| Type |
Details |
Score |
| Publication |
| First Author: |
Bagai S |
| Year: |
2002 |
| Journal: |
J Biol Chem |
| Title: |
Fibroblast growth factor-10 is a mitogen for urothelial cells. |
| Volume: |
277 |
| Issue: |
26 |
| Pages: |
23828-37 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Min H |
| Year: |
1998 |
| Journal: |
Genes Dev |
| Title: |
Fgf-10 is required for both limb and lung development and exhibits striking functional similarity to Drosophila branchless. |
| Volume: |
12 |
| Issue: |
20 |
| Pages: |
3156-61 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sekine K |
| Year: |
1999 |
| Journal: |
Nat Genet |
| Title: |
Fgf10 is essential for limb and lung formation. |
| Volume: |
21 |
| Issue: |
1 |
| Pages: |
138-41 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jimenez PA |
| Year: |
1999 |
| Journal: |
J Surg Res |
| Title: |
Keratinocyte growth factor-2 accelerates wound healing in incisional wounds. |
| Volume: |
81 |
| Issue: |
2 |
| Pages: |
238-42 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Liu Y |
| Year: |
1997 |
| Journal: |
Cytogenet Cell Genet |
| Title: |
Assignment of FGF12, the human FGF homologous factor 1 gene, to chromosome 3q29-->3qter by fluorescence in situ hybridization. |
| Volume: |
78 |
| Issue: |
1 |
| Pages: |
48-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Leung KH |
| Year: |
1998 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Functional effects of FGF-13 on human lung fibroblasts, dermal microvascular endothelial cells, and aortic smooth muscle cells. |
| Volume: |
250 |
| Issue: |
1 |
| Pages: |
137-42 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wittmack EK |
| Year: |
2004 |
| Journal: |
J Neurosci |
| Title: |
Fibroblast growth factor homologous factor 2B: association with Nav1.6 and selective colocalization at nodes of Ranvier of dorsal root axons. |
| Volume: |
24 |
| Issue: |
30 |
| Pages: |
6765-75 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Gecz J |
| Year: |
1999 |
| Journal: |
Hum Genet |
| Title: |
Fibroblast growth factor homologous factor 2 (FHF2): gene structure, expression and mapping to the Börjeson-Forssman-Lehmann syndrome region in Xq26 delineated by a duplication breakpoint in a BFLS-like patient. |
| Volume: |
104 |
| Issue: |
1 |
| Pages: |
56-63 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Wang Q |
| Year: |
2000 |
| Journal: |
Mech Dev |
| Title: |
Subcellular and developmental expression of alternatively spliced forms of fibroblast growth factor 14. |
| Volume: |
90 |
| Issue: |
2 |
| Pages: |
283-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
van Swieten JC |
| Year: |
2003 |
| Journal: |
Am J Hum Genet |
| Title: |
A mutation in the fibroblast growth factor 14 gene is associated with autosomal dominant cerebellar ataxia [corrected]. |
| Volume: |
72 |
| Issue: |
1 |
| Pages: |
191-9 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Goldfarb M |
| Year: |
2007 |
| Journal: |
Neuron |
| Title: |
Fibroblast growth factor homologous factors control neuronal excitability through modulation of voltage-gated sodium channels. |
| Volume: |
55 |
| Issue: |
3 |
| Pages: |
449-63 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Greene JM |
| Year: |
1998 |
| Journal: |
Eur J Neurosci |
| Title: |
Identification and characterization of a novel member of the fibroblast growth factor family. |
| Volume: |
10 |
| Issue: |
5 |
| Pages: |
1911-25 |
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•
•
•
•
•
|
| Publication |
| First Author: |
Xu J |
| Year: |
1999 |
| Journal: |
Mech Dev |
| Title: |
Genomic structure, mapping, activity and expression of fibroblast growth factor 17. |
| Volume: |
83 |
| Issue: |
1-2 |
| Pages: |
165-78 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kirikoshi H |
| Year: |
2000 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
Molecular cloning and characterization of human FGF-20 on chromosome 8p21.3-p22. |
| Volume: |
274 |
| Issue: |
2 |
| Pages: |
337-43 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ohmachi S |
| Year: |
2000 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
FGF-20, a novel neurotrophic factor, preferentially expressed in the substantia nigra pars compacta of rat brain. |
| Volume: |
277 |
| Issue: |
2 |
| Pages: |
355-60 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jeffers M |
| Year: |
2001 |
| Journal: |
Cancer Res |
| Title: |
Identification of a novel human fibroblast growth factor and characterization of its role in oncogenesis. |
| Volume: |
61 |
| Issue: |
7 |
| Pages: |
3131-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Umemori H |
| Year: |
2004 |
| Journal: |
Cell |
| Title: |
FGF22 and its close relatives are presynaptic organizing molecules in the mammalian brain. |
| Volume: |
118 |
| Issue: |
2 |
| Pages: |
257-70 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Quarles LD |
| Year: |
2012 |
| Journal: |
Nat Rev Endocrinol |
| Title: |
Skeletal secretion of FGF-23 regulates phosphate and vitamin D metabolism. |
| Volume: |
8 |
| Issue: |
5 |
| Pages: |
276-86 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jüppner H |
| Year: |
2011 |
| Journal: |
Kidney Int Suppl |
| Title: |
Phosphate and FGF-23. |
|
| Issue: |
121 |
| Pages: |
S24-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fukumoto S |
| Year: |
2008 |
| Journal: |
Intern Med |
| Title: |
Physiological regulation and disorders of phosphate metabolism--pivotal role of fibroblast growth factor 23. |
| Volume: |
47 |
| Issue: |
5 |
| Pages: |
337-43 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Bowe AE |
| Year: |
2001 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
FGF-23 inhibits renal tubular phosphate transport and is a PHEX substrate. |
| Volume: |
284 |
| Issue: |
4 |
| Pages: |
977-81 |
|
•
•
•
•
•
|
| 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 [].This entry represents fibroblast growth factor 22 (FGF22), which plays a role in the fasting response, glucose homeostasis, lipolysis and lipogenesis, and has been shown to stimulate cell proliferation in vitro [, ]. FGF22 is expressed in skin, with low expression found in brain. In mouse FGF22 is preferentially expressed in the inner root sheath of the hair follicle, which suggests a role in hair development []. |
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•
•
•
•
|
| 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 [].This entry represents fibroblast growth factor 21 (FGF21), which stimulates glucose uptake in differentiated adipocytes via the induction of glucose transporter SLC2A1/GLUT1 expression []. FGF21 has been shown to protect animals from diet-induced obesity when overexpressed in transgenic mice. It also lowers blood glucose and triglyceride levels when administered to diabetic rodents [], suggesting it may exhibit the therapeutic characteristics necessary for effective treatment of diabetes. Treatment of animals with FGF21 results in increased energy expenditure, fat utilisation and lipid excretion []. FGF21 is most abundantly expressed in the liver, and also expressed in the thymus at lower levels []. |
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•
•
•
•
•
|
| 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 [].This entry represents fibroblast growth factor 17 (FGF17). The protein plays an important role in the regulation of embryonic development and in the induction and patterning of the embryonic brain. It is required for normal brain development []. In mouse, FGF17 is localised to specific sites in the brain, the developing skeleton and developing arteries, which suggests a role in central nervous system, bone and vascular growth [, , ]. |
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•
•
•
•
•
|
| 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, andirregularities 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 [].This entry represents fibroblast growth factor 14 (FGF14), also known as fibroblast growth factor homologous factor 4. In mouse, FGF14 is widely expressed in the brain, spinal cord, major arteries and thymus []. The protein is involved in neuronal development and function. FGF14-deficient mice suffer from severe ataxia and other neurological deficits []. Defects in the human FGF14 gene cause Spinocerebellar ataxia, characterised by ataxia with tremor, orofacial dyskinesia, psychiatric symptoms and cognitive deficits []. |
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•
•
•
•
•
|
| 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 [].This entry represents fibroblast growth factor 20 (FGF20). It is involved in embryonic development, cell growth, morphogenesis, tissue repair, and tumour growth and invasion [, , ]. FGF20 is expressed in normal brain, particularly the cerebellum [], and has been shown to enhance the survival of midbrain dopaminergic neurons in vitro []. |
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•
•
•
•
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| 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 [].This entry represents fibroblast growth factor 13 (FGF13), also known as fibroblast growth factor homologous factor 2. It is thought to be involved in nervous system development and function []. FGF13 has been shown to induce cell growth of lung fibroblasts and aortic smooth muscle cells, but has no effect on dermal vascular endothelial cells []. It also is thought to regulate voltage-gated sodium channels transport and function, and play a role in MAPK signaling []. The localisation and tissue-specific expression pattern of FGF13 has made it a possible candidate for familial cases of Borjeson-Forssman-Lehmann syndrome (BFLS) and other syndromal and nonspecific forms of X-linked mental retardation []. |
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•
•
•
•
•
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| 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 [].This entry represents fibroblast growth factor 23 (FGF23), which is secreted by osteoblasts and osteoclasts []. FGF23 acts on kidneys, where it decreases the expression of NPT2, a sodium-phosphate cotransporter in the proximal tubule []. FGF23 is responsible for phosphate metabolism, decreasing the reabsorption and increasing excretion of phosphate []. FGF23 is involved in the pathogenesis of three hypophosphatemic disorders; oncogenic osteomalacia (OOM), X-linked hypophosphatemia (XLH) and autosomal dominant hypophosphatemic rickets (ADHR). These conditions are characterised by hypophosphatemia, decreased renal phosphate reabsorption, normal or low serum calcitriol concentrations and defective skeletal mineralisation [, , ]. |
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•
•
•
•
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| 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 [].This entry represents fibroblast growth factor 1 (FGF1), also known as heparin-binding growth factor 1 and acidic fibroblast growth factor. The protein functions as a modifier of endothelial cell migration and proliferation, as well as an angiogenic factor. It acts as a mitogen for a variety of mesoderm- and neuroectoderm-derived cells in vitro, and is therefore thought to be involved in organogenesis [, , ]. In addition to interacting with FGFR1-4, FGF1 has also been shown to interact with casein kinase II subunits [], heat shock proteins []and acidic fibroblast growth factor intracellular-binding protein []. |
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•
•
•
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| 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 [].This entry represents fibroblast growth factor 10 (FGF10), also known as keratinocyte growth factor 2. This protein plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. FGF10 exhibits mitogenic activity for keratinizing epidermal cells, but essentially no activity for fibroblasts, which is similar to the biological activity of FGF7 []. Studies suggest FGF10 is required for embryonic epidermal morphogenesis including brain development, lung morphogenesis, and initiation of limb bud formation [, , ]. FGF10 is also implicated as a primary factor in the process of wound healing [, ]. FGF10 interacts with FGFR1, but has a higher affinity FGFR2 [, ]. |
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•
•
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| 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 [].This entry represents fibroblast growth factor 12 (FGF12), also known as fibroblast growth factor homologous factor 1. It lacks the N-terminal signal sequence present in most of the FGF family members, but it contains clusters of basic residues that have been demonstrated to act as a nuclear localisation signal. When transfected into mammalian cells, it accumulates in the nucleus, but is not secreted []. Although it currently has no known function, it is thought to be involved in nervous system development and function [, ]. |
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•
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| 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 [].This entry represents fibroblast growth factor 9 (FGF9), also known as glia-activating factor and heparin-binding growth factor 9. This protein plays an important role in the regulation of embryonic development, cell proliferation, cell differentiation and cell migration. It is involved in cyclic proliferation of uterine endometrial stroma []and can act as both a paracrine mitogen for epithelial cells and an autocrine mitogen for stromal cells []. FGF9 has also been shown to play a vital role in male development, as it is needed to carry out important masculinising developmental functions, such testicular embryogenesis [, ]. FGF9 Interacts with FGFR1, FGFR2, FGFR3 and FGFR4, but has highest affinity for FGFR3 [, ]. |
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•
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| 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 [].This entry represents fibroblast growth factor 5 (FGF5). This protein plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle, as it functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen, the apoptosis-induced regression phase [, ]. FGF5 has a high affinity for FGFR1 and FGFR2 []. |
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| 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 [].This entry represents fibroblast growth factor 7 (FGF7), also known as keratinocyte growth factor (KGF). This protein plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation. It is a potent epithelial cell-specific growth factor, whose mitogenic activity is predominantly exhibited in keratinocytes, but not in fibroblasts and endothelial cells []. Studies of mouse and rat have implicated FGF7 in morphogenesis of epithelium, wound repair, hair development and early lung organogenesis [, , , ]. FGF7 has a high affinity for FGFR2 and has also been shown to interact with various collagens []and heparan sulfate proteoglycan 2 (perlecan) []. |
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•
•
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| 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 [].This entry represents fibroblast growth factor 3 (FGF3), also known as heparin-binding growth factor 3 and INT-2 proto-oncogene protein. The protein plays an important role in the regulation of embryonic development, cell proliferation and differentiation, and is required for normal ear development [, ]. FGF3 has a high affinity for FGFR3 and FGFR2, but a low affinity for FGFR1 []. |
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•
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•
•
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| 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 [].This entry represents fibroblast growth factor 4 (FGF4), also known as heparin secretory transforming protein 1. This protein plays an important role in the regulation of embryonic development, cell proliferation and differentiation []. Studies on the mouse protein suggest a function in bone morphogenesis and limb development through the sonic hedgehog (SHH) signaling pathway [, ]. |
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•
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| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuousgrowth 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 [].This entry represents fibroblast growth factor 2 (FGF2), also known as heparin-binding growth factor 2 and basic fibroblast growth factor. The protein plays an important role in the regulation of cell survival, cell division, angiogenesis, cell differentiation and cell migration and is a potent mitogen in vitro [, ]. FGF2 has a high affinity for FGFR1, FGFR2 and FGFR4, but a very low affinity with FGFR3 [, , , ]. FGF2 has also been shown to interact with casein kinase II subunit alpha []and some ribosomal proteins [, ]. |
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|
| Publication |
| First Author: |
Smallwood PM |
| Year: |
1996 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Fibroblast growth factor (FGF) homologous factors: new members of the FGF family implicated in nervous system development. |
| Volume: |
93 |
| Issue: |
18 |
| Pages: |
9850-7 |
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•
•
•
•
|
| 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: |
244
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
161
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
215
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
140
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
233
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
191
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
203
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| 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 |
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•
•
•
•
|
| 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 |
|
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•
•
•
•
|
| 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 |
|
•
•
•
•
•
|
| 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 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
210
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
210
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| 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: |
Potthoff MJ |
| Year: |
2012 |
| Journal: |
Genes Dev |
| Title: |
Endocrine fibroblast growth factors 15/19 and 21: from feast to famine. |
| Volume: |
26 |
| Issue: |
4 |
| Pages: |
312-24 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang JH |
| Year: |
2013 |
| Journal: |
Am J Physiol Gastrointest Liver Physiol |
| Title: |
Potent stimulation of fibroblast growth factor 19 expression in the human ileum by bile acids. |
| Volume: |
304 |
| Issue: |
10 |
| Pages: |
G940-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jones SA |
| Year: |
2012 |
| Journal: |
Adv Exp Med Biol |
| Title: |
Physiology of FGF15/19. |
| Volume: |
728 |
|
| Pages: |
171-82 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Xie MH |
| Year: |
1999 |
| Journal: |
Cytokine |
| Title: |
FGF-19, a novel fibroblast growth factor with unique specificity for FGFR4. |
| Volume: |
11 |
| Issue: |
10 |
| Pages: |
729-35 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Kir S |
| Year: |
2011 |
| Journal: |
Science |
| Title: |
FGF19 as a postprandial, insulin-independent activator of hepatic protein and glycogen synthesis. |
| Volume: |
331 |
| Issue: |
6024 |
| Pages: |
1621-4 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Jung D |
| Year: |
2007 |
| Journal: |
J Lipid Res |
| Title: |
FXR agonists and FGF15 reduce fecal bile acid excretion in a mouse model of bile acid malabsorption. |
| Volume: |
48 |
| Issue: |
12 |
| Pages: |
2693-700 |
|
•
•
•
•
•
|
| 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: |
|
|
|
•
•
•
•
•
|
| 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 |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
37
|
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
218
|
| Fragment?: |
false |
|
•
•
•
•
•
|
| 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. |
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•
•
•
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| 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. |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
209
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| Fragment?: |
false |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
245
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| Fragment?: |
false |
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| Publication |
| First Author: |
Santos-Ocampo S |
| Year: |
1996 |
| Journal: |
J Biol Chem |
| Title: |
Expression and biological activity of mouse fibroblast growth factor-9. |
| Volume: |
271 |
| Issue: |
3 |
| Pages: |
1726-31 |
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| Publication |
| First Author: |
Nishimura T |
| Year: |
2000 |
| Journal: |
Biochim Biophys Acta |
| Title: |
Identification of a novel FGF, FGF-21, preferentially expressed in the liver. |
| Volume: |
1492 |
| Issue: |
1 |
| Pages: |
203-6 |
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| Publication |
| First Author: |
Kharitonenkov A |
| Year: |
2005 |
| Journal: |
J Clin Invest |
| Title: |
FGF-21 as a novel metabolic regulator. |
| Volume: |
115 |
| Issue: |
6 |
| Pages: |
1627-35 |
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| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
194
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| Fragment?: |
false |
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