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Search results 2601 to 2700 out of 2725 for Fgfr2

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Hits by Pathway

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Type Details Score
Protein Coding Gene
MGI:98397 | Src
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1321161 | Ppp2cb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P26450
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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Protein
P05480
Organism: Mus musculus/domesticus
Length: 535  
Fragment?: false
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Protein
Q62245
Organism: Mus musculus/domesticus
Length: 1319  
Fragment?: false
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Protein
P62715
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Publication
10713090 | J:61068
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
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Publication
10629055 | -
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
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Publication
7537362 | -
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
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Publication
11030354 | -
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
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Publication
16207751 | J:102949
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
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Publication
2162671 | -
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
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Publication
17360555 | -
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
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Publication
21331089 | -
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
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Protein Domain
IPR028174 | FGF_rcpt_1
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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Protein Domain
IPR016248 | FGF_rcpt_fam
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
D3YWT1
Organism: Mus musculus/domesticus
Length: 331  
Fragment?: false
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Protein
D3Z3N4
Organism: Mus musculus/domesticus
Length: 346  
Fragment?: false
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Publication
16829530 | -
First Author: Duchesne L
Year: 2006
Journal: J Biol Chem
Title: N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate co-receptor binding.
Volume: 281
Issue: 37
Pages: 27178-89
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Publication
9212826 | -
First Author: Hughes SE
Year: 1997
Journal: J Histochem Cytochem
Title: Differential expression of the fibroblast growth factor receptor (FGFR) multigene family in normal human adult tissues.
Volume: 45
Issue: 7
Pages: 1005-19
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Publication
18216218 | -
First Author: Cotton LM
Year: 2008
Journal: Endocr Rev
Title: Cellular signaling by fibroblast growth factors (FGFs) and their receptors (FGFRs) in male reproduction.
Volume: 29
Issue: 2
Pages: 193-216
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Protein Coding Gene
MGI:1321159 | Ppp2ca
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346858 | Mapk1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1926334 | Ppp2r1a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1346859 | Mapk3
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q76MZ3
Organism: Mus musculus/domesticus
Length: 589  
Fragment?: false
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Protein
P63085
Organism: Mus musculus/domesticus
Length: 358  
Fragment?: false
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Protein
Q63844
Organism: Mus musculus/domesticus
Length: 380  
Fragment?: false
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Protein
P63330
Organism: Mus musculus/domesticus
Length: 309  
Fragment?: false
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Protein
Q60631-1
 
Organism: Mus musculus/domesticus
Length:  
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Protein
Q925A1
Organism: Mus musculus/domesticus
Length: 109  
Fragment?: false
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Protein
Q541T2
Organism: Mus musculus/domesticus
Length: 154  
Fragment?: false
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Protein
Q925A2
Organism: Mus musculus/domesticus
Length: 112  
Fragment?: false
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Protein
Q3TH23
Organism: Mus musculus/domesticus
Length: 512  
Fragment?: false
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Protein
A0A7U3L698
Organism: Mus musculus/domesticus
Length: 264  
Fragment?: false
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Protein
Q7TPG9
Organism: Mus musculus/domesticus
Length: 105  
Fragment?: true
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Protein
A0A7U3L4H7
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
Q8C399
Organism: Mus musculus/domesticus
Length: 195  
Fragment?: true
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Protein
Q925A3
Organism: Mus musculus/domesticus
Length: 153  
Fragment?: false
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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
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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
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Publication
15781473 | J:99916
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
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Publication
8663044 | -
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
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Protein
Q3US41
Organism: Mus musculus/domesticus
Length: 680  
Fragment?: false
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Protein
Q8K0G8
Organism: Mus musculus/domesticus
Length: 717  
Fragment?: false
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Protein
Q544I6
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Protein
A0A7U3JW48
Organism: Mus musculus/domesticus
Length: 260  
Fragment?: false
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Protein
D3Z139
Organism: Mus musculus/domesticus
Length: 592  
Fragment?: true
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Protein
Z4YJI3
Organism: Mus musculus/domesticus
Length: 659  
Fragment?: false
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Protein
F8WGU3
Organism: Mus musculus/domesticus
Length: 681  
Fragment?: false
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Protein
Q8C386
Organism: Mus musculus/domesticus
Length: 194  
Fragment?: false
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Publication
16597617 | J:153201
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
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Publication
2549857 | -
 
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
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Publication
7583099 | -
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
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Publication
3072709 | -
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
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Publication
11276432 | J:67832
First Author: Ornitz DM
Year: 2001
Journal: Genome Biol
Title: Fibroblast growth factors.
Volume: 2
Issue: 3
Pages: REVIEWS3005
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Publication
10830168 | -
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
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Publication
8652550 | -
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
1705486 | -
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
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Publication
8760337 | -
First Author: Green PJ
Year: 1996
Journal: Bioessays
Title: Promiscuity of fibroblast growth factor receptors.
Volume: 18
Issue: 8
Pages: 639-46
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Publication
23000357 | -
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
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Publication
15689573 | -
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
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Publication
10441498 | J:56785
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
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Publication
23108135 | -
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
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Publication
23016864 | -
First Author: Kumar SB
Year: 2013
Journal: Curr Pharm Des
Title: Fibroblast growth factor receptor inhibitors.
Volume: 19
Issue: 4
Pages: 687-701
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Publication
1649700 | -
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
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Publication
11746231 | -
First Author: Borland CZ
Year: 2001
Journal: Bioessays
Title: Fibroblast growth factor signaling in Caenorhabditis elegans.
Volume: 23
Issue: 12
Pages: 1120-30
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Publication
14745970 | -
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
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Publication
8978613 | -
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
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Protein Coding Gene
MGI:1925544 | Rps27a
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98887 | Uba52
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98888 | Ubb
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98889 | Ubc
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
P62984
Organism: Mus musculus/domesticus
Length: 128  
Fragment?: false
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Protein
P0CG50
Organism: Mus musculus/domesticus
Length: 734  
Fragment?: false
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Protein
P62983
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
P0CG49
Organism: Mus musculus/domesticus
Length: 305  
Fragment?: false
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Protein
Q3TJ05
Organism: Mus musculus/domesticus
Length: 386  
Fragment?: false
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Protein
P16092
Organism: Mus musculus/domesticus
Length: 822  
Fragment?: false
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Protein
J3QN85
Organism: Mus musculus/domesticus
Length: 833  
Fragment?: false
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Protein
Q60818
Organism: Mus musculus/domesticus
Length: 822  
Fragment?: false
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Protein
Q8CIM9
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
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Protein
Q61851
Organism: Mus musculus/domesticus
Length: 801  
Fragment?: false
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Protein
Q03142
Organism: Mus musculus/domesticus
Length: 799  
Fragment?: false
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Protein
A1YYP0
Organism: Mus musculus/domesticus
Length: 704  
Fragment?: false
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Protein
A1YYN9
Organism: Mus musculus/domesticus
Length: 821  
Fragment?: false
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Protein
Q61563
Organism: Mus musculus/domesticus
Length: 782  
Fragment?: false
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Protein
E9QNJ9
Organism: Mus musculus/domesticus
Length: 802  
Fragment?: false
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Protein
Q7TSI8
Organism: Mus musculus/domesticus
Length: 800  
Fragment?: false
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Protein
A1YYM5
Organism: Mus musculus/domesticus
Length: 707  
Fragment?: false
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Protein
E9Q7T0
Organism: Mus musculus/domesticus
Length: 819  
Fragment?: true
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Protein
E9Q7E8
Organism: Mus musculus/domesticus
Length: 822  
Fragment?: true
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Protein
A1YYM9
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: false
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Protein
A1YYN5
Organism: Mus musculus/domesticus
Length: 695  
Fragment?: false
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Protein
A1YYN0
Organism: Mus musculus/domesticus
Length: 813  
Fragment?: false
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Protein
E9PXV8
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: true
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Protein
Q3TQL1
Organism: Mus musculus/domesticus
Length: 762  
Fragment?: true
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Protein
E9Q5C2
Organism: Mus musculus/domesticus
Length: 723  
Fragment?: false
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Protein
E9PVU6
Organism: Mus musculus/domesticus
Length: 820  
Fragment?: true
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Protein
A1YYM7
Organism: Mus musculus/domesticus
Length: 724  
Fragment?: false
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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.

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Cambridge CB2 3EH, United Kingdom