Type |
Details |
Score |
Publication |
First Author: |
Zhang Y |
Year: |
1999 |
Journal: |
Gene |
Title: |
Genomic organization of the human fibroblast growth factor receptor 2 (FGFR2) gene and comparative analysis of the human FGFR gene family. |
Volume: |
230 |
Issue: |
1 |
Pages: |
69-79 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
724
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
535
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
1319
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
309
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Reilly JF |
Year: |
2000 |
Journal: |
J Biol Chem |
Title: |
Association of fibroblast growth factor receptor 1 with the adaptor protein Grb14. Characterization of a new receptor binding partner. |
Volume: |
275 |
Issue: |
11 |
Pages: |
7771-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ong SH |
Year: |
2000 |
Journal: |
Mol Cell Biol |
Title: |
FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. |
Volume: |
20 |
Issue: |
3 |
Pages: |
979-89 |
|
•
•
•
•
•
|
Publication |
First Author: |
Karlsson T |
Year: |
1995 |
Journal: |
Oncogene |
Title: |
Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins. |
Volume: |
10 |
Issue: |
8 |
Pages: |
1475-83 |
|
•
•
•
•
•
|
Publication |
First Author: |
Schlessinger J |
Year: |
2000 |
Journal: |
Mol Cell |
Title: |
Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. |
Volume: |
6 |
Issue: |
3 |
Pages: |
743-50 |
|
•
•
•
•
•
|
Publication |
First Author: |
Li C |
Year: |
2005 |
Journal: |
Development |
Title: |
FGFR1 function at the earliest stages of mouse limb development plays an indispensable role in subsequent autopod morphogenesis. |
Volume: |
132 |
Issue: |
21 |
Pages: |
4755-64 |
|
•
•
•
•
•
|
Publication |
First Author: |
Itoh N |
Year: |
1990 |
Journal: |
Biochem Biophys Res Commun |
Title: |
The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA. |
Volume: |
169 |
Issue: |
2 |
Pages: |
680-5 |
|
•
•
•
•
•
|
Publication |
First Author: |
Riley BM |
Year: |
2007 |
Journal: |
Proc Natl Acad Sci U S A |
Title: |
Impaired FGF signaling contributes to cleft lip and palate. |
Volume: |
104 |
Issue: |
11 |
Pages: |
4512-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Dixon MJ |
Year: |
2011 |
Journal: |
Nat Rev Genet |
Title: |
Cleft lip and palate: understanding genetic and environmental influences. |
Volume: |
12 |
Issue: |
3 |
Pages: |
167-78 |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Domain |
Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].The FGFRs consist of an extracellular ligand-binding domain composed of three immunoglobulin-like domains (D1-D3), a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity []. The three immunoglobin(Ig)-like domains, D1, D2, and D3, present a stretch of acidic amino acids (known as the acid box) between D1 and D2. This acid box can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. FGFR family members differ from one another in their ligandaffinities and tissue distribution [, ]. Most FGFs can bind to several different FGFR subtypes. Indeed, FGF1 is sometimes referred to as the universal ligand, as it is capable of activating all of the different FGFRs []. However, there are some exceptions. For example, FGF7 only interacts with FGFR2 []and FGF18 was recently shown to only activate FGFR3 []. Fibroblast growth factor receptor 1 (FGFR1) binds both acidic and basic fibroblast growth factors and is involved in limb induction []. FGFR1 has been shown to be associated with Pfeiffer syndrome [], and cleft lip and/or palate [, ]. Fibroblast growth factor receptor 1 has been shown to interact with growth factor receptor-bound protein 14 (GRB14) [], Src homology 2 domain containing adaptor protein B (SHB) [], fibroblast growth factor receptor substrate 2 (FRS2)[]and fibroblast growth factor 1 (FGF1) [, ].This entry represents the catalytic domain of FGFR1. |
|
•
•
•
•
•
|
Protein Domain |
Type: |
Family |
Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].The FGFRs consist of an extracellular ligand-binding domain composed of three immunoglobulin-like domains (D1-D3), a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity []. The three immunoglobin(Ig)-like domains, D1, D2, and D3, present a stretch of acidic amino acids (known as the acid box) between D1 and D2. This acid box can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. FGFR family members differ from one another in their ligand affinities and tissue distribution [, ]. Most FGFs can bind to several different FGFR subtypes. Indeed, FGF1 is sometimes referred to as the universal ligand, as it is capable of activating all of the different FGFRs []. However, there are some exceptions. For example, FGF7 only interacts with FGFR2 []and FGF18 was recently shown to only activate FGFR3 []. This entry represents the fibroblast growth factor receptor family. |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
331
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
346
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Duchesne L |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate co-receptor binding. |
Volume: |
281 |
Issue: |
37 |
Pages: |
27178-89 |
|
•
•
•
•
•
|
Publication |
First Author: |
Hughes SE |
Year: |
1997 |
Journal: |
J Histochem Cytochem |
Title: |
Differential expression of the fibroblast growth factor receptor (FGFR) multigene family in normal human adult tissues. |
Volume: |
45 |
Issue: |
7 |
Pages: |
1005-19 |
|
•
•
•
•
•
|
Publication |
First Author: |
Cotton LM |
Year: |
2008 |
Journal: |
Endocr Rev |
Title: |
Cellular signaling by fibroblast growth factors (FGFs) and their receptors (FGFRs) in male reproduction. |
Volume: |
29 |
Issue: |
2 |
Pages: |
193-216 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
589
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
358
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
380
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
309
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
|
|
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
109
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
154
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
112
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
512
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
264
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
105
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
208
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
195
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
153
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Skjerpen CS |
Year: |
2002 |
Journal: |
EMBO J |
Title: |
Binding of FGF-1 variants to protein kinase CK2 correlates with mitogenicity. |
Volume: |
21 |
Issue: |
15 |
Pages: |
4058-69 |
|
•
•
•
•
•
|
Publication |
First Author: |
Chellaiah A |
Year: |
1999 |
Journal: |
J Biol Chem |
Title: |
Mapping ligand binding domains in chimeric fibroblast growth factor receptor molecules. Multiple regions determine ligand binding specificity. |
Volume: |
274 |
Issue: |
49 |
Pages: |
34785-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Davidson D |
Year: |
2005 |
Journal: |
J Biol Chem |
Title: |
Fibroblast growth factor (FGF) 18 signals through FGF receptor 3 to promote chondrogenesis. |
Volume: |
280 |
Issue: |
21 |
Pages: |
20509-15 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ornitz DM |
Year: |
1996 |
Journal: |
J Biol Chem |
Title: |
Receptor specificity of the fibroblast growth factor family. |
Volume: |
271 |
Issue: |
25 |
Pages: |
15292-7 |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
680
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
717
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
194
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
260
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
592
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
659
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
681
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
194
|
Fragment?: |
false |
|
•
•
•
•
•
|
Publication |
First Author: |
Zhang X |
Year: |
2006 |
Journal: |
J Biol Chem |
Title: |
Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family. |
Volume: |
281 |
Issue: |
23 |
Pages: |
15694-700 |
|
•
•
•
•
•
|
Publication |
First Author: |
Burgess WH |
Year: |
1989 |
Journal: |
Annu Rev Biochem |
Title: |
The heparin-binding (fibroblast) growth factor family of proteins. |
Volume: |
58 |
|
Pages: |
575-606 |
|
•
•
•
•
•
|
Publication |
First Author: |
Wilkie AO |
Year: |
1995 |
Journal: |
Curr Biol |
Title: |
Functions of fibroblast growth factors and their receptors. |
Volume: |
5 |
Issue: |
5 |
Pages: |
500-7 |
|
•
•
•
•
•
|
Publication |
First Author: |
Thomas KA |
Year: |
1988 |
Journal: |
Trends Biochem Sci |
Title: |
Transforming potential of fibroblast growth factor genes. |
Volume: |
13 |
Issue: |
9 |
Pages: |
327-8 |
|
•
•
•
•
•
|
Publication |
First Author: |
Ornitz DM |
Year: |
2001 |
Journal: |
Genome Biol |
Title: |
Fibroblast growth factors. |
Volume: |
2 |
Issue: |
3 |
Pages: |
REVIEWS3005 |
|
•
•
•
•
•
|
Publication |
First Author: |
Plotnikov AN |
Year: |
2000 |
Journal: |
Cell |
Title: |
Crystal structures of two FGF-FGFR complexes reveal the determinants of ligand-receptor specificity. |
Volume: |
101 |
Issue: |
4 |
Pages: |
413-24 |
|
•
•
•
•
•
|
Publication |
First Author: |
Blaber M |
Year: |
1996 |
Journal: |
Biochemistry |
Title: |
X-ray crystal structure of human acidic fibroblast growth factor. |
Volume: |
35 |
Issue: |
7 |
Pages: |
2086-94 |
|
•
•
•
•
•
|
Publication |
First Author: |
Vlodavsky I |
Year: |
1990 |
Journal: |
Cancer Metastasis Rev |
Title: |
Extracellular matrix-resident growth factors and enzymes: possible involvement in tumor metastasis and angiogenesis. |
Volume: |
9 |
Issue: |
3 |
Pages: |
203-26 |
|
•
•
•
•
•
|
Publication |
First Author: |
Green PJ |
Year: |
1996 |
Journal: |
Bioessays |
Title: |
Promiscuity of fibroblast growth factor receptors. |
Volume: |
18 |
Issue: |
8 |
Pages: |
639-46 |
|
•
•
•
•
•
|
Publication |
First Author: |
Yardley N |
Year: |
2012 |
Journal: |
Dev Biol |
Title: |
FGF signaling transforms non-neural ectoderm into neural crest. |
Volume: |
372 |
Issue: |
2 |
Pages: |
166-77 |
|
•
•
•
•
•
|
Publication |
First Author: |
Böttcher RT |
Year: |
2005 |
Journal: |
Endocr Rev |
Title: |
Fibroblast growth factor signaling during early vertebrate development. |
Volume: |
26 |
Issue: |
1 |
Pages: |
63-77 |
|
•
•
•
•
•
|
Publication |
First Author: |
Koga C |
Year: |
1999 |
Journal: |
Biochem Biophys Res Commun |
Title: |
Characterization of a novel member of the FGF family, XFGF-20, in Xenopus laevis. |
Volume: |
261 |
Issue: |
3 |
Pages: |
756-65 |
|
•
•
•
•
•
|
Publication |
First Author: |
Nakamizo S |
Year: |
2013 |
Journal: |
Skin Pharmacol Physiol |
Title: |
Topical treatment with basic fibroblast growth factor promotes wound healing and barrier recovery induced by skin abrasion. |
Volume: |
26 |
Issue: |
1 |
Pages: |
22-9 |
|
•
•
•
•
•
|
Publication |
First Author: |
Kumar SB |
Year: |
2013 |
Journal: |
Curr Pharm Des |
Title: |
Fibroblast growth factor receptor inhibitors. |
Volume: |
19 |
Issue: |
4 |
Pages: |
687-701 |
|
•
•
•
•
•
|
Publication |
First Author: |
Amaya E |
Year: |
1991 |
Journal: |
Cell |
Title: |
Expression of a dominant negative mutant of the FGF receptor disrupts mesoderm formation in Xenopus embryos. |
Volume: |
66 |
Issue: |
2 |
Pages: |
257-70 |
|
•
•
•
•
•
|
Publication |
First Author: |
Borland CZ |
Year: |
2001 |
Journal: |
Bioessays |
Title: |
Fibroblast growth factor signaling in Caenorhabditis elegans. |
Volume: |
23 |
Issue: |
12 |
Pages: |
1120-30 |
|
•
•
•
•
•
|
Publication |
First Author: |
Coumoul X |
Year: |
2003 |
Journal: |
Birth Defects Res C Embryo Today |
Title: |
Roles of FGF receptors in mammalian development and congenital diseases. |
Volume: |
69 |
Issue: |
4 |
Pages: |
286-304 |
|
•
•
•
•
•
|
Publication |
First Author: |
Sutherland D |
Year: |
1996 |
Journal: |
Cell |
Title: |
branchless encodes a Drosophila FGF homolog that controls tracheal cell migration and the pattern of branching. |
Volume: |
87 |
Issue: |
6 |
Pages: |
1091-101 |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein Coding Gene |
Type: |
protein_coding_gene |
Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
128
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
734
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
156
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
305
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
386
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
822
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
833
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
822
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
820
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
801
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
799
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
704
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
821
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
782
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
802
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
800
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
707
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
819
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
822
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
820
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
695
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
813
|
Fragment?: |
false |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
724
|
Fragment?: |
true |
|
•
•
•
•
•
|
Protein |
Organism: |
Mus musculus/domesticus |
Length: |
762
|
Fragment?: |
true |
|
•
•
•
•
•
|