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UniProtKB/Swiss-Prot entry P21802

[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information

Entry name

FGFR2_HUMAN

Primary accession number

P21802

Secondary accession numbers

P18443 Q01742 Q12922 Q14300 Q14301 Q14302 Q14303 Q14304 Q14305 Q14672 Q14718 Q14719 Q1KHY5 Q86YI4 Q96KL9 Q96KM0 Q96KM1 Q96KM2 Q9NZU2 Q9NZU3 Q9UD01 Q9UD02 Q9UIH3 Q9UIH4 Q9UIH5 Q9UIH6 Q9UIH7 Q9UIH8 Q9UM87 Q9UMC6 Q9UNS7 Q9UQH7 Q9UQH8 Q9UQH9 Q9UQI0

Integrated into Swiss-Prot on

May 1, 1991

Sequence was last modified on

May 1, 1991 (Sequence version 1)

Annotations were last modified on

June 16, 2009 (Entry version 133)

Name and origin of the protein

Protein name

Fibroblast growth factor receptor 2 [Precursor]

Synonyms

FGFR-2
EC 2.7.10.1
Keratinocyte growth factor receptor 2
CD332 antigen

Gene name

	Name:	FGFR2
	Synonyms:	BEK, KGFR, KSAM

From

Homo sapiens (Human)

[TaxID: 9606]

Taxonomy

Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Protein existence

1: Evidence at protein level;

References

[1]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). TISSUE=Neonatal brain stem; PubMed=1697263 [NCBI, ExPASy, EBI, Israel, Japan] Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G., Ruta M., Burgess W.H., Jaye M., Schlessinger J.; "Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors."; EMBO J. 9:2685-2692(1990).
[2]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16). DOI=10.1073/pnas.87.20.8180; PubMed=2172978 [NCBI, ExPASy, EBI, Israel, Japan] Houssaint E., Blanquet P.R., Champion-Arnaud P., Gesnel M.-C., Torriglia A., Courtois Y., Breathnach R.; "Related fibroblast growth factor receptor genes exist in the human genome."; Proc. Natl. Acad. Sci. U.S.A. 87:8180-8184(1990).
[3]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 17). DOI=10.1016/0167-4781(91)90015-E; PubMed=1647213 [NCBI, ExPASy, EBI, Israel, Japan] Seno M., Sasada R., Watanabe T., Ishimaru K., Igarashi K.; "Two cDNAs encoding novel human FGF receptor."; Biochim. Biophys. Acta 1089:244-246(1991).
[4]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4). TISSUE=Stomach cancer; DOI=10.1073/pnas.87.15.5983; PubMed=2377625 [NCBI, ExPASy, EBI, Israel, Japan] Hattori Y., Odagiri H., Nakatani H., Miyagawa K., Naito K., Sakamoto H., Katoh O., Yoshida T., Sugimura T., Terada M.; "K-sam, an amplified gene in stomach cancer, is a member of the heparin-binding growth factor receptor genes."; Proc. Natl. Acad. Sci. U.S.A. 87:5983-5987(1990).
[5]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 14 AND 15). DOI=10.1073/pnas.89.7.2960; PubMed=1313574 [NCBI, ExPASy, EBI, Israel, Japan] Katoh M., Hattori Y., Sasaki H., Tanaka M., Sugano K., Yazaki Y., Sugimura T., Terada M.; "K-sam gene encodes secreted as well as transmembrane receptor tyrosine kinase."; Proc. Natl. Acad. Sci. U.S.A. 89:2960-2964(1992).
[6]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3). TISSUE=Placenta; PubMed=1400433 [NCBI, ExPASy, EBI, Israel, Japan] Dell K.R., Williams L.T.; "A novel form of fibroblast growth factor receptor 2. Alternative splicing of the third immunoglobulin-like domain confers ligand binding specificity."; J. Biol. Chem. 267:21225-21229(1992).
[7]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 19), AND VARIANT ARG-613. TISSUE=Mammary gland; DOI=10.1073/pnas.89.1.246; PubMed=1309608 [NCBI, ExPASy, EBI, Israel, Japan] Miki T., Bottaro D.P., Fleming T.P., Smith C.L., Burgess W.H., Chan A.M.-L., Aaronson S.A.; "Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene."; Proc. Natl. Acad. Sci. U.S.A. 89:246-250(1992).
[8]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19). TISSUE=Cornea, and Mammary gland; PubMed=7866434 [NCBI, ExPASy, EBI, Israel, Japan] Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., Shay J.W.; "Hepatocyte growth factor (HGF), keratinocyte growth factor (KGF), and their receptors in human breast cells and tissues: alternative receptors."; Cell. Mol. Biol. Res. 40:337-350(1994).
[9]	ERRATUM. Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., Shay J.W.; Cell. Mol. Biol. Res. 40:707-707(1994).
[10]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CS SER-342. TISSUE=Blood; Steinberger D., Mueller U.; Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases.
[11]	NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 9; 10; 11; 12 AND 13), AND VARIANT ARG-613. PubMed=10626794 [NCBI, ExPASy, EBI, Israel, Japan] Ueda T., Sasaki H., Kuwahara Y., Nezu M., Shibuya T., Sakamoto H., Ishii H., Yanagihara K., Mafune K., Makuuchi M., Terada M.; "Deletion of the carboxyl-terminal exons of K-sam/FGFR2 by short homology-mediated recombination, generating preferential expression of specific messenger RNAs."; Cancer Res. 59:6080-6086(1999).
[12]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 5; 6; 8; 14 AND 18). PubMed=11856867 [NCBI, ExPASy, EBI, Israel, Japan] Ingersoll R.G., Paznekas W.A., Tran A.K., Scott A.F., Jiang G., Jabs E.W.; "Fibroblast growth factor receptor 2 (FGFR2): genomic sequence and variations."; Cytogenet. Cell Genet. 94:121-126(2001).
[13]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3). Lind D.L., Cox D.R.; "Sequence and polymorphisms in fibroblast growth factor receptor 2 (FGFR2) gene in humans."; Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases.
[14]	NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS PRO-6 AND THR-186. NIEHS SNPs program; Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[15]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 20). TISSUE=Brain; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[16]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-427. DOI=10.1086/302831; PubMed=10712195 [NCBI, ExPASy, EBI, Israel, Japan] Glaser R.L., Jiang W., Boyadjiev S.A., Tran A.K., Zachary A.A., Van Maldergem L., Johnson D., Walsh S., Oldridge M., Wall S.A., Wilkie A.O.M., Jabs E.W.; "Paternal origin of FGFR2 mutations in sporadic cases of Crouzon syndrome and Pfeiffer syndrome."; Am. J. Hum. Genet. 66:768-777(2000).
[17]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209; 212-767 AND 771-821 (ISOFORMS 5; 14 AND 18). DOI=10.1016/S0378-1119(99)00047-5; PubMed=10196476 [NCBI, ExPASy, EBI, Israel, Japan] Zhang Y., Gorry M.C., Post J.C., Ehrlich G.D.; "Genomic organization of the human fibroblast growth factor receptor 2 (FGFR2) gene and comparative analysis of the human FGFR gene family."; Gene 230:69-79(1999).
[18]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-313, AND VARIANTS APRS TRP-252 AND ARG-253. PubMed=7668257 [NCBI, ExPASy, EBI, Israel, Japan] Park W.-J., Theda C., Maestri N.E., Meyers G.A., Fryburg J.S., Dufresne C., Cohen M.M. Jr., Jabs E.W.; "Analysis of phenotypic features and FGFR2 mutations in Apert syndrome."; Am. J. Hum. Genet. 57:321-328(1995).
[19]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-259. PubMed=8676562 [NCBI, ExPASy, EBI, Israel, Japan] Wada C., Ishigaki M., Toyo-oka Y., Yamabe H., Ohnuki Y., Takada F., Yamazaki Y., Ohtani H.; "Nucleotide sequences at intron 6 and exon 7 junction of fibroblast growth factor receptor 2 and rapid mutational analysis in Apert syndrome."; Rinsho Byori 44:435-438(1996).
[20]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-318. DOI=10.1038/ng0596-48; PubMed=8673103 [NCBI, ExPASy, EBI, Israel, Japan] Moloney D.M., Slaney S.F., Oldridge M., Wall S.A., Sahlin P., Stenman G., Wilkie A.O.M.; "Exclusive paternal origin of new mutations in Apert syndrome."; Nat. Genet. 13:48-53(1996).
[21]	NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-361, AND VARIANTS CS PRO-289; ARG-338; SER-342; TYR-342; GLY-344 AND CYS-354. DOI=10.1093/hmg/4.8.1387; PubMed=7581378 [NCBI, ExPASy, EBI, Israel, Japan] Gorry M.C., Preston R.A., White G.J., Zhang Y., Singhal V.K., Losken H.W., Parker M.G., Nwokoro N.A., Post J.C., Ehrlich G.D.; "Crouzon syndrome: mutations in two spliceoforms of FGFR2 and a common point mutation shared with Jackson-Weiss syndrome."; Hum. Mol. Genet. 4:1387-1390(1995).
[22]	X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 147-366 IN COMPLEX WITH FGF2. DOI=10.1016/S0092-8674(00)80851-X; PubMed=10830168 [NCBI, ExPASy, EBI, Israel, Japan] Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.; "Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."; Cell 101:413-424(2000).
[23]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 148-366 IN COMPLEX WITH FGF1 AND HEPARIN. DOI=10.1038/35039551; PubMed=11069186 [NCBI, ExPASy, EBI, Israel, Japan] Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.; "Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin."; Nature 407:1029-1034(2000).
[24]	X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 147-362 IN COMPLEX WITH FGF1. DOI=10.1073/pnas.97.1.49; PubMed=10618369 [NCBI, ExPASy, EBI, Israel, Japan] Stauber D.J., DiGabriele A.D., Hendrickson W.A.; "Structural interactions of fibroblast growth factor receptor with its ligands."; Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000).
[25]	X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-366 OF VARIANTS APRS TRP-252 AND ARG-253 IN COMPLEX WITH FGF2. DOI=10.1073/pnas.121183798; PubMed=11390973 [NCBI, ExPASy, EBI, Israel, Japan] Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M.; "Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome."; Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001).
[26]	X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-371 IN COMPLEX WITH FGF10. DOI=10.1073/pnas.0436500100; PubMed=12591959 [NCBI, ExPASy, EBI, Israel, Japan] Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D., Aaronson S.A., Mohammadi M.; "Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors."; Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003).
[27]	X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 149-368 IN COMPLEX WITH FGF8. DOI=10.1101/gad.1365406; PubMed=16384934 [NCBI, ExPASy, EBI, Israel, Japan] Olsen S.K., Li J.Y.H., Bromleigh C., Eliseenkova A.V., Ibrahimi O.A., Lao Z., Zhang F., Linhardt R.J., Joyner A.L., Mohammadi M.; "Structural basis by which alternative splicing modulates the organizer activity of FGF8 in the brain."; Genes Dev. 20:185-198(2006).
[28]	VARIANTS CS HIS-340; ARG-342; SER-342; TYR-342 AND CYS-354. DOI=10.1038/ng0994-98; PubMed=7987400 [NCBI, ExPASy, EBI, Israel, Japan] Reardon W., Winter R.M., Rutland P., Pulleyn L.J., Jones B.M., Malcolm S.; "Mutations in the fibroblast growth factor receptor 2 gene cause Crouzon syndrome."; Nat. Genet. 8:98-103(1994).
[29]	VARIANTS CS CYS-328 AND CYS-347, AND VARIANT JWS GLY-344. DOI=10.1038/ng1194-275; PubMed=7874170 [NCBI, ExPASy, EBI, Israel, Japan] Jabs E.W., Li X., Scott A.F., Meyers G.A., Chen W., Eccles M., Mao J., Charnas L.R., Jackson C.E., Jaye M.; "Jackson-Weiss and Crouzon syndromes are allelic with mutations in fibroblast growth factor receptor 2."; Nat. Genet. 8:275-279(1994).
[30]	VARIANTS CS. DOI=10.1093/hmg/4.6.1077; PubMed=7655462 [NCBI, ExPASy, EBI, Israel, Japan] Oldridge M., Wilkie A.O.M., Slaney S.F., Poole M.D., Pulleyn L.J., Rutland P., Hockley A.D., Wake M.J.C., Goldin J.H., Winter R.M., Reardon W., Malcolm S.; "Mutations in the third immunoglobulin domain of the fibroblast growth factor receptor-2 gene in Crouzon syndrome."; Hum. Mol. Genet. 4:1077-1082(1995).
[31]	VARIANTS CS GLY-290; TRP-342 AND CYS-354, AND VARIANT JWS ARG-342. DOI=10.1093/hmg/4.7.1229; PubMed=8528214 [NCBI, ExPASy, EBI, Israel, Japan] Park W.-J., Meyers G.A., Li X., Theda C., Day D., Orlow S.J., Jones M.C., Jabs E.W.; "Novel FGFR2 mutations in Crouzon and Jackson-Weiss syndromes show allelic heterogeneity and phenotypic variability."; Hum. Mol. Genet. 4:1229-1233(1995).
[32]	VARIANT PS ALA-321. DOI=10.1038/ng0295-108; PubMed=7719333 [NCBI, ExPASy, EBI, Israel, Japan] Lajeunie E., Wei M.H., Bonaventure J., Munnich A., le Merrer M., Renier D.; "FGFR2 mutations in Pfeiffer syndrome."; Nat. Genet. 9:108-108(1995).
[33]	VARIANTS APRS TRP-252 AND ARG-253. DOI=10.1038/ng0295-165; PubMed=7719344 [NCBI, ExPASy, EBI, Israel, Japan] Wilkie A.O.M., Slaney S.F., Oldridge M., Poole M.D., Ashworth G.J., Hockley A.D., Hayward R.D., David D.J., Pulleyn L.J., Rutland P., Malcolm S., Winter R.M., Reardon W.; "Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome."; Nat. Genet. 9:165-172(1995).
[34]	VARIANTS PS PRO-341; ARG-342 AND TYR-342. DOI=10.1038/ng0295-173; PubMed=7719345 [NCBI, ExPASy, EBI, Israel, Japan] Rutland P., Pulleyn L.J., Reardon W., Baraister M., Hayward R., Jones B.M., Malcolm S., Winter R.M., Oldridge M., Slaney S.F., Poole M.D., Wilkie A.O.M.; "Identical mutations in the FGFR2 gene cause both Pfeiffer and Crouzon syndrome phenotypes."; Nat. Genet. 9:173-176(1995).
[35]	VARIANTS CS GLY-268 INS; PHE-342 AND TYR-342, VARIANTS PS PHE-278; ARG-342; SER-342; PRO-344 AND PHE-359, AND VARIANT JWS PRO-289. PubMed=8644708 [NCBI, ExPASy, EBI, Israel, Japan] Meyers G.A., Day D., Goldberg R., Daentl D.L., Przylepa K.A., Abrams L.J., Graham J.M. Jr., Feingold M., Moeschler J.B., Rawnsley E., Scott A.F., Jabs E.W.; "FGFR2 exon IIIa and IIIc mutations in Crouzon, Jackson-Weiss, and Pfeiffer syndromes: evidence for missense changes, insertions, and a deletion due to alternative RNA splicing."; Am. J. Hum. Genet. 58:491-498(1996).
[36]	VARIANTS CS CYS-105; GLU-338; CYS-351 AND ARG-384. PubMed=8946174 [NCBI, ExPASy, EBI, Israel, Japan] Pulleyn L.J., Reardon W., Wilkes D., Rutland P., Jones B.M., Hayward R., Hall C.M., Brueton L., Chun N., Lammer E., Malcolm S., Winter R.M.; "Spectrum of craniosynostosis phenotypes associated with novel mutations at the fibroblast growth factor receptor 2 locus."; Eur. J. Hum. Genet. 4:283-291(1996).
[37]	VARIANTS CS ILE-331; ASN-ALA-337 INS AND 356-TRP--THR-358 DEL. DOI=10.1002/(SICI)1098-1004(1996)8:4<386::AID-HUMU18>3.3.CO;2-A; PubMed=8956050 [NCBI, ExPASy, EBI, Israel, Japan] Steinberger D., Mulliken J.B., Mueller U.; "Crouzon syndrome: previously unrecognized deletion, duplication, and point mutation within FGFR2 gene."; Hum. Mutat. 8:386-390(1996).
[38]	VARIANTS BSCGS CYS-372 AND CYS-375. DOI=10.1038/ng0896-492; PubMed=8696350 [NCBI, ExPASy, EBI, Israel, Japan] Przylepa K.A., Paznekas W.A., Zhang M., Golabi M., Bias W., Bamshad M.J., Carey J.C., Hall B.D., Stevenson R., Orlow S.J., Cohen M.M. Jr., Jabs E.W.; "Fibroblast growth factor receptor 2 mutations in Beare-Stevenson cutis gyrata syndrome."; Nat. Genet. 13:492-494(1996).
[39]	VARIANT PS CYS-290. DOI=10.1007/s004390050413; PubMed=9150725 [NCBI, ExPASy, EBI, Israel, Japan] Tartaglia M., Valeri S., Velardi F., di Rocco C., Battaglia P.A.; "Trp290Cys mutation in exon IIIa of the fibroblast growth factor receptor 2 (FGFR2) gene is associated with Pfeiffer syndrome."; Hum. Genet. 99:602-606(1997).
[40]	VARIANT JWS SER-342. DOI=10.1007/s004390050584; PubMed=9385368 [NCBI, ExPASy, EBI, Israel, Japan] Tartaglia M., Di Rocco C., Lajeunie E., Valeri S., Velardi F., Battaglia P.A.; "Jackson-Weiss syndrome: identification of two novel FGFR2 missense mutations shared with Crouzon and Pfeiffer craniosynostotic disorders."; Hum. Genet. 101:47-50(1997).
[41]	VARIANT CS LEU-252, VARIANT APRS PHE-252, AND VARIANT PS 252-PHE-SER-253. DOI=10.1093/hmg/6.1.137; PubMed=9002682 [NCBI, ExPASy, EBI, Israel, Japan] Oldridge M., Lunt P.W., Zackai E.H., McDonald-Mcginn D.M., Muenke M., Moloney D.M., Twigg S.R.F., Heath J.K., Howard T.D., Hoganson G., Gagnon D.M., Jabs E.W., Wilkie A.O.M.; "Genotype-phenotype correlation for nucleotide substitutions in the IgII-IgIII linker of FGFR2."; Hum. Mol. Genet. 6:137-143(1997).
[42]	VARIANT CS GLU-292. PubMed=9152842 [NCBI, ExPASy, EBI, Israel, Japan] Steinberger D., Collmann H., Schmalenberger B., Mueller U.; "A novel mutation (a886g) in exon 5 of FGFR2 in members of a family with Crouzon phenotype and plagiocephaly."; J. Med. Genet. 34:420-422(1997).
[43]	VARIANTS CS PHE-278; PRO-337; ARG-338; ARG-342; PHE-342 AND TYR-342, VARIANTS APRS TRP-252 AND ARG-253, AND VARIANT JWS PHE-278. DOI=10.1002/(SICI)1096-8628(19980707)78:3<237::AID-AJMG5>3.3.CO;2-5; PubMed=9677057 [NCBI, ExPASy, EBI, Israel, Japan] Passos-Bueno M.R., Sertie A.L., Richieri-Costa A., Alonso L.G., Zatz M., Alonso N., Brunoni D., Ribeiro S.F.M.; "Description of a new mutation and characterization of FGFR1, FGFR2, and FGFR3 mutations among Brazilian patients with syndromic craniosynostoses."; Am. J. Med. Genet. 78:237-241(1998).
[44]	VARIANTS CS VAL-276 AND CYS-301, AND VARIANT CRANIOSYNOSTOSIS SER-314. DOI=10.1007/s004390050668; PubMed=9521581 [NCBI, ExPASy, EBI, Israel, Japan] Steinberger D., Vriend G., Mulliken J.B., Mueller U.; "The mutations in FGFR2-associated craniosynostoses are clustered in five structural elements of immunoglobulin-like domain III of the receptor."; Hum. Genet. 102:145-150(1998).
[45]	VARIANTS APRS TRP-252 AND ARG-253. PubMed=9452027 [NCBI, ExPASy, EBI, Israel, Japan] Tsai F.-J., Hwu W.-L., Lin S.-P., Chang J.-G., Wang T.-R., Tsai C.-H.; "Two common mutations 934C to G and 937C to G of fibroblast growth factor receptor 2 (FGFR2) gene in Chinese patients with Apert syndrome."; Hum. Mutat. Suppl. 1:S18-S19(1998).
[46]	VARIANT PS CYS-351. PubMed=9693549 [NCBI, ExPASy, EBI, Israel, Japan] Mathijssen I.M., Vaandrager J.M., Hoogeboom A.J., Hesseling-Janssen A.L.W., van den Ouweland A.M.W.; "Pfeiffer's syndrome resulting from an S351C mutation in the fibroblast growth factor receptor-2 gene."; J. Craniofac. Surg. 9:207-209(1998).
[47]	VARIANT PS TRP-252. PubMed=9719378 [NCBI, ExPASy, EBI, Israel, Japan] Passos-Bueno M.R., Richieri-Costa A., Sertie A.L., Kneppers A.; "Presence of the Apert canonical S252W FGFR2 mutation in a patient without severe syndactyly."; J. Med. Genet. 35:677-679(1998).
[48]	VARIANT CS SER-362. PubMed=10574673 [NCBI, ExPASy, EBI, Israel, Japan] Everett E.T., Britto D.A., Ward R.E., Hartsfield J.K. Jr.; "A novel FGFR2 gene mutation in Crouzon syndrome associated with apparent nonpenetrance."; Cleft Palate Craniofac. J. 36:533-541(1999).
[49]	VARIANTS PS CYS-340 AND GLY-342. DOI=10.1007/s004390050979; PubMed=10394936 [NCBI, ExPASy, EBI, Israel, Japan] Cornejo-Roldan L.R., Roessler E., Muenke M.; "Analysis of the mutational spectrum of the FGFR2 gene in Pfeiffer syndrome."; Hum. Genet. 104:425-431(1999).
[50]	VARIANT PS ASP-273 DEL. DOI=10.1034/j.1399-0004.2000.580116.x; PubMed=10945669 [NCBI, ExPASy, EBI, Israel, Japan] Priolo M., Lerone M., Baffico M., Baldi M., Ravazzolo R., Cama A., Capra V., Silengo M.; "Pfeiffer syndrome type 2 associated with a single amino acid deletion in the FGFR2 gene."; Clin. Genet. 58:81-83(2000).
[51]	VARIANTS CS/PS ARG-342 AND TYR-342, VARIANTS CS LEU-263; VAL-276; PHE-278; TYR-278; SER-288; PRO-289; PRO-341; TRP-342; CYS-354; TYR-354 AND PHE-359, AND VARIANT PS SER-342. PubMed=11173845 [NCBI, ExPASy, EBI, Israel, Japan] Kress W., Collmann H., Buesse M., Halliger-Keller B., Mueller C.R.; "Clustering of FGFR2 gene mutations inpatients with Pfeiffer and Crouzon syndromes (FGFR2-associated craniosynostoses)."; Cytogenet. Cell Genet. 91:134-137(2000).
[52]	VARIANT SER-315. DOI=10.1038/sj.ejhg.5200499; PubMed=10951518 [NCBI, ExPASy, EBI, Israel, Japan] Johnson D., Wall S.A., Mann S., Wilkie A.O.M.; "A novel mutation, Ala315Ser, in FGFR2: a gene-environment interaction leading to craniosynostosis?"; Eur. J. Hum. Genet. 8:571-577(2000).
[53]	VARIANTS ABS ARG-342; SER-342 AND CYS-351. DOI=10.1136/jmg.37.1.26; PubMed=10633130 [NCBI, ExPASy, EBI, Israel, Japan] Reardon W., Smith A., Honour J.W., Hindmarsh P., Das D., Rumsby G., Nelson I., Malcolm S., Ades L., Sillence D., Kumar D., DeLozier-Blanchet C., McKee S., Kelly T., McKeehan W.L., Baraitser M., Winter R.M.; "Evidence for digenic inheritance in some cases of Antley-Bixler syndrome?"; J. Med. Genet. 37:26-32(2000).
[54]	VARIANTS CS CYS-281; PRO-289; ARG-342 AND TYR-342. DOI=10.1046/j.1442-200x.2001.01392.x; PubMed=11380921 [NCBI, ExPASy, EBI, Israel, Japan] Tsai F.-J., Yang C.-F., Wu J.-Y., Tsai C.-H., Lee C.-C.; "Mutation analysis of Crouzon syndrome and identification of one novel mutation in Taiwanese patients."; Pediatr. Int. 43:263-266(2001).
[55]	VARIANTS CS CYS-105; PRO-267; VAL-276; CYS-281; PRO-289; ARG-338; HIS-340; PHE-342; TRP-342; CYS-347; CYS-354; HIS-549 AND GLY-678, VARIANTS PS PHE-172; 252-PHE-SER-253; CYS-290; CYS-340; PRO-341; ARG-342; SER-342; CYS-375; GLY-565; ARG-641 AND GLU-663, VARIANTS APRS TRP-252 AND ARG-253, VARIANTS CS/PS PHE-278 AND TYR-342, VARIANT CRANIOSYNOSTOSIS ASN-659, AND VARIANTS THR-186 AND SER-315. DOI=10.1086/338758; PubMed=11781872 [NCBI, ExPASy, EBI, Israel, Japan] Kan S.-H., Elanko N., Johnson D., Cornejo-Roldan L.R., Cook J., Reich E.W., Tomkins S., Verloes A., Twigg S.R.F., Rannan-Eliya S., McDonald-McGinn D.M., Zackai E.H., Wall S.A., Muenke M., Wilkie A.O.M.; "Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis."; Am. J. Hum. Genet. 70:472-486(2002).
[56]	VARIANT BSCGS CYS-375. DOI=10.1034/j.1399-0004.2002.610309.x; PubMed=12000365 [NCBI, ExPASy, EBI, Israel, Japan] Wang T.-J., Huang C.-B., Tsai F.-J., Wu J.-Y., Lai R.-B., Hsiao M.; "Mutation in the FGFR2 gene in a Taiwanese patient with Beare-Stevenson cutis gyrata syndrome."; Clin. Genet. 61:218-221(2002).
[57]	VARIANT FSPC GLU-526. DOI=10.1136/jmg.2004.027888; PubMed=16061565 [NCBI, ExPASy, EBI, Israel, Japan] McGillivray G., Savarirayan R., Cox T.C., Stojkoski C., McNeil R., Bankier A., Bateman J.F., Roscioli T., Gardner R.J.M., Lamande S.R.; "Familial scaphocephaly syndrome caused by a novel mutation in the FGFR2 tyrosine kinase domain."; J. Med. Genet. 42:656-662(2005).
[58]	VARIANTS LADDS THR-628; THR-648 AND 649-ARG-ASP-650 DELINS SER. DOI=10.1038/ng1757; PubMed=16501574 [NCBI, ExPASy, EBI, Israel, Japan] Rohmann E., Brunner H.G., Kayserili H., Uyguner O., Nuernberg G., Lew E.D., Dobbie A., Eswarakumar V.P., Uzumcu A., Ulubil-Emeroglu M., Leroy J.G., Li Y., Becker C., Lehnerdt K., Cremers C.W.R.J., Yueksel-Apak M., Nuernberg P., Kubisch C., Schlessinger J., van Bokhoven H., Wollnik B.; "Mutations in different components of FGF signaling in LADD syndrome."; Nat. Genet. 38:414-417(2006).
[59]	VARIANT [LARGE SCALE ANALYSIS] CYS-203. DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan] Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.; "The consensus coding sequences of human breast and colorectal cancers."; Science 314:268-274(2006).
[60]	VARIANTS [LARGE SCALE ANALYSIS] LEU-57; THR-186; CYS-203; VAL-272; ASN-283; CYS-290 AND THR-612. DOI=10.1038/nature05610; PubMed=17344846 [NCBI, ExPASy, EBI, Israel, Japan] Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G., Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.; "Patterns of somatic mutation in human cancer genomes."; Nature 446:153-158(2007).

Comments

FUNCTION: Receptor for acidic and basic fibroblast growth factors.
CATALYTIC ACTIVITY: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
INTERACTION:
P05230:FGF1; NbExp=1; IntAct=EBI-1028658, EBI-698068;
O15520:FGF10; NbExp=1; IntAct=EBI-1028658, EBI-1035684;
P09038:FGF2; NbExp=1; IntAct=EBI-1028732, EBI-977447;
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.
SUBCELLULAR LOCATION: Isoform 14: Secreted.
SUBCELLULAR LOCATION: Isoform 19: Secreted.

ALTERNATIVE PRODUCTS: 20 named isoforms [FASTA] produced by alternative splicing.

Name	1
Synonyms	BEK
Isoform ID	P21802-1
This is the isoform sequence displayed in this entry.

Name	2
Synonyms	Short
Isoform ID	P21802-2
Features which should be applied to build the isoform sequence: VSP_002978.

Name	3
Synonyms	BFR-1
Isoform ID	P21802-3
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972.

Name	4
Synonyms	K-sam
Isoform ID	P21802-4
Features which should be applied to build the isoform sequence: VSP_002964, VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002975, VSP_002976.

Name	5
Synonyms	K-sam-I, BEK, IgIIIc
Isoform ID	P21802-5
Features which should be applied to build the isoform sequence: VSP_002975.

Name	6
Synonyms	K-sam-IIC2
Isoform ID	P21802-6
Features which should be applied to build the isoform sequence: VSP_002975, VSP_002984.

Name	7
Synonyms	K-sam-IIO2
Isoform ID	P21802-7
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002979.

Name	8
Synonyms	K-sam-IIC3
Isoform ID	P21802-8
Features which should be applied to build the isoform sequence: VSP_002975, VSP_002978.

Name	9
Synonyms	K-sam-IIH1
Isoform ID	P21802-9
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002980.

Name	10
Synonyms	K-sam-IIH2
Isoform ID	P21802-10
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002981.

Name	11
Synonyms	K-sam-IIH3, K-sam-IIO4
Isoform ID	P21802-11
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002982.

Name	12
Synonyms	K-sam-IIO1
Isoform ID	P21802-12
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002983.

Name	13
Synonyms	K-sam-IIO3
Isoform ID	P21802-13
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002977.

Name	14
Synonyms	K-sam-IV, Soluble KGFR
Isoform ID	P21802-14
Features which should be applied to build the isoform sequence: VSP_002965, VSP_002966.

Name	15
Synonyms	K-sam-III
Isoform ID	P21802-15
Features which should be applied to build the isoform sequence: VSP_002968.

Name	16
Synonyms	TK14
Isoform ID	P21802-16
Features which should be applied to build the isoform sequence: VSP_002967, VSP_002975.

Name	17
Isoform ID	P21802-17
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002978.

Name	18
Synonyms	K-sam-IIC1, KGFR, IgIIIb
Isoform ID	P21802-18
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002975.

Name	19
Synonyms	Soluble KGFR
Isoform ID	P21802-19
Features which should be applied to build the isoform sequence: VSP_002969, VSP_002970, VSP_002971, VSP_002972, VSP_002973, VSP_002974.

Name	20
Isoform ID	P21802-20
Features which should be applied to build the isoform sequence: VSP_019608, VSP_019609.

DISEASE: Defects in FGFR2 are the cause of Crouzon syndrome (CS) [MIM:123500]; also called craniofacial dysostosis type I (CFD1). CS is an autosomal dominant syndrome characterized by craniosynostosis (premature fusion of the skull sutures), hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism.
DISEASE: Defects in FGFR2 are a cause of Jackson-Weiss syndrome (JWS) [MIM:123150]. JWS is an autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence.
DISEASE: Defects in FGFR2 are a cause of Apert syndrome (APRS) [MIM:101200]; also known as acrocephalosyndactyly type 1 (ACS1). APRS is a syndrome characterized by facio-cranio-synostosis, osseous and membranous syndactyly of the four extremities, and midface hypoplasia. The craniosynostosis is bicoronal and results in acrocephaly of brachysphenocephalic type. Syndactyly of the fingers and toes may be total (mitten hands and sock feet) or partial affecting the second, third, and fourth digits. Intellectual deficit is frequent and often severe, usually being associated with cerebral malformations.
DISEASE: Defects in FGFR2 are a cause of Pfeiffer syndrome (PS) [MIM:101600]; also known as acrocephalosyndactyly type V (ACS5). PS is characterized by craniosynostosis (premature fusion of the skull sutures) with deviation and enlargement of the thumbs and great toes, brachymesophalangy, with phalangeal ankylosis and a varying degree of soft tissue syndactyly. Three subtypes of Pfeiffer syndrome have been described: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3).
DISEASE: Defects in FGFR2 are the cause of Beare-Stevenson cutis gyrata syndrome (BSCGS) [MIM:123790]. BSCGS is an autosomal dominant condition is characterized by the furrowed skin disorder of cutis gyrata, acanthosis nigricans, craniosynostosis, craniofacial dysmorphism, digital anomalies, umbilical and anogenital abnormalities and early death.
DISEASE: Defects in FGFR2 are the cause of familial scaphocephaly syndrome (FSPC) [MIM:609579]; also known as scaphocephaly with maxillary retrusion and mental retardation. FSPC is an autosomal dominant craniosynostosis syndrome characterized by scaphocephaly, macrocephaly, hypertelorism, maxillary retrusion, and mild intellectual disability. Scaphocephaly is the most common of the craniosynostosis conditions and is characterized by a long, narrow head. It is due to premature fusion of the sagittal suture or from external deformation.
DISEASE: Defects in FGFR2 are a cause of lacrimo-auriculo-dento-digital syndrome (LADDS) [MIM:149730]; also known as Levy-Hollister syndrome. LADDS is a form of ectodermal dysplasia, a heterogeneous group of disorders due to abnormal development of two or more ectodermal structures. LADDS is an autosomal dominant syndrome characterized by aplastic/hypoplastic lacrimal and salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia and enamel hypoplasia, and distal limb segments anomalies. In addition to these cardinal features, facial dysmorphism, malformations of the kidney and respiratory system and abnormal genitalia have been reported. Craniosynostosis and severe syndactyly are not observed.
DISEASE: Defects in FGFR2 are the cause of Antley-Bixler syndrome (ABS) [MIM:207410]. ABS is a multiple congenital anomaly syndrome characterized by craniosynostosis, radiohumeral synostosis, midface hypoplasia, malformed ears, arachnodactyly and multiple joint contractures. ABS is a heterogeneous disorder and occurs with and without abnormal genitalia in both sexes.
SIMILARITY: Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.
SIMILARITY: Contains 3 Ig-like C2-type (immunoglobulin-like) domains.
SIMILARITY: Contains 1 protein kinase domain.
WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and Haematology; URL="http://atlasgeneticsoncology.org/Genes/FGFR2ID40570ch10q26.html";.
WEB RESOURCE: Name=GeneReviews; URL="http://www.genetests.org/query?gene=FGFR2";.
WEB RESOURCE: Name=NIEHS-SNPs; URL="http://egp.gs.washington.edu/data/fgfr2/";.

Copyright

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

Cross-references

Sequence databases

EMBL

X52832; CAA37014.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M55614; AAA61188.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
X56191; CAA39654.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M35718; AAA36152.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M87770; AAA59470.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M87771; AAA59471.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M87772; AAA59472.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M97193; AAA52449.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
U11814; AAA68514.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
M80634; AAA36147.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Z71929; CAA96492.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030073; BAA89296.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030074; BAA89297.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030075; BAA89298.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030076; BAA89299.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030077; BAA89300.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AB030078; BAA89301.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360695; AAK94205.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF410480; AAK94205.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360695; AAK94206.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF410480; AAK94206.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360695; AAK94207.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF410480; AAK94207.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360695; AAK94208.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF410480; AAK94208.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF360695; AAK94209.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF410480; AAK94209.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF487553; AAM74056.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
DQ493927; ABE96832.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC039243; AAH39243.2; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF169399; AAF43273.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF169399; AAF43274.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097353; AAD31560.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097341; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097342; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097343; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097345; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097346; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097347; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097348; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097349; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097350; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097351; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097352; AAD31560.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097353; AAD31561.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097341; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097342; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097344; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097345; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097346; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097347; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097348; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097349; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097350; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097351; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097352; AAD31561.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097340; AAD31562.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097337; AAD31562.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097338; AAD31562.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097339; AAD31562.1; JOINED; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097354; AAD31565.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
AF097341; AAD31567.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
S82438; AAD14392.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
Y17131; CAA76643.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L49237; AAC41933.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L49242; AAC41934.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L49238; AAC41935.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L49239; AAC41936.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L49240; AAC41937.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
L49241; AAC41938.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

IPI

IPI00010680; -.
IPI00216602; -.
IPI00216603; -.
IPI00216604; -.
IPI00216605; -.
IPI00218416; -.
IPI00218417; -.
IPI00218418; -.
IPI00218419; -.
IPI00218420; -.
IPI00218421; -.
IPI00218422; -.
IPI00218423; -.
IPI00218424; -.
IPI00218425; -.
IPI00384713; -.
IPI00386650; -.
IPI00647907; -.
IPI00759837; -.
IPI00873362; -.

PIR

A35969; A35969.
A42691; TVHUF2.
A45081; A45081.
C42691; C42691.
S16236; S16236.

RefSeq

NP_000132.3; -.
NP_001138385.1; -.
NP_001138386.1; -.
NP_001138388.1; -.
NP_001138389.1; -.
NP_001138390.1; -.
NP_001138391.1; -.
NP_075259.4; -.

UniGene

Hs.533683

3D structure databases

PDB

1DJS; X-ray; 2.40 A; A=153-362.	[ExPASy / RCSB / EBI]
1E0O; X-ray; 2.80 A; B/D=148-366.	[ExPASy / RCSB / EBI]
1EV2; X-ray; 2.20 A; E/F/G/H=147-366.	[ExPASy / RCSB / EBI]
1GJO; X-ray; 2.40 A; A=456-768.	[ExPASy / RCSB / EBI]
1II4; X-ray; 2.70 A; E/F/G/H=147-366.	[ExPASy / RCSB / EBI]
1IIL; X-ray; 2.30 A; E/F/G/H=147-366.	[ExPASy / RCSB / EBI]
1NUN; X-ray; 2.90 A; B=140-361.	[ExPASy / RCSB / EBI]
1OEC; X-ray; 2.40 A; A=456-768.	[ExPASy / RCSB / EBI]
1WVZ; NMR; -; A=147-249.	[ExPASy / RCSB / EBI]
2FDB; X-ray; 2.28 A; P/R=149-368.	[ExPASy / RCSB / EBI]
2PSQ; X-ray; 2.40 A; A/B=413-768.	[ExPASy / RCSB / EBI]
2PVF; X-ray; 1.80 A; A=458-778, B=764-778.	[ExPASy / RCSB / EBI]
2PVY; X-ray; 2.20 A; A/B/C/D=458-768.	[ExPASy / RCSB / EBI]
2PWL; X-ray; 2.40 A; A/B=458-768.	[ExPASy / RCSB / EBI]
2PY3; X-ray; 2.30 A; A/B=458-768.	[ExPASy / RCSB / EBI]
2PZ5; X-ray; 2.40 A; A/B=458-768.	[ExPASy / RCSB / EBI]
2PZP; X-ray; 2.40 A; A/B=458-768.	[ExPASy / RCSB / EBI]
2PZR; X-ray; 3.00 A; A/B=458-768.	[ExPASy / RCSB / EBI]
2Q0B; X-ray; 2.90 A; A/B=458-768.	[ExPASy / RCSB / EBI]
3B2T; X-ray; 1.80 A; A/B=458-766.	[ExPASy / RCSB / EBI]
3CAF; X-ray; 1.96 A; A=150-249.	[ExPASy / RCSB / EBI]
3CLY; X-ray; 2.00 A; A=458-778.	[ExPASy / RCSB / EBI]
3CU1; X-ray; 2.60 A; A/C=150-249.	[ExPASy / RCSB / EBI]
3DAR; X-ray; 2.20 A; A/B=146-249.	[ExPASy / RCSB / EBI]

Detailed list of linked structures.

PDBsum

1DJS; -.
1E0O; -.
1EV2; -.
1GJO; -.
1II4; -.
1IIL; -.
1NUN; -.
1OEC; -.
1WVZ; -.
2FDB; -.
2PSQ; -.
2PVF; -.
2PVY; -.
2PWL; -.
2PY3; -.
2PZ5; -.
2PZP; -.
2PZR; -.
2Q0B; -.
3B2T; -.
3CAF; -.
3CLY; -.
3CU1; -.
3DAR; -.

ModBase

P21802.

Protein-protein interaction databases

DIP

DIP:3788N; -.
DIP:4011N; -.

IntAct

P21802; 4.

PTM databases

PhosphoSite

P21802; -.

Enzyme and pathway databases

BRENDA

2.7.10.1; 247.

Pathway_Interaction_DB

fgf_pathway; FGF signaling pathway.

Reactome

REACT_9470; Signaling by FGFR.

Organism-specific databases

GC10M123223; -.

HIX0009266; -.

HGNC:3689; FGFR2.

CAB010886; -.

101200; phenotype. [NCBI / EBI]
101600; phenotype. [NCBI / EBI]
123150; phenotype. [NCBI / EBI]
123500; phenotype. [NCBI / EBI]
123790; phenotype. [NCBI / EBI]
149730; phenotype. [NCBI / EBI]
176943; gene. [NCBI / EBI]
207410; phenotype. [NCBI / EBI]
609579; phenotype. [NCBI / EBI]

Orphanet

83; Antley-Bixler syndrome.
87; Apert syndrome.
207; Crouzon disease.
1555; Cutis gyrata - acanthosis nigricans - craniosynostosis.
168624; Familial scaphocephaly syndrome, McGillivray type.
1540; Jackson-Weiss syndrome.
2363; Lacrimo-auriculo-dento-digital syndrome.
710; Pfeiffer syndrome.

PharmGKB

PA28128; -.

Gene expression databases

ArrayExpress

P21802; -.

Bgee

P21802; -.

GermOnline

ENSG00000066468; Homo sapiens.

Ontologies

GO:0009986;	Cellular component: cell surface (inferred from direct assay from UniProtKB).
GO:0005576;	Cellular component: extracellular region (inferred from electronic annotation from UniProtKB-SubCell).
GO:0016021;	Cellular component: integral to membrane (non-traceable author statement from UniProtKB).
GO:0005886;	Cellular component: plasma membrane (inferred from experiment from Reactome).
GO:0005524;	Molecular function: ATP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005007;	Molecular function: fibroblast growth factor receptor activity (non-traceable author statement from UniProtKB).
GO:0008201;	Molecular function: heparin binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515;	Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0016049;	Biological process: cell growth (non-traceable author statement from UniProtKB).
GO:0008543;	Biological process: fibroblast growth factor receptor signaling pathway (inferred from experiment from Reactome).
GO:0006468;	Biological process: protein amino acid phosphorylation (non-traceable author statement from UniProtKB).
QuickGo view.

Family and domain databases

InterPro

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

Gene3D

G3DSA:2.60.40.10; Ig-like_fold; 3.

Pfam

PF00047; ig; 3.
PF07714; Pkinase_Tyr; 1.
Pfam graphical view of domain structure.

PIRSF

PIRSF000628; FGFR; 1.

PRINTS

PR00109; TYRKINASE.

ProDom

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

SMART

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

PROSITE

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

Proteomic databases

PRIDE

P21802; -.

Genome annotation databases

Ensembl

ENSG00000066468; Homo sapiens. [Contig view]

GeneID

2263; -.

KEGG

hsa:2263; -.

Phylogenomic databases

HOVERGEN

P21802; -.

Other

DB00039; Palifermin.

FGFR2; Homo sapiens.

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

Keywords

3D-structure; Alternative splicing; ATP-binding; Cell membrane; Craniosynostosis; Disease mutation; Disulfide bond; Ectodermal dysplasia; Glycoprotein; Heparin-binding; Immunoglobulin domain; Kinase; Lacrimo-auriculo-dento-digital syndrome; Membrane; Nucleotide-binding; Phosphoprotein; Polymorphism; Receptor; Repeat; Secreted; Signal; Transferase; Transmembrane; Tyrosine-protein kinase.

Features

Feature table viewer

Feature aligner

`Key`	`From To`	`Length`	`Description`	`FTId`
`SIGNAL`	`1 21`	`21`	`Potential.`
`CHAIN`	`22 821`	`800`	`Fibroblast growth factor receptor 2.`	`PRO_0000016783`
`TOPO_DOM`	`22 377`	`356`	`Extracellular (Potential).`
`TRANSMEM`	`378 398`	`21`	`Potential.`
`TOPO_DOM`	`399 821`	`423`	`Cytoplasmic (Potential).`
`DOMAIN`	`25 125`	`101`	`Ig-like C2-type 1.`
`DOMAIN`	`154 247`	`94`	`Ig-like C2-type 2.`
`DOMAIN`	`256 358`	`103`	`Ig-like C2-type 3.`
`DOMAIN`	`481 770`	`290`	`Protein kinase.`
`NP_BIND`	`487 495`	`9`	`ATP (By similarity).`
`REGION`	`161 178`	`18`	`Heparin-binding.`
`ACT_SITE`	`626 626`		`Proton acceptor (By similarity).`
`BINDING`	`517 517`		`ATP (By similarity).`
`MOD_RES`	`657 657`		`Phosphotyrosine; by autocatalysis (By similarity).`
`CARBOHYD`	`83 83`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`123 123`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`228 228`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`241 241`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`265 265`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`297 297`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`318 318`		`N-linked (GlcNAc...) (Potential).`
`CARBOHYD`	`331 331`		`N-linked (GlcNAc...) (Potential).`
`DISULFID`	`62 107`		`Potential.`
`DISULFID`	`179 231`		`Potential.`
`DISULFID`	`278 342`		`Potential.`
`VAR_SEQ`	`37 152`		`EPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDG` `VHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSE` `TWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKR -> G (in isoform 20).`	`VSP_019608`
`VAR_SEQ`	`37 125`		`Missing (in isoform 4).`	`VSP_002964`
`VAR_SEQ`	`250 254`		`ERSPH -> GSQGL (in isoform 14).`	`VSP_002965`
`VAR_SEQ`	`255 821`		`Missing (in isoform 14).`	`VSP_002966`
`VAR_SEQ`	`313 313`		`K -> KVLK (in isoform 16).`	`VSP_002967`
`VAR_SEQ`	`314 429`		`Missing (in isoform 15).`	`VSP_002968`
`VAR_SEQ`	`314 330`		`AAGVNTTDKEIEVLYIR -> HSGINSSNAEVLALF (in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18 and isoform 19).`	`VSP_002969`
`VAR_SEQ`	`334 335`		`FE -> EA (in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18 and isoform 19).`	`VSP_002970`
`VAR_SEQ`	`341 353`		`TCLAGNSIGISFH -> ICKVSNYIGQANQ (in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18 and isoform 19).`	`VSP_002971`
`VAR_SEQ`	`361 361`		`P -> PKQQ (in isoform 3, isoform 4, isoform 7, isoform 9, isoform 10, isoform 11, isoform 12, isoform 13, isoform 17, isoform 18 and isoform 19).`	`VSP_002972`
`VAR_SEQ`	`362 365`		`APGR -> GRRC (in isoform 19).`	`VSP_002973`
`VAR_SEQ`	`366 821`		`Missing (in isoform 19).`	`VSP_002974`
`VAR_SEQ`	`428 429`		`Missing (in isoform 4, isoform 5, isoform 6, isoform 8, isoform 16 and isoform 18).`	`VSP_002975`
`VAR_SEQ`	`429 430`		`Missing (in isoform 20).`	`VSP_019609`
`VAR_SEQ`	`761 821`		`LTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSP` `DPMPYEPCLPQYPHINGSVKT -> PPNPSLMSIFRK (in isoform 4).`	`VSP_002976`
`VAR_SEQ`	`768 821`		`EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEP` `CLPQYPHINGSVKT -> SFQSSLKSSSTGIPGWPPGSEVFSEVAFRGILNYDIERPI` `LCAGSKKIYDI (in isoform 10).`	`VSP_002981`
`VAR_SEQ`	`768 821`		`EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEP` `CLPQYPHINGSVKT -> GRLPAWASQEKENSQTSLFAISHVTLSSISKTRSSAKRDE` `KPGSSPHLALVRSQGLPQSVVP (in isoform 11).`	`VSP_002982`
`VAR_SEQ`	`768 821`		`EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEP` `CLPQYPHINGSVKT -> PLS (in isoform 12).`	`VSP_002983`
`VAR_SEQ`	`768 821`		`Missing (in isoform 13).`	`VSP_002977`
`VAR_SEQ`	`768 821`		`EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEP` `CLPQYPHINGSVKT -> I (in isoform 2, isoform 8 and isoform 17).`	`VSP_002978`
`VAR_SEQ`	`768 821`		`EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEP` `CLPQYPHINGSVKT -> RYKLLPCPDKHNKRCKPEERGDLTEAGAAGSSRCVDSRKR` `VRQEKISTG (in isoform 7).`	`VSP_002979`
`VAR_SEQ`	`768 821`		`EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEP` `CLPQYPHINGSVKT -> RILTLTTNENFQSTSGREGTEIHALQCLRSEVTPAISCES` `PLADTGSKVPN (in isoform 9).`	`VSP_002980`
`VAR_SEQ`	`778 821`		`QYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHIN` `GSVKT -> PYSPCYPDPR (in isoform 6).`	`VSP_002984`
`VARIANT`	`6 6`	`1`	`R -> P (in dbSNP:rs3750819 [NCBI]).`	`VAR_017258`
`VARIANT`	`57 57`	`1`	`S -> L.`	`VAR_042204`
`VARIANT`	`105 105`	`1`	`Y -> C (in CS).`	`VAR_004112`
`VARIANT`	`172 172`	`1`	`A -> F (in PS; requires 2 nucleotide substitutions).`	`VAR_017259 [3D]`
`VARIANT`	`186 186`	`1`	`M -> T (in dbSNP:rs755793 [NCBI]).`	`VAR_017260 [3D]`
`VARIANT`	`203 203`	`1`	`R -> C (in breast cancer samples; infiltrating ductal carcinoma; somatic mutation).`	`VAR_036380 [3D]`
`VARIANT`	`252 253`	`2`	`SP -> FS (in PS).`	`VAR_004116`
`VARIANT`	`252 252`	`1`	`S -> F (in APRS; requires 2 nucleotide substitutions).`	`VAR_004114 [3D]`
`VARIANT`	`252 252`	`1`	`S -> L (in CS).`	`VAR_004113 [3D]`
`VARIANT`	`252 252`	`1`	`S -> W (in APRS and PS; common mutation).`	`VAR_004115 [3D]`
`VARIANT`	`253 253`	`1`	`P -> R (in APRS; common mutation).`	`VAR_004117 [3D]`
`VARIANT`	`263 263`	`1`	`P -> L (in CS).`	`VAR_017261 [3D]`
`VARIANT`	`267 267`	`1`	`S -> P (in CS).`	`VAR_004118 [3D]`
`VARIANT`	`268 268`	`1`	`T -> TG (in CS).`	`VAR_004119`
`VARIANT`	`272 272`	`1`	`G -> V (in an ovarian serous carcinoma sample; somatic mutation).`	`VAR_042205 [3D]`
`VARIANT`	`273 273`	`1`	`Missing (in PS; type 2).`	`VAR_017262`
`VARIANT`	`276 276`	`1`	`F -> V (in CS).`	`VAR_004120 [3D]`
`VARIANT`	`278 278`	`1`	`C -> F (in CS, JWS and PS).`	`VAR_004121 [3D]`
`VARIANT`	`278 278`	`1`	`C -> Y (in CS).`	`VAR_017263 [3D]`
`VARIANT`	`281 281`	`1`	`Y -> C (in CS).`	`VAR_017264 [3D]`
`VARIANT`	`283 283`	`1`	`D -> N (in a lung squamous cell carcinoma sample; somatic mutation).`	`VAR_042206 [3D]`
`VARIANT`	`287 289`	`3`	`Missing (in CS).`	`VAR_004122`
`VARIANT`	`288 288`	`1`	`I -> S (in CS).`	`VAR_017265 [3D]`
`VARIANT`	`289 289`	`1`	`Q -> P (in CS and JWS).`	`VAR_004123 [3D]`
`VARIANT`	`290 290`	`1`	`W -> C (in PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation).`	`VAR_004124 [3D]`
`VARIANT`	`290 290`	`1`	`W -> G (in CS).`	`VAR_017266 [3D]`
`VARIANT`	`290 290`	`1`	`W -> R (in CS).`	`VAR_004125 [3D]`
`VARIANT`	`292 292`	`1`	`K -> E (in CS).`	`VAR_004126 [3D]`
`VARIANT`	`301 301`	`1`	`Y -> C (in CS).`	`VAR_004127 [3D]`
`VARIANT`	`314 314`	`1`	`A -> S (in craniosynostosis).`	`VAR_004128 [3D]`
`VARIANT`	`315 315`	`1`	`A -> S (in a non-syndromic craniosynostosis patient with abnormal intrauterine history; confers predisposition to craniosynostosis).`	`VAR_017267 [3D]`
`VARIANT`	`321 321`	`1`	`D -> A (in PS).`	`VAR_004129 [3D]`
`VARIANT`	`328 328`	`1`	`Y -> C (in CS).`	`VAR_004130 [3D]`
`VARIANT`	`331 331`	`1`	`N -> I (in CS).`	`VAR_004131 [3D]`
`VARIANT`	`337 337`	`1`	`A -> ANA (in CS).`	`VAR_004132`
`VARIANT`	`337 337`	`1`	`A -> P (in CS).`	`VAR_017268 [3D]`
`VARIANT`	`338 338`	`1`	`G -> E (in CS).`	`VAR_004133 [3D]`
`VARIANT`	`338 338`	`1`	`G -> R (in CS).`	`VAR_015011 [3D]`
`VARIANT`	`340 340`	`1`	`Y -> C (in PS).`	`VAR_017269 [3D]`
`VARIANT`	`340 340`	`1`	`Y -> H (in CS).`	`VAR_004134 [3D]`
`VARIANT`	`341 341`	`1`	`T -> P (in PS and CS).`	`VAR_004135 [3D]`
`VARIANT`	`342 342`	`1`	`C -> F (in CS).`	`VAR_004136 [3D]`
`VARIANT`	`342 342`	`1`	`C -> G (in PS).`	`VAR_017270 [3D]`
`VARIANT`	`342 342`	`1`	`C -> R (in CS, JWS, PS and ABS).`	`VAR_004137 [3D]`
`VARIANT`	`342 342`	`1`	`C -> S (in CS, JWS, PS and ABS).`	`VAR_004138 [3D]`
`VARIANT`	`342 342`	`1`	`C -> W (in CS).`	`VAR_017271 [3D]`
`VARIANT`	`342 342`	`1`	`C -> Y (in CS and PS).`	`VAR_004139 [3D]`
`VARIANT`	`344 344`	`1`	`A -> G (in CS and JWS).`	`VAR_004140 [3D]`
`VARIANT`	`344 344`	`1`	`A -> P (in CS and PS).`	`VAR_004141 [3D]`
`VARIANT`	`347 347`	`1`	`S -> C (in CS).`	`VAR_004142 [3D]`
`VARIANT`	`351 351`	`1`	`S -> C (in CS, PS and ABS).`	`VAR_004143 [3D]`
`VARIANT`	`354 354`	`1`	`S -> C (in CS).`	`VAR_004144 [3D]`
`VARIANT`	`354 354`	`1`	`S -> Y (in CS).`	`VAR_017272 [3D]`
`VARIANT`	`356 358`	`3`	`Missing (in CS).`	`VAR_004145`
`VARIANT`	`359 359`	`1`	`V -> F (in CS and PS).`	`VAR_004146 [3D]`
`VARIANT`	`362 362`	`1`	`A -> S (in CS).`	`VAR_017273 [3D]`
`VARIANT`	`372 372`	`1`	`S -> C (in Beare-Stevenson cutis gyrata syndrome).`	`VAR_017274`
`VARIANT`	`375 375`	`1`	`Y -> C (in PS and Beare-Stevenson cutis gyrata syndrome).`	`VAR_017275`
`VARIANT`	`384 384`	`1`	`G -> R (in CS).`	`VAR_004147`
`VARIANT`	`526 526`	`1`	`K -> E (in FSPC).`	`VAR_023788`
`VARIANT`	`549 549`	`1`	`N -> H (in CS).`	`VAR_017276`
`VARIANT`	`565 565`	`1`	`E -> G (in PS).`	`VAR_017277`
`VARIANT`	`612 612`	`1`	`R -> T (in a lung adenocarcinoma sample; somatic mutation).`	`VAR_046071`
`VARIANT`	`613 613`	`1`	`G -> R.`	`VAR_015012`
`VARIANT`	`628 628`	`1`	`A -> T (in LADDS).`	`VAR_029884`
`VARIANT`	`641 641`	`1`	`K -> R (in PS).`	`VAR_017278`
`VARIANT`	`648 648`	`1`	`A -> T (in LADDS).`	`VAR_029885`
`VARIANT`	`649 650`	`2`	`RD -> S (in LADDS).`	`VAR_029886`
`VARIANT`	`659 659`	`1`	`K -> N (in craniosynostosis).`	`VAR_017279`
`VARIANT`	`663 663`	`1`	`G -> E (in PS).`	`VAR_017280`
`VARIANT`	`678 678`	`1`	`R -> G (in CS).`	`VAR_017281`
`STRAND`	`153 157`	`5`
`HELIX`	`160 162`	`3`
`STRAND`	`166 170`	`5`
`STRAND`	`175 178`	`4`
`STRAND`	`181 185`	`5`
`STRAND`	`188 193`	`6`
`HELIX`	`200 202`	`3`
`TURN`	`211 213`	`3`
`STRAND`	`215 218`	`4`
`HELIX`	`223 225`	`3`
`STRAND`	`227 235`	`9`
`STRAND`	`238 249`	`12`
`STRAND`	`266 269`	`4`
`STRAND`	`274 277`	`4`
`STRAND`	`287 293`	`7`
`STRAND`	`309 314`	`6`
`HELIX`	`321 325`	`5`
`STRAND`	`326 329`	`4`
`STRAND`	`338 345`	`8`
`STRAND`	`350 360`	`11`
`TURN`	`472 474`	`3`
`HELIX`	`478 480`	`3`
`STRAND`	`481 489`	`9`
`STRAND`	`491 501`	`11`
`STRAND`	`511 518`	`8`
`HELIX`	`525 541`	`17`
`STRAND`	`550 554`	`5`
`STRAND`	`556 559`	`4`
`STRAND`	`561 565`	`5`
`HELIX`	`572 578`	`7`
`HELIX`	`600 619`	`20`
`STRAND`	`632 634`	`3`
`STRAND`	`640 642`	`3`
`TURN`	`657 659`	`3`
`HELIX`	`667 669`	`3`
`HELIX`	`672 676`	`5`
`HELIX`	`682 697`	`16`
`HELIX`	`709 718`	`10`
`HELIX`	`730 739`	`10`
`HELIX`	`744 746`	`3`
`HELIX`	`750 762`	`13`

Sequence information

Length: 821 AA [This is the length of the unprocessed precursor]

Molecular weight: 92025 Da [This is the MW of the unprocessed precursor]

CRC64: 6CD5001C960ED82F [This is a checksum on the sequence]

        10         20         30         40         50         60 
MVSWGRFICL VVVTMATLSL ARPSFSLVED TTLEPEEPPT KYQISQPEVY VAAPGESLEV 

        70         80         90        100        110        120 
RCLLKDAAVI SWTKDGVHLG PNNRTVLIGE YLQIKGATPR DSGLYACTAS RTVDSETWYF 

       130        140        150        160        170        180 
MVNVTDAISS GDDEDDTDGA EDFVSENSNN KRAPYWTNTE KMEKRLHAVP AANTVKFRCP 

       190        200        210        220        230        240 
AGGNPMPTMR WLKNGKEFKQ EHRIGGYKVR NQHWSLIMES VVPSDKGNYT CVVENEYGSI 

       250        260        270        280        290        300 
NHTYHLDVVE RSPHRPILQA GLPANASTVV GGDVEFVCKV YSDAQPHIQW IKHVEKNGSK 

       310        320        330        340        350        360 
YGPDGLPYLK VLKAAGVNTT DKEIEVLYIR NVTFEDAGEY TCLAGNSIGI SFHSAWLTVL 

       370        380        390        400        410        420 
PAPGREKEIT ASPDYLEIAI YCIGVFLIAC MVVTVILCRM KNTTKKPDFS SQPAVHKLTK 

       430        440        450        460        470        480 
RIPLRRQVTV SAESSSSMNS NTPLVRITTR LSSTADTPML AGVSEYELPE DPKWEFPRDK 

       490        500        510        520        530        540 
LTLGKPLGEG CFGQVVMAEA VGIDKDKPKE AVTVAVKMLK DDATEKDLSD LVSEMEMMKM 

       550        560        570        580        590        600 
IGKHKNIINL LGACTQDGPL YVIVEYASKG NLREYLRARR PPGMEYSYDI NRVPEEQMTF 

       610        620        630        640        650        660 
KDLVSCTYQL ARGMEYLASQ KCIHRDLAAR NVLVTENNVM KIADFGLARD INNIDYYKKT 

       670        680        690        700        710        720 
TNGRLPVKWM APEALFDRVY THQSDVWSFG VLMWEIFTLG GSPYPGIPVE ELFKLLKEGH 

       730        740        750        760        770        780 
RMDKPANCTN ELYMMMRDCW HAVPSQRPTF KQLVEDLDRI LTLTTNEEYL DLSQPLEQYS 

       790        800        810        820 
PSYPDTRSSC SSGDDSVFSP DPMPYEPCLP QYPHINGSVK T

P21802 in FASTA format

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