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Database: UniProt
Entry: P21802
LinkDB: P21802
Original site: P21802 
ID   FGFR2_HUMAN             Reviewed;         821 AA.
AC   P21802; B4DFC2; E7EVR6; E9PCR0; P18443; Q01742; Q12922; Q14300;
AC   Q14301; Q14302; Q14303; Q14304; Q14305; Q14672; Q14718; Q14719;
AC   Q1KHY5; Q86YI4; Q8IXC7; Q96KL9; Q96KM0; Q96KM1; Q96KM2; Q9NZU2;
AC   Q9NZU3; Q9UD01; Q9UD02; Q9UIH3; Q9UIH4; Q9UIH5; Q9UIH6; Q9UIH7;
AC   Q9UIH8; Q9UM87; Q9UMC6; Q9UNS7; Q9UQH7; Q9UQH8; Q9UQH9; Q9UQI0;
DT   01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1991, sequence version 1.
DT   01-OCT-2014, entry version 197.
DE   RecName: Full=Fibroblast growth factor receptor 2;
DE            Short=FGFR-2;
DE            EC=2.7.10.1;
DE   AltName: Full=K-sam;
DE            Short=KGFR;
DE   AltName: Full=Keratinocyte growth factor receptor;
DE   AltName: CD_antigen=CD332;
DE   Flags: Precursor;
GN   Name=FGFR2; Synonyms=BEK, KGFR, KSAM;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC   TISSUE=Neonatal brain stem;
RX   PubMed=1697263;
RA   Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G.,
RA   Ruta M., Burgess W.H., Jaye M., Schlessinger J.;
RT   "Cloning and expression of two distinct high-affinity receptors cross-
RT   reacting with acidic and basic fibroblast growth factors.";
RL   EMBO J. 9:2685-2692(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16).
RX   PubMed=2172978; DOI=10.1073/pnas.87.20.8180;
RA   Houssaint E., Blanquet P.R., Champion-Arnaud P., Gesnel M.-C.,
RA   Torriglia A., Courtois Y., Breathnach R.;
RT   "Related fibroblast growth factor receptor genes exist in the human
RT   genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:8180-8184(1990).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 17).
RX   PubMed=1647213; DOI=10.1016/0167-4781(91)90015-E;
RA   Seno M., Sasada R., Watanabe T., Ishimaru K., Igarashi K.;
RT   "Two cDNAs encoding novel human FGF receptor.";
RL   Biochim. Biophys. Acta 1089:244-246(1991).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RC   TISSUE=Stomach cancer;
RX   PubMed=2377625; DOI=10.1073/pnas.87.15.5983;
RA   Hattori Y., Odagiri H., Nakatani H., Miyagawa K., Naito K.,
RA   Sakamoto H., Katoh O., Yoshida T., Sugimura T., Terada M.;
RT   "K-sam, an amplified gene in stomach cancer, is a member of the
RT   heparin-binding growth factor receptor genes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 87:5983-5987(1990).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 14 AND 15).
RX   PubMed=1313574; DOI=10.1073/pnas.89.7.2960;
RA   Katoh M., Hattori Y., Sasaki H., Tanaka M., Sugano K., Yazaki Y.,
RA   Sugimura T., Terada M.;
RT   "K-sam gene encodes secreted as well as transmembrane receptor
RT   tyrosine kinase.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:2960-2964(1992).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), DOMAIN, AND SUBUNIT.
RC   TISSUE=Placenta;
RX   PubMed=1400433;
RA   Dell K.R., Williams L.T.;
RT   "A novel form of fibroblast growth factor receptor 2. Alternative
RT   splicing of the third immunoglobulin-like domain confers ligand
RT   binding specificity.";
RL   J. Biol. Chem. 267:21225-21229(1992).
RN   [7]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 19), SUBUNIT, DOMAIN, AND
RP   VARIANT ARG-613.
RC   TISSUE=Mammary gland;
RX   PubMed=1309608; DOI=10.1073/pnas.89.1.246;
RA   Miki T., Bottaro D.P., Fleming T.P., Smith C.L., Burgess W.H.,
RA   Chan A.M.-L., Aaronson S.A.;
RT   "Determination of ligand-binding specificity by alternative splicing:
RT   two distinct growth factor receptors encoded by a single gene.";
RL   Proc. Natl. Acad. Sci. U.S.A. 89:246-250(1992).
RN   [8]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19).
RC   TISSUE=Cornea, and Mammary gland;
RX   PubMed=7866434;
RA   Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M.,
RA   Shay J.W.;
RT   "Hepatocyte growth factor (HGF), keratinocyte growth factor (KGF), and
RT   their receptors in human breast cells and tissues: alternative
RT   receptors.";
RL   Cell. Mol. Biol. Res. 40:337-350(1994).
RN   [9]
RP   ERRATUM.
RA   Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M.,
RA   Shay J.W.;
RL   Cell. Mol. Biol. Res. 40:707-707(1994).
RN   [10]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CS SER-342.
RC   TISSUE=Blood;
RA   Steinberger D., Mueller U.;
RL   Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
RN   [11]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 9; 10; 11; 12 AND 13), AND
RP   VARIANT ARG-613.
RX   PubMed=10626794;
RA   Ueda T., Sasaki H., Kuwahara Y., Nezu M., Shibuya T., Sakamoto H.,
RA   Ishii H., Yanagihara K., Mafune K., Makuuchi M., Terada M.;
RT   "Deletion of the carboxyl-terminal exons of K-sam/FGFR2 by short
RT   homology-mediated recombination, generating preferential expression of
RT   specific messenger RNAs.";
RL   Cancer Res. 59:6080-6086(1999).
RN   [12]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 5; 6; 8; 14 AND 18).
RX   PubMed=11856867;
RA   Ingersoll R.G., Paznekas W.A., Tran A.K., Scott A.F., Jiang G.,
RA   Jabs E.W.;
RT   "Fibroblast growth factor receptor 2 (FGFR2): genomic sequence and
RT   variations.";
RL   Cytogenet. Cell Genet. 94:121-126(2001).
RN   [13]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
RA   Lind D.L., Cox D.R.;
RT   "Sequence and polymorphisms in fibroblast growth factor receptor 2
RT   (FGFR2) gene in humans.";
RL   Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN   [14]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 23).
RA   Jang J.;
RT   "Identification of a novel variant of FGFR2.";
RL   Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
RN   [15]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-6 AND THR-186.
RG   NIEHS SNPs program;
RL   Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
RN   [16]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 21).
RC   TISSUE=Cerebellum;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [17]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
RA   Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA   Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
RA   Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
RA   Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
RA   Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
RA   Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
RA   Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
RA   Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
RA   Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
RA   Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
RA   Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
RA   Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
RA   Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
RA   Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
RA   Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
RA   Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
RA   Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
RA   Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [18]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 20).
RC   TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [19]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-427.
RX   PubMed=10712195; DOI=10.1086/302831;
RA   Glaser R.L., Jiang W., Boyadjiev S.A., Tran A.K., Zachary A.A.,
RA   Van Maldergem L., Johnson D., Walsh S., Oldridge M., Wall S.A.,
RA   Wilkie A.O.M., Jabs E.W.;
RT   "Paternal origin of FGFR2 mutations in sporadic cases of Crouzon
RT   syndrome and Pfeiffer syndrome.";
RL   Am. J. Hum. Genet. 66:768-777(2000).
RN   [20]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209; 212-767 AND 771-821
RP   (ISOFORMS 5; 14 AND 18).
RX   PubMed=10196476; DOI=10.1016/S0378-1119(99)00047-5;
RA   Zhang Y., Gorry M.C., Post J.C., Ehrlich G.D.;
RT   "Genomic organization of the human fibroblast growth factor receptor 2
RT   (FGFR2) gene and comparative analysis of the human FGFR gene family.";
RL   Gene 230:69-79(1999).
RN   [21]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-313, AND VARIANTS APRS
RP   TRP-252 AND ARG-253.
RX   PubMed=7668257;
RA   Park W.-J., Theda C., Maestri N.E., Meyers G.A., Fryburg J.S.,
RA   Dufresne C., Cohen M.M. Jr., Jabs E.W.;
RT   "Analysis of phenotypic features and FGFR2 mutations in Apert
RT   syndrome.";
RL   Am. J. Hum. Genet. 57:321-328(1995).
RN   [22]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-259.
RX   PubMed=8676562;
RA   Wada C., Ishigaki M., Toyo-oka Y., Yamabe H., Ohnuki Y., Takada F.,
RA   Yamazaki Y., Ohtani H.;
RT   "Nucleotide sequences at intron 6 and exon 7 junction of fibroblast
RT   growth factor receptor 2 and rapid mutational analysis in Apert
RT   syndrome.";
RL   Rinsho Byori 44:435-438(1996).
RN   [23]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-318.
RX   PubMed=8673103; DOI=10.1038/ng0596-48;
RA   Moloney D.M., Slaney S.F., Oldridge M., Wall S.A., Sahlin P.,
RA   Stenman G., Wilkie A.O.M.;
RT   "Exclusive paternal origin of new mutations in Apert syndrome.";
RL   Nat. Genet. 13:48-53(1996).
RN   [24]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-361, AND VARIANTS CS PRO-289;
RP   ARG-338; SER-342; TYR-342; GLY-344 AND CYS-354.
RX   PubMed=7581378; DOI=10.1093/hmg/4.8.1387;
RA   Gorry M.C., Preston R.A., White G.J., Zhang Y., Singhal V.K.,
RA   Losken H.W., Parker M.G., Nwokoro N.A., Post J.C., Ehrlich G.D.;
RT   "Crouzon syndrome: mutations in two spliceoforms of FGFR2 and a common
RT   point mutation shared with Jackson-Weiss syndrome.";
RL   Hum. Mol. Genet. 4:1387-1390(1995).
RN   [25]
RP   FUNCTION (ISOFORM 3), SUBUNIT, AND DOMAIN.
RX   PubMed=8961926; DOI=10.1021/bi961942c;
RA   Gray T.E., Eisenstein M., Yayon A., Givol D.;
RT   "Asparagine-344 is a key residue for ligand binding in keratinocyte
RT   growth factor receptor.";
RL   Biochemistry 35:15640-15645(1996).
RN   [26]
RP   INTERACTION WITH FGF1; FGF2; FGF3; FGF4; FGF6; FGF7 AND FGF9, AND
RP   FUNCTION IN CELL PROLIFERATION.
RX   PubMed=8663044; DOI=10.1074/jbc.271.25.15292;
RA   Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A.,
RA   Coulier F., Gao G., Goldfarb M.;
RT   "Receptor specificity of the fibroblast growth factor family.";
RL   J. Biol. Chem. 271:15292-15297(1996).
RN   [27]
RP   FUNCTION IN PHOSPHORYLATION OF PAK4; REGULATION OF CELL PROLIFERATION
RP   AND APOPTOSIS, AND INTERACTION WITH GRB2 AND PAK4.
RX   PubMed=12529371; DOI=10.1074/jbc.M205875200;
RA   Lu Y., Pan Z.-Z., Devaux Y., Ray P.;
RT   "p21-activated protein kinase 4 (PAK4) interacts with the keratinocyte
RT   growth factor receptor and participates in keratinocyte growth factor-
RT   mediated inhibition of oxidant-induced cell death.";
RL   J. Biol. Chem. 278:10374-10380(2003).
RN   [28]
RP   FUNCTION IN OSTEOBLAST DIFFERENTIATION AND IN PHOSPHORYLATION OF CBL,
RP   INTERACTION WITH CBL, UBIQUITINATION, AND CHARACTERIZATION OF VARIANT
RP   APRS TRP-252.
RX   PubMed=15190072; DOI=10.1074/jbc.M402469200;
RA   Kaabeche K., Lemonnier J., Le Mee S., Caverzasio J., Marie P.J.;
RT   "Cbl-mediated degradation of Lyn and Fyn induced by constitutive
RT   fibroblast growth factor receptor-2 activation supports osteoblast
RT   differentiation.";
RL   J. Biol. Chem. 279:36259-36267(2004).
RN   [29]
RP   FUNCTION IN CELL PROLIFERATION AND ACTIVATION OF SIGNALING PATHWAYS,
RP   MUTAGENESIS OF TYR-769, PHOSPHORYLATION AT TYR-769, AND INTERACTION
RP   WITH PLCG1.
RX   PubMed=15629145; DOI=10.1016/j.bbrc.2004.12.031;
RA   Ceridono M., Belleudi F., Ceccarelli S., Torrisi M.R.;
RT   "Tyrosine 769 of the keratinocyte growth factor receptor is required
RT   for receptor signaling but not endocytosis.";
RL   Biochem. Biophys. Res. Commun. 327:523-532(2005).
RN   [30]
RP   INTERACTION WITH FGF1; FGF7; FGF8; FGF9; FGF10; FGF19; FGF21; FGF22
RP   AND FGF23, AND FUNCTION IN STIMULATION OF CELL PROLIFERATION.
RX   PubMed=16597617; DOI=10.1074/jbc.M601252200;
RA   Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M.,
RA   Ornitz D.M.;
RT   "Receptor specificity of the fibroblast growth factor family. The
RT   complete mammalian FGF family.";
RL   J. Biol. Chem. 281:15694-15700(2006).
RN   [31]
RP   FUNCTION IN PHOSPHORYLATION OF PLCG1 (ISOFORM 1), CATALYTIC ACTIVITY,
RP   AUTOPHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH PLCG1,
RP   SUBCELLULAR LOCATION, MUTAGENESIS OF ASN-265 AND 656-TYR-TYR-657,
RP   UBIQUITINATION, AND CHARACTERIZATION OF VARIANT PS PHE-278.
RX   PubMed=16844695; DOI=10.1074/jbc.M600448200;
RA   Hatch N.E., Hudson M., Seto M.L., Cunningham M.L., Bothwell M.;
RT   "Intracellular retention, degradation, and signaling of glycosylation-
RT   deficient FGFR2 and craniosynostosis syndrome-associated FGFR2C278F.";
RL   J. Biol. Chem. 281:27292-27305(2006).
RN   [32]
RP   INTERACTION WITH FGF19; FGF21 AND KLB, AND FUNCTION IN PHOSPHORYLATION
RP   OF FRS2 AND ACTIVATION OF MAP KINASES.
RX   PubMed=17623664; DOI=10.1074/jbc.M704165200;
RA   Kurosu H., Choi M., Ogawa Y., Dickson A.S., Goetz R.,
RA   Eliseenkova A.V., Mohammadi M., Rosenblatt K.P., Kliewer S.A.,
RA   Kuro-o M.;
RT   "Tissue-specific expression of betaKlotho and fibroblast growth factor
RT   (FGF) receptor isoforms determines metabolic activity of FGF19 and
RT   FGF21.";
RL   J. Biol. Chem. 282:26687-26695(2007).
RN   [33]
RP   FUNCTION IN STAT1 PHOSPHORYLATION, GLYCOSYLATION, SUBCELLULAR
RP   LOCATION, AND PHOSPHORYLATION.
RX   PubMed=17311277; DOI=10.1002/jcp.21014;
RA   Citores L., Bai L., Sorensen V., Olsnes S.;
RT   "Fibroblast growth factor receptor-induced phosphorylation of STAT1 at
RT   the Golgi apparatus without translocation to the nucleus.";
RL   J. Cell. Physiol. 212:148-156(2007).
RN   [34]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18374639; DOI=10.1016/j.bone.2008.02.009;
RA   Dufour C., Guenou H., Kaabeche K., Bouvard D., Sanjay A., Marie P.J.;
RT   "FGFR2-Cbl interaction in lipid rafts triggers attenuation of PI3K/Akt
RT   signaling and osteoblast survival.";
RL   Bone 42:1032-1039(2008).
RN   [35]
RP   FUNCTION AS FGF7 RECEPTOR AND IN PHOSPHORYLATION OF PLCG1 AND FRS2,
RP   CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-466; TYR-586; TYR-588;
RP   TYR-656 AND TYR-657, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=19410646; DOI=10.1016/j.cellsig.2009.04.004;
RA   Luo Y., Yang C., Jin C., Xie R., Wang F., McKeehan W.L.;
RT   "Novel phosphotyrosine targets of FGFR2IIIb signaling.";
RL   Cell. Signal. 21:1370-1378(2009).
RN   [36]
RP   FUNCTION IN FIBROBLAST PROLIFERATION; ACTIVATION OF MAP KINASES AND
RP   PHOSPHORYLATION OF PLCG1 AND FRS2, INTERACTION WITH PLCG1 AND FRS2,
RP   SUBCELLULAR LOCATION, AND MUTAGENESIS OF TYR-769.
RX   PubMed=19103595; DOI=10.1074/jbc.M803998200;
RA   Cha J.Y., Maddileti S., Mitin N., Harden T.K., Der C.J.;
RT   "Aberrant receptor internalization and enhanced FRS2-dependent
RT   signaling contribute to the transforming activity of the fibroblast
RT   growth factor receptor 2 IIIb C3 isoform.";
RL   J. Biol. Chem. 284:6227-6240(2009).
RN   [37]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA   Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA   Mann M., Daub H.;
RT   "Large-scale proteomics analysis of the human kinome.";
RL   Mol. Cell. Proteomics 8:1751-1764(2009).
RN   [38]
RP   FUNCTION, AND UBIQUITINATION.
RX   PubMed=21596750; DOI=10.1074/jbc.M110.197525;
RA   Severe N., Miraoui H., Marie P.J.;
RT   "The Casitas B lineage lymphoma (Cbl) mutant G306E enhances osteogenic
RT   differentiation in human mesenchymal stromal cells in part by
RT   decreased Cbl-mediated platelet-derived growth factor receptor alpha
RT   and fibroblast growth factor receptor 2 ubiquitination.";
RL   J. Biol. Chem. 286:24443-24450(2011).
RN   [39]
RP   REVIEW ON LIGAND SPECIFICITY, ALTERNATIVE SPLICING, AND SIGNALING.
RX   PubMed=15863030; DOI=10.1016/j.cytogfr.2005.01.001;
RA   Eswarakumar V.P., Lax I., Schlessinger J.;
RT   "Cellular signaling by fibroblast growth factor receptors.";
RL   Cytokine Growth Factor Rev. 16:139-149(2005).
RN   [40]
RP   REVIEW ON LIGAND SPECIFICITY, ALTERNATIVE SPLICING, SIGNALING, AND
RP   ROLE IN DISEASE.
RX   PubMed=19387476; DOI=10.1038/jid.2009.97;
RA   Katoh M.;
RT   "FGFR2 abnormalities underlie a spectrum of bone, skin, and cancer
RT   pathologies.";
RL   J. Invest. Dermatol. 129:1861-1867(2009).
RN   [41]
RP   REVIEW ON FUNCTION IN FGF SIGNALING.
RX   PubMed=20094046; DOI=10.1038/nrc2780;
RA   Turner N., Grose R.;
RT   "Fibroblast growth factor signalling: from development to cancer.";
RL   Nat. Rev. Cancer 10:116-129(2010).
RN   [42]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 147-366 IN COMPLEX WITH FGF2.
RX   PubMed=10830168; DOI=10.1016/S0092-8674(00)80851-X;
RA   Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.;
RT   "Crystal structures of two FGF-FGFR complexes reveal the determinants
RT   of ligand-receptor specificity.";
RL   Cell 101:413-424(2000).
RN   [43]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 148-366 IN COMPLEX WITH FGF1
RP   AND HEPARIN, AND INTERACTION WITH FGF1 AND HEPARIN.
RX   PubMed=11069186; DOI=10.1038/35039551;
RA   Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.;
RT   "Crystal structure of fibroblast growth factor receptor ectodomain
RT   bound to ligand and heparin.";
RL   Nature 407:1029-1034(2000).
RN   [44]
RP   X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 147-362 IN COMPLEX WITH FGF1.
RX   PubMed=10618369; DOI=10.1073/pnas.97.1.49;
RA   Stauber D.J., DiGabriele A.D., Hendrickson W.A.;
RT   "Structural interactions of fibroblast growth factor receptor with its
RT   ligands.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000).
RN   [45]
RP   X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-366 OF VARIANTS APRS
RP   TRP-252 AND ARG-253 IN COMPLEX WITH FGF2.
RX   PubMed=11390973; DOI=10.1073/pnas.121183798;
RA   Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M.,
RA   Mohammadi M.;
RT   "Structural basis for fibroblast growth factor receptor 2 activation
RT   in Apert syndrome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001).
RN   [46]
RP   X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-371 IN COMPLEX WITH
RP   FGF10.
RX   PubMed=12591959; DOI=10.1073/pnas.0436500100;
RA   Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I.,
RA   Ron D., Aaronson S.A., Mohammadi M.;
RT   "Structural basis by which alternative splicing confers specificity in
RT   fibroblast growth factor receptors.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003).
RN   [47]
RP   X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 149-368 IN COMPLEX WITH
RP   FGF8, FUNCTION AS FGF8 RECEPTOR, INTERACTION WITH FGF8, AND DISULFIDE
RP   BONDS.
RX   PubMed=16384934; DOI=10.1101/gad.1365406;
RA   Olsen S.K., Li J.Y.H., Bromleigh C., Eliseenkova A.V., Ibrahimi O.A.,
RA   Lao Z., Zhang F., Linhardt R.J., Joyner A.L., Mohammadi M.;
RT   "Structural basis by which alternative splicing modulates the
RT   organizer activity of FGF8 in the brain.";
RL   Genes Dev. 20:185-198(2006).
RN   [48]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP
RP   ANALOG; PEPTIDE SUBSTRATE AND MAGNESIUM, ENZYME REGULATION,
RP   PHOSPHORYLATION AT TYR-586; TYR-656 AND TYR-657, MUTAGENESIS OF
RP   ASN-549 AND GLU-565, CHARACTERIZATION OF VARIANT FSPC GLU-526,
RP   CHARACTERIZATION OF VARIANT CS HIS-549, CHARACTERIZATION OF VARIANTS
RP   PS GLY-565 AND ARG-641, AND CHARACTERIZATION OF VARIANT
RP   CRANIOSYNOSTOSIS ASN-659.
RX   PubMed=17803937; DOI=10.1016/j.molcel.2007.06.028;
RA   Chen H., Ma J., Li W., Eliseenkova A.V., Xu C., Neubert T.A.,
RA   Miller W.T., Mohammadi M.;
RT   "A molecular brake in the kinase hinge region regulates the activity
RT   of receptor tyrosine kinases.";
RL   Mol. Cell 27:717-730(2007).
RN   [49]
RP   X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-766 OF VARIANT LADDS
RP   THR-628 IN COMPLEX WITH ATP ANALOG, CATALYTIC ACTIVITY, SUBUNIT, AND
RP   AUTOPHOSPHORYLATION.
RX   PubMed=18056630; DOI=10.1073/pnas.0709905104;
RA   Lew E.D., Bae J.H., Rohmann E., Wollnik B., Schlessinger J.;
RT   "Structural basis for reduced FGFR2 activity in LADD syndrome:
RT   Implications for FGFR autoinhibition and activation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:19802-19807(2007).
RN   [50]
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP,
RP   ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, AUTOPHOSPHORYLATION,
RP   AND PHOSPHORYLATION AT TYR-466; TYR-586; TYR-588; TYR-656; TYR-657 AND
RP   TYR-769.
RX   PubMed=19060208; DOI=10.1073/pnas.0807752105;
RA   Chen H., Xu C.F., Ma J., Eliseenkova A.V., Li W., Pollock P.M.,
RA   Pitteloud N., Miller W.T., Neubert T.A., Mohammadi M.;
RT   "A crystallographic snapshot of tyrosine trans-phosphorylation in
RT   action.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:19660-19665(2008).
RN   [51]
RP   X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 458-768 IN COMPLEX WITH
RP   INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND ENZYME
RP   REGULATION.
RX   PubMed=21454610; DOI=10.1074/jbc.M110.213736;
RA   Eathiraj S., Palma R., Hirschi M., Volckova E., Nakuci E., Castro J.,
RA   Chen C.R., Chan T.C., France D.S., Ashwell M.A.;
RT   "A novel mode of protein kinase inhibition exploiting hydrophobic
RT   motifs of autoinhibited kinases: discovery of ATP-independent
RT   inhibitors of fibroblast growth factor receptor.";
RL   J. Biol. Chem. 286:20677-20687(2011).
RN   [52]
RP   VARIANTS CS HIS-340; ARG-342; SER-342; TYR-342 AND CYS-354.
RX   PubMed=7987400; DOI=10.1038/ng0994-98;
RA   Reardon W., Winter R.M., Rutland P., Pulleyn L.J., Jones B.M.,
RA   Malcolm S.;
RT   "Mutations in the fibroblast growth factor receptor 2 gene cause
RT   Crouzon syndrome.";
RL   Nat. Genet. 8:98-103(1994).
RN   [53]
RP   VARIANTS CS CYS-328 AND CYS-347, AND VARIANT JWS GLY-344.
RX   PubMed=7874170; DOI=10.1038/ng1194-275;
RA   Jabs E.W., Li X., Scott A.F., Meyers G.A., Chen W., Eccles M., Mao J.,
RA   Charnas L.R., Jackson C.E., Jaye M.;
RT   "Jackson-Weiss and Crouzon syndromes are allelic with mutations in
RT   fibroblast growth factor receptor 2.";
RL   Nat. Genet. 8:275-279(1994).
RN   [54]
RP   VARIANTS CS.
RX   PubMed=7655462; DOI=10.1093/hmg/4.6.1077;
RA   Oldridge M., Wilkie A.O.M., Slaney S.F., Poole M.D., Pulleyn L.J.,
RA   Rutland P., Hockley A.D., Wake M.J.C., Goldin J.H., Winter R.M.,
RA   Reardon W., Malcolm S.;
RT   "Mutations in the third immunoglobulin domain of the fibroblast growth
RT   factor receptor-2 gene in Crouzon syndrome.";
RL   Hum. Mol. Genet. 4:1077-1082(1995).
RN   [55]
RP   VARIANTS CS GLY-290; TRP-342 AND CYS-354, AND VARIANT JWS ARG-342.
RX   PubMed=8528214; DOI=10.1093/hmg/4.7.1229;
RA   Park W.-J., Meyers G.A., Li X., Theda C., Day D., Orlow S.J.,
RA   Jones M.C., Jabs E.W.;
RT   "Novel FGFR2 mutations in Crouzon and Jackson-Weiss syndromes show
RT   allelic heterogeneity and phenotypic variability.";
RL   Hum. Mol. Genet. 4:1229-1233(1995).
RN   [56]
RP   VARIANT PS ALA-321.
RX   PubMed=7719333; DOI=10.1038/ng0295-108;
RA   Lajeunie E., Wei M.H., Bonaventure J., Munnich A., le Merrer M.,
RA   Renier D.;
RT   "FGFR2 mutations in Pfeiffer syndrome.";
RL   Nat. Genet. 9:108-108(1995).
RN   [57]
RP   VARIANTS APRS TRP-252 AND ARG-253.
RX   PubMed=7719344; DOI=10.1038/ng0295-165;
RA   Wilkie A.O.M., Slaney S.F., Oldridge M., Poole M.D., Ashworth G.J.,
RA   Hockley A.D., Hayward R.D., David D.J., Pulleyn L.J., Rutland P.,
RA   Malcolm S., Winter R.M., Reardon W.;
RT   "Apert syndrome results from localized mutations of FGFR2 and is
RT   allelic with Crouzon syndrome.";
RL   Nat. Genet. 9:165-172(1995).
RN   [58]
RP   VARIANTS PS PRO-341; ARG-342 AND TYR-342.
RX   PubMed=7719345; DOI=10.1038/ng0295-173;
RA   Rutland P., Pulleyn L.J., Reardon W., Baraister M., Hayward R.,
RA   Jones B.M., Malcolm S., Winter R.M., Oldridge M., Slaney S.F.,
RA   Poole M.D., Wilkie A.O.M.;
RT   "Identical mutations in the FGFR2 gene cause both Pfeiffer and Crouzon
RT   syndrome phenotypes.";
RL   Nat. Genet. 9:173-176(1995).
RN   [59]
RP   VARIANTS CS GLY-268 INS; PHE-342 AND TYR-342, VARIANTS PS PHE-278;
RP   ARG-342; SER-342; PRO-344 AND PHE-359, AND VARIANT JWS PRO-289.
RX   PubMed=8644708;
RA   Meyers G.A., Day D., Goldberg R., Daentl D.L., Przylepa K.A.,
RA   Abrams L.J., Graham J.M. Jr., Feingold M., Moeschler J.B.,
RA   Rawnsley E., Scott A.F., Jabs E.W.;
RT   "FGFR2 exon IIIa and IIIc mutations in Crouzon, Jackson-Weiss, and
RT   Pfeiffer syndromes: evidence for missense changes, insertions, and a
RT   deletion due to alternative RNA splicing.";
RL   Am. J. Hum. Genet. 58:491-498(1996).
RN   [60]
RP   VARIANTS CS CYS-105; GLU-338; CYS-351 AND ARG-384.
RX   PubMed=8946174;
RA   Pulleyn L.J., Reardon W., Wilkes D., Rutland P., Jones B.M.,
RA   Hayward R., Hall C.M., Brueton L., Chun N., Lammer E., Malcolm S.,
RA   Winter R.M.;
RT   "Spectrum of craniosynostosis phenotypes associated with novel
RT   mutations at the fibroblast growth factor receptor 2 locus.";
RL   Eur. J. Hum. Genet. 4:283-291(1996).
RN   [61]
RP   VARIANTS CS ILE-331; ASN-ALA-337 INS AND 356-TRP--THR-358 DEL.
RX   PubMed=8956050;
RX   DOI=10.1002/(SICI)1098-1004(1996)8:4<386::AID-HUMU18>3.3.CO;2-A;
RA   Steinberger D., Mulliken J.B., Mueller U.;
RT   "Crouzon syndrome: previously unrecognized deletion, duplication, and
RT   point mutation within FGFR2 gene.";
RL   Hum. Mutat. 8:386-390(1996).
RN   [62]
RP   VARIANTS BSTVS CYS-372 AND CYS-375.
RX   PubMed=8696350; DOI=10.1038/ng0896-492;
RA   Przylepa K.A., Paznekas W.A., Zhang M., Golabi M., Bias W.,
RA   Bamshad M.J., Carey J.C., Hall B.D., Stevenson R., Orlow S.J.,
RA   Cohen M.M. Jr., Jabs E.W.;
RT   "Fibroblast growth factor receptor 2 mutations in Beare-Stevenson
RT   cutis gyrata syndrome.";
RL   Nat. Genet. 13:492-494(1996).
RN   [63]
RP   VARIANT PS CYS-290.
RX   PubMed=9150725; DOI=10.1007/s004390050413;
RA   Tartaglia M., Valeri S., Velardi F., di Rocco C., Battaglia P.A.;
RT   "Trp290Cys mutation in exon IIIa of the fibroblast growth factor
RT   receptor 2 (FGFR2) gene is associated with Pfeiffer syndrome.";
RL   Hum. Genet. 99:602-606(1997).
RN   [64]
RP   VARIANT JWS SER-342.
RX   PubMed=9385368; DOI=10.1007/s004390050584;
RA   Tartaglia M., Di Rocco C., Lajeunie E., Valeri S., Velardi F.,
RA   Battaglia P.A.;
RT   "Jackson-Weiss syndrome: identification of two novel FGFR2 missense
RT   mutations shared with Crouzon and Pfeiffer craniosynostotic
RT   disorders.";
RL   Hum. Genet. 101:47-50(1997).
RN   [65]
RP   VARIANT CS LEU-252, VARIANT APRS PHE-252, AND VARIANT PS
RP   252-PHE-SER-253.
RX   PubMed=9002682; DOI=10.1093/hmg/6.1.137;
RA   Oldridge M., Lunt P.W., Zackai E.H., McDonald-Mcginn D.M., Muenke M.,
RA   Moloney D.M., Twigg S.R.F., Heath J.K., Howard T.D., Hoganson G.,
RA   Gagnon D.M., Jabs E.W., Wilkie A.O.M.;
RT   "Genotype-phenotype correlation for nucleotide substitutions in the
RT   IgII-IgIII linker of FGFR2.";
RL   Hum. Mol. Genet. 6:137-143(1997).
RN   [66]
RP   VARIANT CS GLU-292.
RX   PubMed=9152842; DOI=10.1136/jmg.34.5.420;
RA   Steinberger D., Collmann H., Schmalenberger B., Mueller U.;
RT   "A novel mutation (a886g) in exon 5 of FGFR2 in members of a family
RT   with Crouzon phenotype and plagiocephaly.";
RL   J. Med. Genet. 34:420-422(1997).
RN   [67]
RP   VARIANTS CS PHE-278; PRO-337; ARG-338; ARG-342; PHE-342 AND TYR-342,
RP   VARIANTS APRS TRP-252 AND ARG-253, AND VARIANT JWS PHE-278.
RX   PubMed=9677057;
RX   DOI=10.1002/(SICI)1096-8628(19980707)78:3<237::AID-AJMG5>3.3.CO;2-5;
RA   Passos-Bueno M.R., Sertie A.L., Richieri-Costa A., Alonso L.G.,
RA   Zatz M., Alonso N., Brunoni D., Ribeiro S.F.M.;
RT   "Description of a new mutation and characterization of FGFR1, FGFR2,
RT   and FGFR3 mutations among Brazilian patients with syndromic
RT   craniosynostoses.";
RL   Am. J. Med. Genet. 78:237-241(1998).
RN   [68]
RP   VARIANTS CS VAL-276 AND CYS-301, AND VARIANT CRANIOSYNOSTOSIS SER-314.
RX   PubMed=9521581; DOI=10.1007/s004390050668;
RA   Steinberger D., Vriend G., Mulliken J.B., Mueller U.;
RT   "The mutations in FGFR2-associated craniosynostoses are clustered in
RT   five structural elements of immunoglobulin-like domain III of the
RT   receptor.";
RL   Hum. Genet. 102:145-150(1998).
RN   [69]
RP   VARIANTS APRS TRP-252 AND ARG-253.
RX   PubMed=9452027;
RA   Tsai F.-J., Hwu W.-L., Lin S.-P., Chang J.-G., Wang T.-R., Tsai C.-H.;
RT   "Two common mutations 934C to G and 937C to G of fibroblast growth
RT   factor receptor 2 (FGFR2) gene in Chinese patients with Apert
RT   syndrome.";
RL   Hum. Mutat. Suppl. 1:S18-S19(1998).
RN   [70]
RP   VARIANT PS CYS-351.
RX   PubMed=9693549;
RA   Mathijssen I.M., Vaandrager J.M., Hoogeboom A.J.,
RA   Hesseling-Janssen A.L.W., van den Ouweland A.M.W.;
RT   "Pfeiffer's syndrome resulting from an S351C mutation in the
RT   fibroblast growth factor receptor-2 gene.";
RL   J. Craniofac. Surg. 9:207-209(1998).
RN   [71]
RP   VARIANT PS TRP-252.
RX   PubMed=9719378; DOI=10.1136/jmg.35.8.677;
RA   Passos-Bueno M.R., Richieri-Costa A., Sertie A.L., Kneppers A.;
RT   "Presence of the Apert canonical S252W FGFR2 mutation in a patient
RT   without severe syndactyly.";
RL   J. Med. Genet. 35:677-679(1998).
RN   [72]
RP   VARIANT CS SER-362.
RX   PubMed=10574673; DOI=10.1597/1545-1569(1999)036<0533:ANFGMI>2.3.CO;2;
RA   Everett E.T., Britto D.A., Ward R.E., Hartsfield J.K. Jr.;
RT   "A novel FGFR2 gene mutation in Crouzon syndrome associated with
RT   apparent nonpenetrance.";
RL   Cleft Palate Craniofac. J. 36:533-541(1999).
RN   [73]
RP   VARIANTS PS CYS-340 AND GLY-342.
RX   PubMed=10394936; DOI=10.1007/s004390050979;
RA   Cornejo-Roldan L.R., Roessler E., Muenke M.;
RT   "Analysis of the mutational spectrum of the FGFR2 gene in Pfeiffer
RT   syndrome.";
RL   Hum. Genet. 104:425-431(1999).
RN   [74]
RP   VARIANT PS ASP-273 DEL.
RX   PubMed=10945669; DOI=10.1034/j.1399-0004.2000.580116.x;
RA   Priolo M., Lerone M., Baffico M., Baldi M., Ravazzolo R., Cama A.,
RA   Capra V., Silengo M.;
RT   "Pfeiffer syndrome type 2 associated with a single amino acid deletion
RT   in the FGFR2 gene.";
RL   Clin. Genet. 58:81-83(2000).
RN   [75]
RP   VARIANTS CS/PS ARG-342 AND TYR-342, VARIANTS CS LEU-263; VAL-276;
RP   PHE-278; TYR-278; SER-288; PRO-289; PRO-341; TRP-342; CYS-354; TYR-354
RP   AND PHE-359, AND VARIANT PS SER-342.
RX   PubMed=11173845;
RA   Kress W., Collmann H., Buesse M., Halliger-Keller B., Mueller C.R.;
RT   "Clustering of FGFR2 gene mutations in patients with Pfeiffer and
RT   Crouzon syndromes (FGFR2-associated craniosynostoses).";
RL   Cytogenet. Cell Genet. 91:134-137(2000).
RN   [76]
RP   VARIANT SER-315.
RX   PubMed=10951518; DOI=10.1038/sj.ejhg.5200499;
RA   Johnson D., Wall S.A., Mann S., Wilkie A.O.M.;
RT   "A novel mutation, Ala315Ser, in FGFR2: a gene-environment interaction
RT   leading to craniosynostosis?";
RL   Eur. J. Hum. Genet. 8:571-577(2000).
RN   [77]
RP   VARIANTS ABS2 ARG-342; SER-342 AND CYS-351.
RX   PubMed=10633130; DOI=10.1136/jmg.37.1.26;
RA   Reardon W., Smith A., Honour J.W., Hindmarsh P., Das D., Rumsby G.,
RA   Nelson I., Malcolm S., Ades L., Sillence D., Kumar D.,
RA   DeLozier-Blanchet C., McKee S., Kelly T., McKeehan W.L., Baraitser M.,
RA   Winter R.M.;
RT   "Evidence for digenic inheritance in some cases of Antley-Bixler
RT   syndrome?";
RL   J. Med. Genet. 37:26-32(2000).
RN   [78]
RP   VARIANTS CS CYS-281; PRO-289; ARG-342 AND TYR-342.
RX   PubMed=11380921; DOI=10.1046/j.1442-200x.2001.01392.x;
RA   Tsai F.-J., Yang C.-F., Wu J.-Y., Tsai C.-H., Lee C.-C.;
RT   "Mutation analysis of Crouzon syndrome and identification of one novel
RT   mutation in Taiwanese patients.";
RL   Pediatr. Int. 43:263-266(2001).
RN   [79]
RP   VARIANTS CS CYS-105; PRO-267; VAL-276; CYS-281; PRO-289; ARG-338;
RP   HIS-340; PHE-342; TRP-342; CYS-347; CYS-354; HIS-549 AND GLY-678,
RP   VARIANTS PS PHE-172; 252-PHE-SER-253; CYS-290; CYS-340; PRO-341;
RP   ARG-342; SER-342; CYS-375; GLY-565; ARG-641 AND GLU-663, VARIANTS APRS
RP   TRP-252 AND ARG-253, VARIANTS CS/PS PHE-278 AND TYR-342, VARIANT
RP   CRANIOSYNOSTOSIS ASN-659, AND VARIANTS THR-186 AND SER-315.
RX   PubMed=11781872; DOI=10.1086/338758;
RA   Kan S.-H., Elanko N., Johnson D., Cornejo-Roldan L.R., Cook J.,
RA   Reich E.W., Tomkins S., Verloes A., Twigg S.R.F., Rannan-Eliya S.,
RA   McDonald-McGinn D.M., Zackai E.H., Wall S.A., Muenke M.,
RA   Wilkie A.O.M.;
RT   "Genomic screening of fibroblast growth-factor receptor 2 reveals a
RT   wide spectrum of mutations in patients with syndromic
RT   craniosynostosis.";
RL   Am. J. Hum. Genet. 70:472-486(2002).
RN   [80]
RP   VARIANT BSTVS CYS-375.
RX   PubMed=12000365; DOI=10.1034/j.1399-0004.2002.610309.x;
RA   Wang T.-J., Huang C.-B., Tsai F.-J., Wu J.-Y., Lai R.-B., Hsiao M.;
RT   "Mutation in the FGFR2 gene in a Taiwanese patient with Beare-
RT   Stevenson cutis gyrata syndrome.";
RL   Clin. Genet. 61:218-221(2002).
RN   [81]
RP   VARIANT FSPC GLU-526.
RX   PubMed=16061565; DOI=10.1136/jmg.2004.027888;
RA   McGillivray G., Savarirayan R., Cox T.C., Stojkoski C., McNeil R.,
RA   Bankier A., Bateman J.F., Roscioli T., Gardner R.J.M., Lamande S.R.;
RT   "Familial scaphocephaly syndrome caused by a novel mutation in the
RT   FGFR2 tyrosine kinase domain.";
RL   J. Med. Genet. 42:656-662(2005).
RN   [82]
RP   VARIANTS LADDS THR-628; THR-648 AND 649-ARG-ASP-650 DELINS SER.
RX   PubMed=16501574; DOI=10.1038/ng1757;
RA   Rohmann E., Brunner H.G., Kayserili H., Uyguner O., Nuernberg G.,
RA   Lew E.D., Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M.,
RA   Leroy J.G., Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J.,
RA   Yueksel-Apak M., Nuernberg P., Kubisch C., Schlessinger J.,
RA   van Bokhoven H., Wollnik B.;
RT   "Mutations in different components of FGF signaling in LADD
RT   syndrome.";
RL   Nat. Genet. 38:414-417(2006).
RN   [83]
RP   VARIANT [LARGE SCALE ANALYSIS] CYS-203.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
RN   [84]
RP   VARIANTS [LARGE SCALE ANALYSIS] LEU-57; THR-186; CYS-203; VAL-272;
RP   ASN-283; CYS-290 AND THR-612.
RX   PubMed=17344846; DOI=10.1038/nature05610;
RA   Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C.,
RA   Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S.,
RA   O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S.,
RA   Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E.,
RA   Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J.,
RA   Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K.,
RA   Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T.,
RA   West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P.,
RA   Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E.,
RA   DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E.,
RA   Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T.,
RA   Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.;
RT   "Patterns of somatic mutation in human cancer genomes.";
RL   Nature 446:153-158(2007).
RN   [85]
RP   VARIANTS BBDS ASP-381 AND ARG-391, AND CHARACTERIZATION OF VARIANT
RP   BBDS ARG-391.
RX   PubMed=22387015; DOI=10.1016/j.ajhg.2012.02.005;
RA   Merrill A.E., Sarukhanov A., Krejci P., Idoni B., Camacho N.,
RA   Estrada K.D., Lyons K.M., Deixler H., Robinson H., Chitayat D.,
RA   Curry C.J., Lachman R.S., Wilcox W.R., Krakow D.;
RT   "Bent bone dysplasia-FGFR2 type, a distinct skeletal disorder, has
RT   deficient canonical FGF signaling.";
RL   Am. J. Hum. Genet. 90:550-557(2012).
CC   -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface
CC       receptor for fibroblast growth factors and plays an essential role
CC       in the regulation of cell proliferation, differentiation,
CC       migration and apoptosis, and in the regulation of embryonic
CC       development. Required for normal embryonic patterning, trophoblast
CC       function, limb bud development, lung morphogenesis, osteogenesis
CC       and skin development. Plays an essential role in the regulation of
CC       osteoblast differentiation, proliferation and apoptosis, and is
CC       required for normal skeleton development. Promotes cell
CC       proliferation in keratinocytes and immature osteoblasts, but
CC       promotes apoptosis in differentiated osteoblasts. Phosphorylates
CC       PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of
CC       several signaling cascades. Activation of PLCG1 leads to the
CC       production of the cellular signaling molecules diacylglycerol and
CC       inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers
CC       recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates
CC       activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase
CC       signaling pathway, as well as of the AKT1 signaling pathway. FGFR2
CC       signaling is down-regulated by ubiquitination, internalization and
CC       degradation. Mutations that lead to constitutive kinase activation
CC       or impair normal FGFR2 maturation, internalization and degradation
CC       lead to aberrant signaling. Over-expressed FGFR2 promotes
CC       activation of STAT1. {ECO:0000269|PubMed:12529371,
CC       ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:15629145,
CC       ECO:0000269|PubMed:16384934, ECO:0000269|PubMed:16597617,
CC       ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664,
CC       ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19103595,
CC       ECO:0000269|PubMed:19387476, ECO:0000269|PubMed:19410646,
CC       ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:8663044}.
CC   -!- CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a
CC       [protein]-L-tyrosine phosphate. {ECO:0000255|PROSITE-
CC       ProRule:PRU10028, ECO:0000269|PubMed:16844695,
CC       ECO:0000269|PubMed:18056630, ECO:0000269|PubMed:19410646,
CC       ECO:0000269|PubMed:21454610}.
CC   -!- ENZYME REGULATION: Present in an inactive conformation in the
CC       absence of bound ligand. Ligand binding leads to dimerization and
CC       activation by autophosphorylation on tyrosine residues. Inhibited
CC       by ARQ 523 and ARQ 069; these compounds maintain the kinase in an
CC       inactive conformation and inhibit autophosphorylation.
CC       {ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:21454610}.
CC   -!- SUBUNIT: Monomer. Homodimer after ligand binding. Interacts
CC       predominantly with FGF1 and FGF2, but can also interact with FGF3,
CC       FGF4, FGF6, FGF7, FGF8, FGF9, FGF10, FGF17, FGF18 and FGF22 (in
CC       vitro). Ligand specificity is determined by tissue-specific
CC       expression of isoforms, and differences in the third Ig-like
CC       domain are crucial for ligand specificity. Isoform 1 has high
CC       affinity for FGF1 and FGF2, but low affinity for FGF7. Isoform 3
CC       has high affinity for FGF1 and FGF7, and has much higher affinity
CC       for FGF7 than isoform 1 (in vitro). Affinity for fibroblast growth
CC       factors (FGFs) is increased by heparan sulfate glycosaminoglycans
CC       that function as coreceptors. Likewise, KLB increases the affinity
CC       for FGF19 and FGF21. Interacts with PLCG1, GRB2 and PAK4.
CC       {ECO:0000269|PubMed:10618369, ECO:0000269|PubMed:10830168,
CC       ECO:0000269|PubMed:11069186, ECO:0000269|PubMed:11390973,
CC       ECO:0000269|PubMed:12529371, ECO:0000269|PubMed:12591959,
CC       ECO:0000269|PubMed:1309608, ECO:0000269|PubMed:1400433,
CC       ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:15629145,
CC       ECO:0000269|PubMed:16384934, ECO:0000269|PubMed:16597617,
CC       ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:17623664,
CC       ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:18056630,
CC       ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19103595,
CC       ECO:0000269|PubMed:21454610, ECO:0000269|PubMed:8663044,
CC       ECO:0000269|PubMed:8961926}.
CC   -!- INTERACTION:
CC       P03968:FGF1 (xeno); NbExp=2; IntAct=EBI-6354683, EBI-6358090;
CC       P05230:FGF1; NbExp=3; IntAct=EBI-1028658, EBI-698068;
CC       O15520:FGF10; NbExp=2; IntAct=EBI-1028658, EBI-1035684;
CC       P09038:FGF2; NbExp=3; IntAct=EBI-1028658, EBI-977447;
CC       P21781:FGF7; NbExp=2; IntAct=EBI-6354683, EBI-3937699;
CC       P62993:GRB2; NbExp=5; IntAct=EBI-1028658, EBI-401755;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein. Golgi apparatus. Cytoplasmic vesicle. Note=Detected on
CC       osteoblast plasma membrane lipid rafts. After ligand binding, the
CC       activated receptor is rapidly internalized and degraded.
CC   -!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane; Single-pass type I
CC       membrane protein. Note=After ligand binding, the activated
CC       receptor is rapidly internalized and degraded.
CC   -!- SUBCELLULAR LOCATION: Isoform 3: Cell membrane; Single-pass type I
CC       membrane protein. Note=After ligand binding, the activated
CC       receptor is rapidly internalized and degraded.
CC   -!- SUBCELLULAR LOCATION: Isoform 14: Secreted.
CC   -!- SUBCELLULAR LOCATION: Isoform 19: Secreted.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=23;
CC       Name=1; Synonyms=BEK, FGFR2IIIc;
CC         IsoId=P21802-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=P21802-2; Sequence=VSP_002978;
CC       Name=3; Synonyms=BFR-1, FGFR2IIIb, KGFR;
CC         IsoId=P21802-3; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                  VSP_002972;
CC       Name=4; Synonyms=K-sam;
CC         IsoId=P21802-4; Sequence=VSP_002964, VSP_002969, VSP_002970,
CC                                  VSP_002971, VSP_002972, VSP_002975,
CC                                  VSP_002976;
CC       Name=5; Synonyms=K-sam-I, BEK, IgIIIc;
CC         IsoId=P21802-5; Sequence=VSP_002975;
CC       Name=6; Synonyms=K-sam-IIC2;
CC         IsoId=P21802-6; Sequence=VSP_002975, VSP_002984;
CC       Name=7; Synonyms=K-sam-IIO2;
CC         IsoId=P21802-7; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                  VSP_002972, VSP_002979;
CC       Name=8; Synonyms=K-sam-IIC3;
CC         IsoId=P21802-8; Sequence=VSP_002975, VSP_002978;
CC       Name=9; Synonyms=K-sam-IIH1;
CC         IsoId=P21802-9; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                  VSP_002972, VSP_002980;
CC       Name=10; Synonyms=K-sam-IIH2;
CC         IsoId=P21802-10; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002981;
CC       Name=11; Synonyms=K-sam-IIH3, K-sam-IIO4;
CC         IsoId=P21802-11; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002982;
CC       Name=12; Synonyms=K-sam-IIO1;
CC         IsoId=P21802-12; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002983;
CC       Name=13; Synonyms=K-sam-IIO3;
CC         IsoId=P21802-13; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002977;
CC       Name=14; Synonyms=K-sam-IV, Soluble KGFR;
CC         IsoId=P21802-14; Sequence=VSP_002965, VSP_002966;
CC       Name=15; Synonyms=K-sam-III;
CC         IsoId=P21802-15; Sequence=VSP_002968;
CC       Name=16; Synonyms=TK14;
CC         IsoId=P21802-16; Sequence=VSP_002967, VSP_002975;
CC         Note=Ref.2 (AAA61188) sequence is in conflict in position:
CC         315:T->L. {ECO:0000305};
CC       Name=17;
CC         IsoId=P21802-17; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002978;
CC       Name=18; Synonyms=K-sam-IIC1, KGFR, IgIIIb;
CC         IsoId=P21802-18; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002975;
CC       Name=19; Synonyms=Soluble KGFR;
CC         IsoId=P21802-19; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC                                   VSP_002972, VSP_002973, VSP_002974;
CC       Name=20;
CC         IsoId=P21802-20; Sequence=VSP_019608, VSP_019609;
CC       Name=21;
CC         IsoId=P21802-21; Sequence=VSP_002964, VSP_041915;
CC       Name=22;
CC         IsoId=P21802-22; Sequence=VSP_002964, VSP_002969, VSP_002970,
CC                                   VSP_002971, VSP_002972, VSP_002978;
CC       Name=23;
CC         IsoId=P21802-23; Sequence=VSP_041914;
CC   -!- DOMAIN: The second and third Ig-like domains directly interact
CC       with fibroblast growth factors (FGF) and heparan sulfate
CC       proteoglycans. Alternative splicing events affecting the third Ig-
CC       like domain are crucial for ligand selectivity.
CC       {ECO:0000269|PubMed:1309608, ECO:0000269|PubMed:1400433,
CC       ECO:0000269|PubMed:8961926}.
CC   -!- PTM: Autophosphorylated. Binding of FGF family members together
CC       with heparan sulfate proteoglycan or heparin promotes receptor
CC       dimerization and autophosphorylation on several tyrosine residues.
CC       Autophosphorylation occurs in trans between the two FGFR molecules
CC       present in the dimer. Phosphorylation at Tyr-769 is essential for
CC       interaction with PLCG1. {ECO:0000269|PubMed:15629145,
CC       ECO:0000269|PubMed:19060208}.
CC   -!- PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan
CC       chains undergo further maturation to an Endo H-resistant form in
CC       the Golgi apparatus. {ECO:0000269|PubMed:16844695,
CC       ECO:0000269|PubMed:17311277}.
CC   -!- PTM: Ubiquitinated. FGFR2 is rapidly ubiquitinated after
CC       autophosphorylation, leading to internalization and degradation.
CC       Subject to degradation both in lysosomes and by the proteasome.
CC       {ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:16844695,
CC       ECO:0000269|PubMed:21596750}.
CC   -!- DISEASE: Crouzon syndrome (CS) [MIM:123500]: An autosomal dominant
CC       syndrome characterized by craniosynostosis, hypertelorism,
CC       exophthalmos and external strabismus, parrot-beaked nose, short
CC       upper lip, hypoplastic maxilla, and a relative mandibular
CC       prognathism. {ECO:0000269|PubMed:10574673,
CC       ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11380921,
CC       ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7581378,
CC       ECO:0000269|PubMed:7655462, ECO:0000269|PubMed:7874170,
CC       ECO:0000269|PubMed:7987400, ECO:0000269|PubMed:8528214,
CC       ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:8946174,
CC       ECO:0000269|PubMed:8956050, ECO:0000269|PubMed:9002682,
CC       ECO:0000269|PubMed:9152842, ECO:0000269|PubMed:9521581,
CC       ECO:0000269|PubMed:9677057, ECO:0000269|Ref.10}. Note=The disease
CC       is caused by mutations affecting the gene represented in this
CC       entry.
CC   -!- DISEASE: Jackson-Weiss syndrome (JWS) [MIM:123150]: An autosomal
CC       dominant craniosynostosis syndrome characterized by craniofacial
CC       abnormalities and abnormality of the feet: broad great toes with
CC       medial deviation and tarsal-metatarsal coalescence.
CC       {ECO:0000269|PubMed:7874170, ECO:0000269|PubMed:8528214,
CC       ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9385368,
CC       ECO:0000269|PubMed:9677057}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Apert syndrome (APRS) [MIM:101200]: A syndrome
CC       characterized by facio-cranio-synostosis, osseous and membranous
CC       syndactyly of the four extremities, and midface hypoplasia. The
CC       craniosynostosis is bicoronal and results in acrocephaly of
CC       brachysphenocephalic type. Syndactyly of the fingers and toes may
CC       be total (mitten hands and sock feet) or partial affecting the
CC       second, third, and fourth digits. Intellectual deficit is frequent
CC       and often severe, usually being associated with cerebral
CC       malformations. {ECO:0000269|PubMed:11781872,
CC       ECO:0000269|PubMed:7668257, ECO:0000269|PubMed:7719344,
CC       ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9452027,
CC       ECO:0000269|PubMed:9677057}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Pfeiffer syndrome (PS) [MIM:101600]: A syndrome
CC       characterized by the association of craniosynostosis, broad and
CC       deviated thumbs and big toes, and partial syndactyly of the
CC       fingers and toes. Three subtypes are known: mild autosomal
CC       dominant form (type 1); cloverleaf skull, elbow ankylosis, early
CC       death, sporadic (type 2); craniosynostosis, early demise, sporadic
CC       (type 3). {ECO:0000269|PubMed:10394936,
CC       ECO:0000269|PubMed:10945669, ECO:0000269|PubMed:11173845,
CC       ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7719333,
CC       ECO:0000269|PubMed:7719345, ECO:0000269|PubMed:8644708,
CC       ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9150725,
CC       ECO:0000269|PubMed:9693549, ECO:0000269|PubMed:9719378}. Note=The
CC       disease is caused by mutations affecting the gene represented in
CC       this entry.
CC   -!- DISEASE: Beare-Stevenson cutis gyrata syndrome (BSTVS)
CC       [MIM:123790]: An autosomal dominant disease characterized by
CC       craniofacial anomalies, particularly craniosynostosis, and ear
CC       defects, cutis gyrata, acanthosis nigricans, anogenital anomalies,
CC       skin tags, and prominent umbilical stump. The skin furrows have a
CC       corrugated appearance and are widespread. Cutis gyrata variably
CC       affects the scalp, forehead, face, preauricular area, neck, trunk,
CC       hands, and feet. {ECO:0000269|PubMed:12000365,
CC       ECO:0000269|PubMed:8696350}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Familial scaphocephaly syndrome (FSPC) [MIM:609579]: An
CC       autosomal dominant craniosynostosis syndrome characterized by
CC       scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion,
CC       and mild intellectual disability. Scaphocephaly is the most common
CC       of the craniosynostosis conditions and is characterized by a long,
CC       narrow head. It is due to premature fusion of the sagittal suture
CC       or from external deformation. {ECO:0000269|PubMed:16061565}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Lacrimo-auriculo-dento-digital syndrome (LADDS)
CC       [MIM:149730]: An autosomal dominant ectodermal dysplasia, a
CC       heterogeneous group of disorders due to abnormal development of
CC       two or more ectodermal structures. Lacrimo-auriculo-dento-digital
CC       syndrome is characterized by aplastic/hypoplastic lacrimal and
CC       salivary glands and ducts, cup-shaped ears, hearing loss,
CC       hypodontia and enamel hypoplasia, and distal limb segments
CC       anomalies. In addition to these cardinal features, facial
CC       dysmorphism, malformations of the kidney and respiratory system
CC       and abnormal genitalia have been reported. Craniosynostosis and
CC       severe syndactyly are not observed. {ECO:0000269|PubMed:16501574}.
CC       Note=The disease is caused by mutations affecting the gene
CC       represented in this entry.
CC   -!- DISEASE: Antley-Bixler syndrome, without genital anomalies or
CC       disordered steroidogenesis (ABS2) [MIM:207410]: A rare syndrome
CC       characterized by craniosynostosis, radiohumeral synostosis present
CC       from the perinatal period, midface hypoplasia, choanal stenosis or
CC       atresia, femoral bowing and multiple joint contractures.
CC       Arachnodactyly and/or camptodactyly have also been reported.
CC       {ECO:0000269|PubMed:10633130}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- DISEASE: Bent bone dysplasia syndrome (BBDS) [MIM:614592]: A
CC       perinatal lethal skeletal dysplasia characterized by poor
CC       mineralization of the calvarium, craniosynostosis, dysmorphic
CC       facial features, prenatal teeth, hypoplastic pubis and clavicles,
CC       osteopenia, and bent long bones. Dysmorphic facial features
CC       included low-set ears, hypertelorism, midface hypoplasia,
CC       prematurely erupted fetal teeth, and micrognathia.
CC       {ECO:0000269|PubMed:22387015}. Note=The disease is caused by
CC       mutations affecting the gene represented in this entry.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein
CC       kinase family. Fibroblast growth factor receptor subfamily.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like)
CC       domains. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 protein kinase domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00159}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAG57383.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
CC       and Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/FGFR2ID40570ch10q26.html";
CC   -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC       URL="http://egp.gs.washington.edu/data/fgfr2/";
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DR   EMBL; X52832; CAA37014.1; -; mRNA.
DR   EMBL; M55614; AAA61188.1; -; mRNA.
DR   EMBL; X56191; CAA39654.1; -; mRNA.
DR   EMBL; M35718; AAA36152.1; -; mRNA.
DR   EMBL; M87770; AAA59470.1; -; mRNA.
DR   EMBL; M87771; AAA59471.1; -; mRNA.
DR   EMBL; M87772; AAA59472.1; -; mRNA.
DR   EMBL; M97193; AAA52449.1; -; mRNA.
DR   EMBL; U11814; AAA68514.1; -; mRNA.
DR   EMBL; M80634; AAA36147.1; -; mRNA.
DR   EMBL; Z71929; CAA96492.1; -; mRNA.
DR   EMBL; AB030073; BAA89296.1; -; mRNA.
DR   EMBL; AB030074; BAA89297.1; -; mRNA.
DR   EMBL; AB030075; BAA89298.1; -; mRNA.
DR   EMBL; AB030076; BAA89299.1; -; mRNA.
DR   EMBL; AB030077; BAA89300.1; -; mRNA.
DR   EMBL; AB030078; BAA89301.1; -; mRNA.
DR   EMBL; AF360695; AAK94205.1; -; Genomic_DNA.
DR   EMBL; AF410480; AAK94205.1; JOINED; Genomic_DNA.
DR   EMBL; AF360695; AAK94206.1; -; Genomic_DNA.
DR   EMBL; AF410480; AAK94206.1; JOINED; Genomic_DNA.
DR   EMBL; AF360695; AAK94207.1; -; Genomic_DNA.
DR   EMBL; AF410480; AAK94207.1; JOINED; Genomic_DNA.
DR   EMBL; AF360695; AAK94208.1; -; Genomic_DNA.
DR   EMBL; AF410480; AAK94208.1; JOINED; Genomic_DNA.
DR   EMBL; AF360695; AAK94209.1; -; Genomic_DNA.
DR   EMBL; AF410480; AAK94209.1; JOINED; Genomic_DNA.
DR   EMBL; AF487553; AAM74056.1; -; Genomic_DNA.
DR   EMBL; AB084153; BAC45037.1; -; mRNA.
DR   EMBL; DQ493927; ABE96832.1; -; Genomic_DNA.
DR   EMBL; AK294026; BAG57383.1; ALT_INIT; mRNA.
DR   EMBL; AC009988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC039243; AAH39243.2; -; mRNA.
DR   EMBL; AF169399; AAF43273.1; -; Genomic_DNA.
DR   EMBL; AF169399; AAF43274.1; -; Genomic_DNA.
DR   EMBL; AF097353; AAD31560.1; -; Genomic_DNA.
DR   EMBL; AF097341; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097342; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097343; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097345; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097346; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097347; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097348; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097349; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097350; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097351; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097352; AAD31560.1; JOINED; Genomic_DNA.
DR   EMBL; AF097353; AAD31561.1; -; Genomic_DNA.
DR   EMBL; AF097341; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097342; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097344; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097345; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097346; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097347; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097348; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097349; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097350; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097351; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097352; AAD31561.1; JOINED; Genomic_DNA.
DR   EMBL; AF097340; AAD31562.1; -; Genomic_DNA.
DR   EMBL; AF097337; AAD31562.1; JOINED; Genomic_DNA.
DR   EMBL; AF097338; AAD31562.1; JOINED; Genomic_DNA.
DR   EMBL; AF097339; AAD31562.1; JOINED; Genomic_DNA.
DR   EMBL; AF097354; AAD31565.1; -; Genomic_DNA.
DR   EMBL; AF097341; AAD31567.1; -; Genomic_DNA.
DR   EMBL; S82438; AAD14392.1; -; Genomic_DNA.
DR   EMBL; Y17131; CAA76643.1; -; Genomic_DNA.
DR   EMBL; L49237; AAC41933.1; -; Genomic_DNA.
DR   EMBL; L49242; AAC41934.1; -; Genomic_DNA.
DR   EMBL; L49238; AAC41935.1; -; Genomic_DNA.
DR   EMBL; L49239; AAC41936.1; -; Genomic_DNA.
DR   EMBL; L49240; AAC41937.1; -; Genomic_DNA.
DR   EMBL; L49241; AAC41938.1; -; Genomic_DNA.
DR   CCDS; CCDS31298.1; -. [P21802-1]
DR   CCDS; CCDS44485.1; -. [P21802-20]
DR   CCDS; CCDS44486.1; -. [P21802-23]
DR   CCDS; CCDS44487.1; -. [P21802-15]
DR   CCDS; CCDS44488.1; -. [P21802-22]
DR   CCDS; CCDS44489.1; -. [P21802-17]
DR   CCDS; CCDS53584.1; -. [P21802-21]
DR   CCDS; CCDS7620.2; -. [P21802-3]
DR   PIR; A35969; A35969.
DR   PIR; A42691; TVHUF2.
DR   PIR; A45081; A45081.
DR   PIR; C42691; C42691.
DR   PIR; S16236; S16236.
DR   RefSeq; NP_000132.3; NM_000141.4. [P21802-1]
DR   RefSeq; NP_001138385.1; NM_001144913.1. [P21802-17]
DR   RefSeq; NP_001138386.1; NM_001144914.1. [P21802-23]
DR   RefSeq; NP_001138387.1; NM_001144915.1. [P21802-21]
DR   RefSeq; NP_001138388.1; NM_001144916.1.
DR   RefSeq; NP_001138389.1; NM_001144917.1. [P21802-15]
DR   RefSeq; NP_001138390.1; NM_001144918.1. [P21802-20]
DR   RefSeq; NP_001138391.1; NM_001144919.1. [P21802-22]
DR   RefSeq; NP_075259.4; NM_022970.3. [P21802-3]
DR   RefSeq; NP_075418.1; NM_023029.2.
DR   UniGene; Hs.533683; -.
DR   PDB; 1DJS; X-ray; 2.40 A; A=32-362.
DR   PDB; 1E0O; X-ray; 2.80 A; B/D=148-366.
DR   PDB; 1EV2; X-ray; 2.20 A; E/F/G/H=147-366.
DR   PDB; 1GJO; X-ray; 2.40 A; A=456-768.
DR   PDB; 1II4; X-ray; 2.70 A; E/F/G/H=147-366.
DR   PDB; 1IIL; X-ray; 2.30 A; E/F/G/H=147-366.
DR   PDB; 1NUN; X-ray; 2.90 A; B=140-368.
DR   PDB; 1OEC; X-ray; 2.40 A; A=456-768.
DR   PDB; 1WVZ; NMR; -; A=147-249.
DR   PDB; 2FDB; X-ray; 2.28 A; P/R=149-368.
DR   PDB; 2PSQ; X-ray; 2.40 A; A/B=413-768.
DR   PDB; 2PVF; X-ray; 1.80 A; A=458-778, B=764-778.
DR   PDB; 2PVY; X-ray; 2.20 A; A/B/C/D=458-768.
DR   PDB; 2PWL; X-ray; 2.40 A; A/B=458-768.
DR   PDB; 2PY3; X-ray; 2.30 A; A/B=458-768.
DR   PDB; 2PZ5; X-ray; 2.40 A; A/B=458-768.
DR   PDB; 2PZP; X-ray; 2.40 A; A/B=458-768.
DR   PDB; 2PZR; X-ray; 3.00 A; A/B=458-768.
DR   PDB; 2Q0B; X-ray; 2.90 A; A/B=458-768.
DR   PDB; 3B2T; X-ray; 1.80 A; A/B=458-766.
DR   PDB; 3CAF; X-ray; 1.96 A; A=150-249.
DR   PDB; 3CLY; X-ray; 2.00 A; A=458-778.
DR   PDB; 3CU1; X-ray; 2.60 A; A/C=150-249.
DR   PDB; 3DAR; X-ray; 2.20 A; A/B=146-249.
DR   PDB; 3EUU; X-ray; 2.34 A; A/B=150-249.
DR   PDB; 3OJ2; X-ray; 2.20 A; C/D=140-313.
DR   PDB; 3OJM; X-ray; 2.10 A; B=140-313.
DR   PDB; 3RI1; X-ray; 2.10 A; A/B=458-768.
DR   PDB; 4J23; X-ray; 3.88 A; A=147-366.
DR   PDB; 4J95; X-ray; 2.38 A; A/B/C/D=458-768.
DR   PDB; 4J96; X-ray; 2.30 A; A/B=458-768.
DR   PDB; 4J97; X-ray; 2.55 A; A/B/C/D=458-768.
DR   PDB; 4J98; X-ray; 2.31 A; A/B=458-768.
DR   PDB; 4J99; X-ray; 1.85 A; A/B/C/D=458-768.
DR   PDBsum; 1DJS; -.
DR   PDBsum; 1E0O; -.
DR   PDBsum; 1EV2; -.
DR   PDBsum; 1GJO; -.
DR   PDBsum; 1II4; -.
DR   PDBsum; 1IIL; -.
DR   PDBsum; 1NUN; -.
DR   PDBsum; 1OEC; -.
DR   PDBsum; 1WVZ; -.
DR   PDBsum; 2FDB; -.
DR   PDBsum; 2PSQ; -.
DR   PDBsum; 2PVF; -.
DR   PDBsum; 2PVY; -.
DR   PDBsum; 2PWL; -.
DR   PDBsum; 2PY3; -.
DR   PDBsum; 2PZ5; -.
DR   PDBsum; 2PZP; -.
DR   PDBsum; 2PZR; -.
DR   PDBsum; 2Q0B; -.
DR   PDBsum; 3B2T; -.
DR   PDBsum; 3CAF; -.
DR   PDBsum; 3CLY; -.
DR   PDBsum; 3CU1; -.
DR   PDBsum; 3DAR; -.
DR   PDBsum; 3EUU; -.
DR   PDBsum; 3OJ2; -.
DR   PDBsum; 3OJM; -.
DR   PDBsum; 3RI1; -.
DR   PDBsum; 4J23; -.
DR   PDBsum; 4J95; -.
DR   PDBsum; 4J96; -.
DR   PDBsum; 4J97; -.
DR   PDBsum; 4J98; -.
DR   PDBsum; 4J99; -.
DR   ProteinModelPortal; P21802; -.
DR   SMR; P21802; 5-364, 462-801.
DR   BioGrid; 108554; 19.
DR   DIP; DIP-3788N; -.
DR   IntAct; P21802; 16.
DR   MINT; MINT-118359; -.
DR   BindingDB; P21802; -.
DR   ChEMBL; CHEMBL4142; -.
DR   DrugBank; DB00039; Palifermin.
DR   GuidetoPHARMACOLOGY; 1809; -.
DR   MEROPS; I43.001; -.
DR   PhosphoSite; P21802; -.
DR   DMDM; 120049; -.
DR   MaxQB; P21802; -.
DR   PaxDb; P21802; -.
DR   PRIDE; P21802; -.
DR   Ensembl; ENST00000346997; ENSP00000263451; ENSG00000066468. [P21802-5]
DR   Ensembl; ENST00000351936; ENSP00000309878; ENSG00000066468. [P21802-6]
DR   Ensembl; ENST00000356226; ENSP00000348559; ENSG00000066468. [P21802-20]
DR   Ensembl; ENST00000357555; ENSP00000350166; ENSG00000066468. [P21802-21]
DR   Ensembl; ENST00000358487; ENSP00000351276; ENSG00000066468. [P21802-1]
DR   Ensembl; ENST00000359354; ENSP00000352309; ENSG00000066468. [P21802-14]
DR   Ensembl; ENST00000360144; ENSP00000353262; ENSG00000066468. [P21802-22]
DR   Ensembl; ENST00000369056; ENSP00000358052; ENSG00000066468. [P21802-17]
DR   Ensembl; ENST00000369058; ENSP00000358054; ENSG00000066468. [P21802-13]
DR   Ensembl; ENST00000369060; ENSP00000358056; ENSG00000066468. [P21802-15]
DR   Ensembl; ENST00000369061; ENSP00000358057; ENSG00000066468. [P21802-23]
DR   Ensembl; ENST00000457416; ENSP00000410294; ENSG00000066468. [P21802-3]
DR   GeneID; 2263; -.
DR   KEGG; hsa:2263; -.
DR   UCSC; uc001lfg.4; human. [P21802-20]
DR   UCSC; uc001lfn.5; human. [P21802-1]
DR   UCSC; uc010qtl.2; human. [P21802-15]
DR   UCSC; uc021pzv.1; human. [P21802-23]
DR   UCSC; uc021pzx.1; human. [P21802-21]
DR   UCSC; uc021pzy.1; human. [P21802-3]
DR   UCSC; uc021qaa.1; human. [P21802-17]
DR   UCSC; uc021qab.1; human. [P21802-22]
DR   UCSC; uc021qac.1; human. [P21802-4]
DR   CTD; 2263; -.
DR   GeneCards; GC10M123223; -.
DR   GeneReviews; FGFR2; -.
DR   HGNC; HGNC:3689; FGFR2.
DR   HPA; CAB010886; -.
DR   HPA; HPA035305; -.
DR   HPA; HPA056562; -.
DR   MIM; 101200; phenotype.
DR   MIM; 101600; phenotype.
DR   MIM; 123150; phenotype.
DR   MIM; 123500; phenotype.
DR   MIM; 123790; phenotype.
DR   MIM; 149730; phenotype.
DR   MIM; 176943; gene.
DR   MIM; 207410; phenotype.
DR   MIM; 609579; phenotype.
DR   MIM; 614592; phenotype.
DR   neXtProt; NX_P21802; -.
DR   Orphanet; 83; Antley-Bixler syndrome.
DR   Orphanet; 87; Apert syndrome.
DR   Orphanet; 207; Crouzon disease.
DR   Orphanet; 1555; Cutis gyrata - acanthosis nigricans - craniosynostosis.
DR   Orphanet; 168624; Familial scaphocephaly syndrome, McGillivray type.
DR   Orphanet; 313855; FGFR2-related bent bone dysplasia.
DR   Orphanet; 1540; Jackson-Weiss syndrome.
DR   Orphanet; 2363; Lacrimo-auriculo-dento-digital syndrome.
DR   Orphanet; 93258; Pfeiffer syndrome type 1.
DR   Orphanet; 93259; Pfeiffer syndrome type 2.
DR   Orphanet; 93260; Pfeiffer syndrome type 3.
DR   Orphanet; 794; Saethre-Chotzen syndrome.
DR   PharmGKB; PA28128; -.
DR   eggNOG; COG0515; -.
DR   HOGENOM; HOG000263410; -.
DR   HOVERGEN; HBG000345; -.
DR   KO; K05093; -.
DR   OMA; LELRCQL; -.
DR   OrthoDB; EOG7NGQ9N; -.
DR   PhylomeDB; P21802; -.
DR   TreeFam; TF316307; -.
DR   BRENDA; 2.7.10.1; 2681.
DR   Reactome; REACT_111184; Negative regulation of FGFR signaling.
DR   Reactome; REACT_120863; Activated point mutants of FGFR2.
DR   Reactome; REACT_121255; Signaling by FGFR2 amplification mutants.
DR   Reactome; REACT_121398; Signaling by FGFR mutants.
DR   Reactome; REACT_147727; Constitutive PI3K/AKT Signaling in Cancer.
DR   Reactome; REACT_21247; FRS2-mediated cascade.
DR   Reactome; REACT_21270; PI-3K cascade.
DR   Reactome; REACT_21310; Phospholipase C-mediated cascade.
DR   Reactome; REACT_21374; SHC-mediated cascade.
DR   Reactome; REACT_75829; PIP3 activates AKT signaling.
DR   Reactome; REACT_9413; FGFR2c ligand binding and activation.
DR   Reactome; REACT_9416; FGFR2b ligand binding and activation.
DR   Reactome; REACT_976; PI3K Cascade.
DR   SignaLink; P21802; -.
DR   EvolutionaryTrace; P21802; -.
DR   GeneWiki; Fibroblast_growth_factor_receptor_2; -.
DR   GenomeRNAi; 2263; -.
DR   NextBio; 9189; -.
DR   PRO; PR:P21802; -.
DR   ArrayExpress; P21802; -.
DR   Bgee; P21802; -.
DR   Genevestigator; P21802; -.
DR   GO; GO:0005938; C:cell cortex; IDA:UniProtKB.
DR   GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell.
DR   GO; GO:0060076; C:excitatory synapse; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; NAS:UniProtKB.
DR   GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; NAS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0017134; F:fibroblast growth factor binding; IDA:UniProtKB.
DR   GO; GO:0005007; F:fibroblast growth factor-activated receptor activity; IDA:UniProtKB.
DR   GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR   GO; GO:0004713; F:protein tyrosine kinase activity; NAS:UniProtKB.
DR   GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0007409; P:axonogenesis; ISS:UniProtKB.
DR   GO; GO:0060348; P:bone development; ISS:UniProtKB.
DR   GO; GO:0030282; P:bone mineralization; ISS:UniProtKB.
DR   GO; GO:0060349; P:bone morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060667; P:branch elongation involved in salivary gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060670; P:branching involved in labyrinthine layer morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060442; P:branching involved in prostate gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060445; P:branching involved in salivary gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048755; P:branching morphogenesis of a nerve; ISS:UniProtKB.
DR   GO; GO:0060449; P:bud elongation involved in lung branching; ISS:UniProtKB.
DR   GO; GO:0045165; P:cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; ISS:UniProtKB.
DR   GO; GO:0060365; P:coronal suture morphogenesis; IEA:Ensembl.
DR   GO; GO:0048565; P:digestive tract development; ISS:UniProtKB.
DR   GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IMP:BHF-UCL.
DR   GO; GO:0048557; P:embryonic digestive tract morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048568; P:embryonic organ development; ISS:UniProtKB.
DR   GO; GO:0048562; P:embryonic organ morphogenesis; ISS:UniProtKB.
DR   GO; GO:0009880; P:embryonic pattern specification; ISS:UniProtKB.
DR   GO; GO:0061031; P:endodermal digestive tract morphogenesis; IEA:Ensembl.
DR   GO; GO:0007173; P:epidermal growth factor receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0048730; P:epidermis morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030855; P:epithelial cell differentiation; ISS:UniProtKB.
DR   GO; GO:0060664; P:epithelial cell proliferation involved in salivary gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001837; P:epithelial to mesenchymal transition; IEA:Ensembl.
DR   GO; GO:0038095; P:Fc-epsilon receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; IDA:UniProtKB.
DR   GO; GO:0035603; P:fibroblast growth factor receptor signaling pathway involved in hemopoiesis; ISS:UniProtKB.
DR   GO; GO:0060595; P:fibroblast growth factor receptor signaling pathway involved in mammary gland specification; ISS:UniProtKB.
DR   GO; GO:0035602; P:fibroblast growth factor receptor signaling pathway involved in negative regulation of apoptotic process in bone marrow; ISS:UniProtKB.
DR   GO; GO:0035607; P:fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development; ISS:UniProtKB.
DR   GO; GO:0035604; P:fibroblast growth factor receptor signaling pathway involved in positive regulation of cell proliferation in bone marrow; ISS:UniProtKB.
DR   GO; GO:0022612; P:gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0031069; P:hair follicle morphogenesis; ISS:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; ISS:UniProtKB.
DR   GO; GO:0045087; P:innate immune response; TAS:Reactome.
DR   GO; GO:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
DR   GO; GO:0008286; P:insulin receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0032808; P:lacrimal gland development; ISS:UniProtKB.
DR   GO; GO:0060601; P:lateral sprouting from an epithelium; ISS:UniProtKB.
DR   GO; GO:0070307; P:lens fiber cell development; IEA:Ensembl.
DR   GO; GO:0060174; P:limb bud formation; ISS:UniProtKB.
DR   GO; GO:0048286; P:lung alveolus development; ISS:UniProtKB.
DR   GO; GO:0030324; P:lung development; ISS:UniProtKB.
DR   GO; GO:0060463; P:lung lobe morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060484; P:lung-associated mesenchyme development; ISS:UniProtKB.
DR   GO; GO:0060615; P:mammary gland bud formation; ISS:UniProtKB.
DR   GO; GO:0003149; P:membranous septum morphogenesis; ISS:UniProtKB.
DR   GO; GO:0048762; P:mesenchymal cell differentiation; ISS:UniProtKB.
DR   GO; GO:0060915; P:mesenchymal cell differentiation involved in lung development; ISS:UniProtKB.
DR   GO; GO:0060916; P:mesenchymal cell proliferation involved in lung development; ISS:UniProtKB.
DR   GO; GO:0048333; P:mesodermal cell differentiation; IEA:Ensembl.
DR   GO; GO:0030901; P:midbrain development; ISS:UniProtKB.
DR   GO; GO:0016331; P:morphogenesis of embryonic epithelium; ISS:UniProtKB.
DR   GO; GO:0035264; P:multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0050680; P:negative regulation of epithelial cell proliferation; IEA:Ensembl.
DR   GO; GO:0045839; P:negative regulation of mitosis; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0007528; P:neuromuscular junction development; IEA:Ensembl.
DR   GO; GO:0048011; P:neurotrophin TRK receptor signaling pathway; TAS:Reactome.
DR   GO; GO:0042476; P:odontogenesis; ISS:UniProtKB.
DR   GO; GO:0021769; P:orbitofrontal cortex development; ISS:UniProtKB.
DR   GO; GO:0035265; P:organ growth; ISS:UniProtKB.
DR   GO; GO:0009887; P:organ morphogenesis; ISS:UniProtKB.
DR   GO; GO:0030916; P:otic vesicle formation; ISS:UniProtKB.
DR   GO; GO:0003148; P:outflow tract septum morphogenesis; ISS:UniProtKB.
DR   GO; GO:0018108; P:peptidyl-tyrosine phosphorylation; IDA:UniProtKB.
DR   GO; GO:0048015; P:phosphatidylinositol-mediated signaling; TAS:Reactome.
DR   GO; GO:0090263; P:positive regulation of canonical Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060045; P:positive regulation of cardiac muscle cell proliferation; ISS:UniProtKB.
DR   GO; GO:0045787; P:positive regulation of cell cycle; ISS:UniProtKB.
DR   GO; GO:0051781; P:positive regulation of cell division; ISS:UniProtKB.
DR   GO; GO:0008284; P:positive regulation of cell proliferation; IDA:UniProtKB.
DR   GO; GO:0050679; P:positive regulation of epithelial cell proliferation; ISS:UniProtKB.
DR   GO; GO:0060501; P:positive regulation of epithelial cell proliferation involved in lung morphogenesis; ISS:UniProtKB.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IMP:UniProtKB.
DR   GO; GO:0002053; P:positive regulation of mesenchymal cell proliferation; ISS:UniProtKB.
DR   GO; GO:0010518; P:positive regulation of phospholipase activity; IMP:UniProtKB.
DR   GO; GO:0048661; P:positive regulation of smooth muscle cell proliferation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; ISS:UniProtKB.
DR   GO; GO:0009791; P:post-embryonic development; ISS:UniProtKB.
DR   GO; GO:0060527; P:prostate epithelial cord arborization involved in prostate glandular acinus morphogenesis; ISS:UniProtKB.
DR   GO; GO:0060523; P:prostate epithelial cord elongation; ISS:UniProtKB.
DR   GO; GO:0060512; P:prostate gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR   GO; GO:0021860; P:pyramidal neuron development; ISS:UniProtKB.
DR   GO; GO:0060687; P:regulation of branching involved in prostate gland morphogenesis; ISS:UniProtKB.
DR   GO; GO:0010453; P:regulation of cell fate commitment; ISS:UniProtKB.
DR   GO; GO:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR   GO; GO:0040036; P:regulation of fibroblast growth factor receptor signaling pathway; ISS:UniProtKB.
DR   GO; GO:0060688; P:regulation of morphogenesis of a branching structure; ISS:UniProtKB.
DR   GO; GO:0040014; P:regulation of multicellular organism growth; ISS:UniProtKB.
DR   GO; GO:0045667; P:regulation of osteoblast differentiation; TAS:UniProtKB.
DR   GO; GO:0033688; P:regulation of osteoblast proliferation; TAS:UniProtKB.
DR   GO; GO:0051150; P:regulation of smooth muscle cell differentiation; ISS:UniProtKB.
DR   GO; GO:0008589; P:regulation of smoothened signaling pathway; ISS:UniProtKB.
DR   GO; GO:0048608; P:reproductive structure development; ISS:UniProtKB.
DR   GO; GO:0048705; P:skeletal system morphogenesis; TAS:UniProtKB.
DR   GO; GO:0060529; P:squamous basal epithelial stem cell differentiation involved in prostate gland acinus development; ISS:UniProtKB.
DR   GO; GO:0048489; P:synaptic vesicle transport; IEA:Ensembl.
DR   GO; GO:0001657; P:ureteric bud development; ISS:UniProtKB.
DR   GO; GO:0055010; P:ventricular cardiac muscle tissue morphogenesis; ISS:UniProtKB.
DR   GO; GO:0021847; P:ventricular zone neuroblast division; ISS:UniProtKB.
DR   Gene3D; 2.60.40.10; -; 3.
DR   InterPro; IPR028175; FGF_rcpt_2.
DR   InterPro; IPR016248; FGF_rcpt_fam.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR011009; Kinase-like_dom.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008266; Tyr_kinase_AS.
DR   InterPro; IPR020635; Tyr_kinase_cat_dom.
DR   PANTHER; PTHR24416:SF130; PTHR24416:SF130; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF07714; Pkinase_Tyr; 1.
DR   PIRSF; PIRSF000628; FGFR; 1.
DR   PRINTS; PR00109; TYRKINASE.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00219; TyrKc; 1.
DR   SUPFAM; SSF56112; SSF56112; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00109; PROTEIN_KINASE_TYR; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Apoptosis; ATP-binding;
KW   Cell membrane; Complete proteome; Craniosynostosis;
KW   Cytoplasmic vesicle; Disease mutation; Disulfide bond;
KW   Ectodermal dysplasia; Glycoprotein; Golgi apparatus; Heparin-binding;
KW   Immunoglobulin domain; Kinase;
KW   Lacrimo-auriculo-dento-digital syndrome; Membrane; Mental retardation;
KW   Nucleotide-binding; Phosphoprotein; Polymorphism; Proto-oncogene;
KW   Receptor; Reference proteome; Repeat; Secreted; Signal; Transferase;
KW   Transmembrane; Transmembrane helix; Tyrosine-protein kinase;
KW   Ubl conjugation.
FT   SIGNAL        1     21       {ECO:0000255}.
FT   CHAIN        22    821       Fibroblast growth factor receptor 2.
FT                                /FTId=PRO_0000016783.
FT   TOPO_DOM     22    377       Extracellular. {ECO:0000255}.
FT   TRANSMEM    378    398       Helical. {ECO:0000255}.
FT   TOPO_DOM    399    821       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN       25    125       Ig-like C2-type 1.
FT   DOMAIN      154    247       Ig-like C2-type 2.
FT   DOMAIN      256    358       Ig-like C2-type 3.
FT   DOMAIN      481    770       Protein kinase. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159}.
FT   NP_BIND     487    495       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:19060208}.
FT   NP_BIND     565    567       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:19060208}.
FT   REGION      161    178       Heparin-binding.
FT   ACT_SITE    626    626       Proton acceptor. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159, ECO:0000255|PROSITE-
FT                                ProRule:PRU10028,
FT                                ECO:0000269|PubMed:19060208}.
FT   BINDING     517    517       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:19060208}.
FT   BINDING     571    571       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00159,
FT                                ECO:0000269|PubMed:19060208}.
FT   MOD_RES     466    466       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:17311277,
FT                                ECO:0000269|PubMed:19060208,
FT                                ECO:0000269|PubMed:19410646}.
FT   MOD_RES     586    586       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:17311277,
FT                                ECO:0000269|PubMed:17803937,
FT                                ECO:0000269|PubMed:19060208,
FT                                ECO:0000269|PubMed:19410646}.
FT   MOD_RES     588    588       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:17311277,
FT                                ECO:0000269|PubMed:19060208,
FT                                ECO:0000269|PubMed:19410646}.
FT   MOD_RES     656    656       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:17311277,
FT                                ECO:0000269|PubMed:17803937,
FT                                ECO:0000269|PubMed:19060208,
FT                                ECO:0000269|PubMed:19410646}.
FT   MOD_RES     657    657       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:17311277,
FT                                ECO:0000269|PubMed:17803937,
FT                                ECO:0000269|PubMed:19060208,
FT                                ECO:0000269|PubMed:19410646}.
FT   MOD_RES     769    769       Phosphotyrosine; by autocatalysis.
FT                                {ECO:0000269|PubMed:15629145,
FT                                ECO:0000269|PubMed:17311277,
FT                                ECO:0000269|PubMed:19060208}.
FT   CARBOHYD     83     83       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    123    123       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    228    228       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    241    241       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    265    265       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    297    297       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    318    318       N-linked (GlcNAc...). {ECO:0000255}.
FT   CARBOHYD    331    331       N-linked (GlcNAc...). {ECO:0000255}.
FT   DISULFID     62    107       {ECO:0000255|PROSITE-ProRule:PRU00114}.
FT   DISULFID    179    231       {ECO:0000255|PROSITE-ProRule:PRU00114,
FT                                ECO:0000269|PubMed:16384934}.
FT   DISULFID    278    342       {ECO:0000255|PROSITE-ProRule:PRU00114,
FT                                ECO:0000269|PubMed:16384934}.
FT   VAR_SEQ      37    152       EPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGV
FT                                HLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETW
FT                                YFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKR -> G
FT                                (in isoform 20).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_019608.
FT   VAR_SEQ      37    125       Missing (in isoform 4, isoform 21 and
FT                                isoform 22).
FT                                {ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:2377625}.
FT                                /FTId=VSP_002964.
FT   VAR_SEQ     250    361       Missing (in isoform 23).
FT                                {ECO:0000303|Ref.14}.
FT                                /FTId=VSP_041914.
FT   VAR_SEQ     250    254       ERSPH -> GSQGL (in isoform 14).
FT                                {ECO:0000303|PubMed:1313574}.
FT                                /FTId=VSP_002965.
FT   VAR_SEQ     255    821       Missing (in isoform 14).
FT                                {ECO:0000303|PubMed:1313574}.
FT                                /FTId=VSP_002966.
FT   VAR_SEQ     313    313       K -> KVTK (in isoform 16).
FT                                {ECO:0000303|PubMed:2172978}.
FT                                /FTId=VSP_002967.
FT   VAR_SEQ     314    429       Missing (in isoform 15).
FT                                {ECO:0000303|PubMed:1313574}.
FT                                /FTId=VSP_002968.
FT   VAR_SEQ     314    330       AAGVNTTDKEIEVLYIR -> HSGINSSNAEVLALF (in
FT                                isoform 3, isoform 4, isoform 7, isoform
FT                                9, isoform 10, isoform 11, isoform 12,
FT                                isoform 13, isoform 17, isoform 18,
FT                                isoform 19 and isoform 22).
FT                                {ECO:0000303|PubMed:10626794,
FT                                ECO:0000303|PubMed:1309608,
FT                                ECO:0000303|PubMed:1400433,
FT                                ECO:0000303|PubMed:1647213,
FT                                ECO:0000303|PubMed:2377625,
FT                                ECO:0000303|PubMed:7866434}.
FT                                /FTId=VSP_002969.
FT   VAR_SEQ     334    335       FE -> EA (in isoform 3, isoform 4,
FT                                isoform 7, isoform 9, isoform 10, isoform
FT                                11, isoform 12, isoform 13, isoform 17,
FT                                isoform 18, isoform 19 and isoform 22).
FT                                {ECO:0000303|PubMed:10626794,
FT                                ECO:0000303|PubMed:1309608,
FT                                ECO:0000303|PubMed:1400433,
FT                                ECO:0000303|PubMed:1647213,
FT                                ECO:0000303|PubMed:2377625,
FT                                ECO:0000303|PubMed:7866434}.
FT                                /FTId=VSP_002970.
FT   VAR_SEQ     341    353       TCLAGNSIGISFH -> ICKVSNYIGQANQ (in
FT                                isoform 3, isoform 4, isoform 7, isoform
FT                                9, isoform 10, isoform 11, isoform 12,
FT                                isoform 13, isoform 17, isoform 18,
FT                                isoform 19 and isoform 22).
FT                                {ECO:0000303|PubMed:10626794,
FT                                ECO:0000303|PubMed:1309608,
FT                                ECO:0000303|PubMed:1400433,
FT                                ECO:0000303|PubMed:1647213,
FT                                ECO:0000303|PubMed:2377625,
FT                                ECO:0000303|PubMed:7866434}.
FT                                /FTId=VSP_002971.
FT   VAR_SEQ     361    361       P -> PKQQ (in isoform 3, isoform 4,
FT                                isoform 7, isoform 9, isoform 10, isoform
FT                                11, isoform 12, isoform 13, isoform 17,
FT                                isoform 18, isoform 19 and isoform 22).
FT                                {ECO:0000303|PubMed:10626794,
FT                                ECO:0000303|PubMed:1309608,
FT                                ECO:0000303|PubMed:1400433,
FT                                ECO:0000303|PubMed:1647213,
FT                                ECO:0000303|PubMed:2377625,
FT                                ECO:0000303|PubMed:7866434}.
FT                                /FTId=VSP_002972.
FT   VAR_SEQ     362    365       APGR -> GRRC (in isoform 19).
FT                                {ECO:0000303|PubMed:1309608,
FT                                ECO:0000303|PubMed:7866434}.
FT                                /FTId=VSP_002973.
FT   VAR_SEQ     366    821       Missing (in isoform 19).
FT                                {ECO:0000303|PubMed:1309608,
FT                                ECO:0000303|PubMed:7866434}.
FT                                /FTId=VSP_002974.
FT   VAR_SEQ     428    429       Missing (in isoform 4, isoform 5, isoform
FT                                6, isoform 8, isoform 16 and isoform 18).
FT                                {ECO:0000303|PubMed:1313574,
FT                                ECO:0000303|PubMed:2172978,
FT                                ECO:0000303|PubMed:2377625}.
FT                                /FTId=VSP_002975.
FT   VAR_SEQ     429    430       Missing (in isoform 20).
FT                                {ECO:0000303|PubMed:15489334}.
FT                                /FTId=VSP_019609.
FT   VAR_SEQ     761    821       LTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPD
FT                                PMPYEPCLPQYPHINGSVKT -> PPNPSLMSIFRK (in
FT                                isoform 4). {ECO:0000303|PubMed:2377625}.
FT                                /FTId=VSP_002976.
FT   VAR_SEQ     768    821       EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPC
FT                                LPQYPHINGSVKT -> SFQSSLKSSSTGIPGWPPGSEVFS
FT                                EVAFRGILNYDIERPILCAGSKKIYDI (in isoform
FT                                10). {ECO:0000303|PubMed:10626794}.
FT                                /FTId=VSP_002981.
FT   VAR_SEQ     768    821       EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPC
FT                                LPQYPHINGSVKT -> GRLPAWASQEKENSQTSLFAISHV
FT                                TLSSISKTRSSAKRDEKPGSSPHLALVRSQGLPQSVVP
FT                                (in isoform 11).
FT                                {ECO:0000303|PubMed:10626794}.
FT                                /FTId=VSP_002982.
FT   VAR_SEQ     768    821       EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPC
FT                                LPQYPHINGSVKT -> PLS (in isoform 12).
FT                                {ECO:0000303|PubMed:10626794}.
FT                                /FTId=VSP_002983.
FT   VAR_SEQ     768    821       Missing (in isoform 13).
FT                                {ECO:0000303|PubMed:10626794}.
FT                                /FTId=VSP_002977.
FT   VAR_SEQ     768    821       EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPC
FT                                LPQYPHINGSVKT -> I (in isoform 2, isoform
FT                                8, isoform 17 and isoform 22).
FT                                {ECO:0000303|PubMed:1647213}.
FT                                /FTId=VSP_002978.
FT   VAR_SEQ     768    821       EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPC
FT                                LPQYPHINGSVKT -> RYKLLPCPDKHNKRCKPEERGDLT
FT                                EAGAAGSSRCVDSRKRVRQEKISTG (in isoform 7).
FT                                {ECO:0000303|PubMed:10626794}.
FT                                /FTId=VSP_002979.
FT   VAR_SEQ     768    821       EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPC
FT                                LPQYPHINGSVKT -> RILTLTTNENFQSTSGREGTEIHA
FT                                LQCLRSEVTPAISCESPLADTGSKVPN (in isoform
FT                                9). {ECO:0000303|PubMed:10626794}.
FT                                /FTId=VSP_002980.
FT   VAR_SEQ     769    821       YLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCL
FT                                PQYPHINGSVKT -> EKKVSGAVDCHKPPCNPSHLPCVLA
FT                                VDQ (in isoform 21).
FT                                {ECO:0000303|PubMed:14702039}.
FT                                /FTId=VSP_041915.
FT   VAR_SEQ     778    821       QYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGS
FT                                VKT -> PYSPCYPDPR (in isoform 6).
FT                                {ECO:0000305}.
FT                                /FTId=VSP_002984.
FT   VARIANT       6      6       R -> P (in dbSNP:rs3750819).
FT                                {ECO:0000269|Ref.15}.
FT                                /FTId=VAR_017258.
FT   VARIANT      57     57       S -> L (in dbSNP:rs56226109).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042204.
FT   VARIANT     105    105       Y -> C (in CS).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:8946174}.
FT                                /FTId=VAR_004112.
FT   VARIANT     172    172       A -> F (in PS; requires 2 nucleotide
FT                                substitutions).
FT                                {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017259.
FT   VARIANT     186    186       M -> T (in dbSNP:rs755793).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|Ref.15}.
FT                                /FTId=VAR_017260.
FT   VARIANT     203    203       R -> C (in breast cancer samples;
FT                                infiltrating ductal carcinoma; somatic
FT                                mutation). {ECO:0000269|PubMed:16959974,
FT                                ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_036380.
FT   VARIANT     252    253       SP -> FS (in PS).
FT                                /FTId=VAR_004116.
FT   VARIANT     252    252       S -> F (in APRS; requires 2 nucleotide
FT                                substitutions).
FT                                {ECO:0000269|PubMed:9002682}.
FT                                /FTId=VAR_004114.
FT   VARIANT     252    252       S -> L (in CS).
FT                                {ECO:0000269|PubMed:9002682}.
FT                                /FTId=VAR_004113.
FT   VARIANT     252    252       S -> W (in APRS and PS; common mutation).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7668257,
FT                                ECO:0000269|PubMed:7719344,
FT                                ECO:0000269|PubMed:9452027,
FT                                ECO:0000269|PubMed:9677057,
FT                                ECO:0000269|PubMed:9719378}.
FT                                /FTId=VAR_004115.
FT   VARIANT     253    253       P -> R (in APRS; common mutation).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7668257,
FT                                ECO:0000269|PubMed:7719344,
FT                                ECO:0000269|PubMed:9452027,
FT                                ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_004117.
FT   VARIANT     263    263       P -> L (in CS).
FT                                {ECO:0000269|PubMed:11173845}.
FT                                /FTId=VAR_017261.
FT   VARIANT     267    267       S -> P (in CS).
FT                                {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_004118.
FT   VARIANT     268    268       T -> TG (in CS).
FT                                {ECO:0000269|PubMed:8644708}.
FT                                /FTId=VAR_004119.
FT   VARIANT     272    272       G -> V (in an ovarian serous carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042205.
FT   VARIANT     273    273       Missing (in PS; type 2).
FT                                {ECO:0000269|PubMed:10945669}.
FT                                /FTId=VAR_017262.
FT   VARIANT     276    276       F -> V (in CS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:9521581}.
FT                                /FTId=VAR_004120.
FT   VARIANT     278    278       C -> F (in CS, JWS and PS; forms
FT                                disulfide-linked dimers with constitutive
FT                                kinase activity, is retained in an
FT                                intracellular compartment and not
FT                                detected at the cell surface).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:8644708,
FT                                ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_004121.
FT   VARIANT     278    278       C -> Y (in CS).
FT                                {ECO:0000269|PubMed:11173845}.
FT                                /FTId=VAR_017263.
FT   VARIANT     281    281       Y -> C (in CS).
FT                                {ECO:0000269|PubMed:11380921,
FT                                ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017264.
FT   VARIANT     283    283       D -> N (in a lung squamous cell carcinoma
FT                                sample; somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_042206.
FT   VARIANT     287    289       Missing (in CS).
FT                                /FTId=VAR_004122.
FT   VARIANT     288    288       I -> S (in CS).
FT                                {ECO:0000269|PubMed:11173845}.
FT                                /FTId=VAR_017265.
FT   VARIANT     289    289       Q -> P (in CS and JWS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11380921,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7581378,
FT                                ECO:0000269|PubMed:8644708}.
FT                                /FTId=VAR_004123.
FT   VARIANT     290    290       W -> C (in PS; severe; also in a lung
FT                                squamous cell carcinoma sample; somatic
FT                                mutation). {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:17344846,
FT                                ECO:0000269|PubMed:9150725}.
FT                                /FTId=VAR_004124.
FT   VARIANT     290    290       W -> G (in CS).
FT                                {ECO:0000269|PubMed:8528214}.
FT                                /FTId=VAR_017266.
FT   VARIANT     290    290       W -> R (in CS).
FT                                /FTId=VAR_004125.
FT   VARIANT     292    292       K -> E (in CS).
FT                                {ECO:0000269|PubMed:9152842}.
FT                                /FTId=VAR_004126.
FT   VARIANT     301    301       Y -> C (in CS).
FT                                {ECO:0000269|PubMed:9521581}.
FT                                /FTId=VAR_004127.
FT   VARIANT     314    314       A -> S (in craniosynostosis).
FT                                {ECO:0000269|PubMed:9521581}.
FT                                /FTId=VAR_004128.
FT   VARIANT     315    315       A -> S (in a non-syndromic
FT                                craniosynostosis patient with abnormal
FT                                intrauterine history; confers
FT                                predisposition to craniosynostosis).
FT                                {ECO:0000269|PubMed:10951518,
FT                                ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017267.
FT   VARIANT     321    321       D -> A (in PS).
FT                                {ECO:0000269|PubMed:7719333}.
FT                                /FTId=VAR_004129.
FT   VARIANT     328    328       Y -> C (in CS).
FT                                {ECO:0000269|PubMed:7874170}.
FT                                /FTId=VAR_004130.
FT   VARIANT     331    331       N -> I (in CS).
FT                                {ECO:0000269|PubMed:8956050}.
FT                                /FTId=VAR_004131.
FT   VARIANT     337    337       A -> ANA (in CS).
FT                                /FTId=VAR_004132.
FT   VARIANT     337    337       A -> P (in CS).
FT                                {ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_017268.
FT   VARIANT     338    338       G -> E (in CS).
FT                                {ECO:0000269|PubMed:8946174}.
FT                                /FTId=VAR_004133.
FT   VARIANT     338    338       G -> R (in CS).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7581378,
FT                                ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_015011.
FT   VARIANT     340    340       Y -> C (in PS).
FT                                {ECO:0000269|PubMed:10394936,
FT                                ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017269.
FT   VARIANT     340    340       Y -> H (in CS).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7987400}.
FT                                /FTId=VAR_004134.
FT   VARIANT     341    341       T -> P (in PS and CS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7719345}.
FT                                /FTId=VAR_004135.
FT   VARIANT     342    342       C -> F (in CS).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:8644708,
FT                                ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_004136.
FT   VARIANT     342    342       C -> G (in PS).
FT                                {ECO:0000269|PubMed:10394936}.
FT                                /FTId=VAR_017270.
FT   VARIANT     342    342       C -> R (in CS, JWS, PS and ABS2).
FT                                {ECO:0000269|PubMed:10633130,
FT                                ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11380921,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7719345,
FT                                ECO:0000269|PubMed:7987400,
FT                                ECO:0000269|PubMed:8528214,
FT                                ECO:0000269|PubMed:8644708,
FT                                ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_004137.
FT   VARIANT     342    342       C -> S (in CS, JWS, PS and ABS2).
FT                                {ECO:0000269|PubMed:10633130,
FT                                ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7581378,
FT                                ECO:0000269|PubMed:7987400,
FT                                ECO:0000269|PubMed:8644708,
FT                                ECO:0000269|PubMed:9385368,
FT                                ECO:0000269|Ref.10}.
FT                                /FTId=VAR_004138.
FT   VARIANT     342    342       C -> W (in CS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:8528214}.
FT                                /FTId=VAR_017271.
FT   VARIANT     342    342       C -> Y (in CS and PS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11380921,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7581378,
FT                                ECO:0000269|PubMed:7719345,
FT                                ECO:0000269|PubMed:7987400,
FT                                ECO:0000269|PubMed:8644708,
FT                                ECO:0000269|PubMed:9677057}.
FT                                /FTId=VAR_004139.
FT   VARIANT     344    344       A -> G (in CS and JWS).
FT                                {ECO:0000269|PubMed:7581378,
FT                                ECO:0000269|PubMed:7874170}.
FT                                /FTId=VAR_004140.
FT   VARIANT     344    344       A -> P (in CS and PS).
FT                                {ECO:0000269|PubMed:8644708}.
FT                                /FTId=VAR_004141.
FT   VARIANT     347    347       S -> C (in CS).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7874170}.
FT                                /FTId=VAR_004142.
FT   VARIANT     351    351       S -> C (in CS, PS and ABS2).
FT                                {ECO:0000269|PubMed:10633130,
FT                                ECO:0000269|PubMed:8946174,
FT                                ECO:0000269|PubMed:9693549}.
FT                                /FTId=VAR_004143.
FT   VARIANT     354    354       S -> C (in CS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:7581378,
FT                                ECO:0000269|PubMed:7987400,
FT                                ECO:0000269|PubMed:8528214}.
FT                                /FTId=VAR_004144.
FT   VARIANT     354    354       S -> Y (in CS).
FT                                {ECO:0000269|PubMed:11173845}.
FT                                /FTId=VAR_017272.
FT   VARIANT     356    358       Missing (in CS).
FT                                /FTId=VAR_004145.
FT   VARIANT     359    359       V -> F (in CS and PS).
FT                                {ECO:0000269|PubMed:11173845,
FT                                ECO:0000269|PubMed:8644708}.
FT                                /FTId=VAR_004146.
FT   VARIANT     362    362       A -> S (in CS).
FT                                {ECO:0000269|PubMed:10574673}.
FT                                /FTId=VAR_017273.
FT   VARIANT     372    372       S -> C (in BSTVS).
FT                                {ECO:0000269|PubMed:8696350}.
FT                                /FTId=VAR_017274.
FT   VARIANT     375    375       Y -> C (in PS and BSTVS).
FT                                {ECO:0000269|PubMed:11781872,
FT                                ECO:0000269|PubMed:12000365,
FT                                ECO:0000269|PubMed:8696350}.
FT                                /FTId=VAR_017275.
FT   VARIANT     381    381       Y -> D (in BBDS).
FT                                {ECO:0000269|PubMed:22387015}.
FT                                /FTId=VAR_067977.
FT   VARIANT     384    384       G -> R (in CS).
FT                                {ECO:0000269|PubMed:8946174}.
FT                                /FTId=VAR_004147.
FT   VARIANT     391    391       M -> R (in BBDS; the mutation selectively
FT                                reduces plasma-membrane levels of the
FT                                protein and markedly diminishes the
FT                                receptor's responsiveness to
FT                                extracellular FGF).
FT                                {ECO:0000269|PubMed:22387015}.
FT                                /FTId=VAR_067978.
FT   VARIANT     526    526       K -> E (in FSPC; constitutive kinase
FT                                activity). {ECO:0000269|PubMed:16061565}.
FT                                /FTId=VAR_023788.
FT   VARIANT     549    549       N -> H (in CS; constitutive kinase
FT                                activity). {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017276.
FT   VARIANT     565    565       E -> G (in PS; constitutive kinase
FT                                activity). {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017277.
FT   VARIANT     612    612       R -> T (in a lung adenocarcinoma sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:17344846}.
FT                                /FTId=VAR_046071.
FT   VARIANT     613    613       G -> R. {ECO:0000269|PubMed:10626794,
FT                                ECO:0000269|PubMed:1309608}.
FT                                /FTId=VAR_015012.
FT   VARIANT     628    628       A -> T (in LADDS; strongly reduced kinase
FT                                activity). {ECO:0000269|PubMed:16501574}.
FT                                /FTId=VAR_029884.
FT   VARIANT     641    641       K -> R (in PS; constitutive kinase
FT                                activity). {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017278.
FT   VARIANT     648    648       A -> T (in LADDS).
FT                                {ECO:0000269|PubMed:16501574}.
FT                                /FTId=VAR_029885.
FT   VARIANT     649    650       RD -> S (in LADDS).
FT                                /FTId=VAR_029886.
FT   VARIANT     659    659       K -> N (in craniosynostosis; constitutive
FT                                kinase activity).
FT                                {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017279.
FT   VARIANT     663    663       G -> E (in PS).
FT                                {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017280.
FT   VARIANT     678    678       R -> G (in CS).
FT                                {ECO:0000269|PubMed:11781872}.
FT                                /FTId=VAR_017281.
FT   MUTAGEN     265    265       N->Q: Reduced N-glycosylation. Reduced
FT                                expression at the cell surface.
FT                                {ECO:0000269|PubMed:16844695}.
FT   MUTAGEN     549    549       N->T: Constitutive kinase activity.
FT                                {ECO:0000269|PubMed:17803937}.
FT   MUTAGEN     565    565       E->A: Constitutive kinase activity.
FT                                {ECO:0000269|PubMed:17803937}.
FT   MUTAGEN     656    657       Missing: Loss of kinase activity.
FT   MUTAGEN     769    769       Y->F: Increases fibroblast proliferation.
FT                                Decreases phosphorylation of PLCG1 and
FT                                FRS2. Decreases activation of MAP
FT                                kinases. {ECO:0000269|PubMed:15629145,
FT                                ECO:0000269|PubMed:19103595}.
FT   CONFLICT    246    246       L -> P (in Ref. 16; BAG57383).
FT                                {ECO:0000305}.
FT   CONFLICT    310    310       K -> N (in Ref. 16; BAG57383).
FT                                {ECO:0000305}.
FT   STRAND      152    157
FT   TURN        159    162
FT   STRAND      166    170
FT   STRAND      175    178
FT   STRAND      181    185
FT   STRAND      188    193
FT   HELIX       200    202
FT   STRAND      208    210
FT   HELIX       211    213
FT   STRAND      215    218
FT   HELIX       223    225
FT   STRAND      227    235
FT   STRAND      238    249
FT   STRAND      266    269
FT   STRAND      274    277
FT   STRAND      287    293
FT   STRAND      296    298
FT   STRAND      299    301
FT   STRAND      309    313
FT   STRAND      315    319
FT   TURN        321    325
FT   STRAND      326    329
FT   HELIX       334    336
FT   STRAND      338    345
FT   STRAND      350    357
FT   TURN        463    465
FT   TURN        472    474
FT   HELIX       478    480
FT   STRAND      481    489
FT   STRAND      494    500
FT   STRAND      504    506
FT   STRAND      513    518
FT   HELIX       525    541
FT   STRAND      550    554
FT   STRAND      556    558
FT   STRAND      561    565
FT   STRAND      568    571
FT   HELIX       572    577
FT   TURN        582    585
FT   HELIX       594    596
FT   HELIX       600    619
FT   HELIX       629    631
FT   STRAND      632    634
FT   TURN        636    638
FT   STRAND      640    642
FT   HELIX       645    647
FT   TURN        652    654
FT   STRAND      655    658
FT   TURN        659    664
FT   HELIX       667    669
FT   HELIX       672    677
FT   HELIX       682    697
FT   HELIX       709    718
FT   STRAND      726    728
FT   HELIX       730    739
FT   HELIX       744    746
FT   HELIX       750    764
SQ   SEQUENCE   821 AA;  92025 MW;  6CD5001C960ED82F CRC64;
     MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEVY VAAPGESLEV
     RCLLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAS RTVDSETWYF
     MVNVTDAISS GDDEDDTDGA EDFVSENSNN KRAPYWTNTE KMEKRLHAVP AANTVKFRCP
     AGGNPMPTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CVVENEYGSI
     NHTYHLDVVE RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK
     YGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI SFHSAWLTVL
     PAPGREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVILCRM KNTTKKPDFS SQPAVHKLTK
     RIPLRRQVTV SAESSSSMNS NTPLVRITTR LSSTADTPML AGVSEYELPE DPKWEFPRDK
     LTLGKPLGEG CFGQVVMAEA VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM
     IGKHKNIINL LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF
     KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD INNIDYYKKT
     TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH
     RMDKPANCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEEYL DLSQPLEQYS
     PSYPDTRSSC SSGDDSVFSP DPMPYEPCLP QYPHINGSVK T
//
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