[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Placenta; DOI=10.1093/nar/18.7.1906; PubMed=2159626 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Neonatal brain stem; PubMed=1697263 [NCBI, ExPASy, EBI, Israel, Japan] 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] (ISOFORM 1). PubMed=1317750 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12 AND 13). TISSUE=Liver; DOI=10.1126/science.1846977; PubMed=1846977 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14). PubMed=1662973 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[6]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 15). TISSUE=Placenta; DOI=10.1016/0006-291X(90)90384-Y; PubMed=2162671 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[7]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 15; 17 AND 18). PubMed=2167437 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[8]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 14; 15 AND 16). TISSUE=Lung; PubMed=1650441 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[9]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14). TISSUE=Teratocarcinoma; PubMed=1722683 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[10]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6 AND 14). TISSUE=Placenta, and Testis; DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[11]	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.
[12]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 14 AND 15), AND VARIANT GLY-213. TISSUE=Testis, and Uterus; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[13]	NUCLEOTIDE SEQUENCE [MRNA] OF 201-822. 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).
[14]	PARTIAL NUCLEOTIDE SEQUENCE [MRNA]. PubMed=1847500 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[15]	PROTEIN SEQUENCE OF 81-100. DOI=10.1006/bbrc.1994.2203; PubMed=8074689 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[16]	MUTAGENESIS OF TYR-766. DOI=10.1038/358678a0; PubMed=1379697 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[17]	MUTAGENESIS OF TYR-766. DOI=10.1038/358681a0; PubMed=1379698 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[18]	INTERACTION WITH FGF1, AND PHOSPHORYLATION. DOI=10.1038/31741; PubMed=9655399 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[19]	CHROMOSOMAL TRANSLOCATION WITH FGFR1OP. PubMed=9949182 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[20]	CHROMOSOMAL TRANSLOCATION WITH CEP110. PubMed=10688839 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[21]	INTERACTION WITH SHB, AND MUTAGENESIS OF TYR-766. DOI=10.1091/mbc.E02-02-0103; PubMed=12181353 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[22]	CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2. DOI=10.1002/gcc.20023; PubMed=15034873 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[23]	GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296, AND MASS SPECTROMETRY. TISSUE=Plasma; DOI=10.1021/pr0502065; PubMed=16335952 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[24]	CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2. DOI=10.1182/blood-2006-06-026666; PubMed=16946300 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[25]	CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2. DOI=10.1182/blood-2006-12-065615; PubMed=17389761 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[26]	PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-653, AND MASS SPECTROMETRY. DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan] Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; "Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer."; Cell 131:1190-1203(2007).
[27]	X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 464-762. DOI=10.1016/S0092-8674(00)80131-2; PubMed=8752212 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[28]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 464-762. DOI=10.1126/science.276.5314.955; PubMed=9139660 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[29]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 141-364 IN COMPLEX WITH FGF1. DOI=10.1016/S0092-8674(00)80851-X; PubMed=10830168 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[30]	X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 143-364 IN COMPLEX WITH FGF2 AND HEPARIN. DOI=10.1016/S1097-2765(00)00073-3; PubMed=11030354 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[31]	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.
[32]	VARIANT PS ARG-252. DOI=10.1038/ng1194-269; PubMed=7874169 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[33]	VARIANT NON-SYNDROMIC TRIGONOCEPHALY THR-300. PubMed=11173846 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[34]	VARIANTS KAL2 ASP-97; CYS-99; SER-167; TYR-277; MET-607; ARG-666; ARG-719 AND SER-772. DOI=10.1038/ng1122; PubMed=12627230 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[35]	VARIANT KAL2 SER-745. DOI=10.1210/jc.2003-030476; PubMed=15001591 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[36]	VARIANTS OGD ILE-330; CYS-374 AND ARG-381, AND CHARACTERIZATION OF VARIANT OGD CYS-374. DOI=10.1086/427956; PubMed=15625620 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[37]	VARIANTS KAL2 ILE-102; ALA-129; MET-273 AND THR-520. DOI=10.1002/humu.9298; PubMed=15605412 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[38]	VARIANTS KAL2 ARG-687 AND SER-745. DOI=10.1093/humrep/dei052; PubMed=15845591 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[39]	VARIANTS OGD ILE-330 AND ARG-381. DOI=10.1002/ajmg.a.31106; PubMed=16470795 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[40]	VARIANT IHH SER-48, VARIANT IHH/KAL2 LEU-366, AND VARIANTS KAL2 PRO-245; TRP-250; VAL-343; SER-722 AND ILE-795. DOI=10.1210/jc.2005-2793; PubMed=16882753 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[41]	VARIANTS KAL2 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. DOI=10.1016/j.mce.2006.04.021; PubMed=16764984 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[42]	VARIANTS KAL2 SER-178; GLY-622 AND GLN-622. DOI=10.1016/j.mce.2006.04.006; PubMed=16757108 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[43]	VARIANT IHH/KAL2 SER-237, VARIANTS IHH HIS-722 AND LYS-724, CHARACTERIZATION OF VARIANT IHH/KAL2 SER-237, AND CHARACTERIZATION OF VARIANTS IHH HIS-722 AND LYS-724. DOI=10.1073/pnas.0600962103; PubMed=16606836 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[44]	VARIANTS KAL2 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. DOI=10.1002/humu.9470; PubMed=17154279 [NCBI, ExPASy, EBI, Israel, Japan] 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).
[45]	VARIANTS [LARGE SCALE ANALYSIS] LEU-125; THR-252 AND LEU-664. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] 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).

Comments

FUNCTION: Receptor for basic fibroblast growth factor. A shorter form of the receptor could be a receptor for FGF1 (aFGF).
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
SUBUNIT: Interacts with SHB. Interacts with KLB (By similarity).
INTERACTION:
P12830:CDH1; NbExp=1; IntAct=EBI-1028277, EBI-727477;
P35222:CTNNB1; NbExp=1; IntAct=EBI-1028277, EBI-491549;
SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.

ALTERNATIVE PRODUCTS: 18 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	Alpha A1, IV
Isoform ID	P11362-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	Alpha A2
Isoform ID	P11362-8
Features which should be applied to build the isoform sequence: VSP_009842, VSP_009843.

Name	3
Synonyms	Alpha A3
Isoform ID	P11362-17
Features which should be applied to build the isoform sequence: VSP_009836, VSP_009837.

Name	4
Synonyms	Alpha B1
Isoform ID	P11362-2
Features which should be applied to build the isoform sequence: VSP_002960.

Name	5
Synonyms	Alpha B2
Isoform ID	P11362-9
Features which should be applied to build the isoform sequence: VSP_002960, VSP_009842, VSP_009843.

Name	6
Synonyms	Beta A1, II, H2
Isoform ID	P11362-3
Features which should be applied to build the isoform sequence: VSP_002958.

Name	7
Synonyms	Beta A2
Isoform ID	P11362-10
Features which should be applied to build the isoform sequence: VSP_002958, VSP_009842, VSP_009843.

Name	8
Synonyms	Beta B1
Isoform ID	P11362-4
Features which should be applied to build the isoform sequence: VSP_002958, VSP_002960.

Name	9
Synonyms	Beta B2
Isoform ID	P11362-11
Features which should be applied to build the isoform sequence: VSP_002958, VSP_002960, VSP_009842, VSP_009843.

Name	10
Synonyms	Gamma A1
Isoform ID	P11362-5
Features which should be applied to build the isoform sequence: VSP_002957.

Name	11
Synonyms	Gamma A2
Isoform ID	P11362-12
Features which should be applied to build the isoform sequence: VSP_002957, VSP_009842, VSP_009843.

Name	12
Synonyms	Gamma B1
Isoform ID	P11362-6
Features which should be applied to build the isoform sequence: VSP_002957, VSP_002960.

Name	13
Synonyms	Gamma B2
Isoform ID	P11362-13
Features which should be applied to build the isoform sequence: VSP_002957, VSP_002960, VSP_009842, VSP_009843.

Name	14
Synonyms	A, III
Isoform ID	P11362-7
Features which should be applied to build the isoform sequence: VSP_002959.

Name	15
Synonyms	I, H3
Isoform ID	P11362-14
Features which should be applied to build the isoform sequence: VSP_002958, VSP_002959.

Name	16
Synonyms	V
Isoform ID	P11362-15
Features which should be applied to build the isoform sequence: VSP_009838, VSP_009839.

Name	17
Synonyms	H4
Isoform ID	P11362-16
Features which should be applied to build the isoform sequence: VSP_002958, VSP_009840, VSP_009841.

Name	18
Synonyms	H5
Isoform ID	P11362-18
Features which should be applied to build the isoform sequence: VSP_002958, VSP_002959, VSP_009840, VSP_009841.

PTM: Binding of FGF1 and heparin promotes autophosphorylation on tyrosine residues and activation of the receptor.
DISEASE: Defects in FGFR1 are a cause of Pfeiffer syndrome (PS) [MIM:101600]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly.
DISEASE: Defects in FGFR1 are a cause of idiopathic hypogonadotropic hypogonadism (IHH) [MIM:146110]. IHH is defined as a deficiency of the pituitary secretion of follicle-stimulating hormone and luteinizing hormone, which results in the impairment of pubertal maturation and of reproductive function.
DISEASE: Defects in FGFR1 are the cause of Kallmann syndrome type 2 (KAL2) [MIM:147950]; also known as hypogonadotropic hypogonadism and anosmia. 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 some cases, midline cranial anomalies (cleft lip/palate and imperfect fusion) are present and anosmia may be absent or inconspicuous.
DISEASE: Defects in FGFR1 are the cause of osteoglophonic dysplasia (OGD) [MIM:166250]; also known as osteoglophonic dwarfism. OGD is characterized by craniosynostosis, prominent supraorbital ridge, and depressed nasal bridge, as well as by rhizomelic dwarfism and nonossifying bone lesions. Inheritance is autosomal dominant.
DISEASE: Defects in FGFR1 are the cause of non-syndromic trigonocephaly [MIM:190440]; also known as metopic craniosynostosis. The term trigonocephaly describes the typical keel-shaped deformation of the forehead resulting from premature fusion of the frontal suture. Trigonocephaly may occur also as a part of a syndrome.
DISEASE: 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.
DISEASE: 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.
DISEASE: A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with CEP110. 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 CEP110-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.
SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like) domains.
SIMILARITY: Contains 1 protein kinase domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/FGFR1113.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=FGFR1";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgfr1/";.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X51803; CAA36101.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X52833; CAA37015.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X66945; CAA47375.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63887; AAA35958.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63888; AAA35959.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M63889; AAA35960.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M60485; AAA35840.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M37722; AAA75007.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34185; AAA35836.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34186; AAA35837.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34187; AAA35838.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34188; AAA35839.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57118; CAA40400.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57119; CAA40401.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57120; CAA40402.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57121; CAA40403.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X57122; CAA40404.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M34641; AAA35835.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK291754; BAF84443.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AK292470; BAF85159.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AY585209; AAS79322.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC015035; AAH15035.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC018128; AAH18128.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC091494; AAH91494.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y00665; CAA68679.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
A29216; CAA01958.1; -; Unassigned_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00005142; -.
IPI00012036; -.
IPI00012039; -.
IPI00012042; -.
IPI00165947; -.
IPI00216859; -.
IPI00220983; -.
IPI00328245; -.
IPI00332838; -.
IPI00410124; -.
IPI00410125; -.
IPI00410216; -.
IPI00410217; -.
IPI00410218; -.
IPI00410219; -.
IPI00410220; -.
IPI00410223; -.
IPI00455176; -.

PIR

C36464; C36464.
C40862; C40862.
S11692; TVHUFG.
S19167; A40862.

RefSeq

NP_056934.2; -.
NP_075593.1; -.
NP_075594.1; -.
NP_075595.1; -.
NP_075596.1; -.
NP_075598.2; -.
NP_075599.1; -.

UniGene

Hs.264887

3D structure databases

PDB

1AGW; X-ray; 2.40 A; A/B=458-765.	[ExPASy / RCSB / EBI]
1CVS; X-ray; 2.80 A; C/D=141-365.	[ExPASy / RCSB / EBI]
1EVT; X-ray; 2.80 A; C/D=141-365.	[ExPASy / RCSB / EBI]
1FGI; X-ray; 2.50 A; A/B=458-765.	[ExPASy / RCSB / EBI]
1FGK; X-ray; 2.00 A; A/B=458-765.	[ExPASy / RCSB / EBI]
1FQ9; X-ray; 3.00 A; C/D=141-365.	[ExPASy / RCSB / EBI]
1XR0; NMR; -; A=409-430.	[ExPASy / RCSB / EBI]
2CR3; NMR; -; A=38-124.	[ExPASy / RCSB / EBI]
2FGI; X-ray; 2.50 A; A/B=458-765.	[ExPASy / RCSB / EBI]
3C4F; X-ray; 2.07 A; A/B=464-765.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1AGW; -.
1CVS; -.
1EVT; -.
1FGI; -.
1FGK; -.
1FQ9; -.
1XR0; -.
2CR3; -.
2FGI; -.
3C4F; -.

SMR

P11362; 25-119.

ModBase

P11362.

Protein-protein interaction databases

DIP

DIP:4019N; -.

IntAct

P11362; 5.

PTM databases

PhosphoSite

P11362; -.

Enzyme and pathway databases

BRENDA

2.7.10.1; 247.

Pathway_Interaction_DB

fgf_pathway; FGF signaling pathway.
glypican_1pathway; Glypican 1 network.
syndecan_4_pathway; Syndecan-4-mediated signaling events.

Reactome

REACT_9470; Signaling by FGFR.

Organism-specific databases

GC08M038389; -.

HIX0019616; -.

HGNC:3688; FGFR1.

101600; phenotype. [NCBI / EBI]
136350; gene. [NCBI / EBI]
146110; phenotype. [NCBI / EBI]
147950; phenotype. [NCBI / EBI]
166250; phenotype. [NCBI / EBI]
190440; phenotype. [NCBI / EBI]

Orphanet

432; Hypogonadism, hypogonadotropic, congenital, normosmic.
3366; Isolated trigonocephaly.
478; Kallmann syndrome.
2326; Kallmann syndrome - heart disease.
2645; Osteoglophonic dwarfism.
710; Pfeiffer syndrome.

PharmGKB

PA28127; -.

Gene expression databases

ArrayExpress

P11362; -.

Bgee

P11362; -.

CleanEx

HS_FGFR1; -.
HS_FLG; -.

GermOnline

ENSG00000077782; Homo sapiens.

Ontologies

GO:0005887;	Cellular component: integral to plasma membrane (traceable author statement from ProtInc).
GO:0005624;	Cellular component: membrane fraction (non-traceable author statement from UniProtKB).
GO:0005524;	Molecular function: ATP binding (non-traceable author statement from UniProtKB).
GO:0005007;	Molecular function: fibroblast growth factor receptor activity (traceable author statement from UniProtKB).
GO:0008201;	Molecular function: heparin binding (non-traceable author statement from UniProtKB).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0016049;	Biological process: cell growth (non-traceable author statement from UniProtKB).
GO:0008543;	Biological process: fibroblast growth factor receptor signaling pathway (non-traceable author statement from UniProtKB).
GO:0000165;	Biological process: MAPKKK cascade (traceable author statement from ProtInc).
GO:0006468;	Biological process: protein amino acid phosphorylation (non-traceable author statement from UniProtKB).
GO:0001501;	Biological process: skeletal system development (traceable author statement from ProtInc).
QuickGo view.

Family and domain databases

InterPro

IPR016248; Fibroblast_GF_rcpt.
IPR013151; Ig.
IPR007110; Ig-like.
IPR013783; Ig-like_fold.
IPR013098; Ig_I-set.
IPR003598; Ig_sub2.
IPR000719; Prot_kinase_core.
IPR017441; Protein_kinase_ATP_BS.
IPR001245; Tyr_pkinase.
IPR008266; Tyr_pkinase_AS.
Graphical view of domain structure.

Gene3D

G3DSA:2.60.40.10; Ig-like_fold; 3.

Pfam

PF07679; I-set; 2.
PF00047; ig; 1.
PF07714; Pkinase_Tyr; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000628; FGFR; 1.

PRINTS

PR00109; TYRKINASE.

ProDom

PD000001; Prot_kinase; 1.
[Domain structure / List of seq. sharing at least 1 domain]

SMART

SM00408; IGc2; 3.
SM00219; TyrKc; 1.
SMART graphical view of domain structure.

PROSITE

PS50835; IG_LIKE; 3.
PS00107; PROTEIN_KINASE_ATP; 1.
PS50011; PROTEIN_KINASE_DOM; 1.
PS00109; PROTEIN_KINASE_TYR; 1.
PROSITE graphical view of domain structure (profiles).

Proteomic databases

PRIDE

P11362; -.

Genome annotation databases

Ensembl

ENSG00000077782; Homo sapiens. [Contig view]

GeneID

2260; -.

KEGG

hsa:2260; -.

Phylogenomic databases

HOVERGEN

P11362; -.

OMA

P11362; LCTARPA.

Other

DB00039; Palifermin.

9163; -.

P11362; -.

FGFR1; Homo sapiens.

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

3D-structure; Alternative splicing; ATP-binding; Chromosomal rearrangement; Craniosynostosis; Direct protein sequencing; Disease mutation; Disulfide bond; Dwarfism; Glycoprotein; Heparin-binding; Hypogonadotropic hypogonadism; Immunoglobulin domain; Kallmann syndrome; Kinase; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Repeat; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`CHAIN`	`22 822`	`801`	`Basic fibroblast growth factor receptor 1.`	`PRO_0000016780`
`TOPO_DOM`	`22 376`	`355`	`Extracellular (Potential).`
`TRANSMEM`	`377 397`	`21`	`Potential.`
`TOPO_DOM`	`398 822`	`425`	`Cytoplasmic (Potential).`
`DOMAIN`	`25 119`	`95`	`Ig-like C2-type 1.`
`DOMAIN`	`158 246`	`89`	`Ig-like C2-type 2.`
`DOMAIN`	`255 357`	`103`	`Ig-like C2-type 3.`
`DOMAIN`	`478 767`	`290`	`Protein kinase.`
`NP_BIND`	`484 492`	`9`	`ATP (By similarity).`
`REGION`	`160 177`	`18`	`Heparin-binding.`
`ACT_SITE`	`623 623`		`Proton acceptor (By similarity).`
`BINDING`	`514 514`		`ATP (By similarity).`
`SITE`	`428 429`	`2`	`Breakpoint for translocation to form CEP110-FGFR1 OR FGFR1-CEP110 fusion proteins.`
`SITE`	`428 429`	`2`	`Breakpoint for translocation to form FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion proteins.`
`SITE`	`428 429`	`2`	`Breakpoint for translocation to form FGFR1OP2-FGFR1.`
`SITE`	`766 766`	`1`	`Mediates interaction with PLC-gamma and SHB.`
`MOD_RES`	`653 653`		`Phosphotyrosine.`
`MOD_RES`	`654 654`		`Phosphotyrosine; by autocatalysis (By similarity).`
`MOD_RES`	`766 766`		`Phosphotyrosine; by autocatalysis.`
`CARBOHYD`	`77 77`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`117 117`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`227 227`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`240 240`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`264 264`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`296 296`		`N-linked (GlcNAc...).`
`CARBOHYD`	`317 317`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`330 330`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`55 101`		`Potential.`
`DISULFID`	`178 230`		`Potential.`
`DISULFID`	`277 341`		`Potential.`
`VAR_SEQ`	`1 160`		`Missing (in isoform 10, isoform 11, isoform 12 and isoform 13).`	`VSP_002957`
`VAR_SEQ`	`31 119`		`Missing (in isoform 6, isoform 7, isoform 8, isoform 9, isoform 15, isoform 17 and isoform 18).`	`VSP_002958`
`VAR_SEQ`	`32 61`		`QPWGAPVEVESFLVHPGDLLQLRCRLRDDV -> CPDLQEAKSCSASFHSITPLPFGLGTRLSD (in isoform 3).`	`VSP_009836`
`VAR_SEQ`	`62 822`		`Missing (in isoform 3).`	`VSP_009837`
`VAR_SEQ`	`120 150`		`DALPSSEDDDDDDDSSSEEKETDNTKPNRMP -> ACPDLQEAKWCSASFHSITPLPFGLGTRLSD (in isoform 16).`	`VSP_009838`
`VAR_SEQ`	`148 149`		`Missing (in isoform 14, isoform 15 and isoform 18).`	`VSP_002959`
`VAR_SEQ`	`151 822`		`Missing (in isoform 16).`	`VSP_009839`
`VAR_SEQ`	`313 391`		`TAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHH` `SAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMV -> VIMAPVFVGQSTGKETTVSGAQVPVGRLSCPRMGSFLTLQ` `AHTLHLSRDLATSPRTSNRGHKVEVSWEQRAAGMGGAGL (in isoform 17 and isoform 18).`	`VSP_009840`
`VAR_SEQ`	`392 822`		`Missing (in isoform 17 and isoform 18).`	`VSP_009841`
`VAR_SEQ`	`428 429`		`Missing (in isoform 4, isoform 5, isoform 8, isoform 9, isoform 12 and isoform 13).`	`VSP_002960`
`VAR_SEQ`	`619 662`		`CIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKT` `TNGRL -> VWNLKAPLVHTPRPGSQECPGDRGQCDEDSRLWPRTGHS` `PHRLL (in isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13).`	`VSP_009842`
`VAR_SEQ`	`663 822`		`Missing (in isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13).`	`VSP_009843`
`VARIANT`	`22 22`	`1`	`R -> S (in dbSNP:rs17175750 [NCBI]).`	`VAR_019290`
`VARIANT`	`48 48`	`1`	`G -> S (in IHH).`	`VAR_030968`
`VARIANT`	`77 77`	`1`	`N -> K.`	`VAR_030969`
`VARIANT`	`78 78`	`1`	`R -> C (in KAL2).`	`VAR_030970`
`VARIANT`	`97 97`	`1`	`G -> D (in KAL2).`	`VAR_017885`
`VARIANT`	`99 99`	`1`	`Y -> C (in KAL2).`	`VAR_017886`
`VARIANT`	`101 101`	`1`	`C -> F (in KAL2).`	`VAR_030971`
`VARIANT`	`102 102`	`1`	`V -> I (in KAL2).`	`VAR_030972`
`VARIANT`	`125 125`	`1`	`S -> L (in a breast infiltrating ductal carcinoma sample; somatic mutation).`	`VAR_042201`
`VARIANT`	`129 129`	`1`	`D -> A (in KAL2).`	`VAR_030973`
`VARIANT`	`167 167`	`1`	`A -> S (in KAL2; with cleft palate, corpus callosum agenesis, unilateral deafness and fusion of fourth and fifth metacarpal bones).`	`VAR_017887`
`VARIANT`	`178 178`	`1`	`C -> S (in KAL2; with severe ear anomalies).`	`VAR_030974`
`VARIANT`	`213 213`	`1`	`W -> G (in dbSNP:rs17851623 [NCBI]).`	`VAR_030975`
`VARIANT`	`224 224`	`1`	`D -> H (in KAL2).`	`VAR_030976`
`VARIANT`	`237 237`	`1`	`G -> D (in KAL2).`	`VAR_030977`
`VARIANT`	`237 237`	`1`	`G -> S (in IHH/KAL2; also found in a family member with isolated anosmia; may impair proper folding).`	`VAR_030978`
`VARIANT`	`245 245`	`1`	`L -> P (in KAL2).`	`VAR_030979`
`VARIANT`	`250 250`	`1`	`R -> W (in KAL2).`	`VAR_030980`
`VARIANT`	`252 252`	`1`	`P -> R (in PS; seems to be a gain of function).`	`VAR_004111`
`VARIANT`	`252 252`	`1`	`P -> T (in a lung bronchoalveolar carcinoma sample; somatic mutation).`	`VAR_042202`
`VARIANT`	`254 254`	`1`	`R -> Q (in KAL2).`	`VAR_030981`
`VARIANT`	`270 270`	`1`	`G -> D (in KAL2).`	`VAR_030982`
`VARIANT`	`273 273`	`1`	`V -> M (in KAL2).`	`VAR_030983`
`VARIANT`	`274 274`	`1`	`E -> G (in KAL2; also found in a family member with isolated anosmia).`	`VAR_030984`
`VARIANT`	`277 277`	`1`	`C -> Y (in KAL2).`	`VAR_017888`
`VARIANT`	`283 283`	`1`	`P -> R (in KAL2).`	`VAR_030985`
`VARIANT`	`300 300`	`1`	`I -> T (in non-syndromic trigonocephaly).`	`VAR_030986`
`VARIANT`	`330 330`	`1`	`N -> I (in OGD).`	`VAR_030987`
`VARIANT`	`332 332`	`1`	`S -> C (in KAL2).`	`VAR_030988`
`VARIANT`	`339 339`	`1`	`Y -> C (in KAL2).`	`VAR_030989`
`VARIANT`	`343 343`	`1`	`A -> V (in KAL2).`	`VAR_030990`
`VARIANT`	`346 346`	`1`	`S -> C (in KAL2; also found in a family member with isolated anosmia).`	`VAR_030991`
`VARIANT`	`366 366`	`1`	`P -> L (in IHH/KAL2).`	`VAR_030992`
`VARIANT`	`374 374`	`1`	`Y -> C (in OGD; elevated basal activity and increased FGF2-mediated activity).`	`VAR_030993`
`VARIANT`	`381 381`	`1`	`C -> R (in OGD).`	`VAR_030994`
`VARIANT`	`520 520`	`1`	`A -> T (in KAL2).`	`VAR_030995 [3D]`
`VARIANT`	`538 538`	`1`	`I -> V (in KAL2).`	`VAR_030996 [3D]`
`VARIANT`	`607 607`	`1`	`V -> M (in KAL2; with bimanual synkinesis).`	`VAR_017889 [3D]`
`VARIANT`	`621 621`	`1`	`H -> R (in KAL2).`	`VAR_030997 [3D]`
`VARIANT`	`622 622`	`1`	`R -> G (in KAL2; with severe ear anomalies).`	`VAR_030998 [3D]`
`VARIANT`	`622 622`	`1`	`R -> Q (in KAL2).`	`VAR_030999 [3D]`
`VARIANT`	`664 664`	`1`	`V -> L (in a lung large cell carcinoma sample; somatic mutation).`	`VAR_042203 [3D]`
`VARIANT`	`666 666`	`1`	`W -> R (in KAL2; with cleft palate).`	`VAR_017890 [3D]`
`VARIANT`	`685 685`	`1`	`S -> F (in KAL2).`	`VAR_031000 [3D]`
`VARIANT`	`687 687`	`1`	`G -> R (in KAL2).`	`VAR_031001 [3D]`
`VARIANT`	`693 693`	`1`	`I -> F (in KAL2).`	`VAR_031002 [3D]`
`VARIANT`	`703 703`	`1`	`G -> R (in KAL2).`	`VAR_031003 [3D]`
`VARIANT`	`703 703`	`1`	`G -> S (in KAL2).`	`VAR_031004 [3D]`
`VARIANT`	`719 719`	`1`	`M -> R (in KAL2).`	`VAR_017891 [3D]`
`VARIANT`	`722 722`	`1`	`P -> H (in IHH; associated with K-724; also found in a family member with isolated anosmia; reduced tyrosine kinase activity).`	`VAR_031005 [3D]`
`VARIANT`	`722 722`	`1`	`P -> S (in KAL2).`	`VAR_031006 [3D]`
`VARIANT`	`724 724`	`1`	`N -> K (in IHH; associated with H-722; also found in a family member with isolated anosmia; reduced tyrosine kinase activity).`	`VAR_031007 [3D]`
`VARIANT`	`745 745`	`1`	`P -> S (in KAL2).`	`VAR_031008 [3D]`
`VARIANT`	`769 769`	`1`	`L -> V (in dbSNP:rs2956723 [NCBI]).`	`VAR_031009`
`VARIANT`	`772 772`	`1`	`P -> S (in KAL2; with cleft palate, unilateral absence of nasal cartilage, iris coloboma).`	`VAR_017892`
`VARIANT`	`795 795`	`1`	`V -> I (in KAL2; also found in a family member with isolated anosmia).`	`VAR_031010`
`VARIANT`	`818 818`	`1`	`G -> R (in dbSNP:rs17182456 [NCBI]).`	`VAR_019291`
`VARIANT`	`822 822`	`1`	`R -> C (in dbSNP:rs17182463 [NCBI]).`	`VAR_019292`
`MUTAGEN`	`766 766`		`Y->F: Fails to interact with PLC-gamma and SHB.`
`CONFLICT`	`24 24`		`S -> C (in Ref. 4; AAA35958/AAA35959).`
`CONFLICT`	`192 192`		`K -> E (in Ref. 8; AAA35837).`
`CONFLICT`	`194 194`		`G -> S (in Ref. 9; AAA35835).`
`CONFLICT`	`308 308`		`V -> A (in Ref. 4; AAA35958/AAA35959).`
`CONFLICT`	`364 364`		`E -> Q (in Ref. 13; CAA68679).`
`CONFLICT`	`469 469`		`P -> L (in Ref. 6; AAA75007).`
`CONFLICT`	`817 817`		`G -> R (in Ref. 1; CAA36101/CAA01958).`
`STRAND`	`151 156`	`6`
`HELIX`	`158 161`	`4`
`STRAND`	`165 169`	`5`
`STRAND`	`174 177`	`4`
`STRAND`	`180 184`	`5`
`STRAND`	`187 192`	`6`
`HELIX`	`199 201`	`3`
`STRAND`	`207 209`	`3`
`TURN`	`210 213`	`4`
`STRAND`	`214 219`	`6`
`HELIX`	`222 224`	`3`
`STRAND`	`226 234`	`9`
`STRAND`	`237 248`	`12`
`STRAND`	`265 267`	`3`
`STRAND`	`273 276`	`4`
`STRAND`	`286 293`	`8`
`STRAND`	`295 297`	`3`
`STRAND`	`306 313`	`8`
`HELIX`	`320 323`	`4`
`STRAND`	`325 328`	`4`
`HELIX`	`333 335`	`3`
`STRAND`	`337 344`	`8`
`STRAND`	`349 358`	`10`
`TURN`	`469 471`	`3`
`HELIX`	`475 477`	`3`
`STRAND`	`478 483`	`6`
`STRAND`	`492 498`	`7`
`STRAND`	`508 514`	`7`
`HELIX`	`522 538`	`17`
`STRAND`	`547 551`	`5`
`STRAND`	`553 556`	`4`
`STRAND`	`558 561`	`4`
`HELIX`	`569 574`	`6`
`HELIX`	`597 616`	`20`
`HELIX`	`626 628`	`3`
`STRAND`	`629 631`	`3`
`STRAND`	`637 639`	`3`
`HELIX`	`648 650`	`3`
`HELIX`	`663 666`	`4`
`HELIX`	`669 674`	`6`
`HELIX`	`679 693`	`15`
`TURN`	`694 696`	`3`
`HELIX`	`706 714`	`9`
`HELIX`	`727 736`	`10`
`HELIX`	`741 743`	`3`
`HELIX`	`747 760`	`14`

Sequence information

Length: 822 AA [This is the length of the unprocessed precursor]

Molecular weight: 91868 Da [This is the MW of the unprocessed precursor]

CRC64: 93A01B5D78C3E72C [This is a checksum on the sequence]

        10         20         30         40         50         60 
MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 

        70         80         90        100        110        120 
VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD 

       130        140        150        160        170        180 
ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS 

       190        200        210        220        230        240 
SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN 

       250        260        270        280        290        300 
HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI 

       310        320        330        340        350        360 
GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE 

       370        380        390        400        410        420 
ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK SGTKKSDFHS QMAVHKLAKS 

       430        440        450        460        470        480 
IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL 

       490        500        510        520        530        540 
GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK 

       550        560        570        580        590        600 
HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL 

       610        620        630        640        650        660 
VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG 

       670        680        690        700        710        720 
RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD 

       730        740        750        760        770        780 
KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQYSPSF 

       790        800        810        820 
PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR

P11362 in FASTA format

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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools