Fgfr1
entrez
79114
canonical
uniprot
Q04589
canonical
ensembl
ENSRNOG00000016050
resolver
ensp
ENSRNOP00000036885
resolver
ensp
ENSRNOP00000043459
resolver
enst
ENSRNOT00000029284
resolver
genesymbol
Fgfr1
resolver
genesymbol_syn
Flg
resolver
uniprot
F1LM54
resolver
uniprot
F1LPM6
resolver
uniprot
Q63827
resolver
uniprot_entry
F1LM54_RAT
resolver
uniprot_entry
FGFR1_RAT
resolver
uniprot_entry
Q63827_RAT
resolver
uniprot_sec
F1LPM6
resolver
activity_regulation
ACTIVITY REGULATION: Present in an inactive conformation in the absence of bound ligand. Ligand binding leads to dimerization and activation by sequential autophosphorylation on tyrosine residues (By similarity). {ECO:0000250|UniProtKB:P11362}.
uniprot
proteins
amino_acid_sequence
MWGWRGLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVRDSIPADSGLYACVTNSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPSPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYDQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIIYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPNPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWNAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQDSPSFPDTRSSTCSSGEDSVFSHEPFPEEPCLPRHPTQLANGGLNRR
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 embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic development, normal skeletogenesis and normal development of the gonadotropin-releasing hormone (GnRH) neuronal system. Phosphorylates PLCG1, FRS2, GAB1 and SHB. 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. Promotes phosphorylation of SHC1, STAT1 and PTPN11/SHP2. In the nucleus, enhances RPS6KA1 and CREB1 activity and contributes to the regulation of transcription. FGFR1 signaling is down-regulated by IL17RD/SEF, and by FGFR1 ubiquitination, internalization and degradation (By similarity). {ECO:0000250|UniProtKB:P11362, ECO:0000250|UniProtKB:P16092}.
uniprot
proteins
mass_dalton
91825
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 and proceeds in a highly ordered manner. Initial autophosphorylation at Tyr-653 increases the kinase activity by a factor of 50 to 100. After this, Tyr-583 becomes phosphorylated, followed by phosphorylation of Tyr-463, Tyr-766, Tyr-583 and Tyr-585. In a third stage, Tyr-654 is autophosphorylated, resulting in a further tenfold increase of kinase activity. Phosphotyrosine residues provide docking sites for interacting proteins and so are crucial for FGFR1 function and its regulation (By similarity). {ECO:0000250|UniProtKB:P11362}.; PTM: Ubiquitinated. FGFR1 is rapidly ubiquitinated by NEDD4 after autophosphorylation, leading to internalization and lysosomal degradation. CBL is recruited to activated FGFR1 via FRS2 and GRB2, and mediates ubiquitination and subsequent degradation of FGFR1 (By similarity). {ECO:0000250|UniProtKB:P11362}.; 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|UniProtKB:P11362}.
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
15117958
uniprot
proteins
pubmed
17992255
uniprot
proteins
pubmed
22673903
uniprot
proteins
pubmed
8382532
uniprot
proteins
sequence_length
822
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15117958}; Single-pass type I membrane protein {ECO:0000269|PubMed:15117958}. Nucleus {ECO:0000269|PubMed:15117958}. Cytoplasm, cytosol {ECO:0000269|PubMed:15117958}. Cytoplasmic vesicle {ECO:0000250}. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi apparatus to the cytosol, and from there to the nucleus (By similarity). {ECO:0000250}.
uniprot
proteins
transmembrane_region
TRANSMEM 377..397; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins