Fgfr2
entrez
14183
canonical
uniprot
P21803
canonical
ensembl
ENSMUSG00000030849
resolver
ensp
ENSMUSP00000112430
resolver
ensp
ENSMUSP00000113248
resolver
ensp
ENSMUSP00000113994
resolver
enst
ENSMUST00000117872
resolver
enst
ENSMUST00000120187
resolver
enst
ENSMUST00000122054
resolver
genesymbol
Fgfr2
resolver
genesymbol_syn
Bek
resolver
genesymbol_syn
Ect1
resolver
uniprot
E9Q5C2
resolver
uniprot
E9Q7C7
resolver
uniprot
E9QK53
resolver
uniprot
O55141
resolver
uniprot
Q00389
resolver
uniprot
Q61342
resolver
uniprot_entry
E9Q5C2_MOUSE
resolver
uniprot_entry
E9Q7C7_MOUSE
resolver
uniprot_entry
E9QK53_MOUSE
resolver
uniprot_entry
FGFR2_MOUSE
resolver
uniprot_sec
O55141
resolver
uniprot_sec
Q00389
resolver
uniprot_sec
Q61342
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 (By similarity). {ECO:0000250}.
uniprot
proteins
amino_acid_sequence
MVSWGRFICLVLVTMATLSLARPSFSLVEDTTLEPEEPPTKYQISQPEAYVVAPGESLELQCMLKDAAVISWTKDGVHLGPNNRTVLIGEYLQIKGATPRDSGLYACTAARTVDSETWIFMVNVTDAISSGDDEDDTDSSEDVVSENRSNQRAPYWTNTEKMEKRLHACPAANTVKFRCPAGGNPTSTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCLVENEYGSINHTYHLDVVERSPHRPILQAGLPANASTVVGGDVEFVCKVYSDAQPHIQWIKHVEKNGSKNGPDGLPYLKVLKAAGVNTTDKEIEVLYIRNVTFEDAGEYTCLAGNSIGISFHSAWLTVLPAPVREKEITASPDYLEIAIYCIGVFLIACMVVTVIFCRMKTTTKKPDFSSQPAVHKLTKRIPLRRQVTVSAESSSSMNSNTPLVRITTRLSSTADTPMLAGVSEYELPEDPKWEFPRDKLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTVAVKMLKDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINRVPEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLMWEIFTLGGSPYPGIPVEELFKLLKEGHRMDKPTNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRILTLTTNEEYLDLTQPLEQYSPSYPDTSSSCSSGDDSVFSPDPMPYEPCLPQYPHINGSVKT
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:10851026, ECO:0000269|PubMed:15629145, ECO:0000269|PubMed:8393815, ECO:0000269|PubMed:8663044}.
uniprot
proteins
mass_dalton
91984
uniprot
proteins
mutagenesis
MUTAGEN 769; /note="Y->F: Abolishes phosphorylation of FRS2 and activation of MAP kinases."; /evidence="ECO:0000269|PubMed:15629145
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 tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer (By similarity). {ECO:0000250}.; PTM: N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus (By similarity). {ECO:0000250}.; PTM: Ubiquitinated. FGFR2 is rapidly ubiquitinated after autophosphorylation, leading to internalization and degradation. Subject to degradation both in lysosomes and by the proteasome (By similarity). {ECO:0000250}.
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
10518547
uniprot
proteins
pubmed
10851026
uniprot
proteins
pubmed
12135917
uniprot
proteins
pubmed
1373495
uniprot
proteins
pubmed
15629145
uniprot
proteins
pubmed
1711190
uniprot
proteins
pubmed
1846048
uniprot
proteins
pubmed
21765038
uniprot
proteins
pubmed
2468999
uniprot
proteins
pubmed
8393815
uniprot
proteins
pubmed
8663044
uniprot
proteins
pubmed
9435295
uniprot
proteins
pubmed
9499422
uniprot
proteins
pubmed
9560232
uniprot
proteins
sequence_length
821
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity). {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 378..398; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins