bladder cancer is a complex
disorder with both genetic and environmental influences.
{ECO:0000269|PubMed:10471491, ECO:0000269|PubMed:11314002}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry. Somatic mutations
can constitutively activate FGFR3.
-!- DISEASE: Cervical cancer (CERCA) [MIM:603956]: A malignant
neoplasm of the cervix, typically originating from a dysplastic or
premalignant lesion previously present at the active
squamocolumnar junction. The transformation from mild dysplastic
to invasive carcinoma generally occurs slowly within several
years, although the rate of this process varies widely. Carcinoma
in situ is particularly known to precede invasive cervical cancer
in most cases. Cervical cancer is strongly associated with
infection by oncogenic types of human papillomavirus.
{ECO:0000269|PubMed:10471491}. Note=The gene represented in this
entry is involved in disease pathogenesis.
-!- DISEASE: Camptodactyly, tall stature, and hearing loss syndrome
(CATSHLS) [MIM:610474]: An autosomal dominant syndrome
characterized by permanent and irreducible flexion of one or more
fingers of the hand and/or feet, tall stature, scoliosis and/or a
pectus excavatum, and hearing loss. Affected individuals have
developmental delay and/or mental retardation, and several of
these have microcephaly. Radiographic findings included tall
vertebral bodies with irregular borders and broad femoral
metaphyses with long tubular shafts. On audiological exam, each
tested member have bilateral sensorineural hearing loss and absent
otoacoustic emissions. The hearing loss was congenital or
developed in early infancy, progressed variably in early
childhood, and range from mild to severe. Computed tomography and
magnetic resonance imaging reveal that the brain, middle ear, and
inner ear are structurally normal. {ECO:0000269|PubMed:17033969}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Multiple myeloma (MM) [MIM:254500]: A malignant tumor of
plasma cells usually arising in the bone marrow and characterized
by diffuse involvement of the skeletal system, hyperglobulinemia,
Bence-Jones proteinuria and anemia. Complications of multiple
myeloma are bone pain, hypercalcemia, renal failure and spinal
cord compression. The aberrant antibodies that are produced lead
to impaired humoral immunity and patients have a high prevalence
of infection. Amyloidosis may develop in some patients. Multiple
myeloma is part of a spectrum of diseases ranging from monoclonal
gammopathy of unknown significance (MGUS) to plasma cell leukemia.
{ECO:0000269|PubMed:11529856, ECO:0000269|PubMed:9207791}.
Note=The gene represented in this entry may be involved in disease
pathogenesis. A chromosomal aberration involving FGFR3 is found in
multiple myeloma. Translocation t(4;14)(p16.3;q32.3) with the IgH
locus.
-!- DISEASE: Lacrimo-auriculo-dento-digital syndrome (LADDS)
[MIM:149730]: An autosomal dominant ectodermal dysplasia, a
heterogeneous group of disorders due to abnormal development of
two or more ectodermal structures. Lacrimo-auriculo-dento-digital
syndrome is characterized by aplastic/hypoplastic lacrimal and
salivary glands and ducts, cup-shaped ears, hearing loss,
hypodontia and enamel hypoplasia, and distal limb segments
anomalies. In addition to these cardinal features, facial
dysmorphism, malformations of the kidney and respiratory system
and abnormal genitalia have been reported. Craniosynostosis and
severe syndactyly are not observed. {ECO:0000269|PubMed:16501574}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Keratinocytic non-epidermolytic nevus (KNEN)
[MIM:162900]: Epidermal nevi of the common, non-organoid and non-
epidermolytic type are benign skin lesions and may vary in their
extent from a single (usually linear) lesion to widespread and
systematized involvement. They may be present at birth or develop
early during childhood. {ECO:0000269|PubMed:16841094}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Muenke syndrome (MNKS) [MIM:602849]: A condition
characterized by premature closure of coronal suture of skull
during development (coronal craniosynostosis), which affects the
shape of the head and face. It may be uni- or bilateral. When
bilateral, it is characterized by a skull with a small antero-
posterior diameter (brachycephaly), often with a decrease in the
depth of the orbits and hypoplasia of the maxillae. Unilateral
closure of the coronal sutures leads to flattening of the orbit on
the involved side (plagiocephaly). The intellect is normal. In
addition to coronal craniosynostosis some affected individuals
show skeletal abnormalities of hands and feet, sensorineural
hearing loss, mental retardation and respiratory insufficiency.
{ECO:0000269|PubMed:11746040, ECO:0000269|PubMed:9042914,
ECO:0000269|PubMed:9950359}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Keratosis, seborrheic (KERSEB) [MIM:182000]: A common
benign skin tumor. Seborrheic keratoses usually begin with the
appearance of one or more sharply defined, light brown, flat
macules. The lesions may be sparse or numerous. As they initially
grow, they develop a velvety to finely verrucous surface, followed
by an uneven warty surface with multiple plugged follicles and a
dull or lackluster appearance. {ECO:0000269|PubMed:15772091}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Testicular germ cell tumor (TGCT) [MIM:273300]: A common
malignancy in males representing 95% of all testicular neoplasms.
TGCTs have various pathologic subtypes including: unclassified
intratubular germ cell neoplasia, seminoma (including cases with
syncytiotrophoblastic cells), spermatocytic seminoma, embryonal
carcinoma, yolk sac tumor, choriocarcinoma, and teratoma.
{ECO:0000269|PubMed:19855393}. Note=The gene represented in this
entry may be involved in disease pathogenesis.
-!- DISEASE: Achondroplasia, severe, with developmental delay and
acanthosis nigricans (SADDAN) [MIM:616482]: A severe form of
achondroplasia associated with developmental delay and acanthosis
nigricans. Patients manifest short-limb dwarfism, with a long,
narrow trunk, short extremities, particularly in the proximal
(rhizomelic) segments, a large head with frontal bossing,
hypoplasia of the midface and a trident configuration of the
hands. Acanthosis nigricans is a skin condition characterized by
brown-pigmented, velvety verrucosities in body folds and creases.
{ECO:0000269|PubMed:10053006}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
kinase family. Fibroblast growth factor receptor subfamily.
{ECO:0000255|PROSITE-ProRule:PRU00159}.
-!- SEQUENCE CAUTION:
Sequence=BAD92678.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/FGFRID99.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgfr3/";
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EMBL; M58051; AAA52450.1; -; mRNA.
EMBL; AF245114; AAF63380.1; -; mRNA.
EMBL; AB209441; BAD92678.1; ALT_INIT; mRNA.
EMBL; AY768549; AAU89726.1; -; Genomic_DNA.
EMBL; AC016773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471131; EAW82564.1; -; Genomic_DNA.
EMBL; CH471131; EAW82565.1; -; Genomic_DNA.
EMBL; CH471131; EAW82566.1; -; Genomic_DNA.
EMBL; CH471131; EAW82567.1; -; Genomic_DNA.
EMBL; M64347; AAA58470.1; -; mRNA.
EMBL; M59374; AAA63209.1; -; mRNA.
EMBL; S76733; AAB33323.1; -; Genomic_DNA.
EMBL; X84939; CAA59334.1; -; mRNA.
EMBL; U22410; AAA67781.1; -; Genomic_DNA.
CCDS; CCDS3353.1; -. [P22607-1]
CCDS; CCDS3354.1; -. [P22607-3]
CCDS; CCDS54706.1; -. [P22607-2]
PIR; A38576; TVHUF3.
RefSeq; NP_000133.1; NM_000142.4. [P22607-1]
RefSeq; NP_001156685.1; NM_001163213.1. [P22607-2]
RefSeq; NP_075254.1; NM_022965.3. [P22607-3]
UniGene; Hs.1420; -.
PDB; 1RY7; X-ray; 3.20 A; B=33-365.
PDB; 2LZL; NMR; -; A/B=357-399.
PDB; 4K33; X-ray; 2.34 A; A=449-759.
PDBsum; 1RY7; -.
PDBsum; 2LZL; -.
PDBsum; 4K33; -.
ProteinModelPortal; P22607; -.
SMR; P22607; -.
BioGrid; 108552; 50.
DIP; DIP-4016N; -.
IntAct; P22607; 27.
MINT; MINT-1034697; -.
STRING; 9606.ENSP00000339824; -.
BindingDB; P22607; -.
ChEMBL; CHEMBL2742; -.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB09079; Nintedanib.
DrugBank; DB00039; Palifermin.
DrugBank; DB06589; Pazopanib.
DrugBank; DB08901; Ponatinib.
DrugBank; DB05014; XL999.
GuidetoPHARMACOLOGY; 1810; -.
iPTMnet; P22607; -.
PhosphoSitePlus; P22607; -.
BioMuta; FGFR3; -.
DMDM; 120050; -.
PaxDb; P22607; -.
PeptideAtlas; P22607; -.
PRIDE; P22607; -.
DNASU; 2261; -.
Ensembl; ENST00000260795; ENSP00000260795; ENSG00000068078. [P22607-1]
Ensembl; ENST00000340107; ENSP00000339824; ENSG00000068078. [P22607-2]
Ensembl; ENST00000352904; ENSP00000231803; ENSG00000068078. [P22607-3]
Ensembl; ENST00000412135; ENSP00000412903; ENSG00000068078. [P22607-3]
Ensembl; ENST00000440486; ENSP00000414914; ENSG00000068078. [P22607-1]
GeneID; 2261; -.
KEGG; hsa:2261; -.
UCSC; uc003gdr.3; human. [P22607-1]
CTD; 2261; -.
DisGeNET; 2261; -.
EuPathDB; HostDB:ENSG00000068078.17; -.
GeneCards; FGFR3; -.
GeneReviews; FGFR3; -.
HGNC; HGNC:3690; FGFR3.
HPA; CAB004231; -.
HPA; HPA067204; -.
MalaCards; FGFR3; -.
MIM; 100800; phenotype.
MIM; 109800; phenotype.
MIM; 134934; gene.
MIM; 146000; phenotype.
MIM; 149730; phenotype.
MIM; 162900; phenotype.
MIM; 182000; phenotype.
MIM; 187600; phenotype.
MIM; 187601; phenotype.
MIM; 254500; phenotype.
MIM; 273300; phenotype.
MIM; 602849; phenotype.
MIM; 603956; phenotype.
MIM; 610474; phenotype.
MIM; 612247; phenotype.
MIM; 616482; phenotype.
neXtProt; NX_P22607; -.
OpenTargets; ENSG00000068078; -.
Orphanet; 15; Achondroplasia.
Orphanet; 85164; Camptodactyly - tall stature - scoliosis - hearing loss.
Orphanet; 93262; Crouzon syndrome - acanthosis nigricans.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
Orphanet; 429; Hypochondroplasia.
Orphanet; 35099; Isolated brachycephaly.
Orphanet; 35098; Isolated plagiocephaly.
Orphanet; 2363; Lacrimoauriculodentodigital syndrome.
Orphanet; 53271; Muenke syndrome.
Orphanet; 794; Saethre-Chotzen syndrome.
Orphanet; 85165; Severe achondroplasia - developmental delay - acanthosis nigricans.
Orphanet; 1860; Thanatophoric dysplasia type 1.
Orphanet; 93274; Thanatophoric dysplasia type 2.
PharmGKB; PA28129; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; P22607; -.
KO; K05094; -.
OMA; THELYMI; -.
OrthoDB; EOG091G0CQZ; -.
PhylomeDB; P22607; -.
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-1839130; Signaling by activated point mutants of FGFR3.
Reactome; R-HSA-190371; FGFR3b ligand binding and activation.
Reactome; R-HSA-190372; FGFR3c ligand binding and activation.
Reactome; R-HSA-2033514; FGFR3 mutant receptor activation.
Reactome; R-HSA-2033515; t(4;14) translocations of FGFR3.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-5654227; Phospholipase C-mediated cascade, FGFR3.
Reactome; R-HSA-5654704; SHC-mediated cascade:FGFR3.
Reactome; R-HSA-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-HSA-5654710; PI-3K cascade:FGFR3.
Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853334; Signaling by FGFR3 fusions in cancer.
Reactome; R-HSA-8853338; Signaling by FGFR3 point mutants in cancer.
SignaLink; P22607; -.
SIGNOR; P22607; -.
ChiTaRS; FGFR3; human.
EvolutionaryTrace; P22607; -.
GeneWiki; Fibroblast_growth_factor_receptor_3; -.
GenomeRNAi; 2261; -.
PRO; PR:P22607; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000068078; -.
CleanEx; HS_FGFR3; -.
ExpressionAtlas; P22607; baseline and differential.
Genevisible; P22607; HS.
GO; GO:0009986; C:cell surface; IEA:Ensembl.
GO; GO:0005783; C:endoplasmic reticulum; IDA:HPA.
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:0005634; C:nucleus; IEA:Ensembl.
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; IMP:UniProtKB.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0070977; P:bone maturation; ISS:BHF-UCL.
GO; GO:0030282; P:bone mineralization; ISS:BHF-UCL.
GO; GO:0060349; P:bone morphogenesis; ISS:BHF-UCL.
GO; GO:0007267; P:cell-cell signaling; IEA:Ensembl.
GO; GO:0002062; P:chondrocyte differentiation; TAS:UniProtKB.
GO; GO:0035988; P:chondrocyte proliferation; TAS:UniProtKB.
GO; GO:0003416; P:endochondral bone growth; TAS:UniProtKB.
GO; GO:0001958; P:endochondral ossification; TAS:UniProtKB.
GO; GO:1902178; P:fibroblast growth factor receptor apoptotic signaling pathway; IMP:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0007259; P:JAK-STAT cascade; TAS:ProtInc.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0048640; P:negative regulation of developmental growth; ISS:BHF-UCL.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0043552; P:positive regulation of phosphatidylinositol 3-kinase activity; IMP:UniProtKB.
GO; GO:0010518; P:positive regulation of phospholipase activity; IMP:UniProtKB.
GO; GO:0042531; P:positive regulation of tyrosine phosphorylation of STAT protein; IMP:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
Gene3D; 2.60.40.10; -; 4.
InterPro; IPR028176; FGF_rcpt_3.
InterPro; IPR016248; FGF_rcpt_fam.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR011009; Kinase-like_dom.
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.
PANTHER; PTHR24416:SF401; PTHR24416:SF401; 1.
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; 3.
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; Apoptosis; ATP-binding;
Cell membrane; Chromosomal rearrangement; Complete proteome;
Craniosynostosis; Cytoplasmic vesicle; Deafness; Disease mutation;
Disulfide bond; Dwarfism; Ectodermal dysplasia; Endoplasmic reticulum;
Glycoprotein; Immunoglobulin domain; Kinase;
Lacrimo-auriculo-dento-digital syndrome; Membrane; Nucleotide-binding;
Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat;
Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 22
CHAIN 23 806 Fibroblast growth factor receptor 3.
/FTId=PRO_0000016785.
TOPO_DOM 23 375 Extracellular. {ECO:0000255}.
TRANSMEM 376 396 Helical. {ECO:0000255}.
TOPO_DOM 397 806 Cytoplasmic. {ECO:0000255}.
DOMAIN 24 126 Ig-like C2-type 1.
DOMAIN 151 244 Ig-like C2-type 2.
DOMAIN 253 355 Ig-like C2-type 3.
DOMAIN 472 761 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 478 486 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
ACT_SITE 617 617 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028}.
BINDING 508 508 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q61851}.
MOD_RES 445 445 Phosphoserine.
{ECO:0000250|UniProtKB:Q61851}.
MOD_RES 647 647 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:8754806}.
MOD_RES 648 648 Phosphotyrosine; by autocatalysis.
{ECO:0000305|PubMed:8754806}.
MOD_RES 724 724 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:11294897}.
MOD_RES 760 760 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:19286672}.
CARBOHYD 98 98 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 225 225 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 262 262 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 294 294 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 315 315 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 328 328 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 61 109 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 176 228 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 275 339 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 311 422 Missing (in isoform 3).
{ECO:0000303|PubMed:11703096}.
/FTId=VSP_002989.
VAR_SEQ 311 358 TAGANTTDKELEVLSLHNVTFEDAGEYTCLAGNSIGFSHHS
AWLVVLP -> SWISESVEADVRLRLANVSERDGGEYLCRA
TNFIGVAEKAFWLSVHGPRA (in isoform 2).
{ECO:0000303|PubMed:7495869}.
/FTId=VSP_002988.
VAR_SEQ 654 806 GRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIFTLGGSP
YPGIPVEELFKLLKEGHRMDKPANCTHDLYMIMRECWHAAP
SQRPTFKQLVEDLDRVLTVTSTDEYLDLSAPFEQYSPGGQD
TPSSSSSGDDSVFAHDLLPPAPPSSGGSRT -> LVLWGPA
LGDLHAGGLPVPRHPCGGALQAAEGGPPHGQARQLHTRPVH
DHAGVLACRALPEAHLQAAGGGPGPCPYRDVHRRVPGPVGA
FRAVLPGWPGHPQLQLLRGRLRVCPRPAAPGPTQQWGLADV
KGHWSPTM (in isoform 4).
{ECO:0000303|Ref.3}.
/FTId=VSP_040945.
VARIANT 65 65 G -> R (in dbSNP:rs2305178).
{ECO:0000269|Ref.4}.
/FTId=VAR_022167.
VARIANT 79 79 T -> S (in a lung adenocarcinoma sample;
somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042207.
VARIANT 228 228 C -> R (in a colorectal adenocarcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042208.
VARIANT 248 248 R -> C (in KERSEB, BLC, keratinocytic
non-epidermolytic nevus and TD1; severe
and lethal; also found as somatic
mutation in one patient with multiple
myeloma; constitutive dimerization and
kinase activation; dbSNP:rs121913482).
{ECO:0000269|PubMed:10360402,
ECO:0000269|PubMed:10471491,
ECO:0000269|PubMed:11529856,
ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:16841094,
ECO:0000269|PubMed:17509076,
ECO:0000269|PubMed:7773297,
ECO:0000269|PubMed:8845844}.
/FTId=VAR_004148.
VARIANT 249 249 S -> C (in KERSEB, BLC, cervical cancer
and TD1; dbSNP:rs121913483).
{ECO:0000269|PubMed:10360402,
ECO:0000269|PubMed:10471491,
ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:8589699,
ECO:0000269|PubMed:8845844}.
/FTId=VAR_004149.
VARIANT 250 250 P -> R (in MNKS; also some individuals
with autosomal dominant congenital
sensorineural deafness without
craniosynostosis; dbSNP:rs4647924).
{ECO:0000269|PubMed:11746040,
ECO:0000269|PubMed:9042914,
ECO:0000269|PubMed:9525367,
ECO:0000269|PubMed:9950359}.
/FTId=VAR_004150.
VARIANT 322 322 E -> K (in colorectal cancer;
dbSNP:rs121913111).
{ECO:0000269|PubMed:11325814}.
/FTId=VAR_018388.
VARIANT 338 338 T -> M. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042209.
VARIANT 370 370 G -> C (in KERSEB, BLC, keratinocytic
non-epidermolytic nevus and TD1;
dbSNP:rs121913479).
{ECO:0000269|PubMed:10471491,
ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:16841094,
ECO:0000269|PubMed:8845844,
ECO:0000269|PubMed:9790257}.
/FTId=VAR_004151.
VARIANT 371 371 S -> C (in KERSEB and TD1;
dbSNP:rs121913484).
{ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:7773297}.
/FTId=VAR_004152.
VARIANT 373 373 Y -> C (in KERSEB and TD1; disulfide-
linked dimer with constitutive kinase
activation; dbSNP:rs121913485).
{ECO:0000269|PubMed:10360402,
ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:17509076,
ECO:0000269|PubMed:8845844,
ECO:0000269|PubMed:9207791}.
/FTId=VAR_004153.
VARIANT 375 375 G -> C (in ACH; dbSNP:rs75790268).
{ECO:0000269|PubMed:7758520}.
/FTId=VAR_004154.
VARIANT 380 380 G -> R (in keratinocytic non-
epidermolytic nevus and ACH; very common
mutation; constitutively activated kinase
with impaired internalization and
degradation, resulting in prolonged FGFR3
signaling; dbSNP:rs28931614).
{ECO:0000269|PubMed:10611230,
ECO:0000269|PubMed:12297284,
ECO:0000269|PubMed:16841094,
ECO:0000269|PubMed:17561467,
ECO:0000269|PubMed:7847369,
ECO:0000269|PubMed:8078586,
ECO:0000269|PubMed:8599935}.
/FTId=VAR_004155.
VARIANT 384 384 F -> L (in dbSNP:rs17881656).
{ECO:0000269|PubMed:17344846,
ECO:0000269|Ref.4}.
/FTId=VAR_022168.
VARIANT 391 391 A -> E (in CAN; dbSNP:rs28931615).
{ECO:0000269|PubMed:17935505,
ECO:0000269|PubMed:7493034}.
/FTId=VAR_004156.
VARIANT 441 441 A -> T (in dbSNP:rs17884368).
{ECO:0000269|Ref.4}.
/FTId=VAR_022169.
VARIANT 513 513 D -> N (in LADDS; dbSNP:rs121913112).
{ECO:0000269|PubMed:16501574}.
/FTId=VAR_029887.
VARIANT 538 538 I -> V (in hypochondroplasia;
dbSNP:rs80053154).
{ECO:0000269|PubMed:10215410}.
/FTId=VAR_004157.
VARIANT 540 540 N -> K (in hypochondroplasia;
dbSNP:rs28933068).
{ECO:0000269|PubMed:7670477}.
/FTId=VAR_004158.
VARIANT 540 540 N -> S (in hypochondroplasia; mild;
dbSNP:rs77722678).
{ECO:0000269|PubMed:10777366,
ECO:0000269|PubMed:12707965}.
/FTId=VAR_018389.
VARIANT 540 540 N -> T (in hypochondroplasia;
dbSNP:rs77722678).
{ECO:0000269|PubMed:9452043}.
/FTId=VAR_004159.
VARIANT 621 621 R -> H (in CATSHLS; dbSNP:rs121913113).
{ECO:0000269|PubMed:17033969}.
/FTId=VAR_029108.
VARIANT 646 646 D -> N. {ECO:0000269|PubMed:17344846}.
/FTId=VAR_042210.
VARIANT 650 650 K -> E (in KERSEB, TD2, TGCT and BLC;
bladder transitional cell carcinoma;
somatic mutation; constitutively
activated kinase with impaired
internalization and degradation,
resulting in prolonged FGFR3 signaling;
dbSNP:rs78311289).
{ECO:0000269|PubMed:10471491,
ECO:0000269|PubMed:11294897,
ECO:0000269|PubMed:12297284,
ECO:0000269|PubMed:14534538,
ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:17145761,
ECO:0000269|PubMed:17344846,
ECO:0000269|PubMed:17561467,
ECO:0000269|PubMed:19855393,
ECO:0000269|PubMed:7773297,
ECO:0000269|PubMed:8754806,
ECO:0000269|PubMed:9207791}.
/FTId=VAR_004160.
VARIANT 650 650 K -> M (in KERSEB, ACH, TD1 and SADDAN;
constitutively activated kinase with
impaired internalization and degradation,
resulting in prolonged FGFR3 signaling;
dbSNP:rs121913105).
{ECO:0000269|PubMed:10053006,
ECO:0000269|PubMed:10671061,
ECO:0000269|PubMed:15772091,
ECO:0000269|PubMed:17509076,
ECO:0000269|PubMed:17561467,
ECO:0000269|PubMed:9207791}.
/FTId=VAR_004161.
VARIANT 650 650 K -> Q (in hypochondroplasia and BLC; in
hypochondroplasia the form is milder than
that seen in individuals with the K-540
or M-650 mutations; constitutively
activated kinase; dbSNP:rs78311289).
{ECO:0000269|PubMed:11055896,
ECO:0000269|PubMed:11314002,
ECO:0000269|PubMed:8754806}.
/FTId=VAR_018390.
VARIANT 717 717 A -> T (in dbSNP:rs17882190).
{ECO:0000269|Ref.4}.
/FTId=VAR_022170.
VARIANT 726 726 I -> F (in dbSNP:rs17880763).
{ECO:0000269|Ref.4}.
/FTId=VAR_022171.
MUTAGEN 508 508 K->A: Loss of kinase activity. Abolishes
ubiquitination.
{ECO:0000269|PubMed:12297284,
ECO:0000269|PubMed:16410555}.
MUTAGEN 577 577 Y->F: Minor effect on kinase activity.
{ECO:0000269|PubMed:11294897}.
MUTAGEN 650 650 K->D: Constitutively activated kinase.
MUTAGEN 650 650 K->L: Constitutively activated kinase.
MUTAGEN 724 724 Y->F: Strongly reduced kinase activity.
Strongly reduced mitogen activity.
{ECO:0000269|PubMed:11294897}.
MUTAGEN 760 760 Y->F: Minor effect on kinase activity.
{ECO:0000269|PubMed:11294897}.
MUTAGEN 770 770 Y->F: Minor effect on kinase activity.
Increased mitogen activity.
{ECO:0000269|PubMed:11294897}.
CONFLICT 395 395 L -> V (in Ref. 7; AAA58470).
{ECO:0000305}.
CONFLICT 421 421 R -> RQ (in Ref. 3; BAD92678).
{ECO:0000305}.
STRAND 163 167 {ECO:0000244|PDB:1RY7}.
STRAND 172 175 {ECO:0000244|PDB:1RY7}.
STRAND 185 187 {ECO:0000244|PDB:1RY7}.
TURN 208 211 {ECO:0000244|PDB:1RY7}.
STRAND 212 215 {ECO:0000244|PDB:1RY7}.
HELIX 220 222 {ECO:0000244|PDB:1RY7}.
STRAND 226 232 {ECO:0000244|PDB:1RY7}.
STRAND 235 246 {ECO:0000244|PDB:1RY7}.
STRAND 263 268 {ECO:0000244|PDB:1RY7}.
STRAND 271 273 {ECO:0000244|PDB:1RY7}.
STRAND 283 289 {ECO:0000244|PDB:1RY7}.
HELIX 293 295 {ECO:0000244|PDB:1RY7}.
STRAND 302 304 {ECO:0000244|PDB:1RY7}.
STRAND 324 326 {ECO:0000244|PDB:1RY7}.
STRAND 335 345 {ECO:0000244|PDB:1RY7}.
STRAND 348 357 {ECO:0000244|PDB:1RY7}.
STRAND 369 372 {ECO:0000244|PDB:2LZL}.
HELIX 374 398 {ECO:0000244|PDB:2LZL}.
TURN 463 465 {ECO:0000244|PDB:4K33}.
HELIX 469 471 {ECO:0000244|PDB:4K33}.
STRAND 472 480 {ECO:0000244|PDB:4K33}.
STRAND 482 496 {ECO:0000244|PDB:4K33}.
STRAND 503 510 {ECO:0000244|PDB:4K33}.
HELIX 516 532 {ECO:0000244|PDB:4K33}.
STRAND 541 545 {ECO:0000244|PDB:4K33}.
STRAND 547 550 {ECO:0000244|PDB:4K33}.
STRAND 552 556 {ECO:0000244|PDB:4K33}.
HELIX 563 568 {ECO:0000244|PDB:4K33}.
HELIX 591 610 {ECO:0000244|PDB:4K33}.
HELIX 620 622 {ECO:0000244|PDB:4K33}.
STRAND 623 625 {ECO:0000244|PDB:4K33}.
STRAND 631 633 {ECO:0000244|PDB:4K33}.
STRAND 646 649 {ECO:0000244|PDB:4K33}.
HELIX 658 660 {ECO:0000244|PDB:4K33}.
HELIX 663 668 {ECO:0000244|PDB:4K33}.
HELIX 673 688 {ECO:0000244|PDB:4K33}.
HELIX 700 708 {ECO:0000244|PDB:4K33}.
HELIX 721 730 {ECO:0000244|PDB:4K33}.
HELIX 735 737 {ECO:0000244|PDB:4K33}.
HELIX 741 753 {ECO:0000244|PDB:4K33}.
SEQUENCE 806 AA; 87710 MW; BC5EA75EA46F447E CRC64;
MGAPACALAL CVAVAIVAGA SSESLGTEQR VVGRAAEVPG PEPGQQEQLV FGSGDAVELS
CPPPGGGPMG PTVWVKDGTG LVPSERVLVG PQRLQVLNAS HEDSGAYSCR QRLTQRVLCH
FSVRVTDAPS SGDDEDGEDE AEDTGVDTGA PYWTRPERMD KKLLAVPAAN TVRFRCPAAG
NPTPSISWLK NGREFRGEHR IGGIKLRHQQ WSLVMESVVP SDRGNYTCVV ENKFGSIRQT
YTLDVLERSP HRPILQAGLP ANQTAVLGSD VEFHCKVYSD AQPHIQWLKH VEVNGSKVGP
DGTPYVTVLK TAGANTTDKE LEVLSLHNVT FEDAGEYTCL AGNSIGFSHH SAWLVVLPAE
EELVEADEAG SVYAGILSYG VGFFLFILVV AAVTLCRLRS PPKKGLGSPT VHKISRFPLK
RQVSLESNAS MSSNTPLVRI ARLSSGEGPT LANVSELELP ADPKWELSRA RLTLGKPLGE
GCFGQVVMAE AIGIDKDRAA KPVTVAVKML KDDATDKDLS DLVSEMEMMK MIGKHKNIIN
LLGACTQGGP LYVLVEYAAK GNLREFLRAR RPPGLDYSFD TCKPPEEQLT FKDLVSCAYQ
VARGMEYLAS QKCIHRDLAA RNVLVTEDNV MKIADFGLAR DVHNLDYYKK TTNGRLPVKW
MAPEALFDRV YTHQSDVWSF GVLLWEIFTL GGSPYPGIPV EELFKLLKEG HRMDKPANCT
HDLYMIMREC WHAAPSQRPT FKQLVEDLDR VLTVTSTDEY LDLSAPFEQY SPGGQDTPSS
SSSGDDSVFA HDLLPPAPPS SGGSRT


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