FGFR1
entrez
2260
canonical
uniprot
P11362
canonical
ensembl
ENSG00000077782
resolver
ensp
ENSP00000327229
resolver
ensp
ENSP00000337247
resolver
ensp
ENSP00000340636
resolver
ensp
ENSP00000348537
resolver
ensp
ENSP00000380280
resolver
ensp
ENSP00000380302
resolver
ensp
ENSP00000393312
resolver
ensp
ENSP00000400162
resolver
ensp
ENSP00000432972
resolver
ensp
ENSP00000497266
resolver
ensp
ENSP00000507039
resolver
ensp
ENSP00000507205
resolver
ensp
ENSP00000507997
resolver
ensp
ENSP00000527993
resolver
ensp
ENSP00000527998
resolver
ensp
ENSP00000527999
resolver
ensp
ENSP00000604629
resolver
ensp
ENSP00000635902
resolver
ensp
ENSP00000635903
resolver
enst
ENST00000341462
resolver
enst
ENST00000425967
resolver
enst
ENST00000649678
resolver
enst
ENST00000683815
resolver
enst
ENST00000684654
resolver
enst
ENST00000857934
resolver
enst
ENST00000857939
resolver
enst
ENST00000857940
resolver
enst
ENST00000934570
resolver
enst
ENST00000965843
resolver
enst
ENST00000965844
resolver
genesymbol
FGFR1
resolver
genesymbol_syn
BFGFR
resolver
genesymbol_syn
CEK
resolver
genesymbol_syn
FGFBR
resolver
genesymbol_syn
FLG
resolver
genesymbol_syn
FLT2
resolver
genesymbol_syn
HBGFR
resolver
hgnc
HGNC:3688
resolver
uniprot
A0A0S2Z3Q6
resolver
uniprot
A0A0S2Z3T4
resolver
uniprot
A0A3B3ISD1
resolver
uniprot
A0A8I3B1S4
resolver
uniprot
A0ACI8VCD6
resolver
uniprot
A8K6T9
resolver
uniprot
A8K8V5
resolver
uniprot
C1KBH8
resolver
uniprot
P17049
resolver
uniprot
Q02063
resolver
uniprot
Q02065
resolver
uniprot
Q14306
resolver
uniprot
Q14307
resolver
uniprot
Q53H63
resolver
uniprot
Q59H40
resolver
uniprot
Q5BJG2
resolver
uniprot
Q8N685
resolver
uniprot
Q9UD50
resolver
uniprot
Q9UDF0
resolver
uniprot
Q9UDF1
resolver
uniprot
Q9UDF2
resolver
uniprot_entry
A0A0S2Z3Q6_HUMAN
resolver
uniprot_entry
A0A0S2Z3T4_HUMAN
resolver
uniprot_entry
A0A3B3ISD1_HUMAN
resolver
uniprot_entry
A0A8I3B1S4_HUMAN
resolver
uniprot_entry
A0ACI8VCD6_HUMAN
resolver
uniprot_entry
FGFR1_HUMAN
resolver
uniprot_sec
A8K6T9
resolver
uniprot_sec
A8K8V5
resolver
uniprot_sec
C1KBH8
resolver
uniprot_sec
P17049
resolver
uniprot_sec
Q02063
resolver
uniprot_sec
Q02065
resolver
uniprot_sec
Q14306
resolver
uniprot_sec
Q14307
resolver
uniprot_sec
Q53H63
resolver
uniprot_sec
Q59H40
resolver
uniprot_sec
Q5BJG2
resolver
uniprot_sec
Q8N685
resolver
uniprot_sec
Q9UD50
resolver
uniprot_sec
Q9UDF0
resolver
uniprot_sec
Q9UDF1
resolver
uniprot_sec
Q9UDF2
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. Inhibited by ARQ 069; this compound maintains the kinase in an inactive conformation and inhibits autophosphorylation. Inhibited by PD173074. {ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:21454610, ECO:0000269|PubMed:8622701}.
uniprot
proteins
amino_acid_sequence
MWSWKCLLFWAVLVTATLCTARPSPTLPEQAQPWGAPVEVESFLVHPGDLLQLRCRLRDDVQSINWLRDGVQLAESNRTRITGEEVEVQDSVPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRMPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTDKEMEVLHLRNVSFEDAGEYTCLAGNSIGLSHHSAWLTVLEALEERPAVMTSPLYLEIIIYCTGAFLISCMVGSVIVYKMKSGTKKSDFHSQMAVHKLAKSIPLRRQVTVSADSSASMNSGVLLVRPSRLSSSGTPMLAGVSEYELPEDPRWELPRDRLVLGKPLGEGCFGQVVLAEAIGLDKDKPNRVTKVAVKMLKSDATEKDLSDLISEMEMMKMIGKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLQARRPPGLEYCYNPSHNPEEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIFTLGGSPYPGVPVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRPTFKQLVEDLDRIVALTSNQEYLDLSMPLDQYSPSFPDTRSSTCSSGEDSVFSHEPLPEEPCLPRHPAQLANGGLKRR
uniprot
proteins
disease_involvement
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:7874169}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hypogonadotropic hypogonadism 2 with or without anosmia (HH2) [MIM:147950]: A disorder characterized by absent or incomplete sexual maturation by the age of 18 years, in conjunction with low levels of circulating gonadotropins and testosterone and no other abnormalities of the hypothalamic-pituitary axis. In some cases, it is associated with non-reproductive phenotypes, such as anosmia, cleft palate, and sensorineural hearing loss. Anosmia or hyposmia is related to the absence or hypoplasia of the olfactory bulbs and tracts. Hypogonadism is due to deficiency in gonadotropin-releasing hormone and probably results from a failure of embryonic migration of gonadotropin-releasing hormone-synthesizing neurons. In the presence of anosmia, idiopathic hypogonadotropic hypogonadism is referred to as Kallmann syndrome, whereas in the presence of a normal sense of smell, it has been termed normosmic idiopathic hypogonadotropic hypogonadism (nIHH). {ECO:0000269|PubMed:12627230, ECO:0000269|PubMed:15001591, ECO:0000269|PubMed:15605412, ECO:0000269|PubMed:15845591, ECO:0000269|PubMed:16606836, ECO:0000269|PubMed:16757108, ECO:0000269|PubMed:16764984, ECO:0000269|PubMed:16882753, ECO:0000269|PubMed:17154279, ECO:0000269|PubMed:19820032, ECO:0000269|PubMed:21700882, ECO:0000269|PubMed:22927827, ECO:0000269|PubMed:23643382, ECO:0000269|PubMed:25077900, ECO:0000269|PubMed:26277103}. Note=The disease is caused by variants affecting distinct genetic loci, including the gene represented in this entry. Some patients carrying mutations in FGFR1 also have a mutation other HH-associated genes including DUSP6, FGF8, FGF17, FLRT3, GNRH1, GNRHR, HS6ST1, IL17RD, ANOS1, KISS1R, NSMF, PROKR2, SPRY4 and TACR3 (PubMed:23643382). {ECO:0000269|PubMed:23643382}.; DISEASE: Osteoglophonic dysplasia (OGD) [MIM:166250]: Characterized by craniosynostosis, prominent supraorbital ridge, and depressed nasal bridge, as well as by rhizomelic dwarfism and nonossifying bone lesions. Inheritance is autosomal dominant. {ECO:0000269|PubMed:15625620, ECO:0000269|PubMed:16470795}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Hartsfield syndrome (HRTFDS) [MIM:615465]: A syndrome characterized by the triad of holoprosencephaly, ectrodactyly, and cleft/lip palate. Profound intellectual disability is also present. Multiple other congenital anomalies usually occur. {ECO:0000269|PubMed:23812909, ECO:0000269|PubMed:24888332}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Trigonocephaly 1 (TRIGNO1) [MIM:190440]: A keel-shaped deformation of the forehead, caused by premature fusion of the metopic sutures. It results in a triangular shape of the head. {ECO:0000269|PubMed:11173846}. Note=The disease is caused by variants affecting the gene represented in this entry.; DISEASE: Note=Chromosomal aberrations involving FGFR1 are a cause of chromosome 8p11 myeloproliferative syndrome. Translocation t(8;13)(p11;q12) with ZMYM2. Translocation t(6;8)(q27;p11) with CEP43. Insertion ins(12;8)(p11;p11p22) with FGFR1OP2. Translocation t(8;9)(p12;q33) with CNTRL. Translocation t(2;8)(q12;p11) with RANBP2. Chromosome 8p11 myeloproliferative syndrome is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion proteins FGFR1OP2-FGFR1, CEP43-FGFR1 or FGFR1-CEP43 may exhibit constitutive kinase activity and be responsible for the transforming activity. The fusion protein CNTRL-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity. {ECO:0000269|PubMed:10688839, ECO:0000269|PubMed:15034873, ECO:0000269|PubMed:16946300, ECO:0000269|PubMed:17389761, ECO:0000269|PubMed:23041776, ECO:0000269|PubMed:9716603, ECO:0000269|PubMed:9949182}.; DISEASE: Encephalocraniocutaneous lipomatosis (ECCL) [MIM:613001]: A sporadically occurring, neurocutaneous disorder characterized by ocular anomalies, skin lesions, and central nervous system anomalies. Clinical features include a well-demarcated hairless fatty nevus on the scalp, benign ocular tumors, intracranial and intraspinal lipomas, and congenital abnormalities of the meninges. Seizures, spasticity, and intellectual disability can be present. {ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:26942290}. 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:10861678}. 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 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. {ECO:0000250|UniProtKB:P16092, ECO:0000269|PubMed:10830168, ECO:0000269|PubMed:11353842, ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1379697, ECO:0000269|PubMed:1379698, ECO:0000269|PubMed:15117958, ECO:0000269|PubMed:16597617, ECO:0000269|PubMed:17311277, ECO:0000269|PubMed:17623664, ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19261810, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:20133753, ECO:0000269|PubMed:20139426, ECO:0000269|PubMed:21765395, ECO:0000269|PubMed:8622701, ECO:0000269|PubMed:8663044}.
uniprot
proteins
mass_dalton
91868
uniprot
proteins
mutagenesis
MUTAGEN 514; /note="K->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:15117958"; MUTAGEN 577; /note="R->E: Strongly reduced autophosphorylation in response to FGF signaling. No effect on in vitro kinase activity."; /evidence="ECO:0000269|PubMed:20133753"; MUTAGEN 609; /note="R->V: Abolishes interaction with PLCG1."; MUTAGEN 623; /note="D->A: Loss of kinase activity."; /evidence="ECO:0000269|PubMed:19224897"; MUTAGEN 653; /note="Y->F: No effect on kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-654."; /evidence="ECO:0000269|PubMed:8622701"; MUTAGEN 654; /note="Y->F: Reduced kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-653."; /evidence="ECO:0000269|PubMed:8622701"; MUTAGEN 755; /note="D->V: Abolishes interaction with PLCG1."; MUTAGEN 766; /note="Y->F: Abolishes interaction with PLCG1 and SHB. Decreases phosphorylation of FRS2, activation of RAS and MAP kinase signaling and stimulation of cell proliferation."; /evidence="ECO:0000269|PubMed:12181353, ECO:0000269|PubMed:1379697, ECO:0000269|PubMed:1379698, ECO:0000269|PubMed:7516330
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. {ECO:0000269|PubMed:16507368, ECO:0000269|PubMed:19224897, ECO:0000269|PubMed:19665973, ECO:0000269|PubMed:8622701}.; 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. {ECO:0000269|PubMed:18480409, ECO:0000269|PubMed:21765395}.; 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:16335952, ECO:0000269|PubMed:16481405, ECO:0000269|PubMed:17311277}.
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
10454568
uniprot
proteins
pubmed
10688839
uniprot
proteins
pubmed
10830168
uniprot
proteins
pubmed
10861678
uniprot
proteins
pubmed
11030354
uniprot
proteins
pubmed
11173846
uniprot
proteins
pubmed
11353842
uniprot
proteins
pubmed
12141425
uniprot
proteins
pubmed
12181353
uniprot
proteins
pubmed
12627230
uniprot
proteins
pubmed
1317750
uniprot
proteins
pubmed
1379697
uniprot
proteins
pubmed
1379698
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15001591
uniprot
proteins
pubmed
15034873
uniprot
proteins
pubmed
15117958
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15605412
uniprot
proteins
pubmed
15625620
uniprot
proteins
pubmed
15845591
uniprot
proteins
pubmed
15863030
uniprot
proteins
pubmed
16335952
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
16470795
uniprot
proteins
pubmed
16481405
uniprot
proteins
pubmed
1650441
uniprot
proteins
pubmed
16507368
uniprot
proteins
pubmed
1652059
uniprot
proteins
pubmed
1656221
uniprot
proteins
pubmed
16597617
uniprot
proteins
pubmed
16606836
uniprot
proteins
pubmed
1662973
uniprot
proteins
pubmed
16757108
uniprot
proteins
pubmed
16764984
uniprot
proteins
pubmed
16882753
uniprot
proteins
pubmed
16946300
uniprot
proteins
pubmed
1697263
uniprot
proteins
pubmed
17154279
uniprot
proteins
pubmed
1722683
uniprot
proteins
pubmed
17311277
uniprot
proteins
pubmed
17344846
uniprot
proteins
pubmed
17389761
uniprot
proteins
pubmed
17623664
uniprot
proteins
pubmed
18441324
uniprot
proteins
pubmed
1846977
uniprot
proteins
pubmed
18480409
uniprot
proteins
pubmed
19224897
uniprot
proteins
pubmed
19261810
uniprot
proteins
pubmed
19665973
uniprot
proteins
pubmed
19696444
uniprot
proteins
pubmed
19820032
uniprot
proteins
pubmed
19966287
uniprot
proteins
pubmed
20094046
uniprot
proteins
pubmed
20117945
uniprot
proteins
pubmed
20133753
uniprot
proteins
pubmed
20139426
uniprot
proteins
pubmed
20422052
uniprot
proteins
pubmed
21454610
uniprot
proteins
pubmed
2159626
uniprot
proteins
pubmed
2162671
uniprot
proteins
pubmed
2167437
uniprot
proteins
pubmed
21700882
uniprot
proteins
pubmed
21765395
uniprot
proteins
pubmed
22927827
uniprot
proteins
pubmed
23041776
uniprot
proteins
pubmed
23643382
uniprot
proteins
pubmed
23812909
uniprot
proteins
pubmed
24888332
uniprot
proteins
pubmed
25077900
uniprot
proteins
pubmed
26277103
uniprot
proteins
pubmed
26942290
uniprot
proteins
pubmed
38529886
uniprot
proteins
pubmed
7516330
uniprot
proteins
pubmed
7520751
uniprot
proteins
pubmed
7874169
uniprot
proteins
pubmed
8074689
uniprot
proteins
pubmed
8622701
uniprot
proteins
pubmed
8663044
uniprot
proteins
pubmed
8752212
uniprot
proteins
pubmed
9139660
uniprot
proteins
pubmed
9655399
uniprot
proteins
pubmed
9716603
uniprot
proteins
pubmed
9949182
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.
uniprot
proteins
transmembrane_region
TRANSMEM 377..397; /note="Helical"; /evidence="ECO:0000255
uniprot
proteins