Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P21802 (FGFR2_HUMAN)

Last modified February 9, 2010. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Fibroblast growth factor receptor 2
      Short name=FGFR-2
    EC=2.7.10.1
Alternative name(s):
    Keratinocyte growth factor receptor
    K-sam
    CD_antigen=CD332
Gene names
Name: FGFR2
Synonyms: BEK, KGFR, KSAM
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length821 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Receptor for acidic and basic fibroblast growth factors.

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.

Subcellular location

Cell membrane; Single-pass type I membrane protein.

Isoform 14: Secreted.

Isoform 19: Secreted.

Involvement in 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. Ref.10 Ref.21 Ref.29 Ref.30 Ref.31 Ref.32 Ref.36 Ref.37 Ref.38 Ref.42 Ref.43 Ref.44 Ref.45 Ref.49 Ref.52 Ref.55 Ref.56

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. Ref.30 Ref.32 Ref.36 Ref.44 Ref.41

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. Ref.42 Ref.44 Ref.56 Ref.18 Ref.26 Ref.34 Ref.46

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). Ref.36 Ref.42 Ref.52 Ref.56 Ref.33 Ref.35 Ref.40 Ref.47 Ref.48 Ref.50 Ref.51

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. Ref.39 Ref.57

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. Ref.58

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. Ref.59

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. Ref.54

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Ontologies

Keywords
   Cellular componentCell membrane
Membrane
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseCraniosynostosis
Disease mutation
Ectodermal dysplasia
Lacrimo-auriculo-dento-digital syndrome
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
   LigandATP-binding
Heparin-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcell growth Ref.19

Non-traceable author statement. Source: UniProtKB

fibroblast growth factor receptor signaling pathway Ref.23

Inferred from genetic interaction. Source: MGI

positive regulation of cell proliferation

Inferred from genetic interaction. Source: MGI

protein amino acid phosphorylation Ref.1

Non-traceable author statement. Source: UniProtKB

   Cellular componentcell cortex

Inferred from direct assay. Source: UniProtKB

cell surface

Inferred from direct assay. Source: UniProtKB

extracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

integral to membrane Ref.1

Non-traceable author statement. Source: UniProtKB

nucleus

Inferred from direct assay. Source: UniProtKB

plasma membrane Ref.1

Inferred from Experiment. Source: Reactome

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fibroblast growth factor binding

Inferred from physical interaction. Source: UniProtKB

fibroblast growth factor receptor activity Ref.1 Ref.6 Ref.19 Ref.23

Non-traceable author statement. Source: UniProtKB

heparin binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 20 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P21802-1)

Also known as: BEK;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P21802-2)

Also known as: Short;

The sequence of this isoform differs from the canonical sequence as follows:
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 3 (identifier: P21802-3)

Also known as: BFR-1;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
Isoform 4 (identifier: P21802-4)

Also known as: K-sam;

The sequence of this isoform differs from the canonical sequence as follows:
     37-125: Missing.
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     428-429: Missing.
     761-821: LTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → PPNPSLMSIFRK
Isoform 5 (identifier: P21802-5)

Also known as: K-sam-I; BEK; IgIIIc;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
Isoform 6 (identifier: P21802-6)

Also known as: K-sam-IIC2;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     778-821: QYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → PYSPCYPDPR
Isoform 7 (identifier: P21802-7)

Also known as: K-sam-IIO2;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → RYKLLPCPDK...RVRQEKISTG
Isoform 8 (identifier: P21802-8)

Also known as: K-sam-IIC3;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 9 (identifier: P21802-9)

Also known as: K-sam-IIH1;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → RILTLTTNEN...LADTGSKVPN
Isoform 10 (identifier: P21802-10)

Also known as: K-sam-IIH2;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → SFQSSLKSSS...CAGSKKIYDI
Isoform 11 (identifier: P21802-11)

Also known as: K-sam-IIH3; K-sam-IIO4;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLE...YPHINGSVKT → GRLPAWASQE...SQGLPQSVVP
Isoform 12 (identifier: P21802-12)

Also known as: K-sam-IIO1;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → PLS
Isoform 13 (identifier: P21802-13)

Also known as: K-sam-IIO3;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: Missing.
Isoform 14 (identifier: P21802-14)

Also known as: K-sam-IV; Soluble KGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     250-254: ERSPH → GSQGL
     255-821: Missing.
Isoform 15 (identifier: P21802-15)

Also known as: K-sam-III;

The sequence of this isoform differs from the canonical sequence as follows:
     314-429: Missing.
Isoform 16 (identifier: P21802-16)

Also known as: TK14;

The sequence of this isoform differs from the canonical sequence as follows:
     313-313: K → KVLK
     428-429: Missing.
Isoform 17 (identifier: P21802-17)

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     768-821: EYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT → I
Isoform 18 (identifier: P21802-18)

Also known as: K-sam-IIC1; KGFR; IgIIIb;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     428-429: Missing.
Isoform 19 (identifier: P21802-19)

Also known as: Soluble KGFR;

The sequence of this isoform differs from the canonical sequence as follows:
     314-330: AAGVNTTDKEIEVLYIR → HSGINSSNAEVLALF
     334-335: FE → EA
     341-353: TCLAGNSIGISFH → ICKVSNYIGQANQ
     361-361: P → PKQQ
     362-365: APGR → GRRC
     366-821: Missing.
Isoform 20 (identifier: P21802-20)

The sequence of this isoform differs from the canonical sequence as follows:
     37-152: EPPTKYQISQ...FVSENSNNKR → G
     429-430: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 821800Fibroblast growth factor receptor 2
PRO_0000016783

Regions

Topological domain22 – 377356Extracellular Potential
Transmembrane378 – 39821 Potential
Topological domain399 – 821423Cytoplasmic Potential
Domain25 – 125101Ig-like C2-type 1
Domain154 – 24794Ig-like C2-type 2
Domain256 – 358103Ig-like C2-type 3
Domain481 – 770290Protein kinase
Nucleotide binding487 – 4959ATP By similarity
Region161 – 17818Heparin-binding

Sites

Active site6261Proton acceptor By similarity
Binding site5171ATP By similarity

Amino acid modifications

Modified residue4481Phosphothreonine
Modified residue4491Phosphothreonine
Modified residue6571Phosphotyrosine; by autocatalysis By similarity
Glycosylation831N-linked (GlcNAc...) Potential
Glycosylation1231N-linked (GlcNAc...) Potential
Glycosylation2281N-linked (GlcNAc...) Potential
Glycosylation2411N-linked (GlcNAc...) Potential
Glycosylation2651N-linked (GlcNAc...) Potential
Glycosylation2971N-linked (GlcNAc...) Potential
Glycosylation3181N-linked (GlcNAc...) Potential
Glycosylation3311N-linked (GlcNAc...) Potential
Disulfide bond62 ↔ 107 Potential
Disulfide bond179 ↔ 231 Potential
Disulfide bond278 ↔ 342 Potential

Natural variations

Alternative sequence37 – 152116EPPTK…SNNKR → G in isoform 20.
VSP_019608
Alternative sequence37 – 12589Missing in isoform 4.
VSP_002964
Alternative sequence250 – 2545ERSPH → GSQGL in isoform 14.
VSP_002965
Alternative sequence255 – 821567Missing in isoform 14.
VSP_002966
Alternative sequence3131K → KVLK in isoform 16.
VSP_002967
Alternative sequence314 – 429116Missing in isoform 15.
VSP_002968
Alternative sequence314 – 33017AAGVN…VLYIR → 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
Alternative sequence334 – 3352FE → 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
Alternative sequence341 – 35313TCLAG…GISFH → 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
Alternative sequence3611P → 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
Alternative sequence362 – 3654APGR → GRRC in isoform 19.
VSP_002973
Alternative sequence366 – 821456Missing in isoform 19.
VSP_002974
Alternative sequence428 – 4292Missing in isoform 4, isoform 5, isoform 6, isoform 8, isoform 16 and isoform 18.
VSP_002975
Alternative sequence429 – 4302Missing in isoform 20.
VSP_019609
Alternative sequence761 – 82161LTLTT…GSVKT → PPNPSLMSIFRK in isoform 4.
VSP_002976
Alternative sequence768 – 82154EYLDL…GSVKT → SFQSSLKSSSTGIPGWPPGS EVFSEVAFRGILNYDIERPI LCAGSKKIYDI in isoform 10.
VSP_002981
Alternative sequence768 – 82154EYLDL…GSVKT → GRLPAWASQEKENSQTSLFA ISHVTLSSISKTRSSAKRDE KPGSSPHLALVRSQGLPQSV VP in isoform 11.
VSP_002982
Alternative sequence768 – 82154EYLDL…GSVKT → PLS in isoform 12.
VSP_002983
Alternative sequence768 – 82154Missing in isoform 13.
VSP_002977
Alternative sequence768 – 82154EYLDL…GSVKT → I in isoform 2, isoform 8 and isoform 17.
VSP_002978
Alternative sequence768 – 82154EYLDL…GSVKT → RYKLLPCPDKHNKRCKPEER GDLTEAGAAGSSRCVDSRKR VRQEKISTG in isoform 7.
VSP_002979
Alternative sequence768 – 82154EYLDL…GSVKT → RILTLTTNENFQSTSGREGT EIHALQCLRSEVTPAISCES PLADTGSKVPN in isoform 9.
VSP_002980
Alternative sequence778 – 82144QYSPS…GSVKT → PYSPCYPDPR in isoform 6.
VSP_002984
Natural variant61R → P: dbSNP rs3750819. Ref.14
VAR_017258
Natural variant571S → L: dbSNP rs56226109. Ref.61
VAR_042204
Natural variant1051Y → C in CS. Ref.37 Ref.56
VAR_004112
Natural variant1721A → F in PS; requires 2 nucleotide substitutions. Ref.56
VAR_017259
Natural variant1861M → T: dbSNP rs755793. Ref.56 Ref.14 Ref.61
VAR_017260
Natural variant2031R → C in breast cancer samples; infiltrating ductal carcinoma; somatic mutation. Ref.61 Ref.60
VAR_036380
Natural variant252 – 2532SP → FS in PS.
VAR_004116
Natural variant2521S → F in APRS; requires 2 nucleotide substitutions. Ref.42
VAR_004114
Natural variant2521S → L in CS. Ref.42
VAR_004113
Natural variant2521S → W in APRS and PS; common mutation. Ref.44 Ref.56 Ref.18 Ref.26 Ref.34 Ref.46 Ref.48
VAR_004115
Natural variant2531P → R in APRS; common mutation. Ref.44 Ref.56 Ref.18 Ref.26 Ref.34 Ref.46
VAR_004117
Natural variant2631P → L in CS. Ref.52
VAR_017261
Natural variant2671S → P in CS. Ref.56
VAR_004118
Natural variant2681T → TG in CS. Ref.36
VAR_004119
Natural variant2721G → V in an ovarian serous carcinoma sample; somatic mutation. Ref.61
VAR_042205
Natural variant2731Missing in PS; type 2.
VAR_017262
Natural variant2761F → V in CS. Ref.45 Ref.52 Ref.56
VAR_004120
Natural variant2781C → F in CS, JWS and PS. Ref.36 Ref.44 Ref.52 Ref.56
VAR_004121
Natural variant2781C → Y in CS. Ref.52
VAR_017263
Natural variant2811Y → C in CS. Ref.55 Ref.56
VAR_017264
Natural variant2831D → N in a lung squamous cell carcinoma sample; somatic mutation. Ref.61
VAR_042206
Natural variant287 – 2893Missing in CS.
VAR_004122
Natural variant2881I → S in CS. Ref.52
VAR_017265
Natural variant2891Q → P in CS and JWS. Ref.21 Ref.36 Ref.52 Ref.55 Ref.56
VAR_004123
Natural variant2901W → C in PS; severe; also in a lung squamous cell carcinoma sample; somatic mutation. Ref.56 Ref.40 Ref.61
VAR_004124
Natural variant2901W → G in CS. Ref.32
VAR_017266
Natural variant2901W → R in CS.
VAR_004125
Natural variant2921K → E in CS. Ref.43
VAR_004126
Natural variant3011Y → C in CS. Ref.45
VAR_004127
Natural variant3141A → S in craniosynostosis. Ref.45
VAR_004128
Natural variant3151A → S in a non-syndromic craniosynostosis patient with abnormal intrauterine history; confers predisposition to craniosynostosis. Ref.56 Ref.53
VAR_017267
Natural variant3211D → A in PS. Ref.33
VAR_004129
Natural variant3281Y → C in CS. Ref.30
VAR_004130
Natural variant3311N → I in CS. Ref.38
VAR_004131
Natural variant3371A → ANA in CS.
VAR_004132
Natural variant3371A → P in CS. Ref.44
VAR_017268
Natural variant3381G → E in CS. Ref.37
VAR_004133
Natural variant3381G → R in CS. Ref.21 Ref.44 Ref.56
VAR_015011
Natural variant3401Y → C in PS. Ref.56 Ref.50
VAR_017269
Natural variant3401Y → H in CS. Ref.29 Ref.56
VAR_004134
Natural variant3411T → P in PS and CS. Ref.52 Ref.56 Ref.35
VAR_004135
Natural variant3421C → F in CS. Ref.36 Ref.44 Ref.56
VAR_004136
Natural variant3421C → G in PS. Ref.50
VAR_017270
Natural variant3421C → R in CS, JWS, PS and ABS. Ref.29 Ref.32 Ref.36 Ref.44 Ref.52 Ref.55 Ref.56 Ref.35 Ref.54
VAR_004137
Natural variant3421C → S in CS, JWS, PS and ABS. Ref.10 Ref.21 Ref.29 Ref.36 Ref.52 Ref.56 Ref.41 Ref.54
VAR_004138
Natural variant3421C → W in CS. Ref.32 Ref.52 Ref.56
VAR_017271
Natural variant3421C → Y in CS and PS. Ref.21 Ref.29 Ref.36 Ref.44 Ref.52 Ref.55 Ref.56 Ref.35
VAR_004139
Natural variant3441A → G in CS and JWS. Ref.21 Ref.30
VAR_004140
Natural variant3441A → P in CS and PS. Ref.36
VAR_004141
Natural variant3471S → C in CS. Ref.30 Ref.56
VAR_004142
Natural variant3511S → C in CS, PS and ABS. Ref.37 Ref.47 Ref.54
VAR_004143
Natural variant3541S → C in CS. Ref.21 Ref.29 Ref.32 Ref.52 Ref.56
VAR_004144
Natural variant3541S → Y in CS. Ref.52
VAR_017272
Natural variant356 – 3583Missing in CS.
VAR_004145
Natural variant3591V → F in CS and PS. Ref.36 Ref.52
VAR_004146
Natural variant3621A → S in CS. Ref.49
VAR_017273
Natural variant3721S → C in Beare-Stevenson cutis gyrata syndrome. Ref.39
VAR_017274
Natural variant3751Y → C in PS and Beare-Stevenson cutis gyrata syndrome. Ref.56 Ref.39 Ref.57
VAR_017275
Natural variant3841G → R in CS. Ref.37
VAR_004147
Natural variant5261K → E in FSPC. Ref.58
VAR_023788
Natural variant5491N → H in CS. Ref.56
VAR_017276
Natural variant5651E → G in PS. Ref.56
VAR_017277
Natural variant6121R → T in a lung adenocarcinoma sample; somatic mutation. Ref.61
VAR_046071
Natural variant6131G → R
VAR_015012
Natural variant6281A → T in LADDS. Ref.59
VAR_029884
Natural variant6411K → R in PS. Ref.56
VAR_017278
Natural variant6481A → T in LADDS. Ref.59
VAR_029885
Natural variant649 – 6502RD → S in LADDS.
VAR_029886
Natural variant6591K → N in craniosynostosis. Ref.56
VAR_017279
Natural variant6631G → E in PS. Ref.56
VAR_017280
Natural variant6781R → G in CS. Ref.56
VAR_017281

Secondary structure

................................................................................. 821
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (BEK) [UniParc].

Last modified May 1, 1991. Version 1.
Checksum: 6CD5001C960ED82F

FASTA82192,025
        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 

« Hide

Isoform 2 (Short).

Checksum: 8D4734CBEA8E8C8F
Show »

FASTA76886,130
Isoform 3 (BFR-1).

Checksum: 288CF737673BA4AB
Show »

FASTA82292,118
Isoform 4 (K-sam).

Checksum: D56050B4385A6635
Show »

FASTA68276,705
Isoform 5 (K-sam-I) (BEK) (IgIIIc).

Checksum: 4746938783A1D94F
Show »

FASTA81991,825
Isoform 6 (K-sam-IIC2).

Checksum: 042BF83F92CE97F5
Show »

FASTA78588,181
Isoform 7 (K-sam-IIO2).

Checksum: 46BA78E51DB700CD
Show »

FASTA81791,620
Isoform 8 (K-sam-IIC3).

Checksum: FE97A413B085D31E
Show »

FASTA76685,929
Isoform 9 (K-sam-IIH1).

Checksum: C60FE09EC1BE0654
Show »

FASTA81991,566
Isoform 10 (K-sam-IIH2).

Checksum: 467E9BAAD07C5463
Show »

FASTA81991,641
Isoform 11 (K-sam-IIH3) (K-sam-IIO4).

Checksum: E726FA4235995586
Show »

FASTA83092,733
Isoform 12 (K-sam-IIO1).

Checksum: 881C475B4771CA5C
Show »

FASTA77186,407
Isoform 13 (K-sam-IIO3).

Checksum: BB4771CA5CBEEFAA
Show »

FASTA76886,110
Isoform 14 (K-sam-IV) (Soluble KGFR).

Checksum: 1855113266C85F4F
Show »

FASTA25428,299
Isoform 15 (K-sam-III).

Checksum: 590967DCBF5DA25D
Show »

FASTA70579,212
Isoform 16 (TK14).

Checksum: 15D08A690BB44EA0
Show »

FASTA82292,165
Isoform 17.

Checksum: 806B4771CA5CBEEF
Show »

FASTA76986,223
Isoform 18 (K-sam-IIC1) (KGFR) (IgIIIb).

Checksum: 806D62B2FF25AFF6
Show »

FASTA82091,918
Isoform 19 (Soluble KGFR).

Checksum: C02708836203465F
Show »

FASTA36640,614
Isoform 20.

Checksum: 287F39DCF95B9312
Show »

FASTA70479,197

References

« Hide 'large scale' references
[1]"Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors."
Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G., Ruta M., Burgess W.H., Jaye M., Schlessinger J.
EMBO J. 9:2685-2692(1990) [PubMed: 1697263] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Neonatal brain stem.
[2]"Related fibroblast growth factor receptor genes exist in the human genome."
Houssaint E., Blanquet P.R., Champion-Arnaud P., Gesnel M.-C., Torriglia A., Courtois Y., Breathnach R.
Proc. Natl. Acad. Sci. U.S.A. 87:8180-8184(1990) [PubMed: 2172978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 16).
[3]"Two cDNAs encoding novel human FGF receptor."
Seno M., Sasada R., Watanabe T., Ishimaru K., Igarashi K.
Biochim. Biophys. Acta 1089:244-246(1991) [PubMed: 1647213] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 17).
[4]"K-sam, an amplified gene in stomach cancer, is a member of the heparin-binding growth factor receptor genes."
Hattori Y., Odagiri H., Nakatani H., Miyagawa K., Naito K., Sakamoto H., Katoh O., Yoshida T., Sugimura T., Terada M.
Proc. Natl. Acad. Sci. U.S.A. 87:5983-5987(1990) [PubMed: 2377625] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
Tissue: Stomach cancer.
[5]"K-sam gene encodes secreted as well as transmembrane receptor tyrosine kinase."
Katoh M., Hattori Y., Sasaki H., Tanaka M., Sugano K., Yazaki Y., Sugimura T., Terada M.
Proc. Natl. Acad. Sci. U.S.A. 89:2960-2964(1992) [PubMed: 1313574] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 5; 14 AND 15).
[6]"A novel form of fibroblast growth factor receptor 2. Alternative splicing of the third immunoglobulin-like domain confers ligand binding specificity."
Dell K.R., Williams L.T.
J. Biol. Chem. 267:21225-21229(1992) [PubMed: 1400433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Tissue: Placenta.
[7]"Determination of ligand-binding specificity by alternative splicing: two distinct growth factor receptors encoded by a single gene."
Miki T., Bottaro D.P., Fleming T.P., Smith C.L., Burgess W.H., Chan A.M.-L., Aaronson S.A.
Proc. Natl. Acad. Sci. U.S.A. 89:246-250(1992) [PubMed: 1309608] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 19), VARIANT ARG-613.
Tissue: Mammary gland.
[8]"Hepatocyte growth factor (HGF), keratinocyte growth factor (KGF), and their receptors in human breast cells and tissues: alternative receptors."
Wilson S.E., Weng J., Chwang E.L., Gollahon L., Leitch A.M., Shay J.W.
Cell. Mol. Biol. Res. 40:337-350(1994) [PubMed: 7866434] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19).
Tissue: Cornea and Mammary gland.
[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]Steinberger D., Mueller U.
Submitted (APR-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT CS SER-342.
Tissue: Blood.
[11]"Deletion of the carboxyl-terminal exons of K-sam/FGFR2 by short homology-mediated recombination, generating preferential expression of specific messenger RNAs."
Ueda T., Sasaki H., Kuwahara Y., Nezu M., Shibuya T., Sakamoto H., Ishii H., Yanagihara K., Mafune K., Makuuchi M., Terada M.
Cancer Res. 59:6080-6086(1999) [PubMed: 10626794] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 7; 9; 10; 11; 12 AND 13), VARIANT ARG-613.
[12]"Fibroblast growth factor receptor 2 (FGFR2): genomic sequence and variations."
Ingersoll R.G., Paznekas W.A., Tran A.K., Scott A.F., Jiang G., Jabs E.W.
Cytogenet. Cell Genet. 94:121-126(2001) [PubMed: 11856867] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS 5; 6; 8; 14 AND 18).
[13]"Sequence and polymorphisms in fibroblast growth factor receptor 2 (FGFR2) gene in humans."
Lind D.L., Cox D.R.
Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 3).
[14]NIEHS SNPs program
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS PRO-6 AND THR-186.
[15]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 20).
Tissue: Brain.
[16]"Paternal origin of FGFR2 mutations in sporadic cases of Crouzon syndrome and Pfeiffer syndrome."
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.
Am. J. Hum. Genet. 66:768-777(2000) [PubMed: 10712195] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 314-427.
[17]"Genomic organization of the human fibroblast growth factor receptor 2 (FGFR2) gene and comparative analysis of the human FGFR gene family."
Zhang Y., Gorry M.C., Post J.C., Ehrlich G.D.
Gene 230:69-79(1999) [PubMed: 10196476] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209; 212-767 AND 771-821 (ISOFORMS 5; 14 AND 18).
[18]"Analysis of phenotypic features and FGFR2 mutations in Apert syndrome."
Park W.-J., Theda C., Maestri N.E., Meyers G.A., Fryburg J.S., Dufresne C., Cohen M.M. Jr., Jabs E.W.
Am. J. Hum. Genet. 57:321-328(1995) [PubMed: 7668257] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 249-313, VARIANTS APRS TRP-252 AND ARG-253.
[19]"Nucleotide sequences at intron 6 and exon 7 junction of fibroblast growth factor receptor 2 and rapid mutational analysis in Apert syndrome."
Wada C., Ishigaki M., Toyo-oka Y., Yamabe H., Ohnuki Y., Takada F., Yamazaki Y., Ohtani H.
Rinsho Byori 44:435-438(1996) [PubMed: 8676562] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-259.
[20]"Exclusive paternal origin of new mutations in Apert syndrome."
Moloney D.M., Slaney S.F., Oldridge M., Wall S.A., Sahlin P., Stenman G., Wilkie A.O.M.
Nat. Genet. 13:48-53(1996) [PubMed: 8673103] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 251-318.
[21]"Crouzon syndrome: mutations in two spliceoforms of FGFR2 and a common point mutation shared with Jackson-Weiss syndrome."
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.
Hum. Mol. Genet. 4:1387-1390(1995) [PubMed: 7581378] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 263-361, VARIANTS CS PRO-289; ARG-338; SER-342; TYR-342; GLY-344 AND CYS-354.
[22]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-448 AND THR-449, MASS SPECTROMETRY.
[23]"Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."
Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.
Cell 101:413-424(2000) [PubMed: 10830168] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 147-366 IN COMPLEX WITH FGF2.
[24]"Crystal structure of fibroblast growth factor receptor ectodomain bound to ligand and heparin."
Pellegrini L., Burke D.F., von Delft F., Mulloy B., Blundell T.L.
Nature 407:1029-1034(2000) [PubMed: 11069186] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 148-366 IN COMPLEX WITH FGF1 AND HEPARIN.
[25]"Structural interactions of fibroblast growth factor receptor with its ligands."
Stauber D.J., DiGabriele A.D., Hendrickson W.A.
Proc. Natl. Acad. Sci. U.S.A. 97:49-54(2000) [PubMed: 10618369] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 147-362 IN COMPLEX WITH FGF1.
[26]"Structural basis for fibroblast growth factor receptor 2 activation in Apert syndrome."
Ibrahimi O.A., Eliseenkova A.V., Plotnikov A.N., Yu K., Ornitz D.M., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 98:7182-7187(2001) [PubMed: 11390973] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 147-366 OF VARIANTS APRS TRP-252 AND ARG-253 IN COMPLEX WITH FGF2.
[27]"Structural basis by which alternative splicing confers specificity in fibroblast growth factor receptors."
Yeh B.K., Igarashi M., Eliseenkova A.V., Plotnikov A.N., Sher I., Ron D., Aaronson S.A., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 100:2266-2271(2003) [PubMed: 12591959] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 140-371 IN COMPLEX WITH FGF10.
[28]"Structural basis by which alternative splicing modulates the organizer activity of FGF8 in the brain."
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.
Genes Dev. 20:185-198(2006) [PubMed: 16384934] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.28 ANGSTROMS) OF 149-368 IN COMPLEX WITH FGF8.
[29]"Mutations in the fibroblast growth factor receptor 2 gene cause Crouzon syndrome."
Reardon W., Winter R.M., Rutland P., Pulleyn L.J., Jones B.M., Malcolm S.
Nat. Genet. 8:98-103(1994) [PubMed: 7987400] [Abstract]
Cited for: VARIANTS CS HIS-340; ARG-342; SER-342; TYR-342 AND CYS-354.
[30]"Jackson-Weiss and Crouzon syndromes are allelic with mutations in fibroblast growth factor receptor 2."
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.
Nat. Genet. 8:275-279(1994) [PubMed: 7874170] [Abstract]
Cited for: VARIANTS CS CYS-328 AND CYS-347, VARIANT JWS GLY-344.
[31]"Mutations in the third immunoglobulin domain of the fibroblast growth factor receptor-2 gene in Crouzon syndrome."
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.
Hum. Mol. Genet. 4:1077-1082(1995) [PubMed: 7655462] [Abstract]
Cited for: VARIANTS CS.
[32]"Novel FGFR2 mutations in Crouzon and Jackson-Weiss syndromes show allelic heterogeneity and phenotypic variability."
Park W.-J., Meyers G.A., Li X., Theda C., Day D., Orlow S.J., Jones M.C., Jabs E.W.
Hum. Mol. Genet. 4:1229-1233(1995) [PubMed: 8528214] [Abstract]
Cited for: VARIANTS CS GLY-290; TRP-342 AND CYS-354, VARIANT JWS ARG-342.
[33]"FGFR2 mutations in Pfeiffer syndrome."
Lajeunie E., Wei M.H., Bonaventure J., Munnich A., le Merrer M., Renier D.
Nat. Genet. 9:108-108(1995) [PubMed: 7719333] [Abstract]
Cited for: VARIANT PS ALA-321.
[34]"Apert syndrome results from localized mutations of FGFR2 and is allelic with Crouzon syndrome."
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.
Nat. Genet. 9:165-172(1995) [PubMed: 7719344] [Abstract]
Cited for: VARIANTS APRS TRP-252 AND ARG-253.
[35]"Identical mutations in the FGFR2 gene cause both Pfeiffer and Crouzon syndrome phenotypes."
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.
Nat. Genet. 9:173-176(1995) [PubMed: 7719345] [Abstract]
Cited for: VARIANTS PS PRO-341; ARG-342 AND TYR-342.
[36]"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."
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.
Am. J. Hum. Genet. 58:491-498(1996) [PubMed: 8644708] [Abstract]
Cited for: VARIANTS CS GLY-268 INS; PHE-342 AND TYR-342, VARIANTS PS PHE-278; ARG-342; SER-342; PRO-344 AND PHE-359, VARIANT JWS PRO-289.
[37]"Spectrum of craniosynostosis phenotypes associated with novel mutations at the fibroblast growth factor receptor 2 locus."
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.
Eur. J. Hum. Genet. 4:283-291(1996) [PubMed: 8946174] [Abstract]
Cited for: VARIANTS CS CYS-105; GLU-338; CYS-351 AND ARG-384.
[38]"Crouzon syndrome: previously unrecognized deletion, duplication, and point mutation within FGFR2 gene."
Steinberger D., Mulliken J.B., Mueller U.
Hum. Mutat. 8:386-390(1996) [PubMed: 8956050] [Abstract]
Cited for: VARIANTS CS ILE-331; ASN-ALA-337 INS AND 356-TRP--THR-358 DEL.
[39]"Fibroblast growth factor receptor 2 mutations in Beare-Stevenson cutis gyrata syndrome."
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.
Nat. Genet. 13:492-494(1996) [PubMed: 8696350] [Abstract]
Cited for: VARIANTS BSCGS CYS-372 AND CYS-375.
[40]"Trp290Cys mutation in exon IIIa of the fibroblast growth factor receptor 2 (FGFR2) gene is associated with Pfeiffer syndrome."
Tartaglia M., Valeri S., Velardi F., di Rocco C., Battaglia P.A.
Hum. Genet. 99:602-606(1997) [PubMed: 9150725] [Abstract]
Cited for: VARIANT PS CYS-290.
[41]"Jackson-Weiss syndrome: identification of two novel FGFR2 missense mutations shared with Crouzon and Pfeiffer craniosynostotic disorders."
Tartaglia M., Di Rocco C., Lajeunie E., Valeri S., Velardi F., Battaglia P.A.
Hum. Genet. 101:47-50(1997) [PubMed: 9385368] [Abstract]
Cited for: VARIANT JWS SER-342.
[42]"Genotype-phenotype correlation for nucleotide substitutions in the IgII-IgIII linker of FGFR2."
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.
Hum. Mol. Genet. 6:137-143(1997) [PubMed: 9002682] [Abstract]
Cited for: VARIANT CS LEU-252, VARIANT APRS PHE-252, VARIANT PS 252-PHE-SER-253.
[43]"A novel mutation (a886g) in exon 5 of FGFR2 in members of a family with Crouzon phenotype and plagiocephaly."
Steinberger D., Collmann H., Schmalenberger B., Mueller U.
J. Med. Genet. 34:420-422(1997) [PubMed: 9152842] [Abstract]
Cited for: VARIANT CS GLU-292.
[44]"Description of a new mutation and characterization of FGFR1, FGFR2, and FGFR3 mutations among Brazilian patients with syndromic craniosynostoses."
Passos-Bueno M.R., Sertie A.L., Richieri-Costa A., Alonso L.G., Zatz M., Alonso N., Brunoni D., Ribeiro S.F.M.
Am. J. Med. Genet. 78:237-241(1998) [PubMed: 9677057] [Abstract]
Cited for: VARIANTS CS PHE-278; PRO-337; ARG-338; ARG-342; PHE-342 AND TYR-342, VARIANTS APRS TRP-252 AND ARG-253, VARIANT JWS PHE-278.
[45]"The mutations in FGFR2-associated craniosynostoses are clustered in five structural elements of immunoglobulin-like domain III of the receptor."
Steinberger D., Vriend G., Mulliken J.B., Mueller U.
Hum. Genet. 102:145-150(1998) [PubMed: 9521581] [Abstract]
Cited for: VARIANTS CS VAL-276 AND CYS-301, VARIANT CRANIOSYNOSTOSIS SER-314.
[46]"Two common mutations 934C to G and 937C to G of fibroblast growth factor receptor 2 (FGFR2) gene in Chinese patients with Apert syndrome."
Tsai F.-J., Hwu W.-L., Lin S.-P., Chang J.-G., Wang T.-R., Tsai C.-H.
Hum. Mutat. Suppl. 1:S18-S19(1998) [PubMed: 9452027] [Abstract]
Cited for: VARIANTS APRS TRP-252 AND ARG-253.
[47]"Pfeiffer's syndrome resulting from an S351C mutation in the fibroblast growth factor receptor-2 gene."
Mathijssen I.M., Vaandrager J.M., Hoogeboom A.J., Hesseling-Janssen A.L.W., van den Ouweland A.M.W.
J. Craniofac. Surg. 9:207-209(1998) [PubMed: 9693549] [Abstract]
Cited for: VARIANT PS CYS-351.
[48]"Presence of the Apert canonical S252W FGFR2 mutation in a patient without severe syndactyly."
Passos-Bueno M.R., Richieri-Costa A., Sertie A.L., Kneppers A.
J. Med. Genet. 35:677-679(1998) [PubMed: 9719378] [Abstract]
Cited for: VARIANT PS TRP-252.
[49]"A novel FGFR2 gene mutation in Crouzon syndrome associated with apparent nonpenetrance."
Everett E.T., Britto D.A., Ward R.E., Hartsfield J.K. Jr.
Cleft Palate Craniofac. J. 36:533-541(1999) [PubMed: 10574673] [Abstract]
Cited for: VARIANT CS SER-362.
[50]"Analysis of the mutational spectrum of the FGFR2 gene in Pfeiffer syndrome."
Cornejo-Roldan L.R., Roessler E., Muenke M.
Hum. Genet. 104:425-431(1999) [PubMed: 10394936] [Abstract]
Cited for: VARIANTS PS CYS-340 AND GLY-342.
[51]"Pfeiffer syndrome type 2 associated with a single amino acid deletion in the FGFR2 gene."
Priolo M., Lerone M., Baffico M., Baldi M., Ravazzolo R., Cama A., Capra V., Silengo M.
Clin. Genet. 58:81-83(2000) [PubMed: 10945669] [Abstract]
Cited for: VARIANT PS ASP-273 DEL.
[52]"Clustering of FGFR2 gene mutations inpatients with Pfeiffer and Crouzon syndromes (FGFR2-associated craniosynostoses)."
Kress W., Collmann H., Buesse M., Halliger-Keller B., Mueller C.R.
Cytogenet. Cell Genet. 91:134-137(2000) [PubMed: 11173845] [Abstract]
Cited for: 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, VARIANT PS SER-342.
[53]"A novel mutation, Ala315Ser, in FGFR2: a gene-environment interaction leading to craniosynostosis?"
Johnson D., Wall S.A., Mann S., Wilkie A.O.M.
Eur. J. Hum. Genet. 8:571-577(2000) [PubMed: 10951518] [Abstract]
Cited for: VARIANT SER-315.
[54]"Evidence for digenic inheritance in some cases of Antley-Bixler syndrome?"
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.
J. Med. Genet. 37:26-32(2000) [PubMed: 10633130] [Abstract]
Cited for: VARIANTS ABS ARG-342; SER-342 AND CYS-351.
[55]"Mutation analysis of Crouzon syndrome and identification of one novel mutation in Taiwanese patients."
Tsai F.-J., Yang C.-F., Wu J.-Y., Tsai C.-H., Lee C.-C.
Pediatr. Int. 43:263-266(2001) [PubMed: 11380921] [Abstract]
Cited for: VARIANTS CS CYS-281; PRO-289; ARG-342 AND TYR-342.
[56]"Genomic screening of fibroblast growth-factor receptor 2 reveals a wide spectrum of mutations in patients with syndromic craniosynostosis."
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.
Am. J. Hum. Genet. 70:472-486(2002) [PubMed: 11781872] [Abstract]
Cited for: 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, VARIANTS THR-186 AND SER-315.
[57]"Mutation in the FGFR2 gene in a Taiwanese patient with Beare-Stevenson cutis gyrata syndrome."
Wang T.-J., Huang C.-B., Tsai F.-J., Wu J.-Y., Lai R.-B., Hsiao M.
Clin. Genet. 61:218-221(2002) [PubMed: 12000365] [Abstract]
Cited for: VARIANT BSCGS CYS-375.
[58]"Familial scaphocephaly syndrome caused by a novel mutation in the FGFR2 tyrosine kinase domain."
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.
J. Med. Genet. 42:656-662(2005) [PubMed: 16061565] [Abstract]
Cited for: VARIANT FSPC GLU-526.
[59]"Mutations in different components of FGF signaling in LADD syndrome."
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. expand/collapse author list , Schlessinger J., van Bokhoven H., Wollnik B.
Nat. Genet. 38:414-417(2006) [PubMed: 16501574] [Abstract]
Cited for: VARIANTS LADDS THR-628; THR-648 AND 649-ARG-ASP-650 DELINS SER.
[60]"The consensus coding sequences of human breast and colorectal cancers."
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. expand/collapse author list , 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.
Science 314:268-274(2006) [PubMed: 16959974] [Abstract]
Cited for: VARIANT [LARGE SCALE ANALYSIS] CYS-203.
[61]"Patterns of somatic mutation in human cancer genomes."
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. expand/collapse author list , 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.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-57; THR-186; CYS-203; VAL-272; ASN-283; CYS-290 AND THR-612.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X52832 mRNA. Translation: CAA37014.1.
M55614 mRNA. Translation: AAA61188.1.
X56191 mRNA. Translation: CAA39654.1.
M35718 mRNA. Translation: AAA36152.1.
M87770 mRNA. Translation: AAA59470.1.
M87771 mRNA. Translation: AAA59471.1.
M87772 mRNA. Translation: AAA59472.1.
M97193 mRNA. Translation: AAA52449.1.
U11814 mRNA. Translation: AAA68514.1.
M80634 mRNA. Translation: AAA36147.1.
Z71929 mRNA. Translation: CAA96492.1.
AB030073 mRNA. Translation: BAA89296.1.
AB030074 mRNA. Translation: BAA89297.1.
AB030075 mRNA. Translation: BAA89298.1.
AB030076 mRNA. Translation: BAA89299.1.
AB030077 mRNA. Translation: BAA89300.1.
AB030078 mRNA. Translation: BAA89301.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94205.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94206.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94207.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94208.1.
AF360695, AF410480 Genomic DNA. Translation: AAK94209.1.
AF487553 Genomic DNA. Translation: AAM74056.1.
DQ493927 Genomic DNA. Translation: ABE96832.1.
BC039243 mRNA. Translation: AAH39243.2.
AF169399 Genomic DNA. Translation: AAF43273.1.
AF169399 Genomic DNA. Translation: AAF43274.1.
AF097353 expand/collapse EMBL AC list , AF097341, AF097342, AF097343, AF097345, AF097346, AF097347, AF097348, AF097349, AF097350, AF097351, AF097352 Genomic DNA. Translation: AAD31560.1.
AF097353 expand/collapse EMBL AC list , AF097341, AF097342, AF097344, AF097345, AF097346, AF097347, AF097348, AF097349, AF097350, AF097351, AF097352 Genomic DNA. Translation: AAD31561.1.
AF097340 expand/collapse EMBL AC list , AF097337, AF097338, AF097339 Genomic DNA. Translation: AAD31562.1.
AF097354 Genomic DNA. Translation: AAD31565.1.
AF097341 Genomic DNA. Translation: AAD31567.1.
S82438 Genomic DNA. Translation: AAD14392.1.
Y17131 Genomic DNA. Translation: CAA76643.1.
L49237 Genomic DNA. Translation: AAC41933.1.
L49242 Genomic DNA. Translation: AAC41934.1.
L49238 Genomic DNA. Translation: AAC41935.1.
L49239 Genomic DNA. Translation: AAC41936.1.
L49240 Genomic DNA. Translation: AAC41937.1.
L49241 Genomic DNA. Translation: AAC41938.1.
IPIIPI00010680.
IPI00216602.
IPI00216603.
IPI00216604.
IPI00216605.
IPI00218416.
IPI00218417.
IPI00218418.
IPI00218419.
IPI00218420.
IPI00218421.
IPI00218422.
IPI00218423.
IPI00218425.
IPI00384713.
IPI00386650.
IPI00647907.
IPI00759837.
IPI00873362.
IPI00942110.
PIRA35969.
TVHUF2. A42691.
A45081.
C42691.
S16236.
RefSeqNP_000132.3.
NP_001138385.1.
NP_001138386.1.
NP_001138387.1.
NP_001138388.1.
NP_001138389.1.
NP_001138390.1.
NP_001138391.1.
NP_075259.4.
UniGeneHs.533683

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1DJSX-ray2.40A153-362[»]
1E0OX-ray2.80B/D148-366[»]
1EV2X-ray2.20E/F/G/H147-366[»]
1GJOX-ray2.40A456-768[»]
1II4X-ray2.70E/F/G/H147-366[»]
1IILX-ray2.30E/F/G/H147-366[»]
1NUNX-ray2.90B140-361[»]
1OECX-ray2.40A456-768[»]
1WVZNMR-A147-249[»]
2FDBX-ray2.28P/R149-368[»]
2PSQX-ray2.40A/B413-768[»]
2PVFX-ray1.80A458-778[»]
B764-778[»]
2PVYX-ray2.20A/B/C/D458-768[»]
2PWLX-ray2.40A/B458-768[»]
2PY3X-ray2.30A/B458-768[»]
2PZ5X-ray2.40A/B458-768[»]
2PZPX-ray2.40A/B458-768[»]
2PZRX-ray3.00A/B458-768[»]
2Q0BX-ray2.90A/B458-768[»]
3B2TX-ray1.80A/B458-766[»]
3CAFX-ray1.96A150-249[»]
3CLYX-ray2.00A458-778[»]
3CU1X-ray2.60A/C150-249[»]
3DARX-ray2.20A/B146-249[»]
3EUUX-ray2.34A/B150-249[»]
SMRP21802. Positions 44-125, 49-357, 479-792.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-3788N.
DIP-4011N.
IntActP21802. 4 interactions.
STRINGP21802.

PTM databases

PhosphoSiteP21802.

Proteomic databases

PRIDEP21802.

Genome annotation databases

EnsemblENST00000357555; ENSP00000350166; ENSG00000066468; Homo sapiens. [Genome view]
ENST00000358487; ENSP00000351276; ENSG00000066468; Homo sapiens. [Genome view]
GeneID2263.
KEGGhsa:2263.
UCSCuc001lfj.2. human.
uc001lfm.1. human.
uc001lfo.1. human.
uc009xzo.1. human.
uc009xzp.1. human.
uc009xzq.1. human.
uc009xzr.1. human.

Organism-specific databases

CTD2263.
GeneCardsGC10M123223.
H-InvDBHIX0009266.
HGNCHGNC:3689. FGFR2.
HPACAB010886.
MIM101200. phenotype.
101600. phenotype.
123150. phenotype.
123500. phenotype.
123790. phenotype.
149730. phenotype.
176943. gene.
207410. phenotype.
609579. phenotype.
Orphanet83. 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.
93258. Pfeiffer syndrome, type 1.
93259. Pfeiffer syndrome, type 2.
PharmGKBPA28128.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG07516.
HOVERGENP21802.

Enzyme and pathway databases

BRENDA2.7.10.1. 247.
Pathway_Interaction_DBfgf_pathway. FGF signaling pathway.
ReactomeREACT_9470. Signaling by FGFR.

Gene expression databases

ArrayExpressP21802.
BgeeP21802.
GenevestigatorP21802.
GermOnlineENSG00000066468. Homo sapiens.

Family and domain databases

InterProIPR007110. Ig-like.
IPR013783. Ig-like_fold.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_cat_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR020933. Tyr_kin_fibroblast_GF_rcpt_reg.
IPR016248. Tyr_kinase_fibroblast_GF_rcpt.
IPR020635. Tyr_Pkinase_cat_dom.
IPR020685. Tyr_prot_kinase.
IPR008266. Tyr_prot_kinase_AS.
[Graphical view]
Gene3DG3DSA:2.60.40.10. Ig-like_fold. 3 hits.
PANTHERPTHR23256:SF276. Tyr_kinase_fibroblast_GF_rcpt. 1 hit.
PTHR23256. Tyr_prot_kinase. 1 hit.
PIRSFPIRSF000628. FGFR. 1 hit.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

DrugBankDB00039. Palifermin.
SOURCESearch...

Entry information

Entry nameFGFR2_HUMAN
AccessionPrimary (citable) accession number: P21802
Secondary accession number(s): P18443 expand/collapse secondary AC list , 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
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 1991
Last sequence update: May 1, 1991
Last modified: February 9, 2010
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

Human chromosome 10

Human chromosome 10: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents