FGFR2_HUMAN
ID FGFR2_HUMAN Reviewed; 821 AA.
AC P21802; B4DFC2; E7EVR6; E9PCR0; P18443; Q01742; Q12922; Q14300; Q14301;
AC Q14302; Q14303; Q14304; Q14305; Q14672; Q14718; Q14719; Q1KHY5; Q86YI4;
AC Q8IXC7; Q96KL9; Q96KM0; Q96KM1; Q96KM2; Q9NZU2; Q9NZU3; Q9UD01; Q9UD02;
AC Q9UIH3; Q9UIH4; Q9UIH5; Q9UIH6; Q9UIH7; Q9UIH8; Q9UM87; Q9UMC6; Q9UNS7;
AC Q9UQH7; Q9UQH8; Q9UQH9; Q9UQI0;
DT 01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1991, sequence version 1.
DT 03-AUG-2022, entry version 264.
DE RecName: Full=Fibroblast growth factor receptor 2;
DE Short=FGFR-2;
DE EC=2.7.10.1 {ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:18056630, ECO:0000269|PubMed:19410646, ECO:0000269|PubMed:21454610};
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; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Neonatal brain stem;
RX PubMed=1697263; DOI=10.1002/j.1460-2075.1990.tb07454.x;
RA Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G., Ruta M.,
RA 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 10).
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 11).
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., Sakamoto H.,
RA Katoh O., Yoshida T., Sugimura T., Terada M.;
RT "K-sam, an amplified gene in stomach cancer, is a member of the heparin-
RT 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; 8; 9 AND 16).
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 tyrosine
RT kinase.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:2960-2964(1992).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 16), DOMAIN, AND SUBUNIT.
RC TISSUE=Placenta;
RX PubMed=1400433; DOI=10.1016/s0021-9258(19)36821-8;
RA Dell K.R., Williams L.T.;
RT "A novel form of fibroblast growth factor receptor 2. Alternative splicing
RT of the third immunoglobulin-like domain confers ligand binding
RT specificity.";
RL J. Biol. Chem. 267:21225-21229(1992).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3; 13 AND 16), 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: two
RT 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 13).
RC TISSUE=Cornea, and Mammary gland;
RX PubMed=7866434;
RA Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., Shay J.W.;
RT "Hepatocyte growth factor (HGF), keratinocyte growth factor (KGF), and
RT their receptors in human breast cells and tissues: alternative receptors.";
RL Cell. Mol. Biol. Res. 40:337-350(1994).
RN [9]
RP ERRATUM OF PUBMED:7866434.
RA Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., 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], AND 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 homology-
RT mediated recombination, generating preferential expression of specific
RT messenger RNAs.";
RL Cancer Res. 59:6080-6086(1999).
RN [12]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 5; 6; 7; 8 AND 12).
RX PubMed=11856867; DOI=10.1159/000048802;
RA Ingersoll R.G., Paznekas W.A., Tran A.K., Scott A.F., Jiang G., 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 (FGFR2)
RT gene in humans.";
RL Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
RN [14]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 17).
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 15).
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., 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 14).
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 project:
RT 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 syndrome
RT 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 (ISOFORMS
RP 5; 8 AND 12).
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 TRP-252 AND
RP ARG-253.
RX PubMed=7668257;
RA Park W.-J., Theda C., Maestri N.E., Meyers G.A., Fryburg J.S., Dufresne C.,
RA Cohen M.M. Jr., Jabs E.W.;
RT "Analysis of phenotypic features and FGFR2 mutations in Apert 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 growth
RT factor receptor 2 and rapid mutational analysis in Apert 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., Stenman G.,
RA 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., Losken H.W.,
RA 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 growth
RT factor receptor.";
RL Biochemistry 35:15640-15645(1996).
RN [26]
RP INTERACTION WITH FGF1; FGF2; FGF3; FGF4; FGF6; FGF7 AND FGF9, AND FUNCTION
RP 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., Coulier F.,
RA Gao G., Goldfarb M.;
RT "Receptor specificity of the fibroblast growth factor family.";
RL J. Biol. Chem. 271:15292-15297(1996).
RN [27]
RP INVOLVEMENT IN SCS, AND VARIANT SCS 269-VAL-VAL-270 DEL.
RX PubMed=9585583; DOI=10.1086/301855;
RA Paznekas W.A., Cunningham M.L., Howard T.D., Korf B.R., Lipson M.H.,
RA Grix A.W., Feingold M., Goldberg R., Borochowitz Z., Aleck K., Mulliken J.,
RA Yin M., Jabs E.W.;
RT "Genetic heterogeneity of Saethre-Chotzen syndrome, due to TWIST and FGFR
RT mutations.";
RL Am. J. Hum. Genet. 62:1370-1380(1998).
RN [28]
RP FUNCTION IN PHOSPHORYLATION OF PAK4; REGULATION OF CELL PROLIFERATION AND
RP 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 [29]
RP FUNCTION IN OSTEOBLAST DIFFERENTIATION AND IN PHOSPHORYLATION OF CBL,
RP INTERACTION WITH CBL, UBIQUITINATION, AND CHARACTERIZATION OF VARIANT APRS
RP 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 fibroblast
RT growth factor receptor-2 activation supports osteoblast differentiation.";
RL J. Biol. Chem. 279:36259-36267(2004).
RN [30]
RP FUNCTION IN CELL PROLIFERATION AND ACTIVATION OF SIGNALING PATHWAYS,
RP MUTAGENESIS OF TYR-769, PHOSPHORYLATION AT TYR-769, AND INTERACTION WITH
RP 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 for
RT receptor signaling but not endocytosis.";
RL Biochem. Biophys. Res. Commun. 327:523-532(2005).
RN [31]
RP INTERACTION WITH FGF1; FGF7; FGF8; FGF9; FGF10; FGF19; FGF21; FGF22 AND
RP 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., Ornitz D.M.;
RT "Receptor specificity of the fibroblast growth factor family. The complete
RT mammalian FGF family.";
RL J. Biol. Chem. 281:15694-15700(2006).
RN [32]
RP FUNCTION IN PHOSPHORYLATION OF PLCG1 (ISOFORM 1), CATALYTIC ACTIVITY,
RP AUTOPHOSPHORYLATION, GLYCOSYLATION, INTERACTION WITH PLCG1, SUBCELLULAR
RP LOCATION, MUTAGENESIS OF ASN-265 AND 656-TYR-TYR-657, UBIQUITINATION, AND
RP 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 [33]
RP INTERACTION WITH FGF19; FGF21 AND KLB, AND FUNCTION IN PHOSPHORYLATION OF
RP 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., Eliseenkova A.V.,
RA Mohammadi M., Rosenblatt K.P., Kliewer S.A., Kuro-o M.;
RT "Tissue-specific expression of betaKlotho and fibroblast growth factor
RT (FGF) receptor isoforms determines metabolic activity of FGF19 and FGF21.";
RL J. Biol. Chem. 282:26687-26695(2007).
RN [34]
RP FUNCTION IN STAT1 PHOSPHORYLATION, GLYCOSYLATION, SUBCELLULAR LOCATION, AND
RP 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 the
RT Golgi apparatus without translocation to the nucleus.";
RL J. Cell. Physiol. 212:148-156(2007).
RN [35]
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 [36]
RP FUNCTION AS FGF7 RECEPTOR AND IN PHOSPHORYLATION OF PLCG1 AND FRS2,
RP CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-466; TYR-586; TYR-588; TYR-656
RP 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 [37]
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 signaling
RT contribute to the transforming activity of the fibroblast growth factor
RT receptor 2 IIIb C3 isoform.";
RL J. Biol. Chem. 284:6227-6240(2009).
RN [38]
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 [39]
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 decreased
RT Cbl-mediated platelet-derived growth factor receptor alpha and fibroblast
RT growth factor receptor 2 ubiquitination.";
RL J. Biol. Chem. 286:24443-24450(2011).
RN [40]
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 [41]
RP REVIEW ON LIGAND SPECIFICITY, ALTERNATIVE SPLICING, SIGNALING, AND ROLE IN
RP 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 [42]
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 [43]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-780, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [44]
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 of
RT ligand-receptor specificity.";
RL Cell 101:413-424(2000).
RN [45]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 148-366 IN COMPLEX WITH FGF1 AND
RP 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 bound to
RT ligand and heparin.";
RL Nature 407:1029-1034(2000).
RN [46]
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 [47]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-366 OF VARIANTS APRS TRP-252
RP 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 in
RT Apert syndrome.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001).
RN [48]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-371 IN COMPLEX WITH FGF10.
RX PubMed=12591959; DOI=10.1073/pnas.0436500100;
RA Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D.,
RA 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 [49]
RP X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 149-368 IN COMPLEX WITH FGF8,
RP FUNCTION AS FGF8 RECEPTOR, INTERACTION WITH FGF8, AND DISULFIDE 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 organizer
RT activity of FGF8 in the brain.";
RL Genes Dev. 20:185-198(2006).
RN [50]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP
RP ANALOG; PEPTIDE SUBSTRATE AND MAGNESIUM, ACTIVITY REGULATION,
RP PHOSPHORYLATION AT TYR-586; TYR-656 AND TYR-657, MUTAGENESIS OF ASN-549 AND
RP GLU-565, CHARACTERIZATION OF VARIANT FSPC GLU-526, CHARACTERIZATION OF
RP VARIANT CS HIS-549, CHARACTERIZATION OF VARIANTS PS GLY-565 AND ARG-641,
RP AND CHARACTERIZATION OF VARIANT 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., Miller W.T.,
RA Mohammadi M.;
RT "A molecular brake in the kinase hinge region regulates the activity of
RT receptor tyrosine kinases.";
RL Mol. Cell 27:717-730(2007).
RN [51]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 458-766 OF VARIANT LADDS THR-628
RP 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: Implications
RT for FGFR autoinhibition and activation.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:19802-19807(2007).
RN [52]
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 458-778 IN COMPLEX WITH ATP,
RP ACTIVE SITE, IDENTIFICATION BY MASS SPECTROMETRY, AUTOPHOSPHORYLATION, AND
RP PHOSPHORYLATION AT TYR-466; TYR-586; TYR-588; TYR-656; TYR-657 AND 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 action.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:19660-19665(2008).
RN [53]
RP X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 458-768 IN COMPLEX WITH
RP INHIBITOR, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, AND ACTIVITY
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 motifs of
RT autoinhibited kinases: discovery of ATP-independent inhibitors of
RT fibroblast growth factor receptor.";
RL J. Biol. Chem. 286:20677-20687(2011).
RN [54]
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., Malcolm S.;
RT "Mutations in the fibroblast growth factor receptor 2 gene cause Crouzon
RT syndrome.";
RL Nat. Genet. 8:98-103(1994).
RN [55]
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 [56]
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 [57]
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., Jones M.C.,
RA Jabs E.W.;
RT "Novel FGFR2 mutations in Crouzon and Jackson-Weiss syndromes show allelic
RT heterogeneity and phenotypic variability.";
RL Hum. Mol. Genet. 4:1229-1233(1995).
RN [58]
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., Renier D.;
RT "FGFR2 mutations in Pfeiffer syndrome.";
RL Nat. Genet. 9:108-108(1995).
RN [59]
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 allelic
RT with Crouzon syndrome.";
RL Nat. Genet. 9:165-172(1995).
RN [60]
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., Jones B.M.,
RA Malcolm S., Winter R.M., Oldridge M., Slaney S.F., Poole M.D.,
RA 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 [61]
RP VARIANTS CS GLY-268 INS; PHE-342 AND TYR-342, VARIANTS PS PHE-278; ARG-342;
RP 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., Abrams L.J.,
RA Graham J.M. Jr., Feingold M., Moeschler J.B., Rawnsley E., Scott A.F.,
RA Jabs E.W.;
RT "FGFR2 exon IIIa and IIIc mutations in Crouzon, Jackson-Weiss, and Pfeiffer
RT syndromes: evidence for missense changes, insertions, and a deletion due to
RT alternative RNA splicing.";
RL Am. J. Hum. Genet. 58:491-498(1996).
RN [62]
RP VARIANTS CS CYS-105; GLU-338; CYS-351 AND ARG-384.
RX PubMed=8946174; DOI=10.1159/000472215;
RA Pulleyn L.J., Reardon W., Wilkes D., Rutland P., Jones B.M., Hayward R.,
RA Hall C.M., Brueton L., Chun N., Lammer E., Malcolm S., Winter R.M.;
RT "Spectrum of craniosynostosis phenotypes associated with novel mutations at
RT the fibroblast growth factor receptor 2 locus.";
RL Eur. J. Hum. Genet. 4:283-291(1996).
RN [63]
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>3.0.co;2-z;
RA Steinberger D., Mulliken J.B., Mueller U.;
RT "Crouzon syndrome: previously unrecognized deletion, duplication, and point
RT mutation within FGFR2 gene.";
RL Hum. Mutat. 8:386-390(1996).
RN [64]
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., Bamshad M.J.,
RA Carey J.C., Hall B.D., Stevenson R., Orlow S.J., Cohen M.M. Jr., Jabs E.W.;
RT "Fibroblast growth factor receptor 2 mutations in Beare-Stevenson cutis
RT gyrata syndrome.";
RL Nat. Genet. 13:492-494(1996).
RN [65]
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 receptor 2
RT (FGFR2) gene is associated with Pfeiffer syndrome.";
RL Hum. Genet. 99:602-606(1997).
RN [66]
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 disorders.";
RL Hum. Genet. 101:47-50(1997).
RN [67]
RP VARIANT LEU-252, VARIANT APRS PHE-252, AND VARIANT PS 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 IgII-
RT IgIII linker of FGFR2.";
RL Hum. Mol. Genet. 6:137-143(1997).
RN [68]
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 with
RT Crouzon phenotype and plagiocephaly.";
RL J. Med. Genet. 34:420-422(1997).
RN [69]
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>3.0.co;2-m;
RA Passos-Bueno M.R., Sertie A.L., Richieri-Costa A., Alonso L.G., Zatz M.,
RA Alonso N., Brunoni D., Ribeiro S.F.M.;
RT "Description of a new mutation and characterization of FGFR1, FGFR2, and
RT FGFR3 mutations among Brazilian patients with syndromic craniosynostoses.";
RL Am. J. Med. Genet. 78:237-241(1998).
RN [70]
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 five
RT structural elements of immunoglobulin-like domain III of the receptor.";
RL Hum. Genet. 102:145-150(1998).
RN [71]
RP VARIANTS APRS TRP-252 AND ARG-253.
RX PubMed=9452027; DOI=10.1002/humu.1380110106;
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 factor
RT receptor 2 (FGFR2) gene in Chinese patients with Apert syndrome.";
RL Hum. Mutat. Suppl. 1:S18-S19(1998).
RN [72]
RP VARIANT PS CYS-351.
RX PubMed=9693549; DOI=10.1097/00001665-199805000-00004;
RA Mathijssen I.M., Vaandrager J.M., Hoogeboom A.J., Hesseling-Janssen A.L.W.,
RA van den Ouweland A.M.W.;
RT "Pfeiffer's syndrome resulting from an S351C mutation in the fibroblast
RT growth factor receptor-2 gene.";
RL J. Craniofac. Surg. 9:207-209(1998).
RN [73]
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 without
RT severe syndactyly.";
RL J. Med. Genet. 35:677-679(1998).
RN [74]
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 apparent
RT nonpenetrance.";
RL Cleft Palate Craniofac. J. 36:533-541(1999).
RN [75]
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 [76]
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 in
RT the FGFR2 gene.";
RL Clin. Genet. 58:81-83(2000).
RN [77]
RP VARIANTS CS/PS ARG-342 AND TYR-342, VARIANTS CS LEU-263; VAL-276; PHE-278;
RP TYR-278; SER-288; PRO-289; PRO-341; TRP-342; CYS-354; TYR-354 AND PHE-359,
RP AND VARIANT PS SER-342.
RX PubMed=11173845; DOI=10.1159/000056833;
RA Kress W., Collmann H., Buesse M., Halliger-Keller B., Mueller C.R.;
RT "Clustering of FGFR2 gene mutations in patients with Pfeiffer and Crouzon
RT syndromes (FGFR2-associated craniosynostoses).";
RL Cytogenet. Cell Genet. 91:134-137(2000).
RN [78]
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 [79]
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 [80]
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 [81]
RP VARIANTS CS CYS-105; PRO-267; VAL-276; CYS-281; PRO-289; ARG-338; HIS-340;
RP PHE-342; TRP-342; CYS-347; CYS-354; HIS-549 AND GLY-678, VARIANTS PS
RP PHE-172; 252-PHE-SER-253; CYS-290; CYS-340; PRO-341; ARG-342; SER-342;
RP CYS-375; GLY-565; ARG-641 AND GLU-663, VARIANTS APRS TRP-252 AND ARG-253,
RP VARIANTS CS/PS PHE-278 AND TYR-342, VARIANT CRANIOSYNOSTOSIS ASN-659, AND
RP 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., Reich E.W.,
RA Tomkins S., Verloes A., Twigg S.R.F., Rannan-Eliya S.,
RA McDonald-McGinn D.M., Zackai E.H., Wall S.A., Muenke M., Wilkie A.O.M.;
RT "Genomic screening of fibroblast growth-factor receptor 2 reveals a wide
RT spectrum of mutations in patients with syndromic craniosynostosis.";
RL Am. J. Hum. Genet. 70:472-486(2002).
RN [82]
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-Stevenson
RT cutis gyrata syndrome.";
RL Clin. Genet. 61:218-221(2002).
RN [83]
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 FGFR2
RT tyrosine kinase domain.";
RL J. Med. Genet. 42:656-662(2005).
RN [84]
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., Lew E.D.,
RA Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M., Leroy J.G.,
RA Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J., Yueksel-Apak M.,
RA Nuernberg P., Kubisch C., Schlessinger J., van Bokhoven H., Wollnik B.;
RT "Mutations in different components of FGF signaling in LADD syndrome.";
RL Nat. Genet. 38:414-417(2006).
RN [85]
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [86]
RP VARIANTS [LARGE SCALE ANALYSIS] LEU-57; THR-186; CYS-203; VAL-272; ASN-283;
RP CYS-290 AND THR-612.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
RN [87]
RP VARIANTS BBDS ASP-381 AND ARG-391, AND CHARACTERIZATION OF VARIANT BBDS
RP 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., Estrada K.D.,
RA Lyons K.M., Deixler H., Robinson H., Chitayat D., Curry C.J., Lachman R.S.,
RA 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).
RN [88]
RP VARIANT LEU-57.
RX PubMed=26429889; DOI=10.1136/jmedgenet-2015-103336;
RA Perles Z., Moon S., Ta-Shma A., Yaacov B., Francescatto L., Edvardson S.,
RA Rein A.J., Elpeleg O., Katsanis N.;
RT "A human laterality disorder caused by a homozygous deleterious mutation in
RT MMP21.";
RL J. Med. Genet. 52:840-847(2015).
CC -!- FUNCTION: Tyrosine-protein kinase that acts as cell-surface receptor
CC for fibroblast growth factors and plays an essential role in the
CC regulation of cell proliferation, differentiation, migration and
CC apoptosis, and in the regulation of embryonic development. Required for
CC normal embryonic patterning, trophoblast function, limb bud
CC development, lung morphogenesis, osteogenesis and skin development.
CC Plays an essential role in the regulation of osteoblast
CC differentiation, proliferation and apoptosis, and is required for
CC normal skeleton development. Promotes cell proliferation in
CC keratinocytes and immature osteoblasts, but promotes apoptosis in
CC differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand
CC binding leads to the activation of several signaling cascades.
CC Activation of PLCG1 leads to the production of the cellular signaling
CC molecules diacylglycerol and inositol 1,4,5-trisphosphate.
CC Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and
CC SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the
CC MAP kinase signaling pathway, as well as of the AKT1 signaling pathway.
CC FGFR2 signaling is down-regulated by ubiquitination, internalization
CC and degradation. Mutations that lead to constitutive kinase activation
CC or impair normal FGFR2 maturation, internalization and degradation lead
CC to aberrant signaling. Over-expressed FGFR2 promotes activation of
CC STAT1. {ECO:0000269|PubMed:12529371, ECO:0000269|PubMed:15190072,
CC ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16384934,
CC ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277,
CC ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18374639,
CC ECO:0000269|PubMed:19103595, ECO:0000269|PubMed:19387476,
CC ECO:0000269|PubMed:19410646, ECO:0000269|PubMed:21596750,
CC ECO:0000269|PubMed:8663044}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-
CC [protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-
CC COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858,
CC ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU10028,
CC ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:18056630,
CC ECO:0000269|PubMed:19410646, ECO:0000269|PubMed:21454610};
CC -!- ACTIVITY REGULATION: Present in an inactive conformation in the absence
CC of bound ligand. Ligand binding leads to dimerization and activation by
CC autophosphorylation on tyrosine residues. Inhibited by ARQ 523 and ARQ
CC 069; these compounds maintain the kinase in an inactive conformation
CC and inhibit autophosphorylation. {ECO:0000269|PubMed:17803937,
CC 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 vitro).
CC Ligand specificity is determined by tissue-specific expression of
CC isoforms, and differences in the third Ig-like domain are crucial for
CC ligand specificity. Isoform 1 has high affinity for FGF1 and FGF2, but
CC low affinity for FGF7. Isoform 3 has high affinity for FGF1 and FGF7,
CC and has much higher affinity for FGF7 than isoform 1 (in vitro).
CC Affinity for fibroblast growth factors (FGFs) is increased by heparan
CC sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB
CC increases the affinity for FGF19 and FGF21. Interacts with PLCG1, GRB2
CC and PAK4. Interacts with FLRT2 (By similarity).
CC {ECO:0000250|UniProtKB:P21803, ECO:0000269|PubMed:10618369,
CC ECO:0000269|PubMed:10830168, ECO:0000269|PubMed:11069186,
CC ECO:0000269|PubMed:11390973, ECO:0000269|PubMed:12529371,
CC ECO:0000269|PubMed:12591959, ECO:0000269|PubMed:1309608,
CC ECO:0000269|PubMed:1400433, ECO:0000269|PubMed:15190072,
CC ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16384934,
CC ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:16844695,
CC ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:17803937,
CC ECO:0000269|PubMed:18056630, ECO:0000269|PubMed:19060208,
CC ECO:0000269|PubMed:19103595, ECO:0000269|PubMed:21454610,
CC ECO:0000269|PubMed:8663044, ECO:0000269|PubMed:8961926}.
CC -!- INTERACTION:
CC P21802; P05230: FGF1; NbExp=2; IntAct=EBI-1028658, EBI-698068;
CC P21802; PRO_0000008908 [P05230]: FGF1; NbExp=5; IntAct=EBI-1028658, EBI-6880860;
CC P21802; O15520: FGF10; NbExp=2; IntAct=EBI-1028658, EBI-1035684;
CC P21802; P09038: FGF2; NbExp=3; IntAct=EBI-1028658, EBI-977447;
CC P21802; P09038-2: FGF2; NbExp=2; IntAct=EBI-1028658, EBI-11122080;
CC P21802; P62993: GRB2; NbExp=5; IntAct=EBI-1028658, EBI-401755;
CC P21802; P03968: FGF1; Xeno; NbExp=2; IntAct=EBI-1028658, EBI-6358090;
CC P21802-1; P05230-1: FGF1; NbExp=2; IntAct=EBI-15489960, EBI-15489950;
CC P21802-1; P09038: FGF2; NbExp=2; IntAct=EBI-15489960, EBI-977447;
CC P21802-1; P21802-1: FGFR2; NbExp=3; IntAct=EBI-15489960, EBI-15489960;
CC P21802-1; P19174: PLCG1; NbExp=9; IntAct=EBI-15489960, EBI-79387;
CC P21802-3; P21781: FGF7; NbExp=2; IntAct=EBI-6354683, EBI-3937699;
CC P21802-3; P03968: FGF1; Xeno; NbExp=2; IntAct=EBI-6354683, EBI-6358090;
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 receptor is
CC rapidly internalized and degraded.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I
CC membrane protein. Note=After ligand binding, the activated receptor is
CC rapidly internalized and degraded.
CC -!- SUBCELLULAR LOCATION: [Isoform 8]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 13]: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=17;
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-IIC3;
CC IsoId=P21802-8; Sequence=VSP_002975, VSP_002978;
CC Name=8; Synonyms=K-sam-IV, Soluble KGFR;
CC IsoId=P21802-14; Sequence=VSP_002965, VSP_002966;
CC Name=9; Synonyms=K-sam-III;
CC IsoId=P21802-15; Sequence=VSP_002968;
CC Name=10; Synonyms=TK14;
CC IsoId=P21802-16; Sequence=VSP_002967, VSP_002975;
CC Name=11;
CC IsoId=P21802-17; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC VSP_002972, VSP_002978;
CC Name=12; Synonyms=K-sam-IIC1, KGFR, IgIIIb;
CC IsoId=P21802-18; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC VSP_002972, VSP_002975;
CC Name=13; Synonyms=Soluble KGFR;
CC IsoId=P21802-19; Sequence=VSP_002969, VSP_002970, VSP_002971,
CC VSP_002972, VSP_002973, VSP_002974;
CC Name=14;
CC IsoId=P21802-20; Sequence=VSP_019608, VSP_019609;
CC Name=15;
CC IsoId=P21802-21; Sequence=VSP_002964, VSP_041915;
CC Name=16;
CC IsoId=P21802-22; Sequence=VSP_002964, VSP_002969, VSP_002970,
CC VSP_002971, VSP_002972, VSP_002978;
CC Name=17;
CC IsoId=P21802-23; Sequence=VSP_041914;
CC -!- DOMAIN: The second and third Ig-like domains directly interact with
CC fibroblast growth factors (FGF) and heparan sulfate proteoglycans.
CC Alternative splicing events affecting the third Ig-like domain are
CC crucial for ligand selectivity. {ECO:0000269|PubMed:1309608,
CC ECO:0000269|PubMed:1400433, ECO:0000269|PubMed:8961926}.
CC -!- PTM: Autophosphorylated. Binding of FGF family members together with
CC heparan sulfate proteoglycan or heparin promotes receptor dimerization
CC 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 chains
CC undergo further maturation to an Endo H-resistant form in the Golgi
CC apparatus. {ECO:0000269|PubMed:16844695, 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, exophthalmos
CC and external strabismus, parrot-beaked nose, short upper lip,
CC hypoplastic maxilla, and a relative mandibular prognathism.
CC {ECO:0000269|PubMed:10574673, ECO:0000269|PubMed:11173845,
CC ECO:0000269|PubMed:11380921, ECO:0000269|PubMed:11781872,
CC ECO:0000269|PubMed:17803937, 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:9152842,
CC ECO:0000269|PubMed:9521581, ECO:0000269|PubMed:9677057,
CC ECO:0000269|Ref.10}. Note=The disease is caused by variants affecting
CC the gene represented in this 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 medial
CC 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 variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Apert syndrome (APRS) [MIM:101200]: A syndrome characterized
CC by facio-cranio-synostosis, osseous and membranous syndactyly of the
CC four extremities, and midface hypoplasia. The craniosynostosis is
CC bicoronal and results in acrocephaly of brachysphenocephalic type.
CC Syndactyly of the fingers and toes may be total (mitten hands and sock
CC feet) or partial affecting the second, third, and fourth digits.
CC Intellectual deficit is frequent and often severe, usually being
CC associated with cerebral malformations. {ECO:0000269|PubMed:11390973,
CC ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:15190072,
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 variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Pfeiffer syndrome (PS) [MIM:101600]: A syndrome characterized
CC by the association of craniosynostosis, broad and deviated thumbs and
CC big toes, and partial syndactyly of the fingers and toes. Three
CC subtypes are known: mild autosomal dominant form (type 1); cloverleaf
CC skull, elbow ankylosis, early death, sporadic (type 2);
CC craniosynostosis, early demise, sporadic (type 3).
CC {ECO:0000269|PubMed:10394936, ECO:0000269|PubMed:10945669,
CC ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11781872,
CC ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:17803937,
CC ECO:0000269|PubMed:7719333, ECO:0000269|PubMed:7719345,
CC ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9002682,
CC ECO:0000269|PubMed:9150725, ECO:0000269|PubMed:9693549,
CC ECO:0000269|PubMed:9719378}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Beare-Stevenson cutis gyrata syndrome (BSTVS) [MIM:123790]: An
CC autosomal dominant disease characterized by craniofacial anomalies,
CC particularly craniosynostosis, and ear defects, cutis gyrata,
CC acanthosis nigricans, anogenital anomalies, skin tags, and prominent
CC umbilical stump. The skin furrows have a corrugated appearance and are
CC widespread. Cutis gyrata variably affects the scalp, forehead, face,
CC preauricular area, neck, trunk, hands, and feet.
CC {ECO:0000269|PubMed:12000365, ECO:0000269|PubMed:8696350}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Familial scaphocephaly syndrome (FSPC) [MIM:609579]: An
CC autosomal dominant craniosynostosis syndrome characterized by
CC scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and
CC mild intellectual disability. Scaphocephaly is the most common of the
CC craniosynostosis conditions and is characterized by a long, narrow
CC head. It is due to premature fusion of the sagittal suture or from
CC external deformation. {ECO:0000269|PubMed:16061565,
CC ECO:0000269|PubMed:17803937}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]:
CC An autosomal dominant ectodermal dysplasia, a heterogeneous group of
CC disorders due to abnormal development of two or more ectodermal
CC structures. Lacrimo-auriculo-dento-digital syndrome is characterized by
CC aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped
CC ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb
CC segments anomalies. In addition to these cardinal features, facial
CC dysmorphism, malformations of the kidney and respiratory system and
CC abnormal genitalia have been reported. Craniosynostosis and severe
CC syndactyly are not observed. {ECO:0000269|PubMed:16501574,
CC ECO:0000269|PubMed:18056630}. Note=The disease is caused by variants
CC affecting the gene 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 from
CC the perinatal period, midface hypoplasia, choanal stenosis or atresia,
CC femoral bowing and multiple joint contractures. Arachnodactyly and/or
CC camptodactyly have also been reported. {ECO:0000269|PubMed:10633130}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- DISEASE: Bent bone dysplasia syndrome (BBDS) [MIM:614592]: A perinatal
CC lethal skeletal dysplasia characterized by poor mineralization of the
CC calvarium, craniosynostosis, dysmorphic facial features, prenatal
CC teeth, hypoplastic pubis and clavicles, osteopenia, and bent long
CC bones. Dysmorphic facial features included low-set ears, hypertelorism,
CC midface hypoplasia, prematurely erupted fetal teeth, and micrognathia.
CC {ECO:0000269|PubMed:22387015}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Saethre-Chotzen syndrome (SCS) [MIM:101400]: A
CC craniosynostosis syndrome characterized by coronal synostosis,
CC brachycephaly, low frontal hairline, facial asymmetry, hypertelorism,
CC broad halluces, and clinodactyly. {ECO:0000269|PubMed:9585583}.
CC Note=The disease is caused by variants affecting the gene represented
CC 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 -!- SEQUENCE CAUTION:
CC Sequence=BAA89296.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Somatic variant that appeared in a cancer cell line as a result of genome instability.; Evidence={ECO:0000305|PubMed:10626794};
CC Sequence=BAA89297.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Somatic variant that appeared in a cancer cell line as a result of genome instability.; Evidence={ECO:0000305|PubMed:10626794};
CC Sequence=BAA89298.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Somatic variant that appeared in a cancer cell line as a result of genome instability.; Evidence={ECO:0000305|PubMed:10626794};
CC Sequence=BAA89299.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Somatic variant that appeared in a cancer cell line as a result of genome instability.; Evidence={ECO:0000305|PubMed:10626794};
CC Sequence=BAA89300.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Somatic variant that appeared in a cancer cell line as a result of genome instability.; Evidence={ECO:0000305|PubMed:10626794};
CC Sequence=BAA89301.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Somatic variant that appeared in a cancer cell line as a result of genome instability.; Evidence={ECO:0000305|PubMed:10626794};
CC Sequence=BAG57383.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC 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; ALT_SEQ; mRNA.
DR EMBL; AB030074; BAA89297.1; ALT_SEQ; mRNA.
DR EMBL; AB030075; BAA89298.1; ALT_SEQ; mRNA.
DR EMBL; AB030076; BAA89299.1; ALT_SEQ; mRNA.
DR EMBL; AB030077; BAA89300.1; ALT_SEQ; mRNA.
DR EMBL; AB030078; BAA89301.1; ALT_SEQ; 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 CCDS; CCDS81515.1; -. [P21802-5]
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_001307583.1; NM_001320654.1.
DR RefSeq; NP_001307587.1; NM_001320658.1. [P21802-5]
DR RefSeq; NP_075259.4; NM_022970.3. [P21802-3]
DR RefSeq; NP_075418.1; NM_023029.2.
DR PDB; 1DJS; X-ray; 2.40 A; A=153-362.
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 PDB; 4WV1; X-ray; 2.36 A; C/F=153-251.
DR PDB; 5EG3; X-ray; 2.61 A; A=458-778.
DR PDB; 5UGL; X-ray; 1.86 A; A/B=458-768.
DR PDB; 5UGX; X-ray; 2.35 A; A/B=458-768.
DR PDB; 5UHN; X-ray; 2.91 A; A/B=458-768.
DR PDB; 5UI0; X-ray; 2.05 A; A/B=458-768.
DR PDB; 6AGX; X-ray; 2.95 A; A/B/C/D=467-764.
DR PDB; 6LVK; X-ray; 2.29 A; A/B=459-768.
DR PDB; 6LVL; X-ray; 2.98 A; A/B=459-768.
DR PDB; 6V6Q; X-ray; 2.46 A; A/B/C/D=413-821.
DR PDB; 7KIA; X-ray; 2.22 A; A/B=461-768.
DR PDB; 7KIE; X-ray; 2.47 A; A/B=461-768.
DR PDB; 7OZY; X-ray; 2.28 A; AAA/BBB=465-763.
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 PDBsum; 4WV1; -.
DR PDBsum; 5EG3; -.
DR PDBsum; 5UGL; -.
DR PDBsum; 5UGX; -.
DR PDBsum; 5UHN; -.
DR PDBsum; 5UI0; -.
DR PDBsum; 6AGX; -.
DR PDBsum; 6LVK; -.
DR PDBsum; 6LVL; -.
DR PDBsum; 6V6Q; -.
DR PDBsum; 7KIA; -.
DR PDBsum; 7KIE; -.
DR PDBsum; 7OZY; -.
DR AlphaFoldDB; P21802; -.
DR BMRB; P21802; -.
DR SMR; P21802; -.
DR BioGRID; 108554; 128.
DR CORUM; P21802; -.
DR DIP; DIP-3788N; -.
DR IntAct; P21802; 89.
DR MINT; P21802; -.
DR STRING; 9606.ENSP00000410294; -.
DR BindingDB; P21802; -.
DR ChEMBL; CHEMBL4142; -.
DR DrugBank; DB02058; 3-[4-(1-formylpiperazin-4-yl)-benzylidenyl]-2-indolinone.
DR DrugBank; DB02491; 4-[4-(1-Amino-1-Methylethyl)Phenyl]-5-Chloro-N-[4-(2-Morpholin-4-Ylethyl)Phenyl]Pyrimidin-2-Amine.
DR DrugBank; DB12147; Erdafitinib.
DR DrugBank; DB10770; Foreskin fibroblast (neonatal).
DR DrugBank; DB10772; Foreskin keratinocyte (neonatal).
DR DrugBank; DB12010; Fostamatinib.
DR DrugBank; DB01109; Heparin.
DR DrugBank; DB11886; Infigratinib.
DR DrugBank; DB09078; Lenvatinib.
DR DrugBank; DB09079; Nintedanib.
DR DrugBank; DB00039; Palifermin.
DR DrugBank; DB15102; Pemigatinib.
DR DrugBank; DB08901; Ponatinib.
DR DrugBank; DB15822; Pralsetinib.
DR DrugBank; DB08896; Regorafenib.
DR DrugBank; DB15685; Selpercatinib.
DR DrugBank; DB01901; Sucrosofate.
DR DrugBank; DB01041; Thalidomide.
DR DrugCentral; P21802; -.
DR GuidetoPHARMACOLOGY; 1809; -.
DR GlyConnect; 1997; 1 N-Linked glycan (1 site).
DR GlyGen; P21802; 9 sites, 1 N-linked glycan (1 site), 1 O-linked glycan (1 site).
DR iPTMnet; P21802; -.
DR PhosphoSitePlus; P21802; -.
DR BioMuta; FGFR2; -.
DR DMDM; 120049; -.
DR EPD; P21802; -.
DR jPOST; P21802; -.
DR MassIVE; P21802; -.
DR MaxQB; P21802; -.
DR PaxDb; P21802; -.
DR PeptideAtlas; P21802; -.
DR PRIDE; P21802; -.
DR ProteomicsDB; 53905; -. [P21802-1]
DR ProteomicsDB; 53910; -. [P21802-14]
DR ProteomicsDB; 53911; -. [P21802-15]
DR ProteomicsDB; 53912; -. [P21802-16]
DR ProteomicsDB; 53913; -. [P21802-17]
DR ProteomicsDB; 53914; -. [P21802-18]
DR ProteomicsDB; 53915; -. [P21802-19]
DR ProteomicsDB; 53916; -. [P21802-2]
DR ProteomicsDB; 53917; -. [P21802-20]
DR ProteomicsDB; 53918; -. [P21802-21]
DR ProteomicsDB; 53919; -. [P21802-22]
DR ProteomicsDB; 53920; -. [P21802-23]
DR ProteomicsDB; 53921; -. [P21802-3]
DR ProteomicsDB; 53922; -. [P21802-4]
DR ProteomicsDB; 53923; -. [P21802-5]
DR ProteomicsDB; 53924; -. [P21802-6]
DR ProteomicsDB; 53926; -. [P21802-8]
DR TopDownProteomics; P21802-8; -. [P21802-8]
DR ABCD; P21802; 5 sequenced antibodies.
DR Antibodypedia; 4393; 1295 antibodies from 47 providers.
DR DNASU; 2263; -.
DR Ensembl; ENST00000346997.6; ENSP00000263451.5; ENSG00000066468.24. [P21802-5]
DR Ensembl; ENST00000351936.11; ENSP00000309878.10; ENSG00000066468.24. [P21802-5]
DR Ensembl; ENST00000356226.8; ENSP00000348559.4; ENSG00000066468.24. [P21802-20]
DR Ensembl; ENST00000357555.9; ENSP00000350166.5; ENSG00000066468.24. [P21802-21]
DR Ensembl; ENST00000358487.10; ENSP00000351276.6; ENSG00000066468.24. [P21802-1]
DR Ensembl; ENST00000359354.6; ENSP00000352309.2; ENSG00000066468.24. [P21802-14]
DR Ensembl; ENST00000360144.7; ENSP00000353262.3; ENSG00000066468.24. [P21802-22]
DR Ensembl; ENST00000369056.5; ENSP00000358052.1; ENSG00000066468.24. [P21802-17]
DR Ensembl; ENST00000369060.8; ENSP00000358056.4; ENSG00000066468.24. [P21802-15]
DR Ensembl; ENST00000369061.8; ENSP00000358057.4; ENSG00000066468.24. [P21802-23]
DR Ensembl; ENST00000457416.6; ENSP00000410294.2; ENSG00000066468.24. [P21802-3]
DR Ensembl; ENST00000682550.1; ENSP00000507633.1; ENSG00000066468.24. [P21802-20]
DR Ensembl; ENST00000683211.1; ENSP00000508257.1; ENSG00000066468.24. [P21802-5]
DR GeneID; 2263; -.
DR KEGG; hsa:2263; -.
DR MANE-Select; ENST00000358487.10; ENSP00000351276.6; NM_000141.5; NP_000132.3.
DR UCSC; uc010qtl.3; human. [P21802-1]
DR CTD; 2263; -.
DR DisGeNET; 2263; -.
DR GeneCards; FGFR2; -.
DR GeneReviews; FGFR2; -.
DR HGNC; HGNC:3689; FGFR2.
DR HPA; ENSG00000066468; Tissue enhanced (brain, choroid plexus).
DR MalaCards; FGFR2; -.
DR MIM; 101200; phenotype.
DR MIM; 101400; 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 OpenTargets; ENSG00000066468; -.
DR Orphanet; 596008; Antley-Bixler syndrome without genital anomaly or disorder of steroidogenesis.
DR Orphanet; 87; Apert syndrome.
DR Orphanet; 207; Crouzon syndrome.
DR Orphanet; 1555; Cutis gyrata-acanthosis nigricans-craniosynostosis syndrome.
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; Lacrimoauriculodentodigital 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 VEuPathDB; HostDB:ENSG00000066468; -.
DR eggNOG; KOG0200; Eukaryota.
DR GeneTree; ENSGT00940000155447; -.
DR HOGENOM; CLU_000288_74_2_1; -.
DR InParanoid; P21802; -.
DR OMA; VFLIVCM; -.
DR OrthoDB; 543832at2759; -.
DR PhylomeDB; P21802; -.
DR TreeFam; TF316307; -.
DR BRENDA; 2.7.10.1; 2681.
DR PathwayCommons; P21802; -.
DR Reactome; R-HSA-109704; PI3K Cascade.
DR Reactome; R-HSA-1257604; PIP3 activates AKT signaling.
DR Reactome; R-HSA-190375; FGFR2c ligand binding and activation.
DR Reactome; R-HSA-190377; FGFR2b ligand binding and activation.
DR Reactome; R-HSA-2023837; Signaling by FGFR2 amplification mutants.
DR Reactome; R-HSA-2033519; Activated point mutants of FGFR2.
DR Reactome; R-HSA-2219530; Constitutive Signaling by Aberrant PI3K in Cancer.
DR Reactome; R-HSA-5654221; Phospholipase C-mediated cascade, FGFR2.
DR Reactome; R-HSA-5654695; PI-3K cascade:FGFR2.
DR Reactome; R-HSA-5654699; SHC-mediated cascade:FGFR2.
DR Reactome; R-HSA-5654700; FRS-mediated FGFR2 signaling.
DR Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-HSA-5655253; Signaling by FGFR2 in disease.
DR Reactome; R-HSA-5673001; RAF/MAP kinase cascade.
DR Reactome; R-HSA-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-8853333; Signaling by FGFR2 fusions.
DR SignaLink; P21802; -.
DR SIGNOR; P21802; -.
DR BioGRID-ORCS; 2263; 23 hits in 1101 CRISPR screens.
DR ChiTaRS; FGFR2; human.
DR EvolutionaryTrace; P21802; -.
DR GeneWiki; Fibroblast_growth_factor_receptor_2; -.
DR GenomeRNAi; 2263; -.
DR Pharos; P21802; Tclin.
DR PRO; PR:P21802; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P21802; protein.
DR Bgee; ENSG00000066468; Expressed in C1 segment of cervical spinal cord and 200 other tissues.
DR ExpressionAtlas; P21802; baseline and differential.
DR Genevisible; P21802; HS.
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:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
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: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:0043235; C:receptor complex; IBA:GO_Central.
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 receptor activity; IDA:UniProtKB.
DR GO; GO:0008201; F:heparin binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical 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:0004714; F:transmembrane receptor protein tyrosine kinase activity; IBA:GO_Central.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0009887; P:animal organ morphogenesis; 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:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0071560; P:cellular response to transforming growth factor beta stimulus; 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:0003416; P:endochondral bone growth; IEA:Ensembl.
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: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 cell; 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:0042472; P:inner ear morphogenesis; ISS:UniProtKB.
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: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:0010839; P:negative regulation of keratinocyte proliferation; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISS:UniProtKB.
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: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: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 population 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:0033674; P:positive regulation of kinase activity; IBA:GO_Central.
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 by RNA polymerase II; 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:0070372; P:regulation of ERK1 and ERK2 cascade; ISS:UniProtKB.
DR GO; GO:0060688; P:regulation of morphogenesis of a branching structure; 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:0045471; P:response to ethanol; IEA:Ensembl.
DR GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
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:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
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 GO; GO:0042060; P:wound healing; IEA:Ensembl.
DR Gene3D; 2.60.40.10; -; 3.
DR IDEAL; IID00546; -.
DR InterPro; IPR016248; FGF_rcpt_fam.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR011009; Kinase-like_dom_sf.
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 Pfam; PF07679; I-set; 2.
DR Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR PIRSF; PIRSF000628; FGFR; 1.
DR PRINTS; PR00109; TYRKINASE.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SMART; SM00219; TyrKc; 1.
DR SUPFAM; SSF48726; SSF48726; 3.
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; Cell membrane;
KW Craniosynostosis; Cytoplasmic vesicle; Disease variant; Disulfide bond;
KW Ectodermal dysplasia; Glycoprotein; Golgi apparatus; Heparin-binding;
KW Immunoglobulin domain; Intellectual disability; Kinase;
KW Lacrimo-auriculo-dento-digital syndrome; Membrane; Nucleotide-binding;
KW Phosphoprotein; Proto-oncogene; Receptor; Reference proteome; Repeat;
KW Secreted; Signal; Transferase; Transmembrane; Transmembrane helix;
KW Tyrosine-protein kinase; Ubl conjugation.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..821
FT /note="Fibroblast growth factor receptor 2"
FT /id="PRO_0000016783"
FT TOPO_DOM 22..377
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 399..821
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..125
FT /note="Ig-like C2-type 1"
FT DOMAIN 154..247
FT /note="Ig-like C2-type 2"
FT DOMAIN 256..358
FT /note="Ig-like C2-type 3"
FT DOMAIN 481..770
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 131..151
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 161..178
FT /note="Heparin-binding"
FT ACT_SITE 626
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10028,
FT ECO:0000269|PubMed:19060208"
FT BINDING 487..495
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:19060208"
FT BINDING 517
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:19060208"
FT BINDING 565..567
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:19060208"
FT BINDING 571
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000269|PubMed:19060208"
FT MOD_RES 466
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19060208,
FT ECO:0000269|PubMed:19410646"
FT MOD_RES 586
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17803937,
FT ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646"
FT MOD_RES 588
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:19060208,
FT ECO:0000269|PubMed:19410646"
FT MOD_RES 656
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17803937,
FT ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646"
FT MOD_RES 657
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:17803937,
FT ECO:0000269|PubMed:19060208, ECO:0000269|PubMed:19410646"
FT MOD_RES 769
FT /note="Phosphotyrosine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:15629145,
FT ECO:0000269|PubMed:19060208"
FT MOD_RES 780
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 83
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 123
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 228
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 297
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 331
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 62..107
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 179..231
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:16384934"
FT DISULFID 278..342
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:16384934"
FT VAR_SEQ 37..152
FT /note="EPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLI
FT GEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSEN
FT SNNKR -> G (in isoform 14)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019608"
FT VAR_SEQ 37..125
FT /note="Missing (in isoform 4, isoform 15 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:2377625"
FT /id="VSP_002964"
FT VAR_SEQ 250..361
FT /note="Missing (in isoform 17)"
FT /evidence="ECO:0000303|Ref.14"
FT /id="VSP_041914"
FT VAR_SEQ 250..254
FT /note="ERSPH -> GSQGL (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:1313574"
FT /id="VSP_002965"
FT VAR_SEQ 255..821
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:1313574"
FT /id="VSP_002966"
FT VAR_SEQ 313
FT /note="K -> KVTK (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:2172978"
FT /id="VSP_002967"
FT VAR_SEQ 314..429
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:1313574"
FT /id="VSP_002968"
FT VAR_SEQ 314..330
FT /note="AAGVNTTDKEIEVLYIR -> HSGINSSNAEVLALF (in isoform 3,
FT isoform 4, isoform 11, isoform 12, isoform 13 and isoform
FT 16)"
FT /evidence="ECO:0000303|PubMed:10626794,
FT ECO:0000303|PubMed:1309608, ECO:0000303|PubMed:1400433,
FT ECO:0000303|PubMed:1647213, ECO:0000303|PubMed:2377625,
FT ECO:0000303|PubMed:7866434"
FT /id="VSP_002969"
FT VAR_SEQ 334..335
FT /note="FE -> EA (in isoform 3, isoform 4, isoform 11,
FT isoform 12, isoform 13 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:10626794,
FT ECO:0000303|PubMed:1309608, ECO:0000303|PubMed:1400433,
FT ECO:0000303|PubMed:1647213, ECO:0000303|PubMed:2377625,
FT ECO:0000303|PubMed:7866434"
FT /id="VSP_002970"
FT VAR_SEQ 341..353
FT /note="TCLAGNSIGISFH -> ICKVSNYIGQANQ (in isoform 3,
FT isoform 4, isoform 11, isoform 12, isoform 13 and isoform
FT 16)"
FT /evidence="ECO:0000303|PubMed:10626794,
FT ECO:0000303|PubMed:1309608, ECO:0000303|PubMed:1400433,
FT ECO:0000303|PubMed:1647213, ECO:0000303|PubMed:2377625,
FT ECO:0000303|PubMed:7866434"
FT /id="VSP_002971"
FT VAR_SEQ 361
FT /note="P -> PKQQ (in isoform 3, isoform 4, isoform 11,
FT isoform 12, isoform 13 and isoform 16)"
FT /evidence="ECO:0000303|PubMed:10626794,
FT ECO:0000303|PubMed:1309608, ECO:0000303|PubMed:1400433,
FT ECO:0000303|PubMed:1647213, ECO:0000303|PubMed:2377625,
FT ECO:0000303|PubMed:7866434"
FT /id="VSP_002972"
FT VAR_SEQ 362..365
FT /note="APGR -> GRRC (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:1309608,
FT ECO:0000303|PubMed:7866434"
FT /id="VSP_002973"
FT VAR_SEQ 366..821
FT /note="Missing (in isoform 13)"
FT /evidence="ECO:0000303|PubMed:1309608,
FT ECO:0000303|PubMed:7866434"
FT /id="VSP_002974"
FT VAR_SEQ 428..429
FT /note="Missing (in isoform 4, isoform 5, isoform 6, isoform
FT 7, isoform 10 and isoform 12)"
FT /evidence="ECO:0000303|PubMed:1313574,
FT ECO:0000303|PubMed:2172978, ECO:0000303|PubMed:2377625"
FT /id="VSP_002975"
FT VAR_SEQ 429..430
FT /note="Missing (in isoform 14)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019609"
FT VAR_SEQ 761..821
FT /note="LTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQY
FT PHINGSVKT -> PPNPSLMSIFRK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:2377625"
FT /id="VSP_002976"
FT VAR_SEQ 768..821
FT /note="EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSV
FT KT -> I (in isoform 2, isoform 7, isoform 11 and isoform
FT 16)"
FT /evidence="ECO:0000303|PubMed:1647213"
FT /id="VSP_002978"
FT VAR_SEQ 769..821
FT /note="YLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVK
FT T -> EKKVSGAVDCHKPPCNPSHLPCVLAVDQ (in isoform 15)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041915"
FT VAR_SEQ 778..821
FT /note="QYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT -> PYSP
FT CYPDPR (in isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_002984"
FT VARIANT 6
FT /note="R -> P (in dbSNP:rs3750819)"
FT /evidence="ECO:0000269|Ref.15"
FT /id="VAR_017258"
FT VARIANT 57
FT /note="S -> L (in dbSNP:rs56226109)"
FT /evidence="ECO:0000269|PubMed:17344846,
FT ECO:0000269|PubMed:26429889"
FT /id="VAR_042204"
FT VARIANT 105
FT /note="Y -> C (in CS; dbSNP:rs1434545235)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:8946174"
FT /id="VAR_004112"
FT VARIANT 172
FT /note="A -> F (in PS; requires 2 nucleotide substitutions)"
FT /evidence="ECO:0000269|PubMed:11781872"
FT /id="VAR_017259"
FT VARIANT 186
FT /note="M -> T (in dbSNP:rs755793)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:17344846, ECO:0000269|Ref.15"
FT /id="VAR_017260"
FT VARIANT 203
FT /note="R -> C (in breast cancer samples; infiltrating
FT ductal carcinoma; somatic mutation)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_036380"
FT VARIANT 252..253
FT /note="SP -> FS (in PS; dbSNP:rs281865420)"
FT /id="VAR_004116"
FT VARIANT 252
FT /note="S -> F (in APRS; requires 2 nucleotide
FT substitutions; dbSNP:rs121918498)"
FT /evidence="ECO:0000269|PubMed:9002682"
FT /id="VAR_004114"
FT VARIANT 252
FT /note="S -> L (in dbSNP:rs79184941)"
FT /evidence="ECO:0000269|PubMed:9002682"
FT /id="VAR_004113"
FT VARIANT 252
FT /note="S -> W (in APRS and PS; common mutation;
FT dbSNP:rs79184941)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:7668257,
FT ECO:0000269|PubMed:7719344, ECO:0000269|PubMed:9452027,
FT ECO:0000269|PubMed:9677057, ECO:0000269|PubMed:9719378"
FT /id="VAR_004115"
FT VARIANT 253
FT /note="P -> R (in APRS; common mutation; dbSNP:rs77543610)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7668257, ECO:0000269|PubMed:7719344,
FT ECO:0000269|PubMed:9452027, ECO:0000269|PubMed:9677057"
FT /id="VAR_004117"
FT VARIANT 263
FT /note="P -> L (in CS; dbSNP:rs779326224)"
FT /evidence="ECO:0000269|PubMed:11173845"
FT /id="VAR_017261"
FT VARIANT 267
FT /note="S -> P (in CS; dbSNP:rs121918505)"
FT /evidence="ECO:0000269|PubMed:11781872"
FT /id="VAR_004118"
FT VARIANT 268
FT /note="T -> TG (in CS)"
FT /evidence="ECO:0000269|PubMed:8644708"
FT /id="VAR_004119"
FT VARIANT 269..270
FT /note="Missing (in SCS)"
FT /evidence="ECO:0000269|PubMed:9585583"
FT /id="VAR_075856"
FT VARIANT 272
FT /note="G -> V (in an ovarian serous carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042205"
FT VARIANT 273
FT /note="Missing (in PS; type 2; dbSNP:rs121918503)"
FT /evidence="ECO:0000269|PubMed:10945669"
FT /id="VAR_017262"
FT VARIANT 276
FT /note="F -> V (in CS; dbSNP:rs1057519036)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:9521581"
FT /id="VAR_004120"
FT VARIANT 278
FT /note="C -> F (in CS, JWS and PS; forms disulfide-linked
FT dimers with constitutive kinase activity, is retained in an
FT intracellular compartment and not detected at the cell
FT surface; dbSNP:rs776587763)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:16844695,
FT ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9677057"
FT /id="VAR_004121"
FT VARIANT 278
FT /note="C -> Y (in CS; dbSNP:rs776587763)"
FT /evidence="ECO:0000269|PubMed:11173845"
FT /id="VAR_017263"
FT VARIANT 281
FT /note="Y -> C (in CS; dbSNP:rs1057519038)"
FT /evidence="ECO:0000269|PubMed:11380921,
FT ECO:0000269|PubMed:11781872"
FT /id="VAR_017264"
FT VARIANT 283
FT /note="D -> N (in a lung squamous cell carcinoma sample;
FT somatic mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_042206"
FT VARIANT 287..289
FT /note="Missing (in CS)"
FT /id="VAR_004122"
FT VARIANT 288
FT /note="I -> S (in CS)"
FT /evidence="ECO:0000269|PubMed:11173845"
FT /id="VAR_017265"
FT VARIANT 289
FT /note="Q -> P (in CS and JWS; dbSNP:rs121918497)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11380921, ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7581378, ECO:0000269|PubMed:8644708"
FT /id="VAR_004123"
FT VARIANT 290
FT /note="W -> C (in PS; severe; also in a lung squamous cell
FT carcinoma sample; somatic mutation; dbSNP:rs121918499)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:17344846, ECO:0000269|PubMed:9150725"
FT /id="VAR_004124"
FT VARIANT 290
FT /note="W -> G (in CS; dbSNP:rs121918501)"
FT /evidence="ECO:0000269|PubMed:8528214"
FT /id="VAR_017266"
FT VARIANT 290
FT /note="W -> R (in CS; dbSNP:rs121918501)"
FT /id="VAR_004125"
FT VARIANT 292
FT /note="K -> E (in CS; dbSNP:rs121918500)"
FT /evidence="ECO:0000269|PubMed:9152842"
FT /id="VAR_004126"
FT VARIANT 301
FT /note="Y -> C (in CS; dbSNP:rs1554930684)"
FT /evidence="ECO:0000269|PubMed:9521581"
FT /id="VAR_004127"
FT VARIANT 314
FT /note="A -> S (in craniosynostosis; dbSNP:rs1358919643)"
FT /evidence="ECO:0000269|PubMed:9521581"
FT /id="VAR_004128"
FT VARIANT 315
FT /note="A -> S (in a non-syndromic craniosynostosis patient
FT with abnormal intrauterine history; confers predisposition
FT to craniosynostosis; dbSNP:rs121918504)"
FT /evidence="ECO:0000269|PubMed:10951518,
FT ECO:0000269|PubMed:11781872"
FT /id="VAR_017267"
FT VARIANT 321
FT /note="D -> A (in PS; dbSNP:rs121918510)"
FT /evidence="ECO:0000269|PubMed:7719333"
FT /id="VAR_004129"
FT VARIANT 328
FT /note="Y -> C (in CS; dbSNP:rs121918493)"
FT /evidence="ECO:0000269|PubMed:7874170"
FT /id="VAR_004130"
FT VARIANT 331
FT /note="N -> I (in CS)"
FT /evidence="ECO:0000269|PubMed:8956050"
FT /id="VAR_004131"
FT VARIANT 337
FT /note="A -> ANA (in CS)"
FT /id="VAR_004132"
FT VARIANT 337
FT /note="A -> P (in CS; dbSNP:rs387906676)"
FT /evidence="ECO:0000269|PubMed:9677057"
FT /id="VAR_017268"
FT VARIANT 338
FT /note="G -> E (in CS; dbSNP:rs1057519044)"
FT /evidence="ECO:0000269|PubMed:8946174"
FT /id="VAR_004133"
FT VARIANT 338
FT /note="G -> R (in CS; dbSNP:rs1057519043)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7581378, ECO:0000269|PubMed:9677057"
FT /id="VAR_015011"
FT VARIANT 340
FT /note="Y -> C (in PS; dbSNP:rs1554928884)"
FT /evidence="ECO:0000269|PubMed:10394936,
FT ECO:0000269|PubMed:11781872"
FT /id="VAR_017269"
FT VARIANT 340
FT /note="Y -> H (in CS; dbSNP:rs121918489)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7987400"
FT /id="VAR_004134"
FT VARIANT 341
FT /note="T -> P (in PS and CS; dbSNP:rs121918495)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7719345"
FT /id="VAR_004135"
FT VARIANT 342
FT /note="C -> F (in CS; dbSNP:rs121918487)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9677057"
FT /id="VAR_004136"
FT VARIANT 342
FT /note="C -> G (in PS; dbSNP:rs121918488)"
FT /evidence="ECO:0000269|PubMed:10394936"
FT /id="VAR_017270"
FT VARIANT 342
FT /note="C -> R (in CS, JWS, PS and ABS2; dbSNP:rs121918488)"
FT /evidence="ECO:0000269|PubMed:10633130,
FT ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11380921,
FT ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7719345,
FT ECO:0000269|PubMed:7987400, ECO:0000269|PubMed:8528214,
FT ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9677057"
FT /id="VAR_004137"
FT VARIANT 342
FT /note="C -> S (in CS, JWS, PS and ABS2; dbSNP:rs121918488)"
FT /evidence="ECO:0000269|PubMed:10633130,
FT ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7581378, ECO:0000269|PubMed:7987400,
FT ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9385368,
FT ECO:0000269|Ref.10"
FT /id="VAR_004138"
FT VARIANT 342
FT /note="C -> W (in CS; dbSNP:rs121918496)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:8528214"
FT /id="VAR_017271"
FT VARIANT 342
FT /note="C -> Y (in CS and PS; dbSNP:rs121918487)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11380921, ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7581378, ECO:0000269|PubMed:7719345,
FT ECO:0000269|PubMed:7987400, ECO:0000269|PubMed:8644708,
FT ECO:0000269|PubMed:9677057"
FT /id="VAR_004139"
FT VARIANT 344
FT /note="A -> G (in CS and JWS; dbSNP:rs121918492)"
FT /evidence="ECO:0000269|PubMed:7581378,
FT ECO:0000269|PubMed:7874170"
FT /id="VAR_004140"
FT VARIANT 344
FT /note="A -> P (in CS and PS)"
FT /evidence="ECO:0000269|PubMed:8644708"
FT /id="VAR_004141"
FT VARIANT 347
FT /note="S -> C (in CS; dbSNP:rs121918494)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:7874170"
FT /id="VAR_004142"
FT VARIANT 351
FT /note="S -> C (in CS, PS and ABS2; dbSNP:rs121918502)"
FT /evidence="ECO:0000269|PubMed:10633130,
FT ECO:0000269|PubMed:8946174, ECO:0000269|PubMed:9693549"
FT /id="VAR_004143"
FT VARIANT 354
FT /note="S -> C (in CS; dbSNP:rs121918490)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:7581378,
FT ECO:0000269|PubMed:7987400, ECO:0000269|PubMed:8528214"
FT /id="VAR_004144"
FT VARIANT 354
FT /note="S -> Y (in CS)"
FT /evidence="ECO:0000269|PubMed:11173845"
FT /id="VAR_017272"
FT VARIANT 356..358
FT /note="Missing (in CS)"
FT /evidence="ECO:0000269|PubMed:8956050"
FT /id="VAR_004145"
FT VARIANT 359
FT /note="V -> F (in CS and PS)"
FT /evidence="ECO:0000269|PubMed:11173845,
FT ECO:0000269|PubMed:8644708"
FT /id="VAR_004146"
FT VARIANT 362
FT /note="A -> S (in CS)"
FT /evidence="ECO:0000269|PubMed:10574673"
FT /id="VAR_017273"
FT VARIANT 372
FT /note="S -> C (in BSTVS; dbSNP:rs121913477)"
FT /evidence="ECO:0000269|PubMed:8696350"
FT /id="VAR_017274"
FT VARIANT 375
FT /note="Y -> C (in PS and BSTVS; dbSNP:rs121913478)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:12000365, ECO:0000269|PubMed:8696350"
FT /id="VAR_017275"
FT VARIANT 381
FT /note="Y -> D (in BBDS; dbSNP:rs387906678)"
FT /evidence="ECO:0000269|PubMed:22387015"
FT /id="VAR_067977"
FT VARIANT 384
FT /note="G -> R (in CS; dbSNP:rs1554927408)"
FT /evidence="ECO:0000269|PubMed:8946174"
FT /id="VAR_004147"
FT VARIANT 391
FT /note="M -> R (in BBDS; the mutation selectively reduces
FT plasma-membrane levels of the protein and markedly
FT diminishes the receptor's responsiveness to extracellular
FT FGF; dbSNP:rs387906677)"
FT /evidence="ECO:0000269|PubMed:22387015"
FT /id="VAR_067978"
FT VARIANT 526
FT /note="K -> E (in FSPC; constitutive kinase activity;
FT dbSNP:rs121918507)"
FT /evidence="ECO:0000269|PubMed:16061565,
FT ECO:0000269|PubMed:17803937"
FT /id="VAR_023788"
FT VARIANT 549
FT /note="N -> H (in CS; constitutive kinase activity;
FT dbSNP:rs1057519045)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:17803937"
FT /id="VAR_017276"
FT VARIANT 565
FT /note="E -> G (in PS; constitutive kinase activity;
FT dbSNP:rs121918506)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:17803937"
FT /id="VAR_017277"
FT VARIANT 612
FT /note="R -> T (in a lung adenocarcinoma sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_046071"
FT VARIANT 613
FT /note="G -> R"
FT /evidence="ECO:0000269|PubMed:10626794,
FT ECO:0000269|PubMed:1309608"
FT /id="VAR_015012"
FT VARIANT 628
FT /note="A -> T (in LADDS; strongly reduced kinase activity;
FT dbSNP:rs121918509)"
FT /evidence="ECO:0000269|PubMed:16501574"
FT /id="VAR_029884"
FT VARIANT 641
FT /note="K -> R (in PS; constitutive kinase activity;
FT dbSNP:rs1057519047)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:17803937"
FT /id="VAR_017278"
FT VARIANT 648
FT /note="A -> T (in LADDS; dbSNP:rs121918508)"
FT /evidence="ECO:0000269|PubMed:16501574"
FT /id="VAR_029885"
FT VARIANT 649..650
FT /note="RD -> S (in LADDS)"
FT /evidence="ECO:0000269|PubMed:16501574"
FT /id="VAR_029886"
FT VARIANT 659
FT /note="K -> N (in craniosynostosis; constitutive kinase
FT activity; dbSNP:rs1589722765)"
FT /evidence="ECO:0000269|PubMed:11781872,
FT ECO:0000269|PubMed:17803937"
FT /id="VAR_017279"
FT VARIANT 663
FT /note="G -> E (in PS)"
FT /evidence="ECO:0000269|PubMed:11781872"
FT /id="VAR_017280"
FT VARIANT 678
FT /note="R -> G (in CS)"
FT /evidence="ECO:0000269|PubMed:11781872"
FT /id="VAR_017281"
FT MUTAGEN 265
FT /note="N->Q: Reduced N-glycosylation. Reduced expression at
FT the cell surface."
FT /evidence="ECO:0000269|PubMed:16844695"
FT MUTAGEN 549
FT /note="N->T: Constitutive kinase activity."
FT /evidence="ECO:0000269|PubMed:17803937"
FT MUTAGEN 565
FT /note="E->A: Constitutive kinase activity."
FT /evidence="ECO:0000269|PubMed:17803937"
FT MUTAGEN 656..657
FT /note="Missing: Loss of kinase activity."
FT /evidence="ECO:0000269|PubMed:16844695"
FT MUTAGEN 769
FT /note="Y->F: Increases fibroblast proliferation. Decreases
FT phosphorylation of PLCG1 and FRS2. Decreases activation of
FT MAP kinases."
FT /evidence="ECO:0000269|PubMed:15629145,
FT ECO:0000269|PubMed:19103595"
FT CONFLICT 246
FT /note="L -> P (in Ref. 16; BAG57383)"
FT /evidence="ECO:0000305"
FT CONFLICT 310
FT /note="K -> N (in Ref. 16; BAG57383)"
FT /evidence="ECO:0000305"
FT STRAND 152..157
FT /evidence="ECO:0007829|PDB:3CAF"
FT TURN 159..162
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 188..193
FT /evidence="ECO:0007829|PDB:3CAF"
FT HELIX 200..202
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 203..205
FT /evidence="ECO:0007829|PDB:4WV1"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:3CAF"
FT HELIX 211..213
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 215..218
FT /evidence="ECO:0007829|PDB:3CAF"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 227..235
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 238..249
FT /evidence="ECO:0007829|PDB:3CAF"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 274..277
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 287..293
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 296..298
FT /evidence="ECO:0007829|PDB:3OJ2"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:1IIL"
FT STRAND 309..314
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 315..319
FT /evidence="ECO:0007829|PDB:2FDB"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1IIL"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:3OJM"
FT HELIX 334..336
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 338..346
FT /evidence="ECO:0007829|PDB:3OJM"
FT STRAND 349..360
FT /evidence="ECO:0007829|PDB:3OJM"
FT TURN 463..465
FT /evidence="ECO:0007829|PDB:5UI0"
FT TURN 472..474
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 478..480
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 481..489
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 494..500
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 504..506
FT /evidence="ECO:0007829|PDB:3CLY"
FT STRAND 513..518
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 525..541
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 550..554
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 561..565
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 568..571
FT /evidence="ECO:0007829|PDB:1OEC"
FT HELIX 572..577
FT /evidence="ECO:0007829|PDB:2PVF"
FT TURN 585..588
FT /evidence="ECO:0007829|PDB:4J99"
FT HELIX 594..596
FT /evidence="ECO:0007829|PDB:5UI0"
FT HELIX 600..619
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 629..631
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 632..634
FT /evidence="ECO:0007829|PDB:2PVF"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:2PVY"
FT STRAND 640..642
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 645..647
FT /evidence="ECO:0007829|PDB:5UGL"
FT TURN 652..654
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 655..658
FT /evidence="ECO:0007829|PDB:2PVF"
FT TURN 659..662
FT /evidence="ECO:0007829|PDB:2PZR"
FT STRAND 664..666
FT /evidence="ECO:0007829|PDB:5UI0"
FT HELIX 667..669
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 672..677
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 682..697
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 709..718
FT /evidence="ECO:0007829|PDB:2PVF"
FT STRAND 726..728
FT /evidence="ECO:0007829|PDB:2PZ5"
FT HELIX 730..739
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 744..746
FT /evidence="ECO:0007829|PDB:2PVF"
FT HELIX 750..764
FT /evidence="ECO:0007829|PDB:2PVF"
FT CONFLICT P21802-16:315
FT /note="T -> L (in Ref. 2; AAA61188)"
FT /evidence="ECO:0000305"
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
