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Fibroblast growth factor receptor 1 (FGFR-1) (EC 2.7.10.1) (Basic fibroblast growth factor receptor 1) (BFGFR) (bFGF-R-1) (Fms-like tyrosine kinase 2) (FLT-2) (N-sam) (Proto-oncogene c-Fgr) (CD antigen CD331)

 FGFR1_HUMAN             Reviewed;         822 AA.
P11362; A8K6T9; A8K8V5; C1KBH8; P17049; Q02063; Q02065; Q14306;
Q14307; Q53H63; Q59H40; Q5BJG2; Q8N685; Q9UD50; Q9UDF0; Q9UDF1;
Q9UDF2;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 3.
25-OCT-2017, entry version 235.
RecName: Full=Fibroblast growth factor receptor 1;
Short=FGFR-1;
EC=2.7.10.1 {ECO:0000269|PubMed:1379697, ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:20133753, ECO:0000269|PubMed:8622701};
AltName: Full=Basic fibroblast growth factor receptor 1;
Short=BFGFR;
Short=bFGF-R-1;
AltName: Full=Fms-like tyrosine kinase 2;
Short=FLT-2;
AltName: Full=N-sam;
AltName: Full=Proto-oncogene c-Fgr;
AltName: CD_antigen=CD331;
Flags: Precursor;
Name=FGFR1; Synonyms=BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR;
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 15).
TISSUE=Placenta;
PubMed=2162671; DOI=10.1016/0006-291X(90)90384-Y;
Itoh N., Terachi T., Ohta M., Seo M.K.;
"The complete amino acid sequence of the shorter form of human basic
fibroblast growth factor receptor deduced from its cDNA.";
Biochem. Biophys. Res. Commun. 169:680-685(1990).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH FGF1 AND
FGF2.
TISSUE=Neonatal brain stem;
PubMed=1697263;
Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G.,
Ruta M., Burgess W.H., Jaye M., Schlessinger J.;
"Cloning and expression of two distinct high-affinity receptors cross-
reacting with acidic and basic fibroblast growth factors.";
EMBO J. 9:2685-2692(1990).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 15; 17 AND 18).
PubMed=2167437; DOI=10.1128/MCB.10.9.4728;
Johnson D.E., Lee P.L., Lu J., Williams L.T.;
"Diverse forms of a receptor for acidic and basic fibroblast growth
factors.";
Mol. Cell. Biol. 10:4728-4736(1990).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=2159626; DOI=10.1093/nar/18.7.1906;
Isacchi A., Bergonzoni L., Sarmientos P.;
"Complete sequence of a human receptor for acidic and basic fibroblast
growth factors.";
Nucleic Acids Res. 18:1906-1906(1990).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), AND INTERACTION WITH FGF1 AND
FGF2.
TISSUE=Teratocarcinoma;
PubMed=1722683; DOI=10.3109/08977199109104816;
Wennstroem S., Sandstroem C., Claesson-Welsh L.;
"cDNA cloning and expression of a human FGF receptor which binds
acidic and basic FGF.";
Growth Factors 4:197-208(1991).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
PubMed=1662973; DOI=10.3109/08977199109000276;
Kiefer M.C., Baird A., George-Nascimento C., Nguyen T., Mason O.B.,
Boley L.J., Valenzuela P., Barr P.J.;
"Molecular cloning of a human basic fibroblast growth factor receptor
cDNA and expression of a biologically active extracellular domain in a
baculovirus system.";
Growth Factors 5:115-127(1991).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 14; 15 AND 16).
TISSUE=Lung;
PubMed=1650441;
Eisemann A., Ahn J.A., Graziani G., Tronick S.R., Ron D.;
"Alternative splicing generates at least five different isoforms of
the human basic-FGF receptor.";
Oncogene 6:1195-1202(1991).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10;
11; 12 AND 13).
TISSUE=Liver;
PubMed=1846977; DOI=10.1126/science.1846977;
Hou J., Kan M., McKeehan K., McBride G., Adams P., McKeehan W.L.;
"Fibroblast growth factor receptors from liver vary in three
structural domains.";
Science 251:665-668(1991).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1317750;
Hattori Y., Odagiri H., Katoh O., Sakamoto H., Morita T.,
Shimotohno K., Tobinai K., Sugimura T., Terada M.;
"K-sam-related gene, N-sam, encodes fibroblast growth factor receptor
and is expressed in T-lymphocytic tumors.";
Cancer Res. 52:3367-3371(1992).
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19), AND ROLE IN DISEASE.
PubMed=20139426; DOI=10.1093/humrep/deq006;
Miura K., Miura S., Yoshiura K., Seminara S., Hamaguchi D.,
Niikawa N., Masuzaki H.;
"A case of Kallmann syndrome carrying a missense mutation in
alternatively spliced exon 8A encoding the immunoglobulin-like domain
IIIb of fibroblast growth factor receptor 1.";
Hum. Reprod. 25:1076-1080(2010).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6; 14 AND 21).
TISSUE=Placenta, and Testis;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 14 AND 20).
TISSUE=Brain, and Colon;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS SER-22; ARG-818 AND
CYS-822.
NIEHS SNPs program;
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[15]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 14 AND 15), AND
VARIANT GLY-213.
TISSUE=Pancreas, Testis, and Uterus;
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).
[16]
NUCLEOTIDE SEQUENCE [MRNA] OF 1-370 (ISOFORM 15), AND PROTEIN SEQUENCE
OF 22-129 (ISOFORM 15).
PubMed=7520751; DOI=10.1021/bi00200a003;
Pantoliano M.W., Horlick R.A., Springer B.A., Van Dyk D.E., Tobery T.,
Wetmore D.R., Lear J.D., Nahapetian A.T., Bradley J.D., Sisk W.P.;
"Multivalent ligand-receptor binding interactions in the fibroblast
growth factor system produce a cooperative growth factor and heparin
mechanism for receptor dimerization.";
Biochemistry 33:10229-10248(1994).
[17]
PROTEIN SEQUENCE OF 81-100 (ISOFORMS 1/2/4/5/14/16).
PubMed=8074689; DOI=10.1006/bbrc.1994.2203;
Rusnati M., Coltrini D., Caccia P., Dell'Era P., Zoppetti G.,
Oreste P., Valsasina B., Presta M.;
"Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the
formation of the ternary complex with basic fibroblast growth factor
and soluble FGF receptor-1.";
Biochem. Biophys. Res. Commun. 203:450-458(1994).
[18]
NUCLEOTIDE SEQUENCE [MRNA] OF 201-822 (ISOFORMS 1/6/10/14/15).
Ruta M., Howk R., Ricca G., Drohan W., Zabelshansky M., Laureys G.,
Barton D.E., Francke U., Schlessinger J., Givol D.;
"A novel protein tyrosine kinase gene whose expression is modulated
during endothelial cell differentiation.";
Oncogene 3:9-15(1988).
[19]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-391 (ISOFORMS 17/18),
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-360 (ISOFORMS
1/2/4/5/6/7/8/9/10/11/12/13/14/15), NUCLEOTIDE SEQUENCE [GENOMIC DNA /
MRNA] OF 313-360 (ISOFORM 19), AND TISSUE SPECIFICITY.
TISSUE=Foreskin fibroblast, and Umbilical vein;
PubMed=1652059; DOI=10.1128/MCB.11.9.4627;
Johnson D.E., Lu J., Chen H., Werner S., Williams L.T.;
"The human fibroblast growth factor receptor genes: a common
structural arrangement underlies the mechanisms for generating
receptor forms that differ in their third immunoglobulin domain.";
Mol. Cell. Biol. 11:4627-4634(1991).
[20]
PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
PubMed=1847500; DOI=10.1128/MCB.11.3.1500;
Gutkind S.J., Link D.C., Katamine S., Lacal P., Miki T., Ley T.J.,
Robbins K.C.;
"A novel c-fgr exon utilized in Epstein-Barr virus-infected B
lymphocytes but not in normal monocytes.";
Mol. Cell. Biol. 11:1500-1507(1991).
[21]
INTERACTION WITH PLCG1.
PubMed=1656221; DOI=10.1128/MCB.11.10.5068;
Mohammadi M., Honegger A.M., Rotin D., Fischer R., Bellot F., Li W.,
Dionne C.A., Jaye M., Rubinstein M., Schlessinger J.;
"A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast
growth factor receptor (Flg) is a binding site for the SH2 domain of
phospholipase C-gamma 1.";
Mol. Cell. Biol. 11:5068-5078(1991).
[22]
MUTAGENESIS OF TYR-766, FUNCTION, CATALYTIC ACTIVITY,
AUTOPHOSPHORYLATION, AND INTERACTION WITH PLCG1.
PubMed=1379697; DOI=10.1038/358678a0;
Peters K.G., Marie J., Wilson E., Ives H.E., Escobedo J.,
del Rosario M., Mirda D., Williams L.T.;
"Point mutation of an FGF receptor abolishes phosphatidylinositol
turnover and Ca2+ flux but not mitogenesis.";
Nature 358:678-681(1992).
[23]
MUTAGENESIS OF TYR-766, AND FUNCTION IN CELL PROLIFERATION.
PubMed=1379698; DOI=10.1038/358681a0;
Mohammadi M., Dionne C.A., Li W., Lin N., Spivak T., Honegger A.M.,
Jaye M., Schlessinger J.;
"Point mutation in FGF receptor eliminates phosphatidylinositol
hydrolysis without affecting mitogenesis.";
Nature 358:681-684(1992).
[24]
MUTAGENESIS OF TYR-766, AND SUBCELLULAR LOCATION.
PubMed=7516330;
Sorokin A., Mohammadi M., Huang J., Schlessinger J.;
"Internalization of fibroblast growth factor receptor is inhibited by
a point mutation at tyrosine 766.";
J. Biol. Chem. 269:17056-17061(1994).
[25]
PHOSPHORYLATION AT TYR-463; TYR-583; TYR-585; TYR-653; TYR-654 AND
TYR-730, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION IN
PHOSPHORYLATION OF PLCG1 AND SHC1; ACTIVATION OF MAP KINASES AND
REGULATION OF CELL PROLIFERATION AND DIFFERENTIATION, AND MUTAGENESIS
OF TYR-653 AND TYR-654.
PubMed=8622701; DOI=10.1128/MCB.16.3.977;
Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M.,
Schlessinger J.;
"Identification of six novel autophosphorylation sites on fibroblast
growth factor receptor 1 and elucidation of their importance in
receptor activation and signal transduction.";
Mol. Cell. Biol. 16:977-989(1996).
[26]
INTERACTION WITH FGF1; FGF2; FGF4; FGF5; FGF6, 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).
[27]
CHROMOSOMAL TRANSLOCATION WITH ZMYM2.
PubMed=9716603;
Reiter A., Sohal J., Kulkarni S., Chase A., Macdonald D.H.C.,
Aguiar R.C.T., Goncalves C., Hernandez J.M., Jennings B.A.,
Goldman J.M., Cross N.C.P.;
"Consistent fusion of ZNF198 to the fibroblast growth factor receptor-
1 in the t(8;13)(p11;q12) myeloproliferative syndrome.";
Blood 92:1735-1742(1998).
[28]
INTERACTION WITH FGF1, AND PHOSPHORYLATION.
PubMed=9655399; DOI=10.1038/31741;
DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M.,
Schlessinger J., Hendrickson W.A.;
"Structure of a heparin-linked biologically active dimer of fibroblast
growth factor.";
Nature 393:812-817(1998).
[29]
CHROMOSOMAL TRANSLOCATION WITH FGFR1OP.
PubMed=9949182;
Popovici C., Zhang B., Gregoire M.-J., Jonveaux P.,
Lafage-Pochitaloff M., Birnbaum D., Pebusque M.-J.;
"The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative
disorder fuses a novel gene, FOP, to fibroblast growth factor receptor
1.";
Blood 93:1381-1389(1999).
[30]
INTERACTION WITH GRB10.
PubMed=10454568; DOI=10.1128/MCB.19.9.6217;
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A.,
Swamy O.R., Leone M.E., Riedel H.;
"Grb10, a positive, stimulatory signaling adapter in platelet-derived
growth factor BB-, insulin-like growth factor I-, and insulin-mediated
mitogenesis.";
Mol. Cell. Biol. 19:6217-6228(1999).
[31]
INVOLVEMENT IN JWS, AND VARIANT JWS ARG-252.
PubMed=10861678;
DOI=10.1002/1096-8628(20000703)93:1<22::AID-AJMG5>3.0.CO;2-U;
Roscioli T., Flanagan S., Kumar P., Masel J., Gattas M., Hyland V.J.,
Glass I.A.;
"Clinical findings in a patient with FGFR1 P252R mutation and
comparison with the literature.";
Am. J. Med. Genet. 93:22-28(2000).
[32]
CHROMOSOMAL TRANSLOCATION WITH CNTRL.
PubMed=10688839;
Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D.,
Rattner J.B., Pebusque M.-J.;
"FGFR1 is fused to the centrosome-associated protein CEP110 in the
8p12 stem cell myeloproliferative disorder with t(8;9)(p12;q33).";
Blood 95:1788-1796(2000).
[33]
FUNCTION IN PHOSPHORYLATION OF FRS2 AND GAB1 AND IN ACTIVATION OF
PIK3R1.
PubMed=11353842; DOI=10.1073/pnas.111114298;
Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.;
"Stimulation of phosphatidylinositol 3-kinase by fibroblast growth
factor receptors is mediated by coordinated recruitment of multiple
docking proteins.";
Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001).
[34]
FUNCTION IN ACTIVATION OF SIGNALING VIA RAS AND MAP KINASES AND CELL
PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF FRS2; SHB AND
PTPN11/SHP2, INTERACTION WITH SHB AND FGF2, AND MUTAGENESIS OF
TYR-766.
PubMed=12181353; DOI=10.1091/mbc.E02-02-0103;
Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M.,
Claesson-Welsh L.;
"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and
regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in
endothelial cells.";
Mol. Biol. Cell 13:2881-2893(2002).
[35]
CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
PubMed=15034873; DOI=10.1002/gcc.20023;
Grand E.K., Grand F.H., Chase A.J., Ross F.M., Corcoran M.M.,
Oscier D.G., Cross N.C.P.;
"Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11
myeloproliferative syndrome.";
Genes Chromosomes Cancer 40:78-83(2004).
[36]
FUNCTION IN ACTIVATION OF RPS6KA1 AND CREB1, CATALYTIC ACTIVITY,
INTERACTION WITH RPS6KA1, MUTAGENESIS OF LYS-514, AND SUBCELLULAR
LOCATION.
PubMed=15117958; DOI=10.1074/jbc.M311144200;
Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K.,
Stachowiak M.K.;
"90-kDa ribosomal S6 kinase is a direct target for the nuclear
fibroblast growth factor receptor 1 (FGFR1): role in FGFR1
signaling.";
J. Biol. Chem. 279:29325-29335(2004).
[37]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[38]
CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
PubMed=16946300; DOI=10.1182/blood-2006-06-026666;
Gu T.-L., Goss V.L., Reeves C., Popova L., Nardone J., Macneill J.,
Walters D.K., Wang Y., Rush J., Comb M.J., Druker B.J.,
Polakiewicz R.D.;
"Phosphotyrosine profiling identifies the KG-1 cell line as a model
for the study of FGFR1 fusions in acute myeloid leukemia.";
Blood 108:4202-4204(2006).
[39]
INTERACTION WITH FGF1; FGF8; FGF10; FGF19; FGF21; FGF22 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).
[40]
SUBCELLULAR LOCATION, AND GLYCOSYLATION.
PubMed=16481405; DOI=10.1091/mbc.E05-08-0749;
Dunham-Ems S.M., Pudavar H.E., Myers J.M., Maher P.A., Prasad P.N.,
Stachowiak M.K.;
"Factors controlling fibroblast growth factor receptor-1's cytoplasmic
trafficking and its regulation as revealed by FRAP analysis.";
Mol. Biol. Cell 17:2223-2235(2006).
[41]
PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654; TYR-583 AND TYR-585, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=16507368; DOI=10.1016/j.molcel.2006.01.022;
Furdui C.M., Lew E.D., Schlessinger J., Anderson K.S.;
"Autophosphorylation of FGFR1 kinase is mediated by a sequential and
precisely ordered reaction.";
Mol. Cell 21:711-717(2006).
[42]
CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
PubMed=17389761; DOI=10.1182/blood-2006-12-065615;
Dong S., Kang S., Gu T., Kardar S., Fu H., Lonial S., Khoury H.J.,
Khuri F., Chen J.;
"14-3-3 integrates pro-survival signals mediated by the AKT and MAPK
pathways in ZNF198-FGFR1 transformed hematopoietic cells.";
Blood 110:360-369(2007).
[43]
INTERACTION WITH FGF19; FGF21 AND KLB, AND FUNCTION IN REGULATION OF
GLUCOSE UPTAKE IN ADIPOCYTES.
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).
[44]
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).
[45]
BINDING TO FGF1, AND IDENTIFICATION IN A COMPLEX WITH INTEGRIN AND
FGF1.
PubMed=18441324; DOI=10.1074/jbc.M801213200;
Mori S., Wu C.Y., Yamaji S., Saegusa J., Shi B., Ma Z., Kuwabara Y.,
Lam K.S., Isseroff R.R., Takada Y.K., Takada Y.;
"Direct binding of integrin alphavbeta3 to FGF1 plays a role in FGF1
signaling.";
J. Biol. Chem. 283:18066-18075(2008).
[46]
UBIQUITINATION, CATALYTIC ACTIVITY, FUNCTION AS FGF1 RECEPTOR AND IN
ACTIVATION OF PLCG1; FRS2; MAPK1/ERK2 AND MAPK3/ERK1, ENZYME
REGULATION, 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).
[47]
INTERACTION WITH ANOS1.
PubMed=19696444; DOI=10.1074/jbc.M109.049155;
Hu Y., Guimond S.E., Travers P., Cadman S., Hohenester E.,
Turnbull J.E., Kim S.H., Bouloux P.M.;
"Novel mechanisms of fibroblast growth factor receptor 1 regulation by
extracellular matrix protein anosmin-1.";
J. Biol. Chem. 284:29905-29920(2009).
[48]
FUNCTION IN CHROMATIN BINDING AND TRANSCRIPTION REGULATION, AND
SUBCELLULAR LOCATION.
PubMed=19261810; DOI=10.1091/mbc.E08-06-0600;
Dunham-Ems S.M., Lee Y.W., Stachowiak E.K., Pudavar H., Claus P.,
Prasad P.N., Stachowiak M.K.;
"Fibroblast growth factor receptor-1 (FGFR1) nuclear dynamics reveal a
novel mechanism in transcription control.";
Mol. Biol. Cell 20:2401-2412(2009).
[49]
FUNCTION AS PROTO-ONCOGENE, ACTIVE SITE, MUTAGENESIS OF ASP-623,
CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654;
TYR-583; TYR-585 AND TYR-730, CHARACTERIZATION OF VARIANT ECCL
LYS-546, IDENTIFICATION BY MASS SPECTROMETRY, AND ENZYME REGULATION.
PubMed=19224897; DOI=10.1126/scisignal.2000021;
Lew E.D., Furdui C.M., Anderson K.S., Schlessinger J.;
"The precise sequence of FGF receptor autophosphorylation is
kinetically driven and is disrupted by oncogenic mutations.";
Sci. Signal. 2:RA6-RA6(2009).
[50]
BINDING TO FGF1, AND IDENTIFICATION IN A COMPLEX WITH INTEGRIN AND
FGF1.
PubMed=20422052; DOI=10.1371/journal.pone.0010273;
Yamaji S., Saegusa J., Ieguchi K., Fujita M., Mori S., Takada Y.K.,
Takada Y.;
"A novel fibroblast growth factor-1 (FGF1) mutant that acts as an FGF
antagonist.";
PLoS ONE 5:E10273-E10273(2010).
[51]
INTERACTION WITH FGF23 AND KLB.
PubMed=19966287; DOI=10.1073/pnas.0902006107;
Goetz R., Nakada Y., Hu M.C., Kurosu H., Wang L., Nakatani T., Shi M.,
Eliseenkova A.V., Razzaque M.S., Moe O.W., Kuro-o M., Mohammadi M.;
"Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by
inhibiting FGF23-FGFR-Klotho complex formation.";
Proc. Natl. Acad. Sci. U.S.A. 107:407-412(2010).
[52]
FUNCTION IN ACTIVATION OF AKT1; PLCG1; MAPK1/ERK2, MAPK3/ERK1 AND MAP
KINASE SIGNALING, FUNCTION IN REGULATION OF NEURONAL DIFFERENTIATION
AND EMBRYONIC DEVELOPMENT, SUBCELLULAR LOCATION, INTERACTION WITH
NEDD4; PLCG1 AND FRS2, UBIQUITINATION, AND DEGRADATION.
PubMed=21765395; DOI=10.1038/emboj.2011.234;
Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F.,
Dirks P., Ciruna B., Rotin D.;
"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its
endocytosis and function.";
EMBO J. 30:3259-3273(2011).
[53]
REVIEW ON ALTERNATIVE SPLICE FORMS; LIGANDS; SIGNALING PATHWAYS AND
SUBCELLULAR LOCATION.
PubMed=12141425;
Groth C., Lardelli M.;
"The structure and function of vertebrate fibroblast growth factor
receptor 1.";
Int. J. Dev. Biol. 46:393-400(2002).
[54]
REVIEW ON FUNCTION; ROLE IN DISEASE; SIGNALING PATHWAYS; SUBUNIT;
DOMAIN STRUCTURE; LIGAND SELECTIVITY AND ENZYME REGULATION.
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).
[55]
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).
[56]
REVIEW ON SIGNALING AND ROLE IN KALLMAN SYNDROME.
PubMed=20117945; DOI=10.1016/j.tem.2010.01.004;
Hu Y., Bouloux P.M.;
"Novel insights in FGFR1 regulation: lessons from Kallmann syndrome.";
Trends Endocrinol. Metab. 21:385-393(2010).
[57]
INVOLVEMENT IN ECCL, VARIANTS ECCL LYS-546 AND GLU-656, AND VARIANT
MET-561.
PubMed=26942290; DOI=10.1016/j.ajhg.2016.02.006;
University of Washington Center for Mendelian Genomics;
Care4Rare Canada Consortium;
Bennett J.T., Tan T.Y., Alcantara D., Tetrault M., Timms A.E.,
Jensen D., Collins S., Nowaczyk M.J., Lindhurst M.J.,
Christensen K.M., Braddock S.R., Brandling-Bennett H., Hennekam R.C.,
Chung B., Lehman A., Su J., Ng S., Amor D.J., Majewski J.,
Biesecker L.G., Boycott K.M., Dobyns W.B., O'Driscoll M., Moog U.,
McDonell L.M.;
"Mosaic activating mutations in FGFR1 cause encephalocraniocutaneous
lipomatosis.";
Am. J. Hum. Genet. 98:579-587(2016).
[58]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 464-762.
PubMed=8752212; DOI=10.1016/S0092-8674(00)80131-2;
Mohammadi M., Schlessinger J., Hubbard S.R.;
"Structure of the FGF receptor tyrosine kinase domain reveals a novel
autoinhibitory mechanism.";
Cell 86:577-587(1996).
[59]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 464-762 IN COMPLEX WITH
SU4984.
PubMed=9139660; DOI=10.1126/science.276.5314.955;
Mohammadi M., McMahon G., Sun L., Tang C., Hirth P., Yeh B.K.,
Hubbard S.R., Schlessinger J.;
"Structures of the tyrosine kinase domain of fibroblast growth factor
receptor in complex with inhibitors.";
Science 276:955-960(1997).
[60]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 141-365 IN COMPLEX WITH FGF1,
FUNCTION, AND DISULFIDE BONDS.
PubMed=10830168; DOI=10.1016/S0092-8674(00)80851-X;
Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.;
"Crystal structures of two FGF-FGFR complexes reveal the determinants
of ligand-receptor specificity.";
Cell 101:413-424(2000).
[61]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 143-364 IN COMPLEX WITH FGF2
AND HEPARIN, AND DISULFIDE BONDS.
PubMed=11030354; DOI=10.1016/S1097-2765(00)00073-3;
Schlessinger J., Plotnikov A.N., Ibrahimi O.A., Eliseenkova A.V.,
Yeh B.K., Yayon A., Linhardt R.J., Mohammadi M.;
"Crystal structure of a ternary FGF-FGFR-heparin complex reveals a
dual role for heparin in FGFR binding and dimerization.";
Mol. Cell 6:743-750(2000).
[62]
STRUCTURE BY NMR OF 38-124.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first Ig-like domain of human fibroblast
growth factor receptor 1.";
Submitted (NOV-2005) to the PDB data bank.
[63]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 458-774 IN COMPLEX WITH PLCG1
AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
AUTOPHOSPHORYLATION, AND PHOSPHORYLATION AT TYR-653; TYR-654 AND
TYR-766.
PubMed=19665973; DOI=10.1016/j.cell.2009.05.028;
Bae J.H., Lew E.D., Yuzawa S., Tome F., Lax I., Schlessinger J.;
"The selectivity of receptor tyrosine kinase signaling is controlled
by a secondary SH2 domain binding site.";
Cell 138:514-524(2009).
[64]
X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 458-765 OF MUTANT GLU-577,
FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND MUTAGENESIS OF ARG-577.
PubMed=20133753; DOI=10.1073/pnas.0914157107;
Bae J.H., Boggon T.J., Tome F., Mandiyan V., Lax I., Schlessinger J.;
"Asymmetric receptor contact is required for tyrosine
autophosphorylation of fibroblast growth factor receptor in living
cells.";
Proc. Natl. Acad. Sci. U.S.A. 107:2866-2871(2010).
[65]
X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 461-765 IN COMPLEX WITH ARQ
069, AND ENZYME REGULATION.
PubMed=21454610; DOI=10.1074/jbc.M110.213736;
Eathiraj S., Palma R., Hirschi M., Volckova E., Nakuci E., Castro J.,
Chen C.R., Chan T.C., France D.S., Ashwell M.A.;
"A novel mode of protein kinase inhibition exploiting hydrophobic
motifs of autoinhibited kinases: discovery of ATP-independent
inhibitors of fibroblast growth factor receptor.";
J. Biol. Chem. 286:20677-20687(2011).
[66]
VARIANT PS ARG-252.
PubMed=7874169; DOI=10.1038/ng1194-269;
Muenke M., Schell U., Hehr A., Robin N.H., Losken H.W., Schinzel A.,
Pulleyn L.J., Rutland P., Reardon W., Malcolm S., Winter R.M.;
"A common mutation in the fibroblast growth factor receptor 1 gene in
Pfeiffer syndrome.";
Nat. Genet. 8:269-274(1994).
[67]
VARIANT TRIGNO1 THR-300.
PubMed=11173846;
Kress W., Petersen B., Collmann H., Grimm T.;
"An unusual FGFR1 mutation (fibroblast growth factor receptor 1
mutation) in a girl with non-syndromic trigonocephaly.";
Cytogenet. Cell Genet. 91:138-140(2000).
[68]
VARIANTS HH2 ASP-97; CYS-99; SER-167; TYR-277; MET-607; ARG-666;
ARG-719 AND SER-772.
PubMed=12627230; DOI=10.1038/ng1122;
Dode C., Levilliers J., Dupont J.-M., De Paepe A., Le Du N.,
Soussi-Yanicostas N., Coimbra R.S., Delmaghani S.,
Compain-Nouaille S., Baverel F., Pecheux C., Le Tessier D., Cruaud C.,
Delpech M., Speleman F., Vermeulen S., Amalfitano A., Bachelot Y.,
Bouchard P., Cabrol S., Carel J.-C., Delemarre-van de Waal H.,
Goulet-Salmon B., Kottler M.-L., Richard O., Sanchez-Franco F.,
Saura R., Young J., Petit C., Hardelin J.-P.;
"Loss-of-function mutations in FGFR1 cause autosomal dominant Kallmann
syndrome.";
Nat. Genet. 33:463-465(2003).
[69]
VARIANT HH2 SER-745.
PubMed=15001591; DOI=10.1210/jc.2003-030476;
Sato N., Katsumata N., Kagami M., Hasegawa T., Hori N., Kawakita S.,
Minowada S., Shimotsuka A., Shishiba Y., Yokozawa M., Yasuda T.,
Nagasaki K., Hasegawa D., Hasegawa Y., Tachibana K., Naiki Y.,
Horikawa R., Tanaka T., Ogata T.;
"Clinical assessment and mutation analysis of Kallmann syndrome 1
(KAL1) and fibroblast growth factor receptor 1 (FGFR1, or KAL2) in
five families and 18 sporadic patients.";
J. Clin. Endocrinol. Metab. 89:1079-1088(2004).
[70]
VARIANTS OGD ILE-330; CYS-374 AND ARG-381, AND CHARACTERIZATION OF
VARIANT OGD CYS-374.
PubMed=15625620; DOI=10.1086/427956;
White K.E., Cabral J.M., Davis S.I., Fishburn T., Evans W.E.,
Ichikawa S., Fields J., Yu X., Shaw N.J., McLellan N.J., McKeown C.,
FitzPatrick D., Yu K., Ornitz D.M., Econs M.J.;
"Mutations that cause osteoglophonic dysplasia define novel roles for
FGFR1 in bone elongation.";
Am. J. Hum. Genet. 76:361-367(2005).
[71]
VARIANTS HH2 ILE-102; ALA-129; MET-273 AND THR-520.
PubMed=15605412; DOI=10.1002/humu.9298;
Albuisson J., Pecheux C., Carel J.-C., Lacombe D., Leheup B.,
Lapuzina P., Bouchard P., Legius E., Matthijs G., Wasniewska M.,
Delpech M., Young J., Hardelin J.-P., Dode C.;
"Kallmann syndrome: 14 novel mutations in KAL1 and FGFR1 (KAL2).";
Hum. Mutat. 25:98-99(2005).
[72]
VARIANTS HH2 ARG-687 AND SER-745.
PubMed=15845591; DOI=10.1093/humrep/dei052;
Sato N., Hasegawa T., Hori N., Fukami M., Yoshimura Y., Ogata T.;
"Gonadotrophin therapy in Kallmann syndrome caused by heterozygous
mutations of the gene for fibroblast growth factor receptor 1: report
of three families: case report.";
Hum. Reprod. 20:2173-2178(2005).
[73]
VARIANTS OGD ILE-330 AND ARG-381.
PubMed=16470795; DOI=10.1002/ajmg.a.31106;
Farrow E.G., Davis S.I., Mooney S.D., Beighton P., Mascarenhas L.,
Gutierrez Y.R., Pitukcheewanont P., White K.E.;
"Extended mutational analyses of FGFR1 in osteoglophonic dysplasia.";
Am. J. Med. Genet. A 140:537-539(2006).
[74]
VARIANTS HH2 SER-48; PRO-245; TRP-250; VAL-343; LEU-366; SER-722 AND
ILE-795.
PubMed=16882753; DOI=10.1210/jc.2005-2793;
Trarbach E.B., Costa E.M.F., Versiani B., de Castro M.,
Baptista M.T.M., Garmes H.M., de Mendonca B.B., Latronico A.C.;
"Novel fibroblast growth factor receptor 1 mutations in patients with
congenital hypogonadotropic hypogonadism with and without anosmia.";
J. Clin. Endocrinol. Metab. 91:4006-4012(2006).
[75]
VARIANTS HH2 CYS-78; ILE-102; HIS-224; ASP-237; GLN-254; MET-273;
GLY-274 CYS-339; CYS-346; VAL-538; ARG-703 AND SER-703, AND VARIANT
VAL-769.
PubMed=16764984; DOI=10.1016/j.mce.2006.04.021;
Pitteloud N., Meysing A., Quinton R., Acierno J.S. Jr., Dwyer A.A.,
Plummer L., Fliers E., Boepple P., Hayes F., Seminara S., Hughes V.A.,
Ma J., Bouloux P., Mohammadi M., Crowley W.F. Jr.;
"Mutations in fibroblast growth factor receptor 1 cause Kallmann
syndrome with a wide spectrum of reproductive phenotypes.";
Mol. Cell. Endocrinol. 254:60-69(2006).
[76]
VARIANTS HH2 SER-178; GLY-622 AND GLN-622.
PubMed=16757108; DOI=10.1016/j.mce.2006.04.006;
Zenaty D., Bretones P., Lambe C., Guemas I., David M., Leger J.,
de Roux N.;
"Paediatric phenotype of Kallmann syndrome due to mutations of
fibroblast growth factor receptor 1 (FGFR1).";
Mol. Cell. Endocrinol. 254:78-83(2006).
[77]
VARIANTS HH2 SER-237; HIS-722 AND LYS-724, AND CHARACTERIZATION OF
VARIANTS HH2 SER-237; HIS-722 AND LYS-724.
PubMed=16606836; DOI=10.1073/pnas.0600962103;
Pitteloud N., Acierno J.S. Jr., Meysing A., Eliseenkova A.V., Ma J.,
Ibrahimi O.A., Metzger D.L., Hayes F.J., Dwyer A.A., Hughes V.A.,
Yialamas M., Hall J.E., Grant E., Mohammadi M., Crowley W.F. Jr.;
"Mutations in fibroblast growth factor receptor 1 cause both Kallmann
syndrome and normosmic idiopathic hypogonadotropic hypogonadism.";
Proc. Natl. Acad. Sci. U.S.A. 103:6281-6286(2006).
[78]
VARIANTS HH2 PHE-101; TRP-250; ASP-270; ARG-283; CYS-332; ARG-621;
PHE-685; PHE-693 AND SER-772, AND VARIANTS LYS-77 AND CYS-822.
PubMed=17154279; DOI=10.1002/humu.9470;
Dode C., Fouveaut C., Mortier G., Janssens S., Bertherat J.,
Mahoudeau J., Kottler M.-L., Chabrolle C., Gancel A., Francois I.,
Devriendt K., Wolczynski S., Pugeat M., Pineiro-Garcia A., Murat A.,
Bouchard P., Young J., Delpech M., Hardelin J.-P.;
"Novel FGFR1 sequence variants in Kallmann syndrome, and genetic
evidence that the FGFR1c isoform is required in olfactory bulb and
palate morphogenesis.";
Hum. Mutat. 28:97-98(2007).
[79]
VARIANTS [LARGE SCALE ANALYSIS] LEU-125; THR-252 AND LEU-664.
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).
[80]
VARIANTS HH2 CYS-99; SER-117; ASP-228; THR-239; GLN-250; LEU-470;
ASN-618 AND PRO-671, AND CHARACTERIZATION OF VARIANTS HH2 CYS-99;
SER-117; ASP-228; THR-239; GLN-250; LEU-470; ASN-618 AND PRO-671.
PubMed=19820032; DOI=10.1210/jc.2009-0179;
Raivio T., Sidis Y., Plummer L., Chen H., Ma J., Mukherjee A.,
Jacobson-Dickman E., Quinton R., Van Vliet G., Lavoie H., Hughes V.A.,
Dwyer A., Hayes F.J., Xu S., Sparks S., Kaiser U.B., Mohammadi M.,
Pitteloud N.;
"Impaired fibroblast growth factor receptor 1 signaling as a cause of
normosmic idiopathic hypogonadotropic hypogonadism.";
J. Clin. Endocrinol. Metab. 94:4380-4390(2009).
[81]
VARIANT HH2 GLN-250.
PubMed=21700882; DOI=10.1073/pnas.1102284108;
Tornberg J., Sykiotis G.P., Keefe K., Plummer L., Hoang X., Hall J.E.,
Quinton R., Seminara S.B., Hughes V., Van Vliet G., Van Uum S.,
Crowley W.F., Habuchi H., Kimata K., Pitteloud N., Bulow H.E.;
"Heparan sulfate 6-O-sulfotransferase 1, a gene involved in
extracellular sugar modifications, is mutated in patients with
idiopathic hypogonadotrophic hypogonadism.";
Proc. Natl. Acad. Sci. U.S.A. 108:11524-11529(2011).
[82]
VARIANT HH2 ARG-687.
PubMed=22927827; DOI=10.1371/journal.pgen.1002896;
Hanchate N.K., Giacobini P., Lhuillier P., Parkash J., Espy C.,
Fouveaut C., Leroy C., Baron S., Campagne C., Vanacker C., Collier F.,
Cruaud C., Meyer V., Garcia-Pinero A., Dewailly D., Cortet-Rudelli C.,
Gersak K., Metz C., Chabrier G., Pugeat M., Young J., Hardelin J.P.,
Prevot V., Dode C.;
"SEMA3A, a gene involved in axonal pathfinding, is mutated in patients
with Kallmann syndrome.";
PLoS Genet. 8:E1002896-E1002896(2012).
[83]
VARIANTS HH2 SER-117; ASP-228; THR-239; GLN-250; SER-342; ARG-348;
LEU-470; THR-483; ASN-618; LYS-670; GLY-692; HIS-722; LYS-724 AND
TYR-768.
PubMed=23643382; DOI=10.1016/j.ajhg.2013.04.008;
Miraoui H., Dwyer A.A., Sykiotis G.P., Plummer L., Chung W., Feng B.,
Beenken A., Clarke J., Pers T.H., Dworzynski P., Keefe K.,
Niedziela M., Raivio T., Crowley W.F. Jr., Seminara S.B., Quinton R.,
Hughes V.A., Kumanov P., Young J., Yialamas M.A., Hall J.E.,
Van Vliet G., Chanoine J.P., Rubenstein J., Mohammadi M., Tsai P.S.,
Sidis Y., Lage K., Pitteloud N.;
"Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in
individuals with congenital hypogonadotropic hypogonadism.";
Am. J. Hum. Genet. 92:725-743(2013).
[84]
INVOLVEMENT IN HRTFDS, AND VARIANTS HRTFDS SER-165; SER-191; ARG-490;
TYR-623; LYS-628 AND TYR-725.
PubMed=23812909; DOI=10.1136/jmedgenet-2013-101603;
Simonis N., Migeotte I., Lambert N., Perazzolo C., de Silva D.C.,
Dimitrov B., Heinrichs C., Janssens S., Kerr B., Mortier G.,
Van Vliet G., Lepage P., Casimir G., Abramowicz M., Smits G.,
Vilain C.;
"FGFR1 mutations cause Hartsfield syndrome, the unique association of
holoprosencephaly and ectrodactyly.";
J. Med. Genet. 50:585-592(2013).
[85]
VARIANT HRTFDS THR-627.
PubMed=24888332; DOI=10.1002/ajmg.a.36621;
Dhamija R., Kirmani S., Wang X., Ferber M.J., Wieben E.D.,
Lazaridis K.N., Babovic-Vuksanovic D.;
"Novel de novo heterozygous FGFR1 mutation in two siblings with
Hartsfield syndrome: A case of gonadal mosaicism.";
Am. J. Med. Genet. A 164:2356-2359(2014).
[86]
VARIANTS HH2 ARG-70; ILE-116; ALA-174; GLN-250 AND ARG-348.
PubMed=25077900; DOI=10.1210/jc.2014-2110;
Marcos S., Sarfati J., Leroy C., Fouveaut C., Parent P., Metz C.,
Wolczynski S., Gerard M., Bieth E., Kurtz F., Verier-Mine O.,
Perrin L., Archambeaud F., Cabrol S., Rodien P., Hove H., Prescott T.,
Lacombe D., Christin-Maitre S., Touraine P., Hieronimus S.,
Dewailly D., Young J., Pugeat M., Hardelin J.P., Dode C.;
"The prevalence of CHD7 missense versus truncating mutations is higher
in patients with Kallmann syndrome than in typical CHARGE patients.";
J. Clin. Endocrinol. Metab. 99:E2138-2143(2014).
[87]
VARIANTS HH2 CYS-4; CYS-96 AND VAL-719, AND VARIANT HH2 THR-353
(ISOFORM 19).
PubMed=26277103; DOI=10.1016/j.fertnstert.2015.07.1142;
Goncalves C., Bastos M., Pignatelli D., Borges T., Araguees J.M.,
Fonseca F., Pereira B.D., Socorro S., Lemos M.C.;
"Novel FGFR1 mutations in Kallmann syndrome and normosmic idiopathic
hypogonadotropic hypogonadism: evidence for the involvement of an
alternatively spliced isoform.";
Fertil. Steril. 0:0-0(2015).
-!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
receptor for fibroblast growth factors and plays an essential role
in the regulation of embryonic development, cell proliferation,
differentiation and migration. Required for normal mesoderm
patterning and correct axial organization during embryonic
development, normal skeletogenesis and normal development of the
gonadotropin-releasing hormone (GnRH) neuronal system.
Phosphorylates PLCG1, FRS2, GAB1 and SHB. 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 phosphorylation of SHC1, STAT1 and PTPN11/SHP2.
In the nucleus, enhances RPS6KA1 and CREB1 activity and
contributes to the regulation of transcription. FGFR1 signaling is
down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination,
internalization and degradation. {ECO:0000250|UniProtKB:P16092,
ECO:0000269|PubMed:10830168, ECO:0000269|PubMed:11353842,
ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1379697,
ECO:0000269|PubMed:1379698, ECO:0000269|PubMed:15117958,
ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277,
ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18480409,
ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19261810,
ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:20133753,
ECO:0000269|PubMed:20139426, ECO:0000269|PubMed:21765395,
ECO:0000269|PubMed:8622701, 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:1379697,
ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:18480409,
ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973,
ECO:0000269|PubMed:20133753, ECO:0000269|PubMed:8622701}.
-!- ENZYME REGULATION: Present in an inactive conformation in the
absence of bound ligand. Ligand binding leads to dimerization and
activation by sequential autophosphorylation on tyrosine residues.
Inhibited by ARQ 069; this compound maintains the kinase in an
inactive conformation and inhibits autophosphorylation. Inhibited
by PD173074. {ECO:0000269|PubMed:18480409,
ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:21454610,
ECO:0000269|PubMed:8622701}.
-!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts
predominantly with FGF1 and FGF2, but can also interact with FGF3,
FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in
vitro) (PubMed:1697263, PubMed:1722683, PubMed:8663044,
PubMed:9655399, PubMed:12181353, PubMed:16597617,
PubMed:17623664). Ligand specificity is determined by tissue-
specific expression of isoforms, and differences in the third Ig-
like domain are crucial for ligand specificity. Affinity for
fibroblast growth factors (FGFs) is increased by heparan sulfate
glycosaminoglycans that function as coreceptors. Likewise, KLB
increases the affinity for FGF19, FGF21 and FGF23
(PubMed:19966287). Interacts (phosphorylated on Tyr-766) with
PLCG1 (via SH2 domains) (PubMed:1656221, PubMed:1379697,
PubMed:21765395). Interacts with FRS2 (PubMed:21765395). Interacts
with RPS6KA1 (PubMed:15117958). Interacts (via C-terminus) with
NEDD4 (via WW3 domain) (PubMed:21765395). Interacts with KL (By
similarity). Interacts with SHB (via SH2 domain)
(PubMed:12181353). Interacts with GRB10 (PubMed:10454568).
Interacts with ANOS1; this interaction does not interfere with
FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2
(PubMed:19696444). Interacts with SOX2 and SOX3. Interacts with
FLRT1, FLRT2 and FLRT3 (By similarity). Found in a ternary complex
with FGF1 and ITGAV:ITGB3 (PubMed:20422052, PubMed:18441324).
{ECO:0000250|UniProtKB:P16092, ECO:0000269|PubMed:10454568,
ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1379697,
ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:1656221,
ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:1697263,
ECO:0000269|PubMed:1722683, ECO:0000269|PubMed:17623664,
ECO:0000269|PubMed:18441324, ECO:0000269|PubMed:19696444,
ECO:0000269|PubMed:19966287, ECO:0000269|PubMed:20422052,
ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:8663044,
ECO:0000269|PubMed:9655399}.
-!- INTERACTION:
Self; NbExp=4; IntAct=EBI-1028277, EBI-1028277;
P23352:ANOS1; NbExp=7; IntAct=EBI-1028277, EBI-5272188;
P12830:CDH1; NbExp=3; IntAct=EBI-1028277, EBI-727477;
P46108:CRK; NbExp=2; IntAct=EBI-1028277, EBI-886;
P35222:CTNNB1; NbExp=2; IntAct=EBI-1028277, EBI-491549;
P05230:FGF1; NbExp=3; IntAct=EBI-1028277, EBI-698068;
P09038:FGF2; NbExp=5; IntAct=EBI-1028277, EBI-977447;
Q9GZV9:FGF23; NbExp=2; IntAct=EBI-1028277, EBI-6594125;
O88900:Grb14 (xeno); NbExp=3; IntAct=EBI-1028277, EBI-7639197;
P08908:HTR1A; NbExp=11; IntAct=EBI-1028277, EBI-6570214;
O35082:Kl (xeno); NbExp=3; IntAct=EBI-15609945, EBI-1570828;
P46934:NEDD4; NbExp=26; IntAct=EBI-1028277, EBI-726944;
Q8IVI9:NOSTRIN; NbExp=5; IntAct=EBI-1028277, EBI-1391643;
P27986:PIK3R1; NbExp=5; IntAct=EBI-1028277, EBI-79464;
P19174:PLCG1; NbExp=9; IntAct=EBI-1028277, EBI-79387;
P10686:Plcg1 (xeno); NbExp=4; IntAct=EBI-1028277, EBI-520788;
-!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle.
Note=After ligand binding, both receptor and ligand are rapidly
internalized. Can translocate to the nucleus after
internalization, or by translocation from the endoplasmic
reticulum or Golgi apparatus to the cytosol, and from there to the
nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=21;
Name=1; Synonyms=Alpha A1, IV;
IsoId=P11362-1; Sequence=Displayed;
Name=2; Synonyms=Alpha A2;
IsoId=P11362-8; Sequence=VSP_009842, VSP_009843;
Name=3; Synonyms=Alpha A3;
IsoId=P11362-17; Sequence=VSP_009836, VSP_009837;
Name=4; Synonyms=Alpha B1;
IsoId=P11362-2; Sequence=VSP_002960;
Name=5; Synonyms=Alpha B2;
IsoId=P11362-9; Sequence=VSP_002960, VSP_009842, VSP_009843;
Name=6; Synonyms=Beta A1, II, H2;
IsoId=P11362-3; Sequence=VSP_002958;
Name=7; Synonyms=Beta A2;
IsoId=P11362-10; Sequence=VSP_002958, VSP_009842, VSP_009843;
Name=8; Synonyms=Beta B1;
IsoId=P11362-4; Sequence=VSP_002958, VSP_002960;
Name=9; Synonyms=Beta B2;
IsoId=P11362-11; Sequence=VSP_002958, VSP_002960, VSP_009842,
VSP_009843;
Name=10; Synonyms=Gamma A1;
IsoId=P11362-5; Sequence=VSP_002957;
Name=11; Synonyms=Gamma A2;
IsoId=P11362-12; Sequence=VSP_002957, VSP_009842, VSP_009843;
Name=12; Synonyms=Gamma B1;
IsoId=P11362-6; Sequence=VSP_002957, VSP_002960;
Name=13; Synonyms=Gamma B2;
IsoId=P11362-13; Sequence=VSP_002957, VSP_002960, VSP_009842,
VSP_009843;
Name=14; Synonyms=A, III;
IsoId=P11362-7; Sequence=VSP_002959;
Name=15; Synonyms=I, H3;
IsoId=P11362-14; Sequence=VSP_002958, VSP_002959;
Name=16; Synonyms=V;
IsoId=P11362-15; Sequence=VSP_009838, VSP_009839;
Name=17; Synonyms=H4;
IsoId=P11362-16; Sequence=VSP_002958, VSP_009840, VSP_009841;
Name=18; Synonyms=H5;
IsoId=P11362-18; Sequence=VSP_002958, VSP_002959, VSP_009840,
VSP_009841;
Name=19;
IsoId=P11362-19; Sequence=VSP_038470, VSP_002959, VSP_038471;
Note=Variant in position: 353:A->T (in HH2, unknown pathological
significance). {ECO:0000269|PubMed:26277103};
Name=20;
IsoId=P11362-20; Sequence=VSP_041916, VSP_041918;
Name=21;
IsoId=P11362-21; Sequence=VSP_041917, VSP_002959;
-!- TISSUE SPECIFICITY: Detected in astrocytoma, neuroblastoma and
adrenal cortex cell lines. Some isoforms are detected in foreskin
fibroblast cell lines, however isoform 17, isoform 18 and isoform
19 are not detected in these cells. {ECO:0000269|PubMed:1652059}.
-!- DOMAIN: The second and third Ig-like domains directly interact
with fibroblast growth factors (FGF) and heparan sulfate
proteoglycans. Isoforms lacking the first Ig-like domain have
higher affinity for fibroblast growth factors (FGF) and heparan
sulfate proteoglycans than isoforms with all three Ig-like
domains.
-!- 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 and proceeds in a highly ordered manner.
Initial autophosphorylation at Tyr-653 increases the kinase
activity by a factor of 50 to 100. After this, Tyr-583 becomes
phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766,
Tyr-583 and Tyr-585. In a third stage, Tyr-654 is
autophosphorylated, resulting in a further tenfold increase of
kinase activity. Phosphotyrosine residues provide docking sites
for interacting proteins and so are crucial for FGFR1 function and
its regulation. {ECO:0000269|PubMed:16507368,
ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973,
ECO:0000269|PubMed:8622701}.
-!- PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after
autophosphorylation, leading to internalization and lysosomal
degradation. CBL is recruited to activated FGFR1 via FRS2 and
GRB2, and mediates ubiquitination and subsequent degradation of
FGFR1. {ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:21765395}.
-!- 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:16335952,
ECO:0000269|PubMed:16481405, ECO:0000269|PubMed:17311277}.
-!- DISEASE: Pfeiffer syndrome (PS) [MIM:101600]: A syndrome
characterized by the association of craniosynostosis, broad and
deviated thumbs and big toes, and partial syndactyly of the
fingers and toes. Three subtypes are known: mild autosomal
dominant form (type 1); cloverleaf skull, elbow ankylosis, early
death, sporadic (type 2); craniosynostosis, early demise, sporadic
(type 3). {ECO:0000269|PubMed:7874169}. Note=The disease is caused
by mutations affecting the gene represented in this entry.
-!- DISEASE: Hypogonadotropic hypogonadism 2 with or without anosmia
(HH2) [MIM:147950]: A disorder characterized by absent or
incomplete sexual maturation by the age of 18 years, in
conjunction with low levels of circulating gonadotropins and
testosterone and no other abnormalities of the hypothalamic-
pituitary axis. In some cases, it is associated with non-
reproductive phenotypes, such as anosmia, cleft palate, and
sensorineural hearing loss. Anosmia or hyposmia is related to the
absence or hypoplasia of the olfactory bulbs and tracts.
Hypogonadism is due to deficiency in gonadotropin-releasing
hormone and probably results from a failure of embryonic migration
of gonadotropin-releasing hormone-synthesizing neurons. In the
presence of anosmia, idiopathic hypogonadotropic hypogonadism is
referred to as Kallmann syndrome, whereas in the presence of a
normal sense of smell, it has been termed normosmic idiopathic
hypogonadotropic hypogonadism (nIHH).
{ECO:0000269|PubMed:12627230, ECO:0000269|PubMed:15001591,
ECO:0000269|PubMed:15605412, ECO:0000269|PubMed:15845591,
ECO:0000269|PubMed:16606836, ECO:0000269|PubMed:16757108,
ECO:0000269|PubMed:16764984, ECO:0000269|PubMed:16882753,
ECO:0000269|PubMed:17154279, ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:22927827,
ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900,
ECO:0000269|PubMed:26277103}. Note=The disease is caused by
mutations affecting distinct genetic loci, including the gene
represented in this entry. Some patients carrying mutations in
FGFR1 also have a mutation other HH-associated genes including
DUSP6, FGF8, FGF17, FLRT3, GNRH1, GNRHR, HS6ST1, IL17RD, ANOS1,
KISS1R, NSMF, PROKR2, SPRY4 and TACR3 (PubMed:23643382).
{ECO:0000269|PubMed:23643382}.
-!- DISEASE: Osteoglophonic dysplasia (OGD) [MIM:166250]:
Characterized by craniosynostosis, prominent supraorbital ridge,
and depressed nasal bridge, as well as by rhizomelic dwarfism and
nonossifying bone lesions. Inheritance is autosomal dominant.
{ECO:0000269|PubMed:15625620, ECO:0000269|PubMed:16470795}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Hartsfield syndrome (HRTFDS) [MIM:615465]: A syndrome
characterized by the triad of holoprosencephaly, ectrodactyly, and
cleft/lip palate. Profound mental retardation is also present.
Multiple other congenital anomalies usually occur.
{ECO:0000269|PubMed:23812909, ECO:0000269|PubMed:24888332}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Trigonocephaly 1 (TRIGNO1) [MIM:190440]: A keel-shaped
deformation of the forehead, caused by premature fusion of the
metopic sutures. It results in a triangular shape of the head.
{ECO:0000269|PubMed:11173846}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Note=A chromosomal aberration involving FGFR1 may be a
cause of stem cell leukemia lymphoma syndrome (SCLL).
Translocation t(8;13)(p11;q12) with ZMYM2. SCLL usually presents
as lymphoblastic lymphoma in association with a myeloproliferative
disorder, often accompanied by pronounced peripheral eosinophilia
and/or prominent eosinophilic infiltrates in the affected bone
marrow. {ECO:0000269|PubMed:9716603}.
-!- DISEASE: Note=A chromosomal aberration involving FGFR1 may be a
cause of stem cell myeloproliferative disorder (MPD).
Translocation t(6;8)(q27;p11) with FGFR1OP. Insertion
ins(12;8)(p11;p11p22) with FGFR1OP2. MPD is characterized by
myeloid hyperplasia, eosinophilia and T-cell or B-cell
lymphoblastic lymphoma. In general it progresses to acute myeloid
leukemia. The fusion proteins FGFR1OP2-FGFR1, FGFR1OP-FGFR1 or
FGFR1-FGFR1OP may exhibit constitutive kinase activity and be
responsible for the transforming activity.
{ECO:0000269|PubMed:10688839, ECO:0000269|PubMed:15034873,
ECO:0000269|PubMed:16946300, ECO:0000269|PubMed:17389761,
ECO:0000269|PubMed:9949182}.
-!- DISEASE: Note=A chromosomal aberration involving FGFR1 may be a
cause of stem cell myeloproliferative disorder (MPD).
Translocation t(8;9)(p12;q33) with CNTRL. MPD is characterized by
myeloid hyperplasia, eosinophilia and T-cell or B-cell
lymphoblastic lymphoma. In general it progresses to acute myeloid
leukemia. The fusion protein CNTRL-FGFR1 is found in the
cytoplasm, exhibits constitutive kinase activity and may be
responsible for the transforming activity.
-!- DISEASE: Encephalocraniocutaneous lipomatosis (ECCL) [MIM:613001]:
A sporadically occurring, neurocutaneous disorder characterized by
ocular anomalies, skin lesions, and central nervous system
anomalies. Clinical features include a well-demarcated hairless
fatty nevus on the scalp, benign ocular tumors, intracranial and
intraspinal lipomas, and congenital abnormalities of the meninges.
Seizures, spasticity, and intellectual disability can be present.
{ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:26942290}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Jackson-Weiss syndrome (JWS) [MIM:123150]: An autosomal
dominant craniosynostosis syndrome characterized by craniofacial
abnormalities and abnormality of the feet: broad great toes with
medial deviation and tarsal-metatarsal coalescence.
{ECO:0000269|PubMed:10861678}. 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=BAD92156.1; 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/FGFR1ID113.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/fgfr1/";
-----------------------------------------------------------------------
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EMBL; M37722; AAA75007.1; -; mRNA.
EMBL; X52833; CAA37015.1; -; mRNA.
EMBL; M34185; AAA35836.1; -; mRNA.
EMBL; M34186; AAA35837.1; -; mRNA.
EMBL; M34187; AAA35838.1; -; mRNA.
EMBL; M34188; AAA35839.1; -; mRNA.
EMBL; X51803; CAA36101.1; -; mRNA.
EMBL; M34641; AAA35835.1; -; mRNA.
EMBL; M60485; AAA35840.1; -; mRNA.
EMBL; X57118; CAA40400.1; -; mRNA.
EMBL; X57119; CAA40401.1; -; mRNA.
EMBL; X57120; CAA40402.1; -; mRNA.
EMBL; X57121; CAA40403.1; -; mRNA.
EMBL; X57122; CAA40404.1; -; mRNA.
EMBL; M63887; AAA35958.1; -; mRNA.
EMBL; M63888; AAA35959.1; -; mRNA.
EMBL; M63889; AAA35960.1; -; mRNA.
EMBL; X66945; CAA47375.1; -; mRNA.
EMBL; FJ809917; ACO38646.1; -; mRNA.
EMBL; AK291754; BAF84443.1; -; mRNA.
EMBL; AK292470; BAF85159.1; -; mRNA.
EMBL; AK309947; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB208919; BAD92156.1; ALT_INIT; mRNA.
EMBL; AK222718; BAD96438.1; -; mRNA.
EMBL; AY585209; AAS79322.1; -; Genomic_DNA.
EMBL; AC087623; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC015035; AAH15035.1; -; mRNA.
EMBL; BC018128; AAH18128.1; -; mRNA.
EMBL; BC091494; AAH91494.1; -; mRNA.
EMBL; Y00665; CAA68679.1; -; mRNA.
CCDS; CCDS43730.1; -. [P11362-3]
CCDS; CCDS43731.1; -. [P11362-14]
CCDS; CCDS43732.1; -. [P11362-7]
CCDS; CCDS55221.1; -. [P11362-20]
CCDS; CCDS55222.1; -. [P11362-2]
CCDS; CCDS55223.1; -. [P11362-21]
CCDS; CCDS6107.2; -. [P11362-1]
PIR; A41266; A41266.
PIR; C36464; C36464.
PIR; C40862; C40862.
PIR; S11692; TVHUFG.
PIR; S19167; A40862.
RefSeq; NP_001167534.1; NM_001174063.1. [P11362-2]
RefSeq; NP_001167535.1; NM_001174064.1. [P11362-20]
RefSeq; NP_001167536.1; NM_001174065.1. [P11362-7]
RefSeq; NP_001167537.1; NM_001174066.1. [P11362-3]
RefSeq; NP_001167538.1; NM_001174067.1. [P11362-21]
RefSeq; NP_056934.2; NM_015850.3. [P11362-7]
RefSeq; NP_075593.1; NM_023105.2. [P11362-3]
RefSeq; NP_075594.1; NM_023106.2. [P11362-14]
RefSeq; NP_075598.2; NM_023110.2. [P11362-1]
UniGene; Hs.264887; -.
PDB; 1AGW; X-ray; 2.40 A; A/B=456-765.
PDB; 1CVS; X-ray; 2.80 A; C/D=141-365.
PDB; 1EVT; X-ray; 2.80 A; C/D=141-365.
PDB; 1FGI; X-ray; 2.50 A; A/B=456-765.
PDB; 1FGK; X-ray; 2.00 A; A/B=456-765.
PDB; 1FQ9; X-ray; 3.00 A; C/D=141-365.
PDB; 1XR0; NMR; -; A=409-430.
PDB; 2CR3; NMR; -; A=38-123.
PDB; 2FGI; X-ray; 2.50 A; A/B=456-765.
PDB; 3C4F; X-ray; 2.07 A; A/B=464-765.
PDB; 3DPK; X-ray; 1.95 A; A=577-615.
PDB; 3GQI; X-ray; 2.50 A; A=458-774.
PDB; 3GQL; X-ray; 2.80 A; A/B/C=458-774.
PDB; 3JS2; X-ray; 2.20 A; A/B=458-765.
PDB; 3KRJ; X-ray; 2.10 A; A=577-597.
PDB; 3KRL; X-ray; 2.40 A; A=577-597.
PDB; 3KXX; X-ray; 3.20 A; A/B/C/D=458-765.
PDB; 3KY2; X-ray; 2.70 A; A/B=458-765.
PDB; 3OJV; X-ray; 2.60 A; C/D=142-365.
PDB; 3RHX; X-ray; 2.01 A; A/B=461-765.
PDB; 3TT0; X-ray; 2.80 A; A/B=456-765.
PDB; 4F63; X-ray; 2.55 A; A/B=458-765.
PDB; 4F64; X-ray; 2.05 A; A/B=458-765.
PDB; 4F65; X-ray; 2.26 A; A/B=458-765.
PDB; 4NK9; X-ray; 2.57 A; A/B=458-765.
PDB; 4NKA; X-ray; 2.19 A; A/B=458-765.
PDB; 4NKS; X-ray; 2.50 A; A/B=458-765.
PDB; 4RWI; X-ray; 2.29 A; A/B=458-765.
PDB; 4RWJ; X-ray; 2.49 A; A/B=458-765.
PDB; 4RWK; X-ray; 2.98 A; A/B=458-765.
PDB; 4RWL; X-ray; 2.19 A; A/B=458-765.
PDB; 4UWB; X-ray; 2.31 A; A/B=458-765.
PDB; 4UWC; X-ray; 1.96 A; A/B=458-765.
PDB; 4UWY; X-ray; 2.31 A; A/B=458-765.
PDB; 4V01; X-ray; 2.33 A; A/B=458-765.
PDB; 4V04; X-ray; 2.12 A; A/B=458-765.
PDB; 4V05; X-ray; 2.57 A; A/B=458-765.
PDB; 4WUN; X-ray; 1.65 A; A/B=459-765.
PDB; 4ZSA; X-ray; 2.00 A; A/B=458-765.
PDB; 5A46; X-ray; 2.63 A; A/B=437-822.
PDB; 5A4C; X-ray; 2.09 A; A/B=461-765.
PDB; 5AM6; X-ray; 1.96 A; A/B=458-765.
PDB; 5AM7; X-ray; 1.96 A; A/B=458-765.
PDB; 5B7V; X-ray; 2.15 A; A/B=456-765.
PDB; 5EW8; X-ray; 1.63 A; A/B=458-765.
PDB; 5FLF; X-ray; 2.58 A; A/B/C/D/E=458-765.
PDB; 5UQ0; X-ray; 2.30 A; A/B=459-765.
PDB; 5UR1; X-ray; 2.20 A; A/B=459-765.
PDB; 5VND; X-ray; 2.20 A; A/B=458-765.
PDB; 5W59; X-ray; 2.50 A; B=142-365.
PDBsum; 1AGW; -.
PDBsum; 1CVS; -.
PDBsum; 1EVT; -.
PDBsum; 1FGI; -.
PDBsum; 1FGK; -.
PDBsum; 1FQ9; -.
PDBsum; 1XR0; -.
PDBsum; 2CR3; -.
PDBsum; 2FGI; -.
PDBsum; 3C4F; -.
PDBsum; 3DPK; -.
PDBsum; 3GQI; -.
PDBsum; 3GQL; -.
PDBsum; 3JS2; -.
PDBsum; 3KRJ; -.
PDBsum; 3KRL; -.
PDBsum; 3KXX; -.
PDBsum; 3KY2; -.
PDBsum; 3OJV; -.
PDBsum; 3RHX; -.
PDBsum; 3TT0; -.
PDBsum; 4F63; -.
PDBsum; 4F64; -.
PDBsum; 4F65; -.
PDBsum; 4NK9; -.
PDBsum; 4NKA; -.
PDBsum; 4NKS; -.
PDBsum; 4RWI; -.
PDBsum; 4RWJ; -.
PDBsum; 4RWK; -.
PDBsum; 4RWL; -.
PDBsum; 4UWB; -.
PDBsum; 4UWC; -.
PDBsum; 4UWY; -.
PDBsum; 4V01; -.
PDBsum; 4V04; -.
PDBsum; 4V05; -.
PDBsum; 4WUN; -.
PDBsum; 4ZSA; -.
PDBsum; 5A46; -.
PDBsum; 5A4C; -.
PDBsum; 5AM6; -.
PDBsum; 5AM7; -.
PDBsum; 5B7V; -.
PDBsum; 5EW8; -.
PDBsum; 5FLF; -.
PDBsum; 5UQ0; -.
PDBsum; 5UR1; -.
PDBsum; 5VND; -.
PDBsum; 5W59; -.
ProteinModelPortal; P11362; -.
SMR; P11362; -.
BioGrid; 108551; 104.
CORUM; P11362; -.
DIP; DIP-4019N; -.
IntAct; P11362; 29.
MINT; MINT-1499363; -.
STRING; 9606.ENSP00000393312; -.
BindingDB; P11362; -.
ChEMBL; CHEMBL3650; -.
DrugBank; DB08577; 3-[(3-(2-CARBOXYETHYL)-4-METHYLPYRROL-2-YL)METHYLENE]-2-INDOLINONE.
DrugBank; DB09078; Lenvatinib.
DrugBank; DB09079; Nintedanib.
DrugBank; DB00039; Palifermin.
DrugBank; DB08901; Ponatinib.
DrugBank; DB08896; Regorafenib.
DrugBank; DB00398; Sorafenib.
DrugBank; DB02058; SU4984.
DrugBank; DB05014; XL999.
GuidetoPHARMACOLOGY; 1808; -.
TCDB; 8.A.23.1.7; the basigin (basigin) family.
iPTMnet; P11362; -.
PhosphoSitePlus; P11362; -.
SwissPalm; P11362; -.
BioMuta; FGFR1; -.
DMDM; 120046; -.
EPD; P11362; -.
MaxQB; P11362; -.
PaxDb; P11362; -.
PeptideAtlas; P11362; -.
PRIDE; P11362; -.
DNASU; 2260; -.
Ensembl; ENST00000326324; ENSP00000327229; ENSG00000077782. [P11362-14]
Ensembl; ENST00000335922; ENSP00000337247; ENSG00000077782. [P11362-20]
Ensembl; ENST00000356207; ENSP00000348537; ENSG00000077782. [P11362-3]
Ensembl; ENST00000397091; ENSP00000380280; ENSG00000077782. [P11362-7]
Ensembl; ENST00000397108; ENSP00000380297; ENSG00000077782. [P11362-7]
Ensembl; ENST00000397113; ENSP00000380302; ENSG00000077782. [P11362-7]
Ensembl; ENST00000425967; ENSP00000393312; ENSG00000077782. [P11362-21]
Ensembl; ENST00000447712; ENSP00000400162; ENSG00000077782. [P11362-1]
Ensembl; ENST00000484370; ENSP00000433163; ENSG00000077782. [P11362-15]
Ensembl; ENST00000532791; ENSP00000432972; ENSG00000077782. [P11362-2]
GeneID; 2260; -.
KEGG; hsa:2260; -.
UCSC; uc003xlp.4; human. [P11362-1]
CTD; 2260; -.
DisGeNET; 2260; -.
EuPathDB; HostDB:ENSG00000077782.19; -.
GeneCards; FGFR1; -.
GeneReviews; FGFR1; -.
HGNC; HGNC:3688; FGFR1.
HPA; CAB033614; -.
HPA; HPA056402; -.
HPA; HPA076274; -.
MalaCards; FGFR1; -.
MIM; 101600; phenotype.
MIM; 123150; phenotype.
MIM; 136350; gene.
MIM; 147950; phenotype.
MIM; 166250; phenotype.
MIM; 190440; phenotype.
MIM; 613001; phenotype.
MIM; 615465; phenotype.
neXtProt; NX_P11362; -.
OpenTargets; ENSG00000077782; -.
Orphanet; 251579; Giant cell glioblastoma.
Orphanet; 251576; Gliosarcoma.
Orphanet; 2117; Hartsfield-Bixler-Demyer syndrome.
Orphanet; 2227; Hypodontia.
Orphanet; 3366; Isolated trigonocephaly.
Orphanet; 478; Kallmann syndrome.
Orphanet; 168953; Myeloid neoplasm associated with FGFR1 rearrangement.
Orphanet; 432; Normosmic congenital hypogonadotropic hypogonadism.
Orphanet; 99798; Oligodontia.
Orphanet; 2645; Osteoglophonic dwarfism.
Orphanet; 93258; Pfeiffer syndrome type 1.
Orphanet; 251612; Pilocytic astrocytoma.
Orphanet; 314950; Primary hypereosinophilic syndrome.
Orphanet; 3157; Septo-optic dysplasia.
PharmGKB; PA28127; -.
eggNOG; KOG0200; Eukaryota.
eggNOG; COG0515; LUCA.
GeneTree; ENSGT00760000118923; -.
HOGENOM; HOG000263410; -.
HOVERGEN; HBG000345; -.
InParanoid; P11362; -.
KO; K04362; -.
OMA; SVIVYKM; -.
OrthoDB; EOG091G0CQZ; -.
PhylomeDB; P11362; -.
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-1839120; Signaling by FGFR1 amplification mutants.
Reactome; R-HSA-1839122; Signaling by activated point mutants of FGFR1.
Reactome; R-HSA-190370; FGFR1b ligand binding and activation.
Reactome; R-HSA-190373; FGFR1c ligand binding and activation.
Reactome; R-HSA-190374; FGFR1c and Klotho ligand binding and activation.
Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
Reactome; R-HSA-375165; NCAM signaling for neurite out-growth.
Reactome; R-HSA-445144; Signal transduction by L1.
Reactome; R-HSA-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-HSA-5654687; Downstream signaling of activated FGFR1.
Reactome; R-HSA-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-HSA-5654689; PI-3K cascade:FGFR1.
Reactome; R-HSA-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-HSA-5655302; Signaling by FGFR1 in disease.
Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
Reactome; R-HSA-8853336; Signaling by plasma membrane FGFR1 fusions.
SignaLink; P11362; -.
SIGNOR; P11362; -.
ChiTaRS; FGFR1; human.
EvolutionaryTrace; P11362; -.
GeneWiki; Fibroblast_growth_factor_receptor_1; -.
GenomeRNAi; 2260; -.
PMAP-CutDB; P11362; -.
PRO; PR:P11362; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000077782; -.
CleanEx; HS_FGFR1; -.
CleanEx; HS_FLG; -.
ExpressionAtlas; P11362; baseline and differential.
Genevisible; P11362; HS.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0005730; C:nucleolus; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0043235; C:receptor complex; IDA:MGI.
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:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0046934; F:phosphatidylinositol-4,5-bisphosphate 3-kinase activity; TAS:Reactome.
GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
GO; GO:0004713; F:protein tyrosine kinase activity; IDA:UniProtKB.
GO; GO:0005088; F:Ras guanyl-nucleotide exchange factor activity; TAS:Reactome.
GO; GO:0090722; F:receptor-receptor interaction; IDA:ParkinsonsUK-UCL.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0060117; P:auditory receptor cell development; IEA:Ensembl.
GO; GO:0060445; P:branching involved in salivary gland morphogenesis; IEA:Ensembl.
GO; GO:0048469; P:cell maturation; IEA:Ensembl.
GO; GO:0016477; P:cell migration; TAS:UniProtKB.
GO; GO:0002062; P:chondrocyte differentiation; IEA:Ensembl.
GO; GO:0043009; P:chordate embryonic development; TAS:UniProtKB.
GO; GO:0030326; P:embryonic limb morphogenesis; IEA:Ensembl.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; IEA:Ensembl.
GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
GO; GO:0042472; P:inner ear morphogenesis; IEA:Ensembl.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0060484; P:lung-associated mesenchyme development; IEA:Ensembl.
GO; GO:0000165; P:MAPK cascade; TAS:Reactome.
GO; GO:0048762; P:mesenchymal cell differentiation; IEA:Ensembl.
GO; GO:0030901; P:midbrain development; IEA:Ensembl.
GO; GO:0042474; P:middle ear morphogenesis; IEA:Ensembl.
GO; GO:0090272; P:negative regulation of fibroblast growth factor production; IEA:Ensembl.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
GO; GO:0001764; P:neuron migration; TAS:UniProtKB.
GO; GO:0001759; P:organ induction; IEA:Ensembl.
GO; GO:0042473; P:outer ear morphogenesis; IEA:Ensembl.
GO; GO:0048339; P:paraxial mesoderm development; IEA:Ensembl.
GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:UniProtKB.
GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; IEA:Ensembl.
GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
GO; GO:2000546; P:positive regulation of endothelial cell chemotaxis to fibroblast growth factor; IDA:BHF-UCL.
GO; GO:0043406; P:positive regulation of MAP kinase activity; IDA:UniProtKB.
GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IEA:Ensembl.
GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; IEA:Ensembl.
GO; GO:1903465; P:positive regulation of mitotic cell cycle DNA replication; IEA:Ensembl.
GO; GO:0045666; P:positive regulation of neuron differentiation; IMP:UniProtKB.
GO; GO:0010976; P:positive regulation of neuron projection development; IEA:Ensembl.
GO; GO:2000830; P:positive regulation of parathyroid hormone secretion; IEA:Ensembl.
GO; GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase signaling; TAS:UniProtKB.
GO; GO:0010518; P:positive regulation of phospholipase activity; TAS:UniProtKB.
GO; GO:0010863; P:positive regulation of phospholipase C activity; IDA:UniProtKB.
GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
GO; GO:0006468; P:protein phosphorylation; NAS:UniProtKB.
GO; GO:0060665; P:regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling; IEA:Ensembl.
GO; GO:0045595; P:regulation of cell differentiation; TAS:UniProtKB.
GO; GO:2001239; P:regulation of extrinsic apoptotic signaling pathway in absence of ligand; IEA:Ensembl.
GO; GO:0048378; P:regulation of lateral mesodermal cell fate specification; IEA:Ensembl.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; TAS:Reactome.
GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
GO; GO:0048705; P:skeletal system morphogenesis; TAS:UniProtKB.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0001657; P:ureteric bud development; IEA:Ensembl.
GO; GO:0007037; P:vacuolar phosphate transport; IEA:Ensembl.
GO; GO:0021847; P:ventricular zone neuroblast division; IEA:Ensembl.
GO; GO:0070640; P:vitamin D3 metabolic process; IEA:Ensembl.
CDD; cd05098; PTKc_FGFR1; 1.
Gene3D; 2.60.40.10; -; 3.
InterPro; IPR028174; FGF_rcpt_1.
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; IPR013151; Immunoglobulin.
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.
Pfam; PF07679; I-set; 2.
Pfam; PF00047; ig; 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; ATP-binding; Cell membrane;
Chromosomal rearrangement; Complete proteome; Craniosynostosis;
Cytoplasm; Cytoplasmic vesicle; Direct protein sequencing;
Disease mutation; Disulfide bond; Dwarfism; Glycoprotein;
Heparin-binding; Holoprosencephaly; Hypogonadotropic hypogonadism;
Immunoglobulin domain; Kallmann syndrome; Kinase; Membrane;
Mental retardation; Nucleotide-binding; Nucleus; Phosphoprotein;
Polymorphism; Receptor; Reference proteome; Repeat; Signal;
Transcription; Transcription regulation; Transferase; Transmembrane;
Transmembrane helix; Tyrosine-protein kinase; Ubl conjugation.
SIGNAL 1 21
CHAIN 22 822 Fibroblast growth factor receptor 1.
/FTId=PRO_0000016780.
TOPO_DOM 22 376 Extracellular. {ECO:0000255}.
TRANSMEM 377 397 Helical. {ECO:0000255}.
TOPO_DOM 398 822 Cytoplasmic. {ECO:0000255}.
DOMAIN 25 119 Ig-like C2-type 1.
DOMAIN 158 246 Ig-like C2-type 2.
DOMAIN 255 357 Ig-like C2-type 3.
DOMAIN 478 767 Protein kinase. {ECO:0000255|PROSITE-
ProRule:PRU00159}.
NP_BIND 484 490 ATP.
NP_BIND 562 564 ATP.
REGION 160 177 Heparin-binding.
ACT_SITE 623 623 Proton acceptor. {ECO:0000255|PROSITE-
ProRule:PRU00159, ECO:0000255|PROSITE-
ProRule:PRU10028,
ECO:0000269|PubMed:19224897}.
BINDING 514 514 ATP.
BINDING 568 568 ATP.
BINDING 627 627 ATP.
BINDING 641 641 ATP.
SITE 428 429 Breakpoint for translocation to form
CNTRL-FGFR1 OR FGFR1-CNTRL fusion
proteins. {ECO:0000269|PubMed:10688839}.
SITE 428 429 Breakpoint for translocation to form
FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion
proteins. {ECO:0000269|PubMed:9949182}.
SITE 428 429 Breakpoint for translocation to form
FGFR1OP2-FGFR1.
{ECO:0000269|PubMed:15034873,
ECO:0000269|PubMed:16946300,
ECO:0000269|PubMed:17389761}.
SITE 766 766 Mediates interaction with PLCG1 and SHB.
MOD_RES 463 463 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16507368,
ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:8622701}.
MOD_RES 583 583 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16507368,
ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:8622701}.
MOD_RES 585 585 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16507368,
ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:8622701}.
MOD_RES 653 653 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16507368,
ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:19665973,
ECO:0000269|PubMed:8622701}.
MOD_RES 654 654 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:16507368,
ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:19665973,
ECO:0000269|PubMed:8622701}.
MOD_RES 730 730 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:8622701}.
MOD_RES 766 766 Phosphotyrosine; by autocatalysis.
{ECO:0000269|PubMed:19665973}.
CARBOHYD 77 77 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 117 117 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 227 227 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 264 264 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 296 296 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
CARBOHYD 317 317 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 330 330 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 55 101 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 178 230
DISULFID 277 341
VAR_SEQ 1 160 Missing (in isoform 10, isoform 11,
isoform 12 and isoform 13).
{ECO:0000303|PubMed:1846977}.
/FTId=VSP_002957.
VAR_SEQ 1 30 MWSWKCLLFWAVLVTATLCTARPSPTLPEQ -> MAAVTRD
FGEMLLHSGRVLPAE (in isoform 20).
{ECO:0000303|Ref.12}.
/FTId=VSP_041916.
VAR_SEQ 1 1 M -> MEARVSLKRRIELTVEYPWRCGALSPTSNCRTGM
(in isoform 21).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_041917.
VAR_SEQ 31 119 Missing (in isoform 6, isoform 7, isoform
8, isoform 9, isoform 15, isoform 17 and
isoform 18).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1650441,
ECO:0000303|PubMed:1846977,
ECO:0000303|PubMed:2162671,
ECO:0000303|PubMed:2167437,
ECO:0000303|PubMed:7520751}.
/FTId=VSP_002958.
VAR_SEQ 32 61 QPWGAPVEVESFLVHPGDLLQLRCRLRDDV -> CPDLQEA
KSCSASFHSITPLPFGLGTRLSD (in isoform 3).
{ECO:0000303|PubMed:1846977}.
/FTId=VSP_009836.
VAR_SEQ 62 822 Missing (in isoform 3).
{ECO:0000303|PubMed:1846977}.
/FTId=VSP_009837.
VAR_SEQ 119 119 S -> SVPI (in isoform 19).
{ECO:0000303|PubMed:1652059,
ECO:0000303|PubMed:20139426}.
/FTId=VSP_038470.
VAR_SEQ 120 150 DALPSSEDDDDDDDSSSEEKETDNTKPNRMP -> ACPDLQ
EAKWCSASFHSITPLPFGLGTRLSD (in isoform
16). {ECO:0000303|PubMed:1650441}.
/FTId=VSP_009838.
VAR_SEQ 148 149 Missing (in isoform 14, isoform 15,
isoform 18, isoform 19 and isoform 21).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1650441,
ECO:0000303|PubMed:1652059,
ECO:0000303|PubMed:1662973,
ECO:0000303|PubMed:1722683,
ECO:0000303|PubMed:20139426,
ECO:0000303|PubMed:2162671,
ECO:0000303|PubMed:2167437,
ECO:0000303|PubMed:7520751,
ECO:0000303|Ref.12}.
/FTId=VSP_002959.
VAR_SEQ 151 822 Missing (in isoform 16).
{ECO:0000303|PubMed:1650441}.
/FTId=VSP_009839.
VAR_SEQ 313 391 TAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHS
AWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMV ->
VIMAPVFVGQSTGKETTVSGAQVPVGRLSCPRMGSFLTLQA
HTLHLSRDLATSPRTSNRGHKVEVSWEQRAAGMGGAGL
(in isoform 17 and isoform 18).
{ECO:0000303|PubMed:2167437}.
/FTId=VSP_009840.
VAR_SEQ 313 360 TAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHS
AWLTVLE -> HSGINSSDAEVLTLFNVTEAQSGEYVCKVS
NYIGEANQSAWLTVTRP (in isoform 19).
{ECO:0000303|PubMed:1652059,
ECO:0000303|PubMed:20139426}.
/FTId=VSP_038471.
VAR_SEQ 392 822 Missing (in isoform 17 and isoform 18).
{ECO:0000303|PubMed:2167437}.
/FTId=VSP_009841.
VAR_SEQ 427 428 Missing (in isoform 20).
{ECO:0000303|Ref.12}.
/FTId=VSP_041918.
VAR_SEQ 428 429 Missing (in isoform 4, isoform 5, isoform
8, isoform 9, isoform 12 and isoform 13).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:1846977}.
/FTId=VSP_002960.
VAR_SEQ 619 662 CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTN
GRL -> VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWP
RTGHSPHRLL (in isoform 2, isoform 5,
isoform 7, isoform 9, isoform 11 and
isoform 13).
{ECO:0000303|PubMed:1846977}.
/FTId=VSP_009842.
VAR_SEQ 663 822 Missing (in isoform 2, isoform 5, isoform
7, isoform 9, isoform 11 and isoform 13).
{ECO:0000303|PubMed:1846977}.
/FTId=VSP_009843.
VARIANT 4 4 W -> C (in HH2; unknown pathological
significance; dbSNP:rs760884357).
{ECO:0000269|PubMed:26277103}.
/FTId=VAR_074012.
VARIANT 22 22 R -> S (in dbSNP:rs17175750).
{ECO:0000269|Ref.13}.
/FTId=VAR_019290.
VARIANT 48 48 G -> S (in HH2; phenotype consistent with
normosmic idiopathic hypogonadotropic
hypogonadism; dbSNP:rs121909640).
{ECO:0000269|PubMed:16882753}.
/FTId=VAR_030968.
VARIANT 70 70 G -> R (in HH2; dbSNP:rs140254426).
{ECO:0000269|PubMed:25077900}.
/FTId=VAR_072993.
VARIANT 77 77 N -> K (in dbSNP:rs767195580).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_030969.
VARIANT 78 78 R -> C (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030970.
VARIANT 96 96 S -> C (in HH2; unknown pathological
significance).
{ECO:0000269|PubMed:26277103}.
/FTId=VAR_074013.
VARIANT 97 97 G -> D (in HH2).
{ECO:0000269|PubMed:12627230}.
/FTId=VAR_017885.
VARIANT 99 99 Y -> C (in HH2; impairs the tertiary
folding resulting in incomplete
glycosylation and reduced cell surface
expression; dbSNP:rs727505373).
{ECO:0000269|PubMed:12627230,
ECO:0000269|PubMed:19820032}.
/FTId=VAR_017886.
VARIANT 101 101 C -> F (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_030971.
VARIANT 102 102 V -> I (in HH2; dbSNP:rs55642501).
{ECO:0000269|PubMed:15605412,
ECO:0000269|PubMed:16764984}.
/FTId=VAR_030972.
VARIANT 116 116 V -> I (in HH2; dbSNP:rs747842199).
{ECO:0000269|PubMed:25077900}.
/FTId=VAR_072994.
VARIANT 117 117 N -> S (in HH2; some patients also carry
GNRHR mutations; dbSNP:rs780765366).
{ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_069288.
VARIANT 125 125 S -> L (in a breast infiltrating ductal
carcinoma sample; somatic mutation;
dbSNP:rs121913473).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042201.
VARIANT 129 129 D -> A (in HH2; dbSNP:rs765615419).
{ECO:0000269|PubMed:15605412}.
/FTId=VAR_030973.
VARIANT 165 165 L -> S (in HRTFDS; dbSNP:rs397515481).
{ECO:0000269|PubMed:23812909}.
/FTId=VAR_070851.
VARIANT 167 167 A -> S (in HH2; with cleft palate, corpus
callosum agenesis, unilateral deafness
and fusion of fourth and fifth metacarpal
bones; dbSNP:rs121909630).
{ECO:0000269|PubMed:12627230}.
/FTId=VAR_017887.
VARIANT 174 174 V -> A (in HH2).
{ECO:0000269|PubMed:25077900}.
/FTId=VAR_072995.
VARIANT 178 178 C -> S (in HH2; with severe ear
anomalies).
{ECO:0000269|PubMed:16757108}.
/FTId=VAR_030974.
VARIANT 191 191 L -> S (in HRTFDS; dbSNP:rs869025669).
{ECO:0000269|PubMed:23812909}.
/FTId=VAR_070852.
VARIANT 213 213 W -> G (in dbSNP:rs17851623).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_030975.
VARIANT 224 224 D -> H (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030976.
VARIANT 228 228 Y -> D (in HH2; some patients also carry
KISS1R mutations; impairs the tertiary
folding resulting in incomplete
glycosylation and reduced cell surface
expression).
{ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_069289.
VARIANT 237 237 G -> D (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030977.
VARIANT 237 237 G -> S (in HH2; with or without anosmia;
also found in a family member with
isolated anosmia; may impair proper
folding; dbSNP:rs121909635).
{ECO:0000269|PubMed:16606836}.
/FTId=VAR_030978.
VARIANT 239 239 I -> T (in HH2; some patients also carry
PROKR2 and GNRH1 mutations; impairs the
tertiary folding resulting in incomplete
glycosylation and reduced cell surface
expression).
{ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_069290.
VARIANT 245 245 L -> P (in HH2).
{ECO:0000269|PubMed:16882753}.
/FTId=VAR_030979.
VARIANT 250 250 R -> Q (in HH2; with or without anosmia;
results in Kallmann syndrome in the
presence of HS6ST1 mutation TRP-306;
reduces receptor affinity for fibroblast
growth factor; dbSNP:rs121909645).
{ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:21700882,
ECO:0000269|PubMed:23643382,
ECO:0000269|PubMed:25077900}.
/FTId=VAR_069291.
VARIANT 250 250 R -> W (in HH2).
{ECO:0000269|PubMed:16882753,
ECO:0000269|PubMed:17154279}.
/FTId=VAR_030980.
VARIANT 252 252 P -> R (in PS and JWS;
dbSNP:rs121909627).
{ECO:0000269|PubMed:10861678,
ECO:0000269|PubMed:7874169}.
/FTId=VAR_004111.
VARIANT 252 252 P -> T (in a lung bronchoalveolar
carcinoma sample; somatic mutation;
dbSNP:rs121913472).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042202.
VARIANT 254 254 R -> Q (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030981.
VARIANT 270 270 G -> D (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_030982.
VARIANT 273 273 V -> M (in HH2).
{ECO:0000269|PubMed:15605412,
ECO:0000269|PubMed:16764984}.
/FTId=VAR_030983.
VARIANT 274 274 E -> G (in HH2; also found in a family
member with isolated anosmia;
dbSNP:rs727505369).
/FTId=VAR_030984.
VARIANT 277 277 C -> Y (in HH2).
{ECO:0000269|PubMed:12627230}.
/FTId=VAR_017888.
VARIANT 283 283 P -> R (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_030985.
VARIANT 300 300 I -> T (in TRIGNO1; dbSNP:rs121909633).
{ECO:0000269|PubMed:11173846}.
/FTId=VAR_030986.
VARIANT 330 330 N -> I (in OGD; dbSNP:rs121909632).
{ECO:0000269|PubMed:15625620,
ECO:0000269|PubMed:16470795}.
/FTId=VAR_030987.
VARIANT 332 332 S -> C (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_030988.
VARIANT 339 339 Y -> C (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030989.
VARIANT 342 342 L -> S (in HH2; phenotype consistent with
Kallmann syndrome; the patient also
carries a splice site mutation in NSMF;
dbSNP:rs121909638).
{ECO:0000269|PubMed:23643382}.
/FTId=VAR_069954.
VARIANT 343 343 A -> V (in HH2).
{ECO:0000269|PubMed:16882753}.
/FTId=VAR_030990.
VARIANT 346 346 S -> C (in HH2; also found in a family
member with isolated anosmia).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030991.
VARIANT 348 348 G -> R (in HH2; phenotype consistent with
Kallmann syndrome; the patient also
carries a mutation in IL17RD).
{ECO:0000269|PubMed:23643382,
ECO:0000269|PubMed:25077900}.
/FTId=VAR_069955.
VARIANT 366 366 P -> L (in HH2; with or without anosmia;
dbSNP:rs121909641).
{ECO:0000269|PubMed:16882753}.
/FTId=VAR_030992.
VARIANT 374 374 Y -> C (in OGD; elevated basal activity
and increased FGF2-mediated activity;
dbSNP:rs121909631).
{ECO:0000269|PubMed:15625620}.
/FTId=VAR_030993.
VARIANT 381 381 C -> R (in OGD; dbSNP:rs121909634).
{ECO:0000269|PubMed:15625620,
ECO:0000269|PubMed:16470795}.
/FTId=VAR_030994.
VARIANT 470 470 R -> L (in HH2; some patients also carry
GNRHR mutations; dbSNP:rs121909637).
{ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_069292.
VARIANT 483 483 P -> T (in HH2; phenotype consistent with
Kallmann syndrome; the patient also
carries a rare variant in SPRY4;
dbSNP:rs397515444).
{ECO:0000269|PubMed:23643382}.
/FTId=VAR_069956.
VARIANT 490 490 G -> R (in HRTFDS; dbSNP:rs869025670).
{ECO:0000269|PubMed:23812909}.
/FTId=VAR_070853.
VARIANT 520 520 A -> T (in HH2; dbSNP:rs749758370).
{ECO:0000269|PubMed:15605412}.
/FTId=VAR_030995.
VARIANT 538 538 I -> V (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_030996.
VARIANT 546 546 N -> K (in ECCL; somatic mutation;
activating mutation; strongly increased
speed of the first autophosphorylation
and loss of the normal sequential order
of autophosphorylation).
{ECO:0000269|PubMed:19224897,
ECO:0000269|PubMed:26942290}.
/FTId=VAR_075853.
VARIANT 561 561 V -> M. {ECO:0000269|PubMed:26942290}.
/FTId=VAR_075854.
VARIANT 607 607 V -> M (in HH2; with bimanual synkinesis;
dbSNP:rs121909629).
{ECO:0000269|PubMed:12627230}.
/FTId=VAR_017889.
VARIANT 618 618 K -> N (in HH2; some patients also carry
GNRHR mutations; impairs tyrosine kinase
activity). {ECO:0000269|PubMed:19820032,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_069293.
VARIANT 621 621 H -> R (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_030997.
VARIANT 622 622 R -> G (in HH2; with severe ear
anomalies).
{ECO:0000269|PubMed:16757108}.
/FTId=VAR_030998.
VARIANT 622 622 R -> Q (in HH2).
{ECO:0000269|PubMed:16757108}.
/FTId=VAR_030999.
VARIANT 623 623 D -> Y (in HRTFDS; dbSNP:rs398122946).
{ECO:0000269|PubMed:23812909}.
/FTId=VAR_070854.
VARIANT 627 627 R -> T (in HRTFDS; dbSNP:rs869025671).
{ECO:0000269|PubMed:24888332}.
/FTId=VAR_071460.
VARIANT 628 628 N -> K (in HRTFDS; dbSNP:rs869025672).
{ECO:0000269|PubMed:23812909}.
/FTId=VAR_070855.
VARIANT 656 656 K -> E (in ECCL; somatic mutation;
dbSNP:rs869320694).
{ECO:0000269|PubMed:26942290}.
/FTId=VAR_075855.
VARIANT 664 664 V -> L (in a lung large cell carcinoma
sample; somatic mutation).
{ECO:0000269|PubMed:17344846}.
/FTId=VAR_042203.
VARIANT 666 666 W -> R (in HH2; with cleft palate).
{ECO:0000269|PubMed:12627230}.
/FTId=VAR_017890.
VARIANT 670 670 E -> K (in HH2; phenotype consistent with
Kallmann syndrome; the patient also
carries a rare variant in FLRT3;
dbSNP:rs397515446).
{ECO:0000269|PubMed:23643382}.
/FTId=VAR_069957.
VARIANT 671 671 A -> P (in HH2).
{ECO:0000269|PubMed:19820032}.
/FTId=VAR_069294.
VARIANT 685 685 S -> F (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_031000.
VARIANT 687 687 G -> R (in HH2; dbSNP:rs727505376).
{ECO:0000269|PubMed:15845591,
ECO:0000269|PubMed:22927827}.
/FTId=VAR_031001.
VARIANT 692 692 E -> G (in HH2; phenotype consistent with
Kallmann syndrome; the patient also
carries a rare variant in DUSP6;
dbSNP:rs397515445).
{ECO:0000269|PubMed:23643382}.
/FTId=VAR_069958.
VARIANT 693 693 I -> F (in HH2).
{ECO:0000269|PubMed:17154279}.
/FTId=VAR_031002.
VARIANT 703 703 G -> R (in HH2).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_031003.
VARIANT 703 703 G -> S (in HH2; dbSNP:rs768957161).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_031004.
VARIANT 719 719 M -> R (in HH2).
{ECO:0000269|PubMed:12627230}.
/FTId=VAR_017891.
VARIANT 719 719 M -> V (in HH2; unknown pathological
significance).
{ECO:0000269|PubMed:26277103}.
/FTId=VAR_074014.
VARIANT 722 722 P -> H (in HH2; associated with K-724;
also found in a family member with
isolated anosmia; reduced tyrosine kinase
activity; dbSNP:rs267606805).
{ECO:0000269|PubMed:16606836,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_031005.
VARIANT 722 722 P -> S (in HH2; dbSNP:rs121909642).
{ECO:0000269|PubMed:16882753}.
/FTId=VAR_031006.
VARIANT 724 724 N -> K (in HH2; associated with H-722;
also found in a family member with
isolated anosmia; reduced tyrosine kinase
activity; dbSNP:rs267606806).
{ECO:0000269|PubMed:16606836,
ECO:0000269|PubMed:23643382}.
/FTId=VAR_031007.
VARIANT 725 725 C -> Y (in HRTFDS; dbSNP:rs398122945).
{ECO:0000269|PubMed:23812909}.
/FTId=VAR_070856.
VARIANT 745 745 P -> S (in HH2).
{ECO:0000269|PubMed:15001591,
ECO:0000269|PubMed:15845591}.
/FTId=VAR_031008.
VARIANT 768 768 D -> Y (in HH2; the patient also carries
a rare variant in FGF8;
dbSNP:rs121909644).
{ECO:0000269|PubMed:23643382}.
/FTId=VAR_069959.
VARIANT 769 769 L -> V (in dbSNP:rs2956723).
{ECO:0000269|PubMed:16764984}.
/FTId=VAR_031009.
VARIANT 772 772 P -> S (in HH2; with cleft palate,
unilateral absence of nasal cartilage,
iris coloboma; dbSNP:rs56234888).
{ECO:0000269|PubMed:12627230,
ECO:0000269|PubMed:17154279}.
/FTId=VAR_017892.
VARIANT 795 795 V -> I (in HH2; also found in a family
member with isolated anosmia;
dbSNP:rs781328162).
{ECO:0000269|PubMed:16882753}.
/FTId=VAR_031010.
VARIANT 818 818 G -> R (in dbSNP:rs17182456).
{ECO:0000269|Ref.13}.
/FTId=VAR_019291.
VARIANT 822 822 R -> C (in dbSNP:rs17182463).
{ECO:0000269|PubMed:17154279,
ECO:0000269|Ref.13}.
/FTId=VAR_019292.
MUTAGEN 514 514 K->A: Loss of kinase activity.
{ECO:0000269|PubMed:15117958}.
MUTAGEN 577 577 R->E: Strongly reduced
autophosphorylation in response to FGF
signaling. No effect on in vitro kinase
activity. {ECO:0000269|PubMed:20133753}.
MUTAGEN 609 609 R->V: Abolishes interaction with PLCG1.
MUTAGEN 623 623 D->A: Loss of kinase activity.
{ECO:0000269|PubMed:19224897}.
MUTAGEN 653 653 Y->F: No effect on kinase activity. Loss
of autophosphorylation and kinase
activity; when associated with F-654.
{ECO:0000269|PubMed:8622701}.
MUTAGEN 654 654 Y->F: Reduced kinase activity. Loss of
autophosphorylation and kinase activity;
when associated with F-653.
{ECO:0000269|PubMed:8622701}.
MUTAGEN 755 755 D->V: Abolishes interaction with PLCG1.
MUTAGEN 766 766 Y->F: Abolishes interaction with PLCG1
and SHB. Decreases phosphorylation of
FRS2, activation of RAS and MAP kinase
signaling and stimulation of cell
proliferation.
{ECO:0000269|PubMed:12181353,
ECO:0000269|PubMed:1379697,
ECO:0000269|PubMed:1379698,
ECO:0000269|PubMed:7516330}.
CONFLICT 24 24 S -> C (in Ref. 8; AAA35958/AAA35959).
{ECO:0000305}.
CONFLICT 192 192 K -> E (in Ref. 3; AAA35837).
{ECO:0000305}.
CONFLICT 194 194 G -> S (in Ref. 5; AAA35835).
{ECO:0000305}.
CONFLICT 196 196 E -> G (in Ref. 16; no nucleotide entry).
{ECO:0000305}.
CONFLICT 223 223 S -> F (in Ref. 12; BAD96438).
{ECO:0000305}.
CONFLICT 308 308 V -> A (in Ref. 8; AAA35958/AAA35959).
{ECO:0000305}.
CONFLICT 364 364 E -> Q (in Ref. 18; CAA68679).
{ECO:0000305}.
CONFLICT 469 469 P -> L (in Ref. 1; AAA75007).
{ECO:0000305}.
CONFLICT 482 482 K -> R (in Ref. 12; BAD96438).
{ECO:0000305}.
CONFLICT 576 576 R -> W (in Ref. 12; BAD96438).
{ECO:0000305}.
CONFLICT 817 817 G -> R (in Ref. 4; CAA36101).
{ECO:0000305}.
STRAND 40 42 {ECO:0000244|PDB:2CR3}.
STRAND 51 54 {ECO:0000244|PDB:2CR3}.
STRAND 63 72 {ECO:0000244|PDB:2CR3}.
STRAND 77 81 {ECO:0000244|PDB:2CR3}.
STRAND 83 88 {ECO:0000244|PDB:2CR3}.
TURN 93 95 {ECO:0000244|PDB:2CR3}.
STRAND 97 105 {ECO:0000244|PDB:2CR3}.
STRAND 108 116 {ECO:0000244|PDB:2CR3}.
STRAND 151 156 {ECO:0000244|PDB:1CVS}.
HELIX 158 161 {ECO:0000244|PDB:1CVS}.
STRAND 165 169 {ECO:0000244|PDB:1CVS}.
STRAND 174 177 {ECO:0000244|PDB:1CVS}.
STRAND 180 184 {ECO:0000244|PDB:1CVS}.
STRAND 187 192 {ECO:0000244|PDB:1CVS}.
HELIX 199 201 {ECO:0000244|PDB:1CVS}.
STRAND 207 209 {ECO:0000244|PDB:1CVS}.
TURN 210 213 {ECO:0000244|PDB:1CVS}.
STRAND 214 219 {ECO:0000244|PDB:1CVS}.
HELIX 222 224 {ECO:0000244|PDB:1CVS}.
STRAND 226 234 {ECO:0000244|PDB:1CVS}.
STRAND 237 248 {ECO:0000244|PDB:1CVS}.
STRAND 265 267 {ECO:0000244|PDB:1CVS}.
STRAND 273 276 {ECO:0000244|PDB:1CVS}.
STRAND 286 293 {ECO:0000244|PDB:1CVS}.
STRAND 295 297 {ECO:0000244|PDB:1CVS}.
STRAND 306 313 {ECO:0000244|PDB:1CVS}.
HELIX 320 323 {ECO:0000244|PDB:1CVS}.
STRAND 325 328 {ECO:0000244|PDB:1CVS}.
HELIX 333 335 {ECO:0000244|PDB:1CVS}.
STRAND 337 344 {ECO:0000244|PDB:1CVS}.
STRAND 349 358 {ECO:0000244|PDB:1CVS}.
HELIX 460 462 {ECO:0000244|PDB:4UWC}.
TURN 469 471 {ECO:0000244|PDB:5EW8}.
HELIX 475 477 {ECO:0000244|PDB:5EW8}.
STRAND 478 486 {ECO:0000244|PDB:5EW8}.
STRAND 488 499 {ECO:0000244|PDB:5EW8}.
STRAND 501 503 {ECO:0000244|PDB:5EW8}.
STRAND 508 516 {ECO:0000244|PDB:5EW8}.
HELIX 522 538 {ECO:0000244|PDB:5EW8}.
STRAND 547 551 {ECO:0000244|PDB:5EW8}.
STRAND 553 555 {ECO:0000244|PDB:5EW8}.
STRAND 558 562 {ECO:0000244|PDB:5EW8}.
HELIX 569 574 {ECO:0000244|PDB:5EW8}.
STRAND 579 583 {ECO:0000244|PDB:4RWI}.
STRAND 584 586 {ECO:0000244|PDB:5A4C}.
HELIX 591 593 {ECO:0000244|PDB:3KXX}.
HELIX 597 616 {ECO:0000244|PDB:5EW8}.
HELIX 626 628 {ECO:0000244|PDB:5EW8}.
STRAND 629 631 {ECO:0000244|PDB:5EW8}.
STRAND 637 639 {ECO:0000244|PDB:5EW8}.
STRAND 641 643 {ECO:0000244|PDB:3JS2}.
HELIX 648 650 {ECO:0000244|PDB:5EW8}.
STRAND 653 655 {ECO:0000244|PDB:4UWY}.
STRAND 658 660 {ECO:0000244|PDB:5AM7}.
HELIX 663 666 {ECO:0000244|PDB:5EW8}.
HELIX 669 674 {ECO:0000244|PDB:5EW8}.
STRAND 676 678 {ECO:0000244|PDB:3GQI}.
HELIX 679 694 {ECO:0000244|PDB:5EW8}.
HELIX 706 714 {ECO:0000244|PDB:5EW8}.
STRAND 722 724 {ECO:0000244|PDB:4RWL}.
HELIX 727 736 {ECO:0000244|PDB:5EW8}.
HELIX 741 743 {ECO:0000244|PDB:5EW8}.
HELIX 747 760 {ECO:0000244|PDB:5EW8}.
SEQUENCE 822 AA; 91868 MW; 93A01B5D78C3E72C CRC64;
MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD
VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD
ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS
SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN
HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI
GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE
ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK SGTKKSDFHS QMAVHKLAKS
IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL
GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK
HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL
VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG
RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD
KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQYSPSF
PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR


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E0074r ELISA Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Proto-oncogene c-Fgr,Rat,Rattus norvegicus 96T
E0074m ELISA Basic fibroblast growth factor receptor 1,bFGF-R-1,Fgfr1,FGFR-1,Fibroblast growth factor receptor 1,Flg,MFR,Mouse,Mus musculus,Proto-oncogene c-Fgr 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
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
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
201-11-0838 Rat basic fibroblast growth factor receptor(bFGFR)ELISA Kit 96T
UB-E10807 Rat basic fibroblast growth factor receptor(bFGFR)ELISA Kit 96T
QY-E10807 Rat basic fibroblast growth factor receptor(bFGFR)ELISA Kit 96T
E02F0006 Rat Basic Fibroblast growth factor receptor ELISA , bFGFR 96 Tests/kit
E02F0006 Rat Basic Fibroblast growth factor receptor ELISA , bFGFR
201-11-0838 Rat basic fibroblast growth factor receptor ,bFGFR ELISA Kit 96T
201-12-2094 Human basic fibroblast growth factor receptor ,bFGFR ELISA Kit 48T
UB-E02862 Human basic fibroblast growth factor receptor(bFGFR)ELISA Kit 96T
E2093Hu Human basic fibroblast growth factor receptor ,bFGFR ELISA Kit 48T
E08F0006 Canine Basic Fibroblast growth factor receptor ELISA , bFGFR
E03F0006 Mouse Basic Fibroblast growth factor receptor ELISA ,bFGFR 96 Tests/kit
E04F0006 Rabbit Basic Fibroblast growth factor receptor ELISA , bFGFR 96 Tests/kit
UB-E20184 Mouse basic fibroblast growth factor receptor(bFGFR)ELISA Kit 96T


 

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