|  Help  |  About  |  Contact Us

Search our database by keyword

Examples

  • Search this entire website. Enter identifiers, names or keywords for genes, diseases, strains, ontology terms, etc. (e.g. Pax6, Parkinson, ataxia)
  • Use OR to search for either of two terms (e.g. OR mus) or quotation marks to search for phrases (e.g. "dna binding").
  • Boolean search syntax is supported: e.g. Balb* for partial matches or mus AND NOT embryo to exclude a term

Search results 2201 to 2300 out of 2538 for Fgfr1

<< First    < Previous  |  Next >    Last >>
0.038s

Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Protein
Q71UP6
Organism: Mus musculus/domesticus
Length: 64  
Fragment?: true
•
•
•
•
•
Protein
Q8C471
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
•
•
•
•
•
Protein
A0A7U3JW73
Organism: Mus musculus/domesticus
Length: 276  
Fragment?: false
•
•
•
•
•
Protein
A0A7U3JW52
Organism: Mus musculus/domesticus
Length: 162  
Fragment?: false
•
•
•
•
•
Protein
Q0VF19
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
•
•
•
•
•
Protein
A0A140LIV6
Organism: Mus musculus/domesticus
Length: 52  
Fragment?: true
•
•
•
•
•
Protein
D3Z6H1
Organism: Mus musculus/domesticus
Length: 60  
Fragment?: false
•
•
•
•
•
Protein
O35340
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
•
•
•
•
•
Protein
O54837
Organism: Mus musculus/domesticus
Length: 70  
Fragment?: true
•
•
•
•
•
Protein
A0A7U3JW80
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
•
•
•
•
•
Protein
Q7TPG9
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
•
•
•
•
•
Protein
A0A338P752
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
•
•
•
•
•
Protein
A0A7U3L4H7
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
•
•
•
•
•
Protein
Q0VBJ8
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
•
•
•
•
•
Protein
Q5SQB3
Organism: Mus musculus/domesticus
Length: 98  
Fragment?: false
•
•
•
•
•
Protein
A0A338P764
Organism: Mus musculus/domesticus
Length: 171  
Fragment?: true
•
•
•
•
•
Protein
D3Z192
Organism: Mus musculus/domesticus
Length: 49  
Fragment?: true
•
•
•
•
•
Protein
C6EQH1
Organism: Mus musculus/domesticus
Length: 115  
Fragment?: false
•
•
•
•
•
Protein
A0A7U3L4H2
Organism: Mus musculus/domesticus
Length: 225  
Fragment?: false
•
•
•
•
•
Protein
Q8C399
Organism: Mus musculus/domesticus
Length: 195  
Fragment?: true
•
•
•
•
•
Protein
A0A7U3JW65
Organism: Mus musculus/domesticus
Length: 243  
Fragment?: false
•
•
•
•
•
Protein
A0A067XG51
Organism: Mus musculus/domesticus
Length: 97  
Fragment?: true
•
•
•
•
•
Protein
A0A7U3JW97
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
•
•
•
•
•
Protein
Q60757
Organism: Mus musculus/domesticus
Length: 159  
Fragment?: true
•
•
•
•
•
Protein
D3Z6E2
Organism: Mus musculus/domesticus
Length: 78  
Fragment?: true
•
•
•
•
•
Protein
Q6ZWS1
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: false
•
•
•
•
•
Protein
O89096
Organism: Mus musculus/domesticus
Length: 252  
Fragment?: false
•
•
•
•
•
Protein
Q925A3
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
•
•
•
•
•
Protein
A0A494BBG9
Organism: Mus musculus/domesticus
Length: 104  
Fragment?: false
•
•
•
•
•
Protein
Q059W0
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
•
•
•
•
•
Protein
A0A0R4J063
Organism: Mus musculus/domesticus
Length: 247  
Fragment?: false
•
•
•
•
•
Protein
Q0VER9
Organism: Mus musculus/domesticus
Length: 126  
Fragment?: false
•
•
•
•
•
Publication
25040546 | -
First Author: Beesley PW
Year: 2014
Journal: J Neurochem
Title: The Neuroplastin adhesion molecules: key regulators of neuronal plasticity and synaptic function.
Volume: 131
Issue: 3
Pages: 268-83
•
•
•
•
•
Publication
12145206 | -
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
10574949 | -
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
19665973 | -
First Author: Bae JH
Year: 2009
Journal: Cell
Title: The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site.
Volume: 138
Issue: 3
Pages: 514-24
•
•
•
•
•
Publication
28380381 | J:251896
First Author: BonDurant LD
Year: 2017
Journal: Cell Metab
Title: FGF21 Regulates Metabolism Through Adipose-Dependent and -Independent Mechanisms.
Volume: 25
Issue: 4
Pages: 935-944.e4
•
•
•
•
•
Publication
36445537 | J:332874
First Author: Jones MR
Year: 2022
Journal: Cell Mol Life Sci
Title: FGFR2b signalling restricts lineage-flexible alveolar progenitors during mouse lung development and converges in mature alveolar type 2 cells.
Volume: 79
Issue: 12
Pages: 609
•
•
•
•
•
Publication
11062477 | J:65463
First Author: ADHR Consortium.
Year: 2000
Journal: Nat Genet
Title: Autosomal dominant hypophosphataemic rickets is associated with mutations in FGF23.
Volume: 26
Issue: 3
Pages: 345-8
•
•
•
•
•
Publication
9514906 | J:46389
First Author: Hoshikawa M
Year: 1998
Journal: Biochem Biophys Res Commun
Title: Structure and expression of a novel fibroblast growth factor, FGF-17, preferentially expressed in the embryonic brain.
Volume: 244
Issue: 1
Pages: 187-91
•
•
•
•
•
Publication
11342227 | J:67825
First Author: Nakatake Y
Year: 2001
Journal: Biochim Biophys Acta
Title: Identification of a novel fibroblast growth factor, FGF-22, preferentially expressed in the inner root sheath of the hair follicle.
Volume: 1517
Issue: 3
Pages: 460-3
•
•
•
•
•
Publication
20145243 | -
First Author: Fernández IS
Year: 2010
Journal: J Biol Chem
Title: Gentisic acid, a compound associated with plant defense and a metabolite of aspirin, heads a new class of in vivo fibroblast growth factor inhibitors.
Volume: 285
Issue: 15
Pages: 11714-29
•
•
•
•
•
Publication
10510314 | -
 
First Author: Mizukoshi E
Year: 1999
Journal: Biochem J
Title: Fibroblast growth factor-1 interacts with the glucose-regulated protein GRP75/mortalin.
Volume: 343 Pt 2
Pages: 461-6
•
•
•
•
•
Publication
9806903 | -
 
First Author: Kolpakova E
Year: 1998
Journal: Biochem J
Title: Cloning of an intracellular protein that binds selectively to mitogenic acidic fibroblast growth factor.
Volume: 336 ( Pt 1)
Pages: 213-22
•
•
•
•
•
Publication
1721615 | -
First Author: Shimoyama Y
Year: 1991
Journal: Jpn J Cancer Res
Title: Characterization of high-molecular-mass forms of basic fibroblast growth factor produced by hepatocellular carcinoma cells: possible involvement of basic fibroblast growth factor in hepatocarcinogenesis.
Volume: 82
Issue: 11
Pages: 1263-70
•
•
•
•
•
Publication
8530375 | -
First Author: Reich-Slotky R
Year: 1995
Journal: J Biol Chem
Title: Chimeric molecules between keratinocyte growth factor and basic fibroblast growth factor define domains that confer receptor binding specificities.
Volume: 270
Issue: 50
Pages: 29813-8
•
•
•
•
•
Publication
9826564 | J:51038
First Author: Shen B
Year: 1998
Journal: Biochem Biophys Res Commun
Title: Intracellular association of FGF-2 with the ribosomal protein L6/TAXREB107.
Volume: 252
Issue: 2
Pages: 524-8
•
•
•
•
•
Publication
11716516 | -
First Author: Soulet F
Year: 2001
Journal: Biochem Biophys Res Commun
Title: Fibroblast growth factor-2 interacts with free ribosomal protein S19.
Volume: 289
Issue: 2
Pages: 591-6
•
•
•
•
•
Publication
9477322 | J:47321
First Author: Kim HJ
Year: 1998
Journal: Development
Title: FGF-, BMP- and Shh-mediated signalling pathways in the regulation of cranial suture morphogenesis and calvarial bone development.
Volume: 125
Issue: 7
Pages: 1241-51
•
•
•
•
•
Publication
8001146 | -
First Author: Laufer E
Year: 1994
Journal: Cell
Title: Sonic hedgehog and Fgf-4 act through a signaling cascade and feedback loop to integrate growth and patterning of the developing limb bud.
Volume: 79
Issue: 6
Pages: 993-1003
•
•
•
•
•
Publication
15672378 | -
First Author: Armand AS
Year: 2005
Journal: J Cell Physiol
Title: FGF6 regulates muscle differentiation through a calcineurin-dependent pathway in regenerating soleus of adult mice.
Volume: 204
Issue: 1
Pages: 297-308
•
•
•
•
•
Publication
20458746 | -
First Author: Bosetti M
Year: 2010
Journal: J Cell Physiol
Title: Regulation of osteoblast and osteoclast functions by FGF-6.
Volume: 225
Issue: 2
Pages: 466-71
•
•
•
•
•
Publication
2915979 | J:29167
First Author: Rubin JS
Year: 1989
Journal: Proc Natl Acad Sci U S A
Title: Purification and characterization of a newly identified growth factor specific for epithelial cells.
Volume: 86
Issue: 3
Pages: 802-6
•
•
•
•
•
Publication
10541313 | -
First Author: Graeff RW
Year: 1999
Journal: Pediatr Res
Title: KGF and FGF-10 stimulate liquid secretion in human fetal lung.
Volume: 46
Issue: 5
Pages: 523-9
•
•
•
•
•
Publication
9740653 | J:50000
First Author: Park WY
Year: 1998
Journal: Dev Biol
Title: FGF-10 is a chemotactic factor for distal epithelial buds during lung development.
Volume: 201
Issue: 2
Pages: 125-34
•
•
•
•
•
Publication
17292422 | -
First Author: Pereira CT
Year: 2007
Journal: J Surg Res
Title: Liposomal gene transfer of keratinocyte growth factor improves wound healing by altering growth factor and collagen expression.
Volume: 139
Issue: 2
Pages: 222-8
•
•
•
•
•
Publication
11973338 | -
First Author: Ruehl M
Year: 2002
Journal: J Biol Chem
Title: The epithelial mitogen keratinocyte growth factor binds to collagens via the consensus sequence glycine-proline-hydroxyproline.
Volume: 277
Issue: 30
Pages: 26872-8
•
•
•
•
•
Publication
10702276 | -
First Author: Mongiat M
Year: 2000
Journal: J Biol Chem
Title: The protein core of the proteoglycan perlecan binds specifically to fibroblast growth factor-7.
Volume: 275
Issue: 10
Pages: 7095-100
•
•
•
•
•
Publication
7687739 | -
First Author: Yan G
Year: 1993
Journal: Mol Cell Biol
Title: Exon switching and activation of stromal and embryonic fibroblast growth factor (FGF)-FGF receptor genes in prostate epithelial cells accompany stromal independence and malignancy.
Volume: 13
Issue: 8
Pages: 4513-22
•
•
•
•
•
Publication
7768185 | J:23136
First Author: Crossley PH
Year: 1995
Journal: Development
Title: The mouse Fgf8 gene encodes a family of polypeptides and is expressed in regions that direct outgrowth and patterning in the developing embryo.
Volume: 121
Issue: 2
Pages: 439-51
•
•
•
•
•
Publication
22273727 | -
First Author: Liu SB
Year: 2012
Journal: Toxicology
Title: The role of androgen-induced growth factor (FGF8) on genital tubercle development in a hypospadiac male rat model of prenatal exposure to di-n-butyl phthalate.
Volume: 293
Issue: 1-3
Pages: 53-8
•
•
•
•
•
Publication
11420691 | -
First Author: Mattila MM
Year: 2001
Journal: Oncogene
Title: FGF-8b increases angiogenic capacity and tumor growth of androgen-regulated S115 breast cancer cells.
Volume: 20
Issue: 22
Pages: 2791-804
•
•
•
•
•
Publication
9332670 | J:43312
First Author: Yoshiura K
Year: 1997
Journal: Am J Med Genet
Title: Genomic structure, sequence, and mapping of human FGF8 with no evidence for its role in craniosynostosis/limb defect syndromes.
Volume: 72
Issue: 3
Pages: 354-62
•
•
•
•
•
Publication
12072406 | -
First Author: Tsai SJ
Year: 2002
Journal: Endocrinology
Title: Fibroblast growth factor-9 is an endometrial stromal growth factor.
Volume: 143
Issue: 7
Pages: 2715-21
•
•
•
•
•
Publication
10362017 | -
First Author: Giri D
Year: 1999
Journal: J Cell Physiol
Title: FGF9 is an autocrine and paracrine prostatic growth factor expressed by prostatic stromal cells.
Volume: 180
Issue: 1
Pages: 53-60
•
•
•
•
•
Publication
16700629 | J:110252
First Author: Kim Y
Year: 2006
Journal: PLoS Biol
Title: Fgf9 and Wnt4 act as antagonistic signals to regulate mammalian sex determination.
Volume: 4
Issue: 6
Pages: e187
•
•
•
•
•
Publication
11290325 | J:68379
First Author: Colvin JS
Year: 2001
Journal: Cell
Title: Male-to-female sex reversal in mice lacking fibroblast growth factor 9.
Volume: 104
Issue: 6
Pages: 875-89
•
•
•
•
•
Publication
9287324 | J:42892
First Author: Emoto H
Year: 1997
Journal: J Biol Chem
Title: Structure and expression of human fibroblast growth factor-10.
Volume: 272
Issue: 37
Pages: 23191-4
•
•
•
•
•
Publication
11923311 | J:113981
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
9784490 | J:50768
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
9916808 | J:51966
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
9927546 | -
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
9345906 | -
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
9735346 | -
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
15282281 | -
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
10071193 | -
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
10640713 | J:60428
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
12489043 | -
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
17678857 | J:128732
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
10766846 | -
First Author: Konishi M
Year: 2000
Journal: J Biol Chem
Title: Fibroblast growth factor-16 is a growth factor for embryonic brown adipocytes.
Volume: 275
Issue: 16
Pages: 12119-22
•
•
•
•
•
Publication
9751161 | J:47850
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
•
•
•
•
•
Publication
10381577 | J:56088
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
10913340 | -
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
11032730 | -
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
11306498 | -
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
15260994 | J:91948
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
22249518 | -
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
21346724 | -
 
First Author: Jüppner H
Year: 2011
Journal: Kidney Int Suppl
Title: Phosphate and FGF-23.
Issue: 121
Pages: S24-7
•
•
•
•
•
Publication
18310961 | -
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
11409890 | -
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
IPR028296 | FGF22
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 [].
•
•
•
•
•
Protein Domain
IPR028292 | FGF21
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 [].
•
•
•
•
•
Protein Domain
IPR028285 | FGF16
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 16 (FGF16). The protein plays an important role in the regulation of embryonic development, cell proliferation and cell differentiation, and is required for normal cardiomyocyte proliferation and heart development []. In rat embryos, FGF16 is detected predominantly in brown adipose tissue, where it shows significant mitogenic activity for primary brown adipocytes, mediated by activation of FGFR4 [].
•
•
•
•
•
Protein Domain
IPR028287 | FGF17
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 [, , ].
•
•
•
•
•
Protein Domain
IPR028284 | FGF14
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 [].
•
•
•
•
•
Protein Domain
IPR028291 | FGF20
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 [].
•
•
•
•
•
Protein Domain
IPR028279 | FGF13
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 [].
•
•
•
•
•
Protein Domain
IPR028304 | FGF23
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 [, , ].
•
•
•
•
•
Protein Domain
IPR028210 | FGF1
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 [].
•
•
•
•
•
Protein Domain
IPR028252 | FGF10
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 [, ].
•
•
•
•
•




MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

Copyright © 2017 by The Jackson Laboratory. All Rights Reserved

© 2002 - 2017 Department of Genetics, University of Cambridge, Downing Street,
Cambridge CB2 3EH, United Kingdom