FGFR2
entrez
2263
canonical
uniprot
P21802
canonical
ensembl
ENSG00000066468
resolver
ensp
ENSP00000309878
resolver
ensp
ENSP00000337665
resolver
ensp
ENSP00000348559
resolver
ensp
ENSP00000350166
resolver
ensp
ENSP00000351276
resolver
ensp
ENSP00000353262
resolver
ensp
ENSP00000358052
resolver
ensp
ENSP00000358055
resolver
ensp
ENSP00000358056
resolver
ensp
ENSP00000358057
resolver
ensp
ENSP00000410294
resolver
ensp
ENSP00000474011
resolver
ensp
ENSP00000484154
resolver
ensp
ENSP00000506937
resolver
ensp
ENSP00000655451
resolver
ensp
ENSP00000714255
resolver
ensp
ENSP00000714256
resolver
ensp
ENSP00000714259
resolver
enst
ENST00000478859
resolver
enst
ENST00000613048
resolver
enst
ENST00000684153
resolver
genesymbol
FGFR2
resolver
genesymbol_syn
BEK
resolver
genesymbol_syn
KGFR
resolver
genesymbol_syn
KSAM
resolver
hgnc
HGNC:3689
resolver
uniprot
A0A087X1F2
resolver
uniprot
A0A141AXF1
resolver
uniprot
A0A804HI76
resolver
uniprot
B4DFC2
resolver
uniprot
D2CGD1
resolver
uniprot
E7EVR6
resolver
uniprot
E9PCR0
resolver
uniprot
P18443
resolver
uniprot
Q01742
resolver
uniprot
Q12922
resolver
uniprot
Q14300
resolver
uniprot
Q14301
resolver
uniprot
Q14302
resolver
uniprot
Q14303
resolver
uniprot
Q14304
resolver
uniprot
Q14305
resolver
uniprot
Q14672
resolver
uniprot
Q14718
resolver
uniprot
Q14719
resolver
uniprot
Q1KHY5
resolver
uniprot
Q86YI4
resolver
uniprot
Q8IXC7
resolver
uniprot
Q96KL9
resolver
uniprot
Q96KM0
resolver
uniprot
Q96KM1
resolver
uniprot
Q96KM2
resolver
uniprot
Q9NZU2
resolver
uniprot
Q9NZU3
resolver
uniprot
Q9UD01
resolver
uniprot
Q9UD02
resolver
uniprot
Q9UIH3
resolver
uniprot
Q9UIH4
resolver
uniprot
Q9UIH5
resolver
uniprot
Q9UIH6
resolver
uniprot
Q9UIH7
resolver
uniprot
Q9UIH8
resolver
uniprot
Q9UM87
resolver
uniprot
Q9UMC6
resolver
uniprot
Q9UNS7
resolver
uniprot
Q9UQH7
resolver
uniprot
Q9UQH8
resolver
uniprot
Q9UQH9
resolver
uniprot
Q9UQI0
resolver
uniprot
S4R381
resolver
uniprot_entry
A0A087X1F2_HUMAN
resolver
uniprot_entry
A0A141AXF1_HUMAN
resolver
uniprot_entry
A0A804HI76_HUMAN
resolver
uniprot_entry
D2CGD1_HUMAN
resolver
uniprot_entry
FGFR2_HUMAN
resolver
uniprot_entry
S4R381_HUMAN
resolver
uniprot_sec
B4DFC2
resolver
uniprot_sec
E7EVR6
resolver
uniprot_sec
E9PCR0
resolver
uniprot_sec
P18443
resolver
uniprot_sec
Q01742
resolver
uniprot_sec
Q12922
resolver
uniprot_sec
Q14300
resolver
uniprot_sec
Q14301
resolver
uniprot_sec
Q14302
resolver
uniprot_sec
Q14303
resolver
uniprot_sec
Q14304
resolver
uniprot_sec
Q14305
resolver
uniprot_sec
Q14672
resolver
uniprot_sec
Q14718
resolver
uniprot_sec
Q14719
resolver
uniprot_sec
Q1KHY5
resolver
uniprot_sec
Q86YI4
resolver
uniprot_sec
Q8IXC7
resolver
uniprot_sec
Q96KL9
resolver
uniprot_sec
Q96KM0
resolver
uniprot_sec
Q96KM1
resolver
uniprot_sec
Q96KM2
resolver
uniprot_sec
Q9NZU2
resolver
uniprot_sec
Q9NZU3
resolver
uniprot_sec
Q9UD01
resolver
uniprot_sec
Q9UD02
resolver
uniprot_sec
Q9UIH3
resolver
uniprot_sec
Q9UIH4
resolver
uniprot_sec
Q9UIH5
resolver
uniprot_sec
Q9UIH6
resolver
uniprot_sec
Q9UIH7
resolver
uniprot_sec
Q9UIH8
resolver
uniprot_sec
Q9UM87
resolver
uniprot_sec
Q9UMC6
resolver
uniprot_sec
Q9UNS7
resolver
uniprot_sec
Q9UQH7
resolver
uniprot_sec
Q9UQH8
resolver
uniprot_sec
Q9UQH9
resolver
uniprot_sec
Q9UQI0
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by autophosphorylation on tyrosine residues. Inhibited by ARQ 523 and ARQ 069; these compounds maintain the kinase in an inactive conformation and inhibit autophosphorylation. {ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:21454610}.
uniprot
proteins
amino_acid_sequence
MVSWGRFICLVVVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEVYVAAPGESLEVRCLLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTASRTVDSETWYFMVNVTDAISSGDDEDDTDGAEDFVSENSNNKRAPYWTNTEKMEKRLHAVPAANTVKFRCPAGGNPMPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCVVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKYGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPGREKEITASPDYLEIAIYCIGVFLIACMVVTVILCRMKNTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLSQPLEQYSPSYPDTRSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT
uniprot
proteins
disease_involvement
DISEASE: Crouzon syndrome (CS) [MIM:123500]: An autosomal dominant syndrome characterized by craniosynostosis, hypertelorism, exophthalmos and external strabismus, parrot-beaked nose, short upper lip, hypoplastic maxilla, and a relative mandibular prognathism. {ECO:0000269|PubMed:10574673, ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11380921, ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:7581378, ECO:0000269|PubMed:7655462, ECO:0000269|PubMed:7874170, ECO:0000269|PubMed:7987400, ECO:0000269|PubMed:8528214, ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:8946174, ECO:0000269|PubMed:8956050, ECO:0000269|PubMed:9152842, ECO:0000269|PubMed:9521581, ECO:0000269|PubMed:9677057, ECO:0000269|Ref.10}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Jackson-Weiss syndrome (JWS) [MIM:123150]: An autosomal dominant craniosynostosis syndrome characterized by craniofacial abnormalities and abnormality of the feet: broad great toes with medial deviation and tarsal-metatarsal coalescence. {ECO:0000269|PubMed:7874170, ECO:0000269|PubMed:8528214, ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9385368, ECO:0000269|PubMed:9677057}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Apert syndrome (APRS) [MIM:101200]: 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. {ECO:0000269|PubMed:11390973, ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:7668257, ECO:0000269|PubMed:7719344, ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9452027, ECO:0000269|PubMed:9677057}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Pfeiffer syndrome (PS) [MIM:101600]: A syndrome characterized by the association of craniosynostosis, broad and deviated thumbs and big toes, and partial syndactyly of the fingers and toes. Three subtypes are known: mild autosomal dominant form (type 1); cloverleaf skull, elbow ankylosis, early death, sporadic (type 2); craniosynostosis, early demise, sporadic (type 3). {ECO:0000269|PubMed:10394936, ECO:0000269|PubMed:10945669, ECO:0000269|PubMed:11173845, ECO:0000269|PubMed:11781872, ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:17803937, ECO:0000269|PubMed:7719333, ECO:0000269|PubMed:7719345, ECO:0000269|PubMed:8644708, ECO:0000269|PubMed:9002682, ECO:0000269|PubMed:9150725, ECO:0000269|PubMed:9693549, ECO:0000269|PubMed:9719378}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Beare-Stevenson cutis gyrata syndrome (BSTVS) [MIM:123790]: An autosomal dominant disease characterized by craniofacial anomalies, particularly craniosynostosis, and ear defects, cutis gyrata, acanthosis nigricans, anogenital anomalies, skin tags, and prominent umbilical stump. The skin furrows have a corrugated appearance and are widespread. Cutis gyrata variably affects the scalp, forehead, face, preauricular area, neck, trunk, hands, and feet. {ECO:0000269|PubMed:12000365, ECO:0000269|PubMed:8696350}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Familial scaphocephaly syndrome (FSPC) [MIM:609579]: 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. {ECO:0000269|PubMed:16061565, ECO:0000269|PubMed:17803937}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Lacrimo-auriculo-dento-digital syndrome 1 (LADD1) [MIM:149730]: A form of lacrimo-auriculo-dento-digital syndrome, an autosomal dominant disease 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. {ECO:0000269|PubMed:16501574, ECO:0000269|PubMed:18056630}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Antley-Bixler syndrome, without genital anomalies or disordered steroidogenesis (ABS2) [MIM:207410]: A rare syndrome characterized by craniosynostosis, radiohumeral synostosis present from the perinatal period, midface hypoplasia, choanal stenosis or atresia, femoral bowing and multiple joint contractures. Arachnodactyly and/or camptodactyly have also been reported. {ECO:0000269|PubMed:10633130}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Bent bone dysplasia syndrome 1 (BBDS1) [MIM:614592]: A perinatal lethal skeletal dysplasia characterized by poor mineralization of the calvarium, craniosynostosis, dysmorphic facial features, prenatal teeth, hypoplastic pubis and clavicles, osteopenia, and bent long bones. Dysmorphic facial features included low-set ears, hypertelorism, midface hypoplasia, prematurely erupted fetal teeth, and micrognathia. {ECO:0000269|PubMed:22387015}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Saethre-Chotzen syndrome (SCS) [MIM:101400]: A craniosynostosis syndrome characterized by coronal synostosis, brachycephaly, low frontal hairline, facial asymmetry, hypertelorism, broad halluces, and clinodactyly. {ECO:0000269|PubMed:9585583}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.7.10.1
uniprot
proteins
function
FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, trophoblast function, limb bud development, lung morphogenesis, osteogenesis and skin development. Plays an essential role in the regulation of osteoblast differentiation, proliferation and apoptosis, and is required for normal skeleton development. Promotes cell proliferation in keratinocytes and immature osteoblasts, but promotes apoptosis in differentiated osteoblasts. Phosphorylates PLCG1, FRS2 and PAK4. Ligand binding leads to the activation of several signaling cascades. Activation of PLCG1 leads to the production of the cellular signaling molecules diacylglycerol and inositol 1,4,5-trisphosphate. Phosphorylation of FRS2 triggers recruitment of GRB2, GAB1, PIK3R1 and SOS1, and mediates activation of RAS, MAPK1/ERK2, MAPK3/ERK1 and the MAP kinase signaling pathway, as well as of the AKT1 signaling pathway. FGFR2 signaling is down-regulated by ubiquitination, internalization and degradation. Mutations that lead to constitutive kinase activation or impair normal FGFR2 maturation, internalization and degradation lead to aberrant signaling. Over-expressed FGFR2 promotes activation of STAT1. {ECO:0000269|PubMed:12529371, ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:16384934, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18374639, ECO:0000269|PubMed:19103595, ECO:0000269|PubMed:19387476, ECO:0000269|PubMed:19410646, ECO:0000269|PubMed:21596750, ECO:0000269|PubMed:8663044}.
uniprot
proteins
mass_dalton
92025
uniprot
proteins
mutagenesis
MUTAGEN 265; /note="N->Q: Reduced N-glycosylation. Reduced expression at the cell surface."; /evidence="ECO:0000269|PubMed:16844695"; MUTAGEN 549; /note="N->T: Constitutive kinase activity."; /evidence="ECO:0000269|PubMed:17803937"; MUTAGEN 565; /note="E->A: Constitutive kinase activity."; /evidence="ECO:0000269|PubMed:17803937"; MUTAGEN 656..657; /note="Missing: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:16844695"; MUTAGEN 769; /note="Y->F: Increases fibroblast proliferation. Decreases phosphorylation of PLCG1 and FRS2. Decreases activation of MAP kinases."; /evidence="ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:19103595
uniprot
proteins
post_translational_modification
PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on several tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer. Phosphorylation at Tyr-769 is essential for interaction with PLCG1. {ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:19060208}.; PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. {ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:17311277}.; PTM: Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome. {ECO:0000269|PubMed:15190072, ECO:0000269|PubMed:16844695, ECO:0000269|PubMed:21596750}.
uniprot
proteins
protein_family
Fibroblast growth factor receptor subfamily
uniprot
proteins
protein_family
Protein kinase superfamily
uniprot
proteins
protein_family
Tyr protein kinase family
uniprot
proteins
pubmed
10196476
uniprot
proteins
pubmed
10394936
uniprot
proteins
pubmed
10574673
uniprot
proteins
pubmed
10618369
uniprot
proteins
pubmed
10626794
uniprot
proteins
pubmed
10633130
uniprot
proteins
pubmed
10712195
uniprot
proteins
pubmed
10830168
uniprot
proteins
pubmed
10945669
uniprot
proteins
pubmed
10951518
uniprot
proteins
pubmed
11069186
uniprot
proteins
pubmed
11173845
uniprot
proteins
pubmed
11380921
uniprot
proteins
pubmed
11390973
uniprot
proteins
pubmed
11781872
uniprot
proteins
pubmed
11856867
uniprot
proteins
pubmed
12000365
uniprot
proteins
pubmed
12529371
uniprot
proteins
pubmed
12591959
uniprot
proteins
pubmed
1309608
uniprot
proteins
pubmed
1313574
uniprot
proteins
pubmed
1400433
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15164054
uniprot
proteins
pubmed
15190072
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15629145
uniprot
proteins
pubmed
15863030
uniprot
proteins
pubmed
16061565
uniprot
proteins
pubmed
16384934
uniprot
proteins
pubmed
1647213
uniprot
proteins
pubmed
16501574
uniprot
proteins
pubmed
16597617
uniprot
proteins
pubmed
16844695
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
1697263
uniprot
proteins
pubmed
17311277
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17623664
uniprot
proteins
pubmed
17803937
uniprot
proteins
pubmed
18056630
uniprot
proteins
pubmed
18374639
uniprot
proteins
pubmed
19060208
uniprot
proteins
pubmed
19103595
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19387476
uniprot
proteins
pubmed
19410646
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
21454610
uniprot
proteins
pubmed
21596750
uniprot
proteins
pubmed
2172978
uniprot
proteins
pubmed
22387015
uniprot
proteins
pubmed
2377625
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26429889
uniprot
proteins
pubmed
7581378
uniprot
proteins
pubmed
7655462
uniprot
proteins
pubmed
7668257
uniprot
proteins
pubmed
7719333
uniprot
proteins
pubmed
7719344
uniprot
proteins
pubmed
7719345
uniprot
proteins
pubmed
7866434
uniprot
proteins
pubmed
7874170
uniprot
proteins
pubmed
7987400
uniprot
proteins
pubmed
8528214
uniprot
proteins
pubmed
8644708
uniprot
proteins
pubmed
8663044
uniprot
proteins
pubmed
8673103
uniprot
proteins
pubmed
8676562
uniprot
proteins
pubmed
8696350
uniprot
proteins
pubmed
8946174
uniprot
proteins
pubmed
8956050
uniprot
proteins
pubmed
8961926
uniprot
proteins
pubmed
9002682
uniprot
proteins
pubmed
9150725
uniprot
proteins
pubmed
9152842
uniprot
proteins
pubmed
9385368
uniprot
proteins
pubmed
9452027
uniprot
proteins
pubmed
9521581
uniprot
proteins
pubmed
9585583
uniprot
proteins
pubmed
9677057
uniprot
proteins
pubmed
9693549
uniprot
proteins
pubmed
9719378
uniprot
proteins
sequence_length
821
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus. Cytoplasmic vesicle. Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein. Note=After ligand binding, the activated receptor is rapidly internalized and degraded.; SUBCELLULAR LOCATION: [Isoform 3]: Cell membrane; Single-pass type I membrane protein. Note=After ligand binding, the activated receptor is rapidly internalized and degraded.; SUBCELLULAR LOCATION: [Isoform 8]: Secreted.; SUBCELLULAR LOCATION: [Isoform 13]: Secreted.
uniprot
proteins
transmembrane_region
TRANSMEM 378..398; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins