Fgfr1
entrez
14182
canonical
uniprot
P16092
canonical
ensembl
ENSMUSG00000031565
resolver
ensp
ENSMUSP00000081041
resolver
ensp
ENSMUSP00000113855
resolver
ensp
ENSMUSP00000113909
resolver
genesymbol
Fgfr1
resolver
genesymbol_syn
Flg
resolver
uniprot
E9Q2P4
resolver
uniprot
Q01736
resolver
uniprot
Q60830
resolver
uniprot
Q61562
resolver
uniprot
Q80T10
resolver
uniprot
Q8CBY7
resolver
uniprot
Q8CFK8
resolver
uniprot
Q8CIM9
resolver
uniprot
Q9QZM7
resolver
uniprot_entry
FGFR1_MOUSE
resolver
uniprot_entry
Q8CBY7_MOUSE
resolver
uniprot_entry
Q8CIM9_MOUSE
resolver
uniprot_sec
E9Q2P4
resolver
uniprot_sec
Q01736
resolver
uniprot_sec
Q60830
resolver
uniprot_sec
Q61562
resolver
uniprot_sec
Q80T10
resolver
uniprot_sec
Q8CFK8
resolver
uniprot_sec
Q9QZM7
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}.
uniprot
proteins
amino_acid_sequence
MWGWKCLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLVESNRTRITGEEVEVRDSIPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMLGSVIIYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSIPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPTQLANSGLKRR
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:0000269|PubMed:10821861, ECO:0000269|PubMed:10896947, ECO:0000269|PubMed:1309590, ECO:0000269|PubMed:17086194, ECO:0000269|PubMed:8001822, ECO:0000269|PubMed:8001823}.
uniprot
proteins
mass_dalton
91981
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. {ECO:0000269|PubMed:10821861, ECO:0000269|PubMed:19349973}.
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
10821861
uniprot
proteins
pubmed
10896947
uniprot
proteins
pubmed
12181353
uniprot
proteins
pubmed
1309590
uniprot
proteins
pubmed
15383174
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16141072
uniprot
proteins
pubmed
16731982
uniprot
proteins
pubmed
16872596
uniprot
proteins
pubmed
1689490
uniprot
proteins
pubmed
1708247
uniprot
proteins
pubmed
17086194
uniprot
proteins
pubmed
17452648
uniprot
proteins
pubmed
17728342
uniprot
proteins
pubmed
19349973
uniprot
proteins
pubmed
19468303
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
2161096
uniprot
proteins
pubmed
2161540
uniprot
proteins
pubmed
7802632
uniprot
proteins
pubmed
7897669
uniprot
proteins
pubmed
8001822
uniprot
proteins
pubmed
8001823
uniprot
proteins
pubmed
8663044
uniprot
proteins
sequence_length
822
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. 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.; SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 5]: Cell membrane; Single-pass type I membrane protein.
uniprot
proteins
transmembrane_region
TRANSMEM 377..397; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins