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P11362 (FGFR1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 199. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Fibroblast growth factor receptor 1

Short name=FGFR-1
EC=2.7.10.1
Alternative name(s):
Basic fibroblast growth factor receptor 1
Short name=BFGFR
Short name=bFGF-R-1
Fms-like tyrosine kinase 2
Short name=FLT-2
N-sam
Proto-oncogene c-Fgr
CD_antigen=CD331
Gene names
Name:FGFR1
Synonyms:BFGFR, CEK, FGFBR, FLG, FLT2, HBGFR
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length822 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Tyrosine-protein kinase that acts as 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. Ref.10 Ref.22 Ref.23 Ref.25 Ref.26 Ref.31 Ref.32 Ref.34 Ref.37 Ref.41 Ref.42 Ref.43 Ref.45 Ref.46 Ref.48 Ref.55 Ref.58 Ref.59

Catalytic activity

ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate. Ref.22 Ref.25 Ref.34 Ref.43 Ref.46 Ref.58 Ref.59

Enzyme 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. Ref.25 Ref.43 Ref.46 Ref.60

Subunit structure

Monomer. Homodimer after ligand binding. Interacts predominantly with FGF1 and FGF2, but can also interact with FGF3, FGF4, FGF5, FGF6, FGF8, FGF10, FGF19, FGF21, FGF22 and FGF23 (in vitro). Ligand specificity is determined by tissue-specific expression of isoforms, and differences in the third Ig-like domain are crucial for ligand specificity. Affinity for fibroblast growth factors (FGFs) is increased by heparan sulfate glycosaminoglycans that function as coreceptors. Likewise, KLB increases the affinity for FGF19, FGF21 and FGF23. Interacts (phosphorylated on Tyr-766) with PLCG1 (via SH2 domains). Interacts with FRS2. Interacts (via C-terminus) with NEDD4 (via WW3 domain). Interacts with KL By similarity. Interacts with SHB (via SH2 domain) and GRB10. Interacts with KAL1; this interaction does not interfere with FGF2-binding to FGFR1, but prevents binding of heparin-bound FGF2. Interacts with SOX2 and SOX3 By similarity. Ref.2 Ref.5 Ref.21 Ref.22 Ref.26 Ref.27 Ref.29 Ref.32 Ref.34 Ref.37 Ref.41 Ref.44 Ref.47 Ref.48 Ref.58 Ref.59

Subcellular location

Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasmcytosol. 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. Ref.24 Ref.34 Ref.38 Ref.43 Ref.45 Ref.48

Tissue specificity

Detected in astrocytoma, neuroblastoma and adrenal cortex cell lines. Some isoforms are detected in foreskin fibroblast cell lines, however isoform 17, isoform 18 and isoform 19 are not detected in these cells. Ref.19

Domain

The second and third Ig-like domains directly interact with fibroblast growth factors (FGF) and heparan sulfate proteoglycans. Isoforms lacking the first Ig-like domain have higher affinity for fibroblast growth factors (FGF) and heparan sulfate proteoglycans than isoforms with all three Ig-like domains.

Post-translational modification

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. Ref.22 Ref.25 Ref.27 Ref.39 Ref.42 Ref.46 Ref.58

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. Ref.43 Ref.48

N-glycosylated in the endoplasmic reticulum. The N-glycan chains undergo further maturation to an Endo H-resistant form in the Golgi apparatus. Ref.38 Ref.42

Involvement in 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).
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.61

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).
Note: The disease is caused by mutations 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, KAL1, KISS1R, NSMF, PROKR2, SPRY4 and TACR3 (Ref.78). Ref.10 Ref.63 Ref.64 Ref.66 Ref.67 Ref.69 Ref.70 Ref.71 Ref.72 Ref.73 Ref.75 Ref.76 Ref.77 Ref.78

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.65 Ref.68

Hartsfield syndrome (HRTFDS) [MIM:615465]: A syndrome characterized by the triad of holoprosencephaly, ectrodactyly, and cleft/lip palate. Profound mental retardation is also present. Multiple other congenital anomalies usually occur.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.79

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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.10 Ref.62

A chromosomal aberration involving FGFR1 may be a cause of stem cell leukemia lymphoma syndrome (SCLL). Translocation t(8;13)(p11;q12) with ZMYM2. SCLL usually presents as lymphoblastic lymphoma in association with a myeloproliferative disorder, often accompanied by pronounced peripheral eosinophilia and/or prominent eosinophilic infiltrates in the affected bone marrow. Ref.10

A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(6;8)(q27;p11) with FGFR1OP. Insertion ins(12;8)(p11;p11p22) with FGFR1OP2. MPD 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, FGFR1OP-FGFR1 or FGFR1-FGFR1OP may exhibit constitutive kinase activity and be responsible for the transforming activity.

A chromosomal aberration involving FGFR1 may be a cause of stem cell myeloproliferative disorder (MPD). Translocation t(8;9)(p12;q33) with CNTRL. MPD is characterized by myeloid hyperplasia, eosinophilia and T-cell or B-cell lymphoblastic lymphoma. In general it progresses to acute myeloid leukemia. The fusion protein CNTRL-FGFR1 is found in the cytoplasm, exhibits constitutive kinase activity and may be responsible for the transforming activity.

Sequence similarities

Belongs to the protein kinase superfamily. Tyr protein kinase family. Fibroblast growth factor receptor subfamily.

Contains 3 Ig-like C2-type (immunoglobulin-like) domains.

Contains 1 protein kinase domain.

Sequence caution

The sequence BAD92156.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell membrane
Cytoplasm
Cytoplasmic vesicle
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Chromosomal rearrangement
Polymorphism
   DiseaseCraniosynostosis
Disease mutation
Dwarfism
Holoprosencephaly
Hypogonadotropic hypogonadism
Kallmann syndrome
Mental retardation
   DomainImmunoglobulin domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandATP-binding
Heparin-binding
Nucleotide-binding
   Molecular functionKinase
Receptor
Transferase
Tyrosine-protein kinase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processFc-epsilon receptor signaling pathway

Traceable author statement. Source: Reactome

MAPK cascade

Traceable author statement PubMed 10748122. Source: ProtInc

angiogenesis

Inferred from electronic annotation. Source: Ensembl

auditory receptor cell development

Inferred from electronic annotation. Source: Ensembl

axon guidance

Traceable author statement. Source: Reactome

branching involved in salivary gland morphogenesis

Inferred from electronic annotation. Source: Ensembl

cell maturation

Inferred from electronic annotation. Source: Ensembl

cell migration

Traceable author statement Ref.50. Source: UniProtKB

chondrocyte differentiation

Inferred from electronic annotation. Source: Ensembl

chordate embryonic development

Traceable author statement Ref.50. Source: UniProtKB

embryonic limb morphogenesis

Inferred from electronic annotation. Source: Ensembl

epidermal growth factor receptor signaling pathway

Traceable author statement. Source: Reactome

fibroblast growth factor receptor signaling pathway

Inferred from direct assay Ref.26. Source: UniProtKB

fibroblast growth factor receptor signaling pathway involved in orbitofrontal cortex development

Inferred from electronic annotation. Source: Ensembl

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

innate immune response

Traceable author statement. Source: Reactome

inner ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

insulin receptor signaling pathway

Traceable author statement. Source: Reactome

lung-associated mesenchyme development

Inferred from electronic annotation. Source: Ensembl

mesenchymal cell differentiation

Inferred from electronic annotation. Source: Ensembl

midbrain development

Inferred from electronic annotation. Source: Ensembl

middle ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

negative regulation of transcription from RNA polymerase II promoter

Inferred from electronic annotation. Source: Ensembl

neuron migration

Traceable author statement Ref.50. Source: UniProtKB

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

organ induction

Inferred from electronic annotation. Source: Ensembl

outer ear morphogenesis

Inferred from electronic annotation. Source: Ensembl

paraxial mesoderm development

Inferred from electronic annotation. Source: Ensembl

peptidyl-tyrosine phosphorylation

Inferred from direct assay Ref.43Ref.25. Source: UniProtKB

phosphatidylinositol-mediated signaling

Traceable author statement Ref.49. Source: UniProtKB

positive regulation of MAP kinase activity

Inferred from direct assay Ref.43Ref.25. Source: UniProtKB

positive regulation of MAPK cascade

Inferred from mutant phenotype Ref.25. Source: UniProtKB

positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway

Inferred from electronic annotation. Source: Ensembl

positive regulation of cardiac muscle cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell cycle

Inferred from electronic annotation. Source: Ensembl

positive regulation of cell proliferation

Inferred from direct assay Ref.26. Source: UniProtKB

positive regulation of mesenchymal cell proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of neuron differentiation

Inferred from mutant phenotype Ref.25. Source: UniProtKB

positive regulation of neuron projection development

Inferred from electronic annotation. Source: Ensembl

positive regulation of phosphatidylinositol 3-kinase signaling

Traceable author statement Ref.50. Source: UniProtKB

positive regulation of phospholipase C activity

Inferred from direct assay Ref.43. Source: UniProtKB

positive regulation of phospholipase activity

Traceable author statement Ref.49. Source: UniProtKB

protein autophosphorylation

Inferred from direct assay Ref.25. Source: UniProtKB

protein phosphorylation

Non-traceable author statement Ref.8Ref.4. Source: UniProtKB

regulation of branching involved in salivary gland morphogenesis by mesenchymal-epithelial signaling

Inferred from electronic annotation. Source: Ensembl

regulation of cell differentiation

Traceable author statement Ref.49. Source: UniProtKB

regulation of extrinsic apoptotic signaling pathway in absence of ligand

Inferred from electronic annotation. Source: Ensembl

regulation of lateral mesodermal cell fate specification

Inferred from electronic annotation. Source: Ensembl

sensory perception of sound

Inferred from electronic annotation. Source: Ensembl

skeletal system development

Traceable author statement Ref.61. Source: ProtInc

skeletal system morphogenesis

Traceable author statement Ref.50. Source: UniProtKB

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

ureteric bud development

Inferred from electronic annotation. Source: Ensembl

ventricular zone neuroblast division

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcytoplasmic membrane-bounded vesicle

Inferred from electronic annotation. Source: UniProtKB-SubCell

cytosol

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Non-traceable author statement Ref.19. Source: UniProtKB

integral component of membrane

Non-traceable author statement Ref.19Ref.8Ref.4. Source: UniProtKB

integral component of plasma membrane

Traceable author statement PubMed 10918587. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

plasma membrane

Inferred from direct assay Ref.43. Source: UniProtKB

receptor complex

Inferred from direct assay PubMed 23382219. Source: MGI

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

fibroblast growth factor binding

Inferred from direct assay Ref.43Ref.26. Source: UniProtKB

fibroblast growth factor-activated receptor activity

Inferred from direct assay Ref.43Ref.59. Source: UniProtKB

heparin binding

Inferred from direct assay Ref.43. Source: UniProtKB

identical protein binding

Inferred from physical interaction Ref.44. Source: IntAct

protein binding

Inferred from physical interaction PubMed 23597562. Source: IntAct

protein homodimerization activity

Inferred from physical interaction Ref.59. Source: UniProtKB

protein tyrosine kinase activity

Inferred from direct assay Ref.25. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 21 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P11362-1)

Also known as: Alpha A1; IV;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P11362-8)

Also known as: Alpha A2;

The sequence of this isoform differs from the canonical sequence as follows:
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.
Isoform 3 (identifier: P11362-17)

Also known as: Alpha A3;

The sequence of this isoform differs from the canonical sequence as follows:
     32-61: QPWGAPVEVESFLVHPGDLLQLRCRLRDDV → CPDLQEAKSCSASFHSITPLPFGLGTRLSD
     62-822: Missing.
Isoform 4 (identifier: P11362-2)

Also known as: Alpha B1;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
Isoform 5 (identifier: P11362-9)

Also known as: Alpha B2;

The sequence of this isoform differs from the canonical sequence as follows:
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.
Isoform 6 (identifier: P11362-3)

Also known as: Beta A1; II; H2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
Isoform 7 (identifier: P11362-10)

Also known as: Beta A2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.
Isoform 8 (identifier: P11362-4)

Also known as: Beta B1;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     428-429: Missing.
Isoform 9 (identifier: P11362-11)

Also known as: Beta B2;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.
Isoform 10 (identifier: P11362-5)

Also known as: Gamma A1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
Isoform 11 (identifier: P11362-12)

Also known as: Gamma A2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.
Isoform 12 (identifier: P11362-6)

Also known as: Gamma B1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     428-429: Missing.
Isoform 13 (identifier: P11362-13)

Also known as: Gamma B2;

The sequence of this isoform differs from the canonical sequence as follows:
     1-160: Missing.
     428-429: Missing.
     619-662: CIHRDLAARN...YYKKTTNGRL → VWNLKAPLVH...RTGHSPHRLL
     663-822: Missing.
Isoform 14 (identifier: P11362-7)

Also known as: A; III;

The sequence of this isoform differs from the canonical sequence as follows:
     148-149: Missing.
Isoform 15 (identifier: P11362-14)

Also known as: I; H3;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.
Isoform 16 (identifier: P11362-15)

Also known as: V;

The sequence of this isoform differs from the canonical sequence as follows:
     120-150: DALPSSEDDDDDDDSSSEEKETDNTKPNRMP → ACPDLQEAKWCSASFHSITPLPFGLGTRLSD
     151-822: Missing.
Isoform 17 (identifier: P11362-16)

Also known as: H4;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     313-391: TAGVNTTDKE...TGAFLISCMV → VIMAPVFVGQ...RAAGMGGAGL
     392-822: Missing.
Isoform 18 (identifier: P11362-18)

Also known as: H5;

The sequence of this isoform differs from the canonical sequence as follows:
     31-119: Missing.
     148-149: Missing.
     313-391: TAGVNTTDKE...TGAFLISCMV → VIMAPVFVGQ...RAAGMGGAGL
     392-822: Missing.
Isoform 19 (identifier: P11362-19)

The sequence of this isoform differs from the canonical sequence as follows:
     119-119: S → SVPI
     148-149: Missing.
     313-360: TAGVNTTDKE...HHSAWLTVLE → HSGINSSDAE...QSAWLTVTRP
Isoform 20 (identifier: P11362-20)

The sequence of this isoform differs from the canonical sequence as follows:
     1-30: MWSWKCLLFWAVLVTATLCTARPSPTLPEQ → MAAVTRDFGEMLLHSGRVLPAE
     427-428: Missing.
Isoform 21 (identifier: P11362-21)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MEARVSLKRRIELTVEYPWRCGALSPTSNCRTGM
     148-149: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Ref.16
Chain22 – 822801Fibroblast growth factor receptor 1
PRO_0000016780

Regions

Topological domain22 – 376355Extracellular Potential
Transmembrane377 – 39721Helical; Potential
Topological domain398 – 822425Cytoplasmic Potential
Domain25 – 11995Ig-like C2-type 1
Domain158 – 24689Ig-like C2-type 2
Domain255 – 357103Ig-like C2-type 3
Domain478 – 767290Protein kinase
Nucleotide binding484 – 4907ATP
Nucleotide binding562 – 5643ATP
Region160 – 17718Heparin-binding

Sites

Active site6231Proton acceptor Ref.46
Binding site5141ATP
Binding site5681ATP
Binding site6271ATP
Binding site6411ATP
Site428 – 4292Breakpoint for translocation to form CNTRL-FGFR1 OR FGFR1-CNTRL fusion proteins
Site428 – 4292Breakpoint for translocation to form FGFR1OP-FGFR1 or FGFR1-FGFR1OP fusion proteins
Site428 – 4292Breakpoint for translocation to form FGFR1OP2-FGFR1
Site7661Mediates interaction with PLCG1 and SHB

Amino acid modifications

Modified residue4631Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46
Modified residue5831Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46
Modified residue5851Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46
Modified residue6531Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46 Ref.58
Modified residue6541Phosphotyrosine; by autocatalysis Ref.25 Ref.39 Ref.46 Ref.58
Modified residue7301Phosphotyrosine; by autocatalysis Ref.25 Ref.46
Modified residue7661Phosphotyrosine; by autocatalysis Ref.58
Glycosylation771N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2401N-linked (GlcNAc...) Potential
Glycosylation2641N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Ref.35
Glycosylation3171N-linked (GlcNAc...) Potential
Glycosylation3301N-linked (GlcNAc...) Potential
Disulfide bond55 ↔ 101 By similarity
Disulfide bond178 ↔ 230 Ref.55 Ref.56
Disulfide bond277 ↔ 341 Ref.55 Ref.56

Natural variations

Alternative sequence1 – 160160Missing in isoform 10, isoform 11, isoform 12 and isoform 13.
VSP_002957
Alternative sequence1 – 3030MWSWK…TLPEQ → MAAVTRDFGEMLLHSGRVLP AE in isoform 20.
VSP_041916
Alternative sequence11M → MEARVSLKRRIELTVEYPWR CGALSPTSNCRTGM in isoform 21.
VSP_041917
Alternative sequence31 – 11989Missing in isoform 6, isoform 7, isoform 8, isoform 9, isoform 15, isoform 17 and isoform 18.
VSP_002958
Alternative sequence32 – 6130QPWGA…LRDDV → CPDLQEAKSCSASFHSITPL PFGLGTRLSD in isoform 3.
VSP_009836
Alternative sequence62 – 822761Missing in isoform 3.
VSP_009837
Alternative sequence1191S → SVPI in isoform 19.
VSP_038470
Alternative sequence120 – 15031DALPS…PNRMP → ACPDLQEAKWCSASFHSITP LPFGLGTRLSD in isoform 16.
VSP_009838
Alternative sequence148 – 1492Missing in isoform 14, isoform 15, isoform 18, isoform 19 and isoform 21.
VSP_002959
Alternative sequence151 – 822672Missing in isoform 16.
VSP_009839
Alternative sequence313 – 39179TAGVN…ISCMV → VIMAPVFVGQSTGKETTVSG AQVPVGRLSCPRMGSFLTLQ AHTLHLSRDLATSPRTSNRG HKVEVSWEQRAAGMGGAGL in isoform 17 and isoform 18.
VSP_009840
Alternative sequence313 – 36048TAGVN…LTVLE → HSGINSSDAEVLTLFNVTEA QSGEYVCKVSNYIGEANQSA WLTVTRP in isoform 19.
VSP_038471
Alternative sequence392 – 822431Missing in isoform 17 and isoform 18.
VSP_009841
Alternative sequence427 – 4282Missing in isoform 20.
VSP_041918
Alternative sequence428 – 4292Missing in isoform 4, isoform 5, isoform 8, isoform 9, isoform 12 and isoform 13.
VSP_002960
Alternative sequence619 – 66244CIHRD…TNGRL → VWNLKAPLVHTPRPGSQECP GDRGQCDEDSRLWPRTGHSP HRLL in isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13.
VSP_009842
Alternative sequence663 – 822160Missing in isoform 2, isoform 5, isoform 7, isoform 9, isoform 11 and isoform 13.
VSP_009843
Natural variant221R → S. Ref.13
Corresponds to variant rs17175750 [ dbSNP | Ensembl ].
VAR_019290
Natural variant481G → S in HH2; phenotype consistent with normosmic idiopathic hypogonadotropic hypogonadism. Ref.69
VAR_030968
Natural variant771N → K. Ref.73
VAR_030969
Natural variant781R → C in HH2. Ref.70
VAR_030970
Natural variant971G → D in HH2. Ref.63
VAR_017885
Natural variant991Y → C in HH2; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression. Ref.63 Ref.75
VAR_017886
Natural variant1011C → F in HH2. Ref.73
VAR_030971
Natural variant1021V → I in HH2. Ref.66 Ref.70
Corresponds to variant rs55642501 [ dbSNP | Ensembl ].
VAR_030972
Natural variant1171N → S in HH2; some patients also carry GNRHR mutations. Ref.75 Ref.78
VAR_069288
Natural variant1251S → L in a breast infiltrating ductal carcinoma sample; somatic mutation. Ref.74
VAR_042201
Natural variant1291D → A in HH2. Ref.66
VAR_030973
Natural variant1651L → S in HRTFDS. Ref.79
VAR_070851
Natural variant1671A → S in HH2; with cleft palate, corpus callosum agenesis, unilateral deafness and fusion of fourth and fifth metacarpal bones. Ref.63
VAR_017887
Natural variant1781C → S in HH2; with severe ear anomalies. Ref.71
VAR_030974
Natural variant1911L → S in HRTFDS. Ref.79
VAR_070852
Natural variant2131W → G. Ref.15
Corresponds to variant rs17851623 [ dbSNP | Ensembl ].
VAR_030975
Natural variant2241D → H in HH2. Ref.70
VAR_030976
Natural variant2281Y → D in HH2; some patients also carry KISS1R mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression. Ref.75 Ref.78
VAR_069289
Natural variant2371G → D in HH2. Ref.70
VAR_030977
Natural variant2371G → S in HH2; with or without anosmia; also found in a family member with isolated anosmia; may impair proper folding. Ref.72
VAR_030978
Natural variant2391I → T in HH2; some patients also carry PROKR2 and GNRH1 mutations; impairs the tertiary folding resulting in incomplete glycosylation and reduced cell surface expression. Ref.75 Ref.78
VAR_069290
Natural variant2451L → P in HH2. Ref.69
VAR_030979
Natural variant2501R → Q in HH2; with or without anosmia; results in Kallmann syndrome in the presence of HS6ST1 mutation TRP-306; reduces receptor affinity for fibroblast growth factor. Ref.75 Ref.76 Ref.78
VAR_069291
Natural variant2501R → W in HH2. Ref.69 Ref.73
VAR_030980
Natural variant2521P → R in PS; seems to be a gain of function. Ref.61
VAR_004111
Natural variant2521P → T in a lung bronchoalveolar carcinoma sample; somatic mutation. Ref.74
VAR_042202
Natural variant2541R → Q in HH2. Ref.70
VAR_030981
Natural variant2701G → D in HH2. Ref.73
VAR_030982
Natural variant2731V → M in HH2. Ref.66 Ref.70
VAR_030983
Natural variant2741E → G in HH2; also found in a family member with isolated anosmia. Ref.70
VAR_030984
Natural variant2771C → Y in HH2. Ref.63
VAR_017888
Natural variant2831P → R in HH2. Ref.73
VAR_030985
Natural variant3001I → T in TRIGNO1. Ref.62
VAR_030986
Natural variant3301N → I in OGD. Ref.65 Ref.68
VAR_030987
Natural variant3321S → C in HH2. Ref.73
VAR_030988
Natural variant3391Y → C in HH2. Ref.70
VAR_030989
Natural variant3421L → S in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a splice site mutation in NSMF. Ref.78
VAR_069954
Natural variant3431A → V in HH2. Ref.69
VAR_030990
Natural variant3461S → C in HH2; also found in a family member with isolated anosmia. Ref.70
VAR_030991
Natural variant3481G → R in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a mutation in IL17RD. Ref.78
VAR_069955
Natural variant3661P → L in HH2; with or without anosmia. Ref.69
VAR_030992
Natural variant3741Y → C in OGD; elevated basal activity and increased FGF2-mediated activity. Ref.65
VAR_030993
Natural variant3811C → R in OGD. Ref.65 Ref.68
VAR_030994
Natural variant4701R → L in HH2; some patients also carry GNRHR mutations. Ref.75 Ref.78
VAR_069292
Natural variant4831P → T in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in SPRY4. Ref.78
VAR_069956
Natural variant4901G → R in HRTFDS. Ref.79
VAR_070853
Natural variant5201A → T in HH2. Ref.66
VAR_030995
Natural variant5381I → V in HH2. Ref.70
VAR_030996
Natural variant6071V → M in HH2; with bimanual synkinesis. Ref.63
VAR_017889
Natural variant6181K → N in HH2; some patients also carry GNRHR mutations; impairs tyrosine kinase activity. Ref.75 Ref.78
VAR_069293
Natural variant6211H → R in HH2. Ref.73
VAR_030997
Natural variant6221R → G in HH2; with severe ear anomalies. Ref.71
VAR_030998
Natural variant6221R → Q in HH2. Ref.71
VAR_030999
Natural variant6231D → Y in HRTFDS. Ref.79
VAR_070854
Natural variant6281N → K in HRTFDS. Ref.79
VAR_070855
Natural variant6641V → L in a lung large cell carcinoma sample; somatic mutation. Ref.74
VAR_042203
Natural variant6661W → R in HH2; with cleft palate. Ref.63
VAR_017890
Natural variant6701E → K in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in FLRT3. Ref.78
VAR_069957
Natural variant6711A → P in HH2. Ref.75
VAR_069294
Natural variant6851S → F in HH2. Ref.73
VAR_031000
Natural variant6871G → R in HH2. Ref.67 Ref.77
VAR_031001
Natural variant6921E → G in HH2; phenotype consistent with Kallmann syndrome; the patient also carries a rare variant in DUSP6. Ref.78
VAR_069958
Natural variant6931I → F in HH2. Ref.73
VAR_031002
Natural variant7031G → R in HH2. Ref.70
VAR_031003
Natural variant7031G → S in HH2. Ref.70
VAR_031004
Natural variant7191M → R in HH2. Ref.63
VAR_017891
Natural variant7221P → H in HH2; associated with K-724; also found in a family member with isolated anosmia; reduced tyrosine kinase activity. Ref.72 Ref.78
VAR_031005
Natural variant7221P → S in HH2. Ref.69
VAR_031006
Natural variant7241N → K in HH2; associated with H-722; also found in a family member with isolated anosmia; reduced tyrosine kinase activity. Ref.72 Ref.78
VAR_031007
Natural variant7251C → Y in HRTFDS. Ref.79
VAR_070856
Natural variant7451P → S in HH2. Ref.64 Ref.67
VAR_031008
Natural variant7681D → Y in HH2; the patient also carries a rare variant in FGF8. Ref.78
VAR_069959
Natural variant7691L → V. Ref.70
Corresponds to variant rs2956723 [ dbSNP | Ensembl ].
VAR_031009
Natural variant7721P → S in HH2; with cleft palate, unilateral absence of nasal cartilage, iris coloboma. Ref.63 Ref.73
Corresponds to variant rs56234888 [ dbSNP | Ensembl ].
VAR_017892
Natural variant7951V → I in HH2; also found in a family member with isolated anosmia. Ref.69
VAR_031010
Natural variant8181G → R. Ref.13
Corresponds to variant rs17182456 [ dbSNP | Ensembl ].
VAR_019291
Natural variant8221R → C. Ref.13 Ref.73
Corresponds to variant rs17182463 [ dbSNP | Ensembl ].
VAR_019292

Experimental info

Mutagenesis5141K → A: Loss of kinase activity. Ref.34
Mutagenesis5461N → K: Strongly increased speed of the first autophosphorylation, and loss of the normal sequential order of autophosphorylation. Ref.46
Mutagenesis5771R → E: Strongly reduced autophosphorylation in response to FGF signaling. No effect on in vitro kinase activity. Ref.59
Mutagenesis6091R → V: Abolishes interaction with PLCG1.
Mutagenesis6231D → A: Loss of kinase activity. Ref.46
Mutagenesis6531Y → F: No effect on kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-654. Ref.25
Mutagenesis6541Y → F: Reduced kinase activity. Loss of autophosphorylation and kinase activity; when associated with F-653. Ref.25
Mutagenesis7551D → V: Abolishes interaction with PLCG1.
Mutagenesis7661Y → F: Abolishes interaction with PLCG1 and SHB. Decreases phosphorylation of FRS2, activation of RAS and MAP kinase signaling and stimulation of cell proliferation. Ref.22 Ref.23 Ref.24 Ref.32
Sequence conflict241S → C in AAA35958. Ref.8
Sequence conflict241S → C in AAA35959. Ref.8
Sequence conflict1921K → E in AAA35837. Ref.3
Sequence conflict1941G → S in AAA35835. Ref.5
Sequence conflict1961E → G no nucleotide entry Ref.16
Sequence conflict2231S → F in BAD96438. Ref.12
Sequence conflict3081V → A in AAA35958. Ref.8
Sequence conflict3081V → A in AAA35959. Ref.8
Sequence conflict3641E → Q in CAA68679. Ref.18
Sequence conflict4691P → L in AAA75007. Ref.1
Sequence conflict4821K → R in BAD96438. Ref.12
Sequence conflict5761R → W in BAD96438. Ref.12
Sequence conflict8171G → R in CAA36101. Ref.4

Secondary structure

.................................................................................................................... 822
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (Alpha A1) (IV) [UniParc].

Last modified May 1, 1991. Version 3.
Checksum: 93A01B5D78C3E72C

FASTA82291,868
        10         20         30         40         50         60 
MWSWKCLLFW AVLVTATLCT ARPSPTLPEQ AQPWGAPVEV ESFLVHPGDL LQLRCRLRDD 

        70         80         90        100        110        120 
VQSINWLRDG VQLAESNRTR ITGEEVEVQD SVPADSGLYA CVTSSPSGSD TTYFSVNVSD 

       130        140        150        160        170        180 
ALPSSEDDDD DDDSSSEEKE TDNTKPNRMP VAPYWTSPEK MEKKLHAVPA AKTVKFKCPS 

       190        200        210        220        230        240 
SGTPNPTLRW LKNGKEFKPD HRIGGYKVRY ATWSIIMDSV VPSDKGNYTC IVENEYGSIN 

       250        260        270        280        290        300 
HTYQLDVVER SPHRPILQAG LPANKTVALG SNVEFMCKVY SDPQPHIQWL KHIEVNGSKI 

       310        320        330        340        350        360 
GPDNLPYVQI LKTAGVNTTD KEMEVLHLRN VSFEDAGEYT CLAGNSIGLS HHSAWLTVLE 

       370        380        390        400        410        420 
ALEERPAVMT SPLYLEIIIY CTGAFLISCM VGSVIVYKMK SGTKKSDFHS QMAVHKLAKS 

       430        440        450        460        470        480 
IPLRRQVTVS ADSSASMNSG VLLVRPSRLS SSGTPMLAGV SEYELPEDPR WELPRDRLVL 

       490        500        510        520        530        540 
GKPLGEGCFG QVVLAEAIGL DKDKPNRVTK VAVKMLKSDA TEKDLSDLIS EMEMMKMIGK 

       550        560        570        580        590        600 
HKNIINLLGA CTQDGPLYVI VEYASKGNLR EYLQARRPPG LEYCYNPSHN PEEQLSSKDL 

       610        620        630        640        650        660 
VSCAYQVARG MEYLASKKCI HRDLAARNVL VTEDNVMKIA DFGLARDIHH IDYYKKTTNG 

       670        680        690        700        710        720 
RLPVKWMAPE ALFDRIYTHQ SDVWSFGVLL WEIFTLGGSP YPGVPVEELF KLLKEGHRMD 

       730        740        750        760        770        780 
KPSNCTNELY MMMRDCWHAV PSQRPTFKQL VEDLDRIVAL TSNQEYLDLS MPLDQYSPSF 

       790        800        810        820 
PDTRSSTCSS GEDSVFSHEP LPEEPCLPRH PAQLANGGLK RR 

« Hide

Isoform 2 (Alpha A2) [UniParc].

Checksum: E9419E4DCB3D8A15
Show »

FASTA66273,475
Isoform 3 (Alpha A3) [UniParc].

Checksum: 13F5DEE578AF5D86
Show »

FASTA616,682
Isoform 4 (Alpha B1) [UniParc].

Checksum: 16B07518ECFC98F5
Show »

FASTA82091,668
Isoform 5 (Alpha B2) [UniParc].

Checksum: 2D2E9EEAC7BDDE3F
Show »

FASTA66073,274
Isoform 6 (Beta A1) (II) (H2) [UniParc].

Checksum: ED3CD2B1CA825F7E
Show »

FASTA73382,162
Isoform 7 (Beta A2) [UniParc].

Checksum: BA9898B9E682D31C
Show »

FASTA57363,769
Isoform 8 (Beta B1) [UniParc].

Checksum: EF5CC75954AEC7FC
Show »

FASTA73181,962
Isoform 9 (Beta B2) [UniParc].

Checksum: 0BDAB3559EB4B141
Show »

FASTA57163,569
Isoform 10 (Gamma A1) [UniParc].

Checksum: F51EB57977705DE1
Show »

FASTA66274,133
Isoform 11 (Gamma A2) [UniParc].

Checksum: 3D3E866B4D4CEBEF
Show »

FASTA50255,740
Isoform 12 (Gamma B1) [UniParc].

Checksum: E8947AAB5631D58E
Show »

FASTA66073,933
Isoform 13 (Gamma B2) [UniParc].

Checksum: D508189BA6475745
Show »

FASTA50055,540
Isoform 14 (A) (III) [UniParc].

Checksum: 4644ADCC15A696FD
Show »

FASTA82091,580
Isoform 15 (I) (H3) [UniParc].

Checksum: BFA81F8DADF4C9F4
Show »

FASTA73181,875
Isoform 16 (V) [UniParc].

Checksum: BA69FDD207CBBDFB
Show »

FASTA15016,487
Isoform 17 (H4) [UniParc].

Checksum: A2FF0FB217358001
Show »

FASTA30233,412
Isoform 18 (H5) [UniParc].

Checksum: 00836E542E75EFA3
Show »

FASTA30033,125
Isoform 19 [UniParc].

Checksum: 657DE58FE3072EA2
Show »

FASTA82291,760
Isoform 20 [UniParc].

Checksum: 817D54D21F3669F0
Show »

FASTA81290,618
Isoform 21 [UniParc].

Checksum: ADA3C30F9F9DE084
Show »

FASTA85395,344

References

« Hide 'large scale' references
[1]"The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA."
Itoh N., Terachi T., Ohta M., Seo M.K.
Biochem. Biophys. Res. Commun. 169:680-685(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 15).
Tissue: Placenta.
[2]"Cloning and expression of two distinct high-affinity receptors cross-reacting with acidic and basic fibroblast growth factors."
Dionne C.A., Crumley G.R., Bellot F., Kaplow J.M., Searfoss G., Ruta M., Burgess W.H., Jaye M., Schlessinger J.
EMBO J. 9:2685-2692(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH FGF1 AND FGF2.
Tissue: Neonatal brain stem.
[3]"Diverse forms of a receptor for acidic and basic fibroblast growth factors."
Johnson D.E., Lee P.L., Lu J., Williams L.T.
Mol. Cell. Biol. 10:4728-4736(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 6; 15; 17 AND 18).
[4]"Complete sequence of a human receptor for acidic and basic fibroblast growth factors."
Isacchi A., Bergonzoni L., Sarmientos P.
Nucleic Acids Res. 18:1906-1906(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Placenta.
[5]"cDNA cloning and expression of a human FGF receptor which binds acidic and basic FGF."
Wennstroem S., Sandstroem C., Claesson-Welsh L.
Growth Factors 4:197-208(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14), INTERACTION WITH FGF1 AND FGF2.
Tissue: Teratocarcinoma.
[6]"Molecular cloning of a human basic fibroblast growth factor receptor cDNA and expression of a biologically active extracellular domain in a baculovirus system."
Kiefer M.C., Baird A., George-Nascimento C., Nguyen T., Mason O.B., Boley L.J., Valenzuela P., Barr P.J.
Growth Factors 5:115-127(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 14).
[7]"Alternative splicing generates at least five different isoforms of the human basic-FGF receptor."
Eisemann A., Ahn J.A., Graziani G., Tronick S.R., Ron D.
Oncogene 6:1195-1202(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 6; 14; 15 AND 16).
Tissue: Lung.
[8]"Fibroblast growth factor receptors from liver vary in three structural domains."
Hou J., Kan M., McKeehan K., McBride G., Adams P., McKeehan W.L.
Science 251:665-668(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8; 9; 10; 11; 12 AND 13).
Tissue: Liver.
[9]"K-sam-related gene, N-sam, encodes fibroblast growth factor receptor and is expressed in T-lymphocytic tumors."
Hattori Y., Odagiri H., Katoh O., Sakamoto H., Morita T., Shimotohno K., Tobinai K., Sugimura T., Terada M.
Cancer Res. 52:3367-3371(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[10]"A case of Kallmann syndrome carrying a missense mutation in alternatively spliced exon 8A encoding the immunoglobulin-like domain IIIb of fibroblast growth factor receptor 1."
Miura K., Miura S., Yoshiura K., Seminara S., Hamaguchi D., Niikawa N., Masuzaki H.
Hum. Reprod. 25:1076-1080(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 19), ROLE IN DISEASE.
[11]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 6; 14 AND 21).
Tissue: Placenta and Testis.
[12]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 14 AND 20).
Tissue: Brain and Colon.
[13]NIEHS SNPs program
Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SER-22; ARG-818 AND CYS-822.
[14]"DNA sequence and analysis of human chromosome 8."
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T. expand/collapse author list , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[15]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 14 AND 15), VARIANT GLY-213.
Tissue: Pancreas, Testis and Uterus.
[16]"Multivalent ligand-receptor binding interactions in the fibroblast growth factor system produce a cooperative growth factor and heparin mechanism for receptor dimerization."
Pantoliano M.W., Horlick R.A., Springer B.A., Van Dyk D.E., Tobery T., Wetmore D.R., Lear J.D., Nahapetian A.T., Bradley J.D., Sisk W.P.
Biochemistry 33:10229-10248(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-370 (ISOFORM 15), PROTEIN SEQUENCE OF 22-129 (ISOFORM 15).
[17]"Distinct role of 2-O-, N-, and 6-O-sulfate groups of heparin in the formation of the ternary complex with basic fibroblast growth factor and soluble FGF receptor-1."
Rusnati M., Coltrini D., Caccia P., Dell'Era P., Zoppetti G., Oreste P., Valsasina B., Presta M.
Biochem. Biophys. Res. Commun. 203:450-458(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 81-100 (ISOFORMS 1/2/4/5/14/16).
[18]"A novel protein tyrosine kinase gene whose expression is modulated during endothelial cell differentiation."
Ruta M., Howk R., Ricca G., Drohan W., Zabelshansky M., Laureys G., Barton D.E., Francke U., Schlessinger J., Givol D.
Oncogene 3:9-15(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 201-822 (ISOFORMS 1/6/10/14/15).
[19]"The human fibroblast growth factor receptor genes: a common structural arrangement underlies the mechanisms for generating receptor forms that differ in their third immunoglobulin domain."
Johnson D.E., Lu J., Chen H., Werner S., Williams L.T.
Mol. Cell. Biol. 11:4627-4634(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-391 (ISOFORMS 17/18), NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 313-360 (ISOFORMS 1/2/4/5/6/7/8/9/10/11/12/13/14/15), NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] OF 313-360 (ISOFORM 19), TISSUE SPECIFICITY.
Tissue: Foreskin fibroblast and Umbilical vein.
[20]"A novel c-fgr exon utilized in Epstein-Barr virus-infected B lymphocytes but not in normal monocytes."
Gutkind S.J., Link D.C., Katamine S., Lacal P., Miki T., Ley T.J., Robbins K.C.
Mol. Cell. Biol. 11:1500-1507(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: PARTIAL NUCLEOTIDE SEQUENCE [MRNA].
[21]"A tyrosine-phosphorylated carboxy-terminal peptide of the fibroblast growth factor receptor (Flg) is a binding site for the SH2 domain of phospholipase C-gamma 1."
Mohammadi M., Honegger A.M., Rotin D., Fischer R., Bellot F., Li W., Dionne C.A., Jaye M., Rubinstein M., Schlessinger J.
Mol. Cell. Biol. 11:5068-5078(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PLCG1.
[22]"Point mutation of an FGF receptor abolishes phosphatidylinositol turnover and Ca2+ flux but not mitogenesis."
Peters K.G., Marie J., Wilson E., Ives H.E., Escobedo J., del Rosario M., Mirda D., Williams L.T.
Nature 358:678-681(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-766, FUNCTION, CATALYTIC ACTIVITY, AUTOPHOSPHORYLATION, INTERACTION WITH PLCG1.
[23]"Point mutation in FGF receptor eliminates phosphatidylinositol hydrolysis without affecting mitogenesis."
Mohammadi M., Dionne C.A., Li W., Lin N., Spivak T., Honegger A.M., Jaye M., Schlessinger J.
Nature 358:681-684(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-766, FUNCTION IN CELL PROLIFERATION.
[24]"Internalization of fibroblast growth factor receptor is inhibited by a point mutation at tyrosine 766."
Sorokin A., Mohammadi M., Huang J., Schlessinger J.
J. Biol. Chem. 269:17056-17061(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF TYR-766, SUBCELLULAR LOCATION.
[25]"Identification of six novel autophosphorylation sites on fibroblast growth factor receptor 1 and elucidation of their importance in receptor activation and signal transduction."
Mohammadi M., Dikic I., Sorokin A., Burgess W.H., Jaye M., Schlessinger J.
Mol. Cell. Biol. 16:977-989(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-463; TYR-583; TYR-585; TYR-653; TYR-654 AND TYR-730, CATALYTIC ACTIVITY, ENZYME REGULATION, FUNCTION IN PHOSPHORYLATION OF PLCG1 AND SHC1; ACTIVATION OF MAP KINASES AND REGULATION OF CELL PROLIFERATION AND DIFFERENTIATION, MUTAGENESIS OF TYR-653 AND TYR-654.
[26]"Receptor specificity of the fibroblast growth factor family."
Ornitz D.M., Xu J., Colvin J.S., McEwen D.G., MacArthur C.A., Coulier F., Gao G., Goldfarb M.
J. Biol. Chem. 271:15292-15297(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF1; FGF2; FGF4; FGF5; FGF6, FUNCTION IN CELL PROLIFERATION.
[27]"Structure of a heparin-linked biologically active dimer of fibroblast growth factor."
DiGabriele A.D., Lax I., Chen D.I., Svahn C.M., Jaye M., Schlessinger J., Hendrickson W.A.
Nature 393:812-817(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF1, PHOSPHORYLATION.
[28]"The t(6;8)(q27;p11) translocation in a stem cell myeloproliferative disorder fuses a novel gene, FOP, to fibroblast growth factor receptor 1."
Popovici C., Zhang B., Gregoire M.-J., Jonveaux P., Lafage-Pochitaloff M., Birnbaum D., Pebusque M.-J.
Blood 93:1381-1389(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP.
[29]"Grb10, a positive, stimulatory signaling adapter in platelet-derived growth factor BB-, insulin-like growth factor I-, and insulin-mediated mitogenesis."
Wang J., Dai H., Yousaf N., Moussaif M., Deng Y., Boufelliga A., Swamy O.R., Leone M.E., Riedel H.
Mol. Cell. Biol. 19:6217-6228(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH GRB10.
[30]"FGFR1 is fused to the centrosome-associated protein CEP110 in the 8p12 stem cell myeloproliferative disorder with t(8;9)(p12;q33)."
Guasch G., Mack G.J., Popovici C., Dastugue N., Birnbaum D., Rattner J.B., Pebusque M.-J.
Blood 95:1788-1796(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH CNTRL.
[31]"Stimulation of phosphatidylinositol 3-kinase by fibroblast growth factor receptors is mediated by coordinated recruitment of multiple docking proteins."
Ong S.H., Hadari Y.R., Gotoh N., Guy G.R., Schlessinger J., Lax I.
Proc. Natl. Acad. Sci. U.S.A. 98:6074-6079(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN PHOSPHORYLATION OF FRS2 AND GAB1 AND IN ACTIVATION OF PIK3R1.
[32]"The Shb adaptor protein binds to tyrosine 766 in the FGFR-1 and regulates the Ras/MEK/MAPK pathway via FRS2 phosphorylation in endothelial cells."
Cross M.J., Lu L., Magnusson P., Nyqvist D., Holmqvist K., Welsh M., Claesson-Welsh L.
Mol. Biol. Cell 13:2881-2893(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF SIGNALING VIA RAS AND MAP KINASES AND CELL PROLIFERATION, FUNCTION IN PHOSPHORYLATION OF FRS2; SHB AND PTPN11/SHP2, INTERACTION WITH SHB AND FGF2, MUTAGENESIS OF TYR-766.
[33]"Identification of a novel gene, FGFR1OP2, fused to FGFR1 in 8p11 myeloproliferative syndrome."
Grand E.K., Grand F.H., Chase A.J., Ross F.M., Corcoran M.M., Oscier D.G., Cross N.C.P.
Genes Chromosomes Cancer 40:78-83(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
[34]"90-kDa ribosomal S6 kinase is a direct target for the nuclear fibroblast growth factor receptor 1 (FGFR1): role in FGFR1 signaling."
Hu Y., Fang X., Dunham S.M., Prada C., Stachowiak E.K., Stachowiak M.K.
J. Biol. Chem. 279:29325-29335(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF RPS6KA1 AND CREB1, CATALYTIC ACTIVITY, INTERACTION WITH RPS6KA1, MUTAGENESIS OF LYS-514, SUBCELLULAR LOCATION.
[35]"Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry."
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J., Smith R.D.
J. Proteome Res. 4:2070-2080(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-296.
Tissue: Plasma.
[36]"Phosphotyrosine profiling identifies the KG-1 cell line as a model for the study of FGFR1 fusions in acute myeloid leukemia."
Gu T.-L., Goss V.L., Reeves C., Popova L., Nardone J., Macneill J., Walters D.K., Wang Y., Rush J., Comb M.J., Druker B.J., Polakiewicz R.D.
Blood 108:4202-4204(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
[37]"Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family."
Zhang X., Ibrahimi O.A., Olsen S.K., Umemori H., Mohammadi M., Ornitz D.M.
J. Biol. Chem. 281:15694-15700(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF1; FGF8; FGF10; FGF19; FGF21; FGF22 AND FGF23, FUNCTION IN STIMULATION OF CELL PROLIFERATION.
[38]"Factors controlling fibroblast growth factor receptor-1's cytoplasmic trafficking and its regulation as revealed by FRAP analysis."
Dunham-Ems S.M., Pudavar H.E., Myers J.M., Maher P.A., Prasad P.N., Stachowiak M.K.
Mol. Biol. Cell 17:2223-2235(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
[39]"Autophosphorylation of FGFR1 kinase is mediated by a sequential and precisely ordered reaction."
Furdui C.M., Lew E.D., Schlessinger J., Anderson K.S.
Mol. Cell 21:711-717(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654; TYR-583 AND TYR-585, IDENTIFICATION BY MASS SPECTROMETRY.
[40]"14-3-3 integrates pro-survival signals mediated by the AKT and MAPK pathways in ZNF198-FGFR1 transformed hematopoietic cells."
Dong S., Kang S., Gu T., Kardar S., Fu H., Lonial S., Khoury H.J., Khuri F., Chen J.
Blood 110:360-369(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: CHROMOSOMAL TRANSLOCATION WITH FGFR1OP2.
[41]"Tissue-specific expression of betaKlotho and fibroblast growth factor (FGF) receptor isoforms determines metabolic activity of FGF19 and FGF21."
Kurosu H., Choi M., Ogawa Y., Dickson A.S., Goetz R., Eliseenkova A.V., Mohammadi M., Rosenblatt K.P., Kliewer S.A., Kuro-o M.
J. Biol. Chem. 282:26687-26695(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF19; FGF21 AND KLB, FUNCTION IN REGULATION OF GLUCOSE UPTAKE IN ADIPOCYTES.
[42]"Fibroblast growth factor receptor-induced phosphorylation of STAT1 at the Golgi apparatus without translocation to the nucleus."
Citores L., Bai L., Sorensen V., Olsnes S.
J. Cell. Physiol. 212:148-156(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN STAT1 PHOSPHORYLATION, GLYCOSYLATION, PHOSPHORYLATION.
[43]"Ubiquitination of fibroblast growth factor receptor 1 is required for its intracellular sorting but not for its endocytosis."
Haugsten E.M., Malecki J., Bjorklund S.M., Olsnes S., Wesche J.
Mol. Biol. Cell 19:3390-3403(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: UBIQUITINATION, CATALYTIC ACTIVITY, FUNCTION AS FGF1 RECEPTOR AND IN ACTIVATION OF PLCG1; FRS2; MAPK1/ERK2 AND MAPK3/ERK1, ENZYME REGULATION, SUBCELLULAR LOCATION.
[44]"Novel mechanisms of fibroblast growth factor receptor 1 regulation by extracellular matrix protein anosmin-1."
Hu Y., Guimond S.E., Travers P., Cadman S., Hohenester E., Turnbull J.E., Kim S.H., Bouloux P.M.
J. Biol. Chem. 284:29905-29920(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH KAL1.
[45]"Fibroblast growth factor receptor-1 (FGFR1) nuclear dynamics reveal a novel mechanism in transcription control."
Dunham-Ems S.M., Lee Y.W., Stachowiak E.K., Pudavar H., Claus P., Prasad P.N., Stachowiak M.K.
Mol. Biol. Cell 20:2401-2412(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CHROMATIN BINDING AND TRANSCRIPTION REGULATION, SUBCELLULAR LOCATION.
[46]"The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations."
Lew E.D., Furdui C.M., Anderson K.S., Schlessinger J.
Sci. Signal. 2:RA6-RA6(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION AS PROTO-ONCOGENE, ACTIVE SITE, MUTAGENESIS OF ASN-546 AND ASP-623, CATALYTIC ACTIVITY, PHOSPHORYLATION AT TYR-463; TYR-653; TYR-654; TYR-583; TYR-585 AND TYR-730, IDENTIFICATION BY MASS SPECTROMETRY, ENZYME REGULATION.
[47]"Isolated C-terminal tail of FGF23 alleviates hypophosphatemia by inhibiting FGF23-FGFR-Klotho complex formation."
Goetz R., Nakada Y., Hu M.C., Kurosu H., Wang L., Nakatani T., Shi M., Eliseenkova A.V., Razzaque M.S., Moe O.W., Kuro-o M., Mohammadi M.
Proc. Natl. Acad. Sci. U.S.A. 107:407-412(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH FGF23 AND KLB.
[48]"Nedd4-1 binds and ubiquitylates activated FGFR1 to control its endocytosis and function."
Persaud A., Alberts P., Hayes M., Guettler S., Clarke I., Sicheri F., Dirks P., Ciruna B., Rotin D.
EMBO J. 30:3259-3273(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN ACTIVATION OF AKT1; PLCG1; MAPK1/ERK2, MAPK3/ERK1 AND MAP KINASE SIGNALING, FUNCTION IN REGULATION OF NEURONAL DIFFERENTIATION AND EMBRYONIC DEVELOPMENT, SUBCELLULAR LOCATION, INTERACTION WITH NEDD4; PLCG1 AND FRS2, UBIQUITINATION, DEGRADATION.
[49]"The structure and function of vertebrate fibroblast growth factor receptor 1."
Groth C., Lardelli M.
Int. J. Dev. Biol. 46:393-400(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON ALTERNATIVE SPLICE FORMS; LIGANDS; SIGNALING PATHWAYS AND SUBCELLULAR LOCATION.
[50]"Cellular signaling by fibroblast growth factor receptors."
Eswarakumar V.P., Lax I., Schlessinger J.
Cytokine Growth Factor Rev. 16:139-149(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION; ROLE IN DISEASE; SIGNALING PATHWAYS; SUBUNIT; DOMAIN STRUCTURE; LIGAND SELECTIVITY AND ENZYME REGULATION.
[51]"Fibroblast growth factor signalling: from development to cancer."
Turner N., Grose R.
Nat. Rev. Cancer 10:116-129(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON FUNCTION IN FGF SIGNALING.
[52]"Novel insights in FGFR1 regulation: lessons from Kallmann syndrome."
Hu Y., Bouloux P.M.
Trends Endocrinol. Metab. 21:385-393(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON SIGNALING AND ROLE IN KALLMAN SYNDROME.
[53]"Structure of the FGF receptor tyrosine kinase domain reveals a novel autoinhibitory mechanism."
Mohammadi M., Schlessinger J., Hubbard S.R.
Cell 86:577-587(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 464-762.
[54]"Structures of the tyrosine kinase domain of fibroblast growth factor receptor in complex with inhibitors."
Mohammadi M., McMahon G., Sun L., Tang C., Hirth P., Yeh B.K., Hubbard S.R., Schlessinger J.
Science 276:955-960(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 464-762 IN COMPLEX WITH SU4984.
[55]"Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity."
Plotnikov A.N., Hubbard S.R., Schlessinger J., Mohammadi M.
Cell 101:413-424(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 141-365 IN COMPLEX WITH FGF1, FUNCTION, DISULFIDE BONDS.
[56]"Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization."
Schlessinger J., Plotnikov A.N., Ibrahimi O.A., Eliseenkova A.V., Yeh B.K., Yayon A., Linhardt R.J., Mohammadi M.
Mol. Cell 6:743-750(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 143-364 IN COMPLEX WITH FGF2 AND HEPARIN, DISULFIDE BONDS.
[57]"Solution structure of the first Ig-like domain of human fibroblast growth factor receptor 1."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 38-124.
[58]"The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site."
Bae J.H., Lew E.D., Yuzawa S., Tome F., Lax I., Schlessinger J.
Cell 138:514-524(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 458-774 IN COMPLEX WITH PLCG1 AND ATP ANALOG, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AUTOPHOSPHORYLATION, PHOSPHORYLATION AT TYR-653; TYR-654 AND TYR-766.
[59]"Asymmetric receptor contact is required for tyrosine autophosphorylation of fibroblast growth factor receptor in living cells."
Bae J.H., Boggon T.J., Tome F., Mandiyan V., Lax I., Schlessinger J.
Proc. Natl. Acad. Sci. U.S.A. 107:2866-2871(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 458-765 OF MUTANT GLU-577, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, MUTAGENESIS OF ARG-577.
[60]"A novel mode of protein kinase inhibition exploiting hydrophobic motifs of autoinhibited kinases: discovery of ATP-independent inhibitors of fibroblast growth factor receptor."
Eathiraj S., Palma R., Hirschi M., Volckova E., Nakuci E., Castro J., Chen C.R., Chan T.C., France D.S., Ashwell M.A.
J. Biol. Chem. 286:20677-20687(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.01 ANGSTROMS) OF 461-765 IN COMPLEX WITH ARQ 069, ENZYME REGULATION.
[61]"A common mutation in the fibroblast growth factor receptor 1 gene in Pfeiffer syndrome."
Muenke M., Schell U., Hehr A., Robin N.H., Losken H.W., Schinzel A., Pulleyn L.J., Rutland P., Reardon W., Malcolm S., Winter R.M.
Nat. Genet. 8:269-274(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT PS ARG-252.
[62]"An unusual FGFR1 mutation (fibroblast growth factor receptor 1 mutation) in a girl with non-syndromic trigonocephaly."
Kress W., Petersen B., Collmann H., Grimm T.
Cytogenet. Cell Genet. 91:138-140(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT TRIGNO1 THR-300.
[63]"Loss-of-function mutations in FGFR1 cause autosomal dominant Kallmann syndrome."
Dode C., Levilliers J., Dupont J.-M., De Paepe A., Le Du N., Soussi-Yanicostas N., Coimbra R.S., Delmaghani S., Compain-Nouaille S., Baverel F., Pecheux C., Le Tessier D., Cruaud C., Delpech M., Speleman F., Vermeulen S., Amalfitano A., Bachelot Y. expand/collapse author list , Bouchard P., Cabrol S., Carel J.-C., Delemarre-van de Waal H., Goulet-Salmon B., Kottler M.-L., Richard O., Sanchez-Franco F., Saura R., Young J., Petit C., Hardelin J.-P.
Nat. Genet. 33:463-465(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 ASP-97; CYS-99; SER-167; TYR-277; MET-607; ARG-666; ARG-719 AND SER-772.
[64]"Clinical assessment and mutation analysis of Kallmann syndrome 1 (KAL1) and fibroblast growth factor receptor 1 (FGFR1, or KAL2) in five families and 18 sporadic patients."
Sato N., Katsumata N., Kagami M., Hasegawa T., Hori N., Kawakita S., Minowada S., Shimotsuka A., Shishiba Y., Yokozawa M., Yasuda T., Nagasaki K., Hasegawa D., Hasegawa Y., Tachibana K., Naiki Y., Horikawa R., Tanaka T., Ogata T.
J. Clin. Endocrinol. Metab. 89:1079-1088(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HH2 SER-745.
[65]"Mutations that cause osteoglophonic dysplasia define novel roles for FGFR1 in bone elongation."
White K.E., Cabral J.M., Davis S.I., Fishburn T., Evans W.E., Ichikawa S., Fields J., Yu X., Shaw N.J., McLellan N.J., McKeown C., FitzPatrick D., Yu K., Ornitz D.M., Econs M.J.
Am. J. Hum. Genet. 76:361-367(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OGD ILE-330; CYS-374 AND ARG-381, CHARACTERIZATION OF VARIANT OGD CYS-374.
[66]"Kallmann syndrome: 14 novel mutations in KAL1 and FGFR1 (KAL2)."
Albuisson J., Pecheux C., Carel J.-C., Lacombe D., Leheup B., Lapuzina P., Bouchard P., Legius E., Matthijs G., Wasniewska M., Delpech M., Young J., Hardelin J.-P., Dode C.
Hum. Mutat. 25:98-99(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 ILE-102; ALA-129; MET-273 AND THR-520.
[67]"Gonadotrophin therapy in Kallmann syndrome caused by heterozygous mutations of the gene for fibroblast growth factor receptor 1: report of three families: case report."
Sato N., Hasegawa T., Hori N., Fukami M., Yoshimura Y., Ogata T.
Hum. Reprod. 20:2173-2178(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 ARG-687 AND SER-745.
[68]"Extended mutational analyses of FGFR1 in osteoglophonic dysplasia."
Farrow E.G., Davis S.I., Mooney S.D., Beighton P., Mascarenhas L., Gutierrez Y.R., Pitukcheewanont P., White K.E.
Am. J. Med. Genet. A 140:537-539(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS OGD ILE-330 AND ARG-381.
[69]"Novel fibroblast growth factor receptor 1 mutations in patients with congenital hypogonadotropic hypogonadism with and without anosmia."
Trarbach E.B., Costa E.M.F., Versiani B., de Castro M., Baptista M.T.M., Garmes H.M., de Mendonca B.B., Latronico A.C.
J. Clin. Endocrinol. Metab. 91:4006-4012(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 SER-48; PRO-245; TRP-250; VAL-343; LEU-366; SER-722 AND ILE-795.
[70]"Mutations in fibroblast growth factor receptor 1 cause Kallmann syndrome with a wide spectrum of reproductive phenotypes."
Pitteloud N., Meysing A., Quinton R., Acierno J.S. Jr., Dwyer A.A., Plummer L., Fliers E., Boepple P., Hayes F., Seminara S., Hughes V.A., Ma J., Bouloux P., Mohammadi M., Crowley W.F. Jr.
Mol. Cell. Endocrinol. 254:60-69(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 CYS-78; ILE-102; HIS-224; ASP-237; GLN-254; MET-273; GLY-274 CYS-339; CYS-346; VAL-538; ARG-703 AND SER-703, VARIANT VAL-769.
[71]"Paediatric phenotype of Kallmann syndrome due to mutations of fibroblast growth factor receptor 1 (FGFR1)."
Zenaty D., Bretones P., Lambe C., Guemas I., David M., Leger J., de Roux N.
Mol. Cell. Endocrinol. 254:78-83(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 SER-178; GLY-622 AND GLN-622.
[72]"Mutations in fibroblast growth factor receptor 1 cause both Kallmann syndrome and normosmic idiopathic hypogonadotropic hypogonadism."
Pitteloud N., Acierno J.S. Jr., Meysing A., Eliseenkova A.V., Ma J., Ibrahimi O.A., Metzger D.L., Hayes F.J., Dwyer A.A., Hughes V.A., Yialamas M., Hall J.E., Grant E., Mohammadi M., Crowley W.F. Jr.
Proc. Natl. Acad. Sci. U.S.A. 103:6281-6286(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 SER-237; HIS-722 AND LYS-724, CHARACTERIZATION OF VARIANTS HH2 SER-237; HIS-722 AND LYS-724.
[73]"Novel FGFR1 sequence variants in Kallmann syndrome, and genetic evidence that the FGFR1c isoform is required in olfactory bulb and palate morphogenesis."
Dode C., Fouveaut C., Mortier G., Janssens S., Bertherat J., Mahoudeau J., Kottler M.-L., Chabrolle C., Gancel A., Francois I., Devriendt K., Wolczynski S., Pugeat M., Pineiro-Garcia A., Murat A., Bouchard P., Young J., Delpech M., Hardelin J.-P.
Hum. Mutat. 28:97-98(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 PHE-101; TRP-250; ASP-270; ARG-283; CYS-332; ARG-621; PHE-685; PHE-693 AND SER-772, VARIANTS LYS-77 AND CYS-822.
[74]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] LEU-125; THR-252 AND LEU-664.
[75]"Impaired fibroblast growth factor receptor 1 signaling as a cause of normosmic idiopathic hypogonadotropic hypogonadism."
Raivio T., Sidis Y., Plummer L., Chen H., Ma J., Mukherjee A., Jacobson-Dickman E., Quinton R., Van Vliet G., Lavoie H., Hughes V.A., Dwyer A., Hayes F.J., Xu S., Sparks S., Kaiser U.B., Mohammadi M., Pitteloud N.
J. Clin. Endocrinol. Metab. 94:4380-4390(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 CYS-99; SER-117; ASP-228; THR-239; GLN-250; LEU-470; ASN-618 AND PRO-671, CHARACTERIZATION OF VARIANTS HH2 CYS-99; SER-117; ASP-228; THR-239; GLN-250; LEU-470; ASN-618 AND PRO-671.
[76]"Heparan sulfate 6-O-sulfotransferase 1, a gene involved in extracellular sugar modifications, is mutated in patients with idiopathic hypogonadotrophic hypogonadism."
Tornberg J., Sykiotis G.P., Keefe K., Plummer L., Hoang X., Hall J.E., Quinton R., Seminara S.B., Hughes V., Van Vliet G., Van Uum S., Crowley W.F., Habuchi H., Kimata K., Pitteloud N., Bulow H.E.
Proc. Natl. Acad. Sci. U.S.A. 108:11524-11529(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HH2 GLN-250.
[77]"SEMA3A, a gene involved in axonal pathfinding, is mutated in patients with Kallmann syndrome."
Hanchate N.K., Giacobini P., Lhuillier P., Parkash J., Espy C., Fouveaut C., Leroy C., Baron S., Campagne C., Vanacker C., Collier F., Cruaud C., Meyer V., Garcia-Pinero A., Dewailly D., Cortet-Rudelli C., Gersak K., Metz C. expand/collapse author list , Chabrier G., Pugeat M., Young J., Hardelin J.P., Prevot V., Dode C.
PLoS Genet. 8:E1002896-E1002896(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANT HH2 ARG-687.
[78]"Mutations in FGF17, IL17RD, DUSP6, SPRY4, and FLRT3 are identified in individuals with congenital hypogonadotropic hypogonadism."
Miraoui H., Dwyer A.A., Sykiotis G.P., Plummer L., Chung W., Feng B., Beenken A., Clarke J., Pers T.H., Dworzynski P., Keefe K., Niedziela M., Raivio T., Crowley W.F. Jr., Seminara S.B., Quinton R., Hughes V.A., Kumanov P. expand/collapse author list , Young J., Yialamas M.A., Hall J.E., Van Vliet G., Chanoine J.P., Rubenstein J., Mohammadi M., Tsai P.S., Sidis Y., Lage K., Pitteloud N.
Am. J. Hum. Genet. 92:725-743(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HH2 SER-117; ASP-228; THR-239; GLN-250; SER-342; ARG-348; LEU-470; THR-483; ASN-618; LYS-670; GLY-692; HIS-722; LYS-724 AND TYR-768.
[79]"FGFR1 mutations cause Hartsfield syndrome, the unique association of holoprosencephaly and ectrodactyly."
Simonis N., Migeotte I., Lambert N., Perazzolo C., de Silva D.C., Dimitrov B., Heinrichs C., Janssens S., Kerr B., Mortier G., Van Vliet G., Lepage P., Casimir G., Abramowicz M., Smits G., Vilain C.
J. Med. Genet. 50:585-592(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS HRTFDS SER-165; SER-191; ARG-490; TYR-623; LYS-628 AND TYR-725.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M37722 mRNA. Translation: AAA75007.1.
X52833 mRNA. Translation: CAA37015.1.
M34185 mRNA. Translation: AAA35836.1.
M34186 mRNA. Translation: AAA35837.1.
M34187 mRNA. Translation: AAA35838.1.
M34188 mRNA. Translation: AAA35839.1.
X51803 mRNA. Translation: CAA36101.1.
M34641 mRNA. Translation: AAA35835.1.
M60485 mRNA. Translation: AAA35840.1.
X57118 mRNA. Translation: CAA40400.1.
X57119 mRNA. Translation: CAA40401.1.
X57120 mRNA. Translation: CAA40402.1.
X57121 mRNA. Translation: CAA40403.1.
X57122 mRNA. Translation: CAA40404.1.
M63887 mRNA. Translation: AAA35958.1.
M63888 mRNA. Translation: AAA35959.1.
M63889 mRNA. Translation: AAA35960.1.
X66945 mRNA. Translation: CAA47375.1.
FJ809917 mRNA. Translation: ACO38646.1.
AK291754 mRNA. Translation: BAF84443.1.
AK292470 mRNA. Translation: BAF85159.1.
AK309947 mRNA. No translation available.
AB208919 mRNA. Translation: BAD92156.1. Different initiation.
AK222718 mRNA. Translation: BAD96438.1.
AY585209 Genomic DNA. Translation: AAS79322.1.
AC087623 Genomic DNA. No translation available.
BC015035 mRNA. Translation: AAH15035.1.
BC018128 mRNA. Translation: AAH18128.1.
BC091494 mRNA. Translation: AAH91494.1.
Y00665 mRNA. Translation: CAA68679.1.
CCDSCCDS43730.1. [P11362-3]
CCDS43731.1. [P11362-14]
CCDS43732.1. [P11362-7]
CCDS55221.1. [P11362-20]
CCDS55222.1. [P11362-2]
CCDS55223.1. [P11362-21]
CCDS6107.2. [P11362-1]
PIRA41266.
C36464.
C40862.
TVHUFG. S11692.
A40862. S19167.
RefSeqNP_001167534.1. NM_001174063.1. [P11362-2]
NP_001167535.1. NM_001174064.1. [P11362-20]
NP_001167536.1. NM_001174065.1. [P11362-7]
NP_001167537.1. NM_001174066.1. [P11362-3]
NP_001167538.1. NM_001174067.1. [P11362-21]
NP_056934.2. NM_015850.3. [P11362-7]
NP_075593.1. NM_023105.2. [P11362-3]
NP_075594.1. NM_023106.2. [P11362-14]
NP_075598.2. NM_023110.2. [P11362-1]
UniGeneHs.264887.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1AGWX-ray2.40A/B456-765[»]
1CVSX-ray2.80C/D141-365[»]
1EVTX-ray2.80C/D141-365[»]
1FGIX-ray2.50A/B456-765[»]
1FGKX-ray2.00A/B456-765[»]
1FQ9X-ray3.00C/D141-365[»]
1XR0NMR-A409-430[»]
2CR3NMR-A38-123[»]
2FGIX-ray2.50A/B456-765[»]
3C4FX-ray2.07A/B464-765[»]
3DPKX-ray1.95A577-615[»]
3GQIX-ray2.50A458-774[»]
3GQLX-ray2.80A/B/C458-774[»]
3JS2X-ray2.20A/B458-765[»]
3KRJX-ray2.10A577-597[»]
3KRLX-ray2.40A577-597[»]
3KXXX-ray3.20A/B/C/D458-765[»]
3KY2X-ray2.70A/B458-765[»]
3OJVX-ray2.60C/D142-365[»]
3RHXX-ray2.01A/B461-765[»]
3TT0X-ray2.80A/B456-765[»]
4F63X-ray2.55A/B458-765[»]
4F64X-ray2.05A/B458-765[»]
4F65X-ray2.26A/B458-765[»]
4NK9X-ray2.57A/B458-765[»]
4NKAX-ray2.19A/B458-765[»]
4NKSX-ray2.50A/B458-765[»]
ProteinModelPortalP11362.
SMRP11362. Positions 38-385, 420-801.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108551. 29 interactions.
DIPDIP-4019N.
IntActP11362. 21 interactions.
MINTMINT-1499363.

Chemistry

BindingDBP11362.
ChEMBLCHEMBL2095217.
DrugBankDB00039. Palifermin.
GuidetoPHARMACOLOGY1808.

PTM databases

PhosphoSiteP11362.

Polymorphism databases

DMDM120046.

Proteomic databases

MaxQBP11362.
PaxDbP11362.
PRIDEP11362.

Protocols and materials databases

DNASU2260.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000326324; ENSP00000327229; ENSG00000077782. [P11362-14]
ENST00000335922; ENSP00000337247; ENSG00000077782. [P11362-20]
ENST00000356207; ENSP00000348537; ENSG00000077782. [P11362-3]
ENST00000397091; ENSP00000380280; ENSG00000077782. [P11362-7]
ENST00000397108; ENSP00000380297; ENSG00000077782. [P11362-7]
ENST00000397113; ENSP00000380302; ENSG00000077782. [P11362-7]
ENST00000425967; ENSP00000393312; ENSG00000077782. [P11362-21]
ENST00000447712; ENSP00000400162; ENSG00000077782. [P11362-1]
ENST00000484370; ENSP00000433163; ENSG00000077782. [P11362-15]
ENST00000532791; ENSP00000432972; ENSG00000077782. [P11362-2]
GeneID2260.
KEGGhsa:2260.
UCSCuc003xlp.3. human. [P11362-2]
uc003xlu.3. human. [P11362-18]
uc003xlv.3. human. [P11362-16]
uc010lwk.3. human. [P11362-20]
uc011lbu.2. human. [P11362-21]
uc011lbv.2. human. [P11362-7]
uc011lbw.2. human. [P11362-3]
uc022aua.1. human. [P11362-1]
uc022aud.1. human. [P11362-14]

Organism-specific databases

CTD2260.
GeneCardsGC08M038268.
GeneReviewsFGFR1.
HGNCHGNC:3688. FGFR1.
HPACAB033614.
HPA056402.
MIM101600. phenotype.
136350. gene.
147950. phenotype.
166250. phenotype.
190440. phenotype.
615465. phenotype.
neXtProtNX_P11362.
Orphanet251579. Giant cell glioblastoma.
251576. Gliosarcoma.
2117. Hartsfield-Bixler-Demyer syndrome.
2227. Hypodontia.
3366. Isolated trigonocephaly.
478. Kallmann syndrome.
168953. Myeloid neoplasm associated with FGFR1 rearrangement.
432. Normosmic congenital hypogonadotropic hypogonadism.
99798. Oligodontia.
2645. Osteoglophonic dwarfism.
93258. Pfeiffer syndrome type 1.
251612. Pilocytic astrocytoma.
3157. Septo-optic dysplasia.
PharmGKBPA28127.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0515.
HOGENOMHOG000263410.
HOVERGENHBG000345.
InParanoidP11362.
KOK04362.
OMAIVYKMKS.
OrthoDBEOG7NGQ9N.
PhylomeDBP11362.
TreeFamTF316307.

Enzyme and pathway databases

BRENDA2.7.10.1. 2681.
ReactomeREACT_111045. Developmental Biology.
REACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_6900. Immune System.
SignaLinkP11362.

Gene expression databases

ArrayExpressP11362.
BgeeP11362.
CleanExHS_FGFR1.
HS_FLG.
GenevestigatorP11362.

Family and domain databases

Gene3D2.60.40.10. 3 hits.
InterProIPR028174. FGF_rcpt_1/4.
IPR016248. FGF_rcpt_fam.
IPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003598. Ig_sub2.
IPR011009. Kinase-like_dom.
IPR000719. Prot_kinase_dom.
IPR017441. Protein_kinase_ATP_BS.
IPR001245. Ser-Thr/Tyr_kinase_cat_dom.
IPR008266. Tyr_kinase_AS.
IPR020635. Tyr_kinase_cat_dom.
[Graphical view]
PANTHERPTHR24416:SF131. PTHR24416:SF131. 1 hit.
PfamPF07679. I-set. 3 hits.
PF07714. Pkinase_Tyr. 1 hit.
[Graphical view]
PIRSFPIRSF000628. FGFR. 1 hit.
PRINTSPR00109. TYRKINASE.
SMARTSM00408. IGc2. 3 hits.
SM00219. TyrKc. 1 hit.
[Graphical view]
SUPFAMSSF56112. SSF56112. 1 hit.
PROSITEPS50835. IG_LIKE. 3 hits.
PS00107. PROTEIN_KINASE_ATP. 1 hit.
PS50011. PROTEIN_KINASE_DOM. 1 hit.
PS00109. PROTEIN_KINASE_TYR. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSFGFR1. human.
EvolutionaryTraceP11362.
GeneWikiFibroblast_growth_factor_receptor_1.
GenomeRNAi2260.
NextBio9163.
PMAP-CutDBP11362.
PROP11362.
SOURCESearch...

Entry information

Entry nameFGFR1_HUMAN
AccessionPrimary (citable) accession number: P11362
Secondary accession number(s): A8K6T9 expand/collapse secondary AC list , A8K8V5, C1KBH8, P17049, Q02063, Q02065, Q14306, Q14307, Q53H63, Q59H40, Q5BJG2, Q8N685, Q9UD50, Q9UDF0, Q9UDF1, Q9UDF2
Entry history
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: May 1, 1991
Last modified: July 9, 2014
This is version 199 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Human and mouse protein kinases

Human and mouse protein kinases: classification and index

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries