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Search results 2501 to 2600 out of 2720 for Fgfr2

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Categories

Hits by Pathway

Hits by Strain

Hits by Category

Type Details Score
Protein Coding Gene
MGI:1891427 | Fgf23
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1913741 | Polr2l
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:95518 | Fgf4
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1891346 | Fgf20
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:1931627 | Fgf16
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q9EPC2
Organism: Mus musculus/domesticus
Length: 251  
Fragment?: false
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Protein
Q3UYV9
Organism: Mus musculus/domesticus
Length: 790  
Fragment?: false
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Protein
Q9CQ49
Organism: Mus musculus/domesticus
Length: 156  
Fragment?: false
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Protein
O89101
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
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Protein
P11403
Organism: Mus musculus/domesticus
Length: 202  
Fragment?: false
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Protein
P37237
Organism: Mus musculus/domesticus
Length: 268  
Fragment?: false
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Protein
Q9ESL9
Organism: Mus musculus/domesticus
Length: 211  
Fragment?: false
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Protein
P54130
Organism: Mus musculus/domesticus
Length: 208  
Fragment?: false
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Protein
P63075
Organism: Mus musculus/domesticus
Length: 216  
Fragment?: false
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Protein
Q8C180
Organism: Mus musculus/domesticus
Length: 508  
Fragment?: false
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Protein
Q9ESL8
Organism: Mus musculus/domesticus
Length: 207  
Fragment?: false
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Protein
P61148
Organism: Mus musculus/domesticus
Length: 155  
Fragment?: false
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Protein
P61219
Organism: Mus musculus/domesticus
Length: 127  
Fragment?: false
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Protein
Q923G2
Organism: Mus musculus/domesticus
Length: 150  
Fragment?: false
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Protein
P62876
Organism: Mus musculus/domesticus
Length: 67  
Fragment?: false
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Protein
Q80UW8
Organism: Mus musculus/domesticus
Length: 210  
Fragment?: false
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Protein
Q63871
Organism: Mus musculus/domesticus
Length: 58  
Fragment?: false
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Protein
P98083-3
Organism: Mus musculus/domesticus
Length: 424  
Fragment?: false
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Protein
Q62077
Organism: Mus musculus/domesticus
Length: 1302  
Fragment?: false
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Protein Domain
IPR034969 | hnRNPH3_RRM3
Type: Domain
Description: This entry represents the RNA recognition motif 3 (RRM3) of heterogeneous nuclear ribonucleoprotein H3 (hnRNP H3). hnRNP H3 (also termed hnRNP 2H9) is a nuclear RNA binding protein that belongs to the hnRNP H protein family that also includes hnRNP H, hnRNP H2, and hnRNP F. This family is involved in mRNA processing and exhibit extensive sequence homology. Little is known about the functions of hnRNP H3 except for its role in the splicing arrest induced by heat shock [, ]. The typical hnRNP H proteins contain contain three RNA recognition motifs (RRMs), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. Members in this family can regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. In addition, like other hnRNP H protein family members, hnRNP H3 has an extensive glycine-rich region near the C terminus, which may allow it to homo- or heterodimerize [].
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Protein Domain
IPR034970 | hnRNPH3_RRM2
Type: Domain
Description: This entry represents the RNA recognition motif 2 (RRM2) of heterogeneous nuclear ribonucleoprotein H3 (hnRNP H3).hnRNP H3 (also termed hnRNP 2H9) is a nuclear RNA binding protein that belongs to the hnRNP H protein family that also includes hnRNP H, hnRNP H2, and hnRNP F. This family is involved in mRNA processing and exhibit extensive sequence homology. Little is known about the functions of hnRNP H3 except for its role in the splicing arrest induced by heat shock [, ]. The typical hnRNP H proteins contain contain three RNA recognition motifs (RRMs), except for hnRNP H3, in which the RRM1 is absent. RRM1 and RRM2 are responsible for the binding to the RNA at DGGGD motifs, and they play an important role in efficiently silencing the exon. Members in this family can regulate the alternative splicing of the fibroblast growth factor receptor 2 (FGFR2) transcripts, and function as silencers of FGFR2 exon IIIc through an interaction with the exonic GGG motifs. The lack of RRM1 could account for the reduced silencing activity within hnRNP H3. In addition, like other hnRNP H protein family members, hnRNP H3 has an extensive glycine-rich region near the C terminus, which may allow it to homo- or heterodimerize [].
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Publication
30232710 | J:297327
First Author: Ohta K
Year: 2019
Journal: J Cell Commun Signal
Title: CCN2/CTGF binds the small leucine rich proteoglycan protein Tsukushi.
Volume: 13
Issue: 1
Pages: 113-118
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Publication
7512569 | J:30011
First Author: Chellaiah AT
Year: 1994
Journal: J Biol Chem
Title: Fibroblast growth factor receptor (FGFR) 3. Alternative splicing in immunoglobulin-like domain III creates a receptor highly specific for acidic FGF/FGF-1.
Volume: 269
Issue: 15
Pages: 11620-7
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Publication
10821861 | J:62309
First Author: Beer HD
Year: 2000
Journal: J Biol Chem
Title: Fibroblast growth factor (FGF) receptor 1-IIIb is a naturally occurring functional receptor for FGFs that is preferentially expressed in the skin and the brain.
Volume: 275
Issue: 21
Pages: 16091-7
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Publication
11134040 | J:68797
First Author: Shimizu A
Year: 2001
Journal: J Biol Chem
Title: A novel alternatively spliced fibroblast growth factor receptor 3 isoform lacking the acid box domain is expressed during chondrogenic differentiation of ATDC5 cells.
Volume: 276
Issue: 14
Pages: 11031-40
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Publication
26138642 | J:232527
First Author: McGowan SE
Year: 2015
Journal: Am J Physiol Lung Cell Mol Physiol
Title: Fibroblast growth factor signaling in myofibroblasts differs from lipofibroblasts during alveolar septation in mice.
Volume: 309
Issue: 5
Pages: L463-74
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Publication
27404344 | J:235363
First Author: Bebee TW
Year: 2016
Journal: Dev Dyn
Title: Ablation of the epithelial-specific splicing factor Esrp1 results in ureteric branching defects and reduced nephron number.
Volume: 245
Issue: 10
Pages: 991-1000
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Publication
30093411 | J:270679
First Author: Wang C
Year: 2018
Journal: J Biol Chem
Title: Ectopic fibroblast growth factor receptor 1 promotes inflammation by promoting nuclear factor-κB signaling in prostate cancer cells.
Volume: 293
Issue: 38
Pages: 14839-14849
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Publication
30342227 | J:270467
 
First Author: Nam HK
Year: 2019
Journal: Bone
Title: Tissue nonspecific alkaline phosphatase promotes calvarial progenitor cell cycle progression and cytokinesis via Erk1,2.
Volume: 120
Pages: 125-136
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Publication
29135976 | J:320346
First Author: Narla D
Year: 2017
Journal: Pediatr Res
Title: Loss of peri-Wolffian duct stromal Frs2α expression in mice leads to abnormal ureteric bud induction and vesicoureteral reflux.
Volume: 82
Issue: 6
Pages: 1022-1029
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Publication
22652199 | J:201241
First Author: Chen L
Year: 2012
Journal: Am J Respir Cell Mol Biol
Title: Dynamic regulation of platelet-derived growth factor receptor α expression in alveolar fibroblasts during realveolarization.
Volume: 47
Issue: 4
Pages: 517-27
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Publication
22951928 | J:187973
First Author: Azim K
Year: 2012
Journal: Glia
Title: Intraventricular injection of FGF-2 promotes generation of oligodendrocyte-lineage cells in the postnatal and adult forebrain.
Volume: 60
Issue: 12
Pages: 1977-90
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Publication
20501844 | J:160915
First Author: Pond AC
Year: 2010
Journal: Cancer Res
Title: Fibroblast growth factor receptor signaling dramatically accelerates tumorigenesis and enhances oncoprotein translation in the mouse mammary tumor virus-Wnt-1 mouse model of breast cancer.
Volume: 70
Issue: 12
Pages: 4868-79
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Publication
23754280 | J:298139
First Author: Wang C
Year: 2013
Journal: J Biol Chem
Title: Type 1 fibroblast growth factor receptor in cranial neural crest cell-derived mesenchyme is required for palatogenesis.
Volume: 288
Issue: 30
Pages: 22174-83
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Publication
32452519 | J:293772
First Author: Bird AD
Year: 2020
Journal: Hum Mol Genet
Title: Ovotesticular disorders of sex development in FGF9 mouse models of human synostosis syndromes.
Volume: 29
Issue: 13
Pages: 2148-2161
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Publication
24224032 | J:209320
First Author: Dol-Gleizes F
Year: 2013
Journal: PLoS One
Title: A new synthetic FGF receptor antagonist inhibits arteriosclerosis in a mouse vein graft model and atherosclerosis in apolipoprotein E-deficient mice.
Volume: 8
Issue: 11
Pages: e80027
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Publication
16446698 | J:106041
 
First Author: Zhao H
Year: 2006
Journal: Mol Vis
Title: Fibroblast growth factor receptor 1 (Fgfr1) is not essential for lens fiber differentiation in mice.
Volume: 12
Pages: 15-25
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Publication
24971743 | J:216816
First Author: Huang Y
Year: 2014
Journal: PLoS One
Title: Twist1- and Twist2-haploinsufficiency results in reduced bone formation.
Volume: 9
Issue: 6
Pages: e99331
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Publication
17592127 | J:189985
First Author: Simarro M
Year: 2007
Journal: Proc Natl Acad Sci U S A
Title: Fas-activated serine/threonine phosphoprotein (FAST) is a regulator of alternative splicing.
Volume: 104
Issue: 27
Pages: 11370-5
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Publication
17360777 | J:135130
First Author: Ota S
Year: 2007
Journal: Development
Title: Activities of N-Myc in the developing limb link control of skeletal size with digit separation.
Volume: 134
Issue: 8
Pages: 1583-92
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Publication
8432397 | J:3825
First Author: Peters K
Year: 1993
Journal: Dev Biol
Title: Unique expression pattern of the FGF receptor 3 gene during mouse organogenesis.
Volume: 155
Issue: 2
Pages: 423-30
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Publication
12215437 | J:80049
First Author: Trowbridge JM
Year: 2002
Journal: J Biol Chem
Title: Dermatan sulfate binds and potentiates activity of keratinocyte growth factor (FGF-7).
Volume: 277
Issue: 45
Pages: 42815-20
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Publication
20532173 | J:161810
First Author: Takeuchi A
Year: 2010
Journal: PLoS One
Title: Splicing reporter mice revealed the evolutionally conserved switching mechanism of tissue-specific alternative exon selection.
Volume: 5
Issue: 6
Pages: e10946
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Publication
23880303 | J:202530
First Author: Kelleher FC
Year: 2013
Journal: Carcinogenesis
Title: Fibroblast growth factor receptors, developmental corruption and malignant disease.
Volume: 34
Issue: 10
Pages: 2198-205
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Publication
25704602 | J:230349
First Author: Leslie EJ
Year: 2015
Journal: Am J Hum Genet
Title: Identification of functional variants for cleft lip with or without cleft palate in or near PAX7, FGFR2, and NOG by targeted sequencing of GWAS loci.
Volume: 96
Issue: 3
Pages: 397-411
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Publication
26878171 | J:232422
First Author: Rossaint J
Year: 2016
Journal: J Clin Invest
Title: FGF23 signaling impairs neutrophil recruitment and host defense during CKD.
Volume: 126
Issue: 3
Pages: 962-74
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Publication
36211556 | J:330047
 
First Author: Matsiukevich D
Year: 2022
Journal: Front Cardiovasc Med
Title: Fibroblast growth factor receptor signaling in cardiomyocytes is protective in the acute phase following ischemia-reperfusion injury.
Volume: 9
Pages: 1011167
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Publication
37503695 | J:340449
First Author: Guo K
Year: 2023
Journal: Aging Cell
Title: Fibroblast growth factor 10 ameliorates neurodegeneration in mouse and cellular models of Alzheimer's disease via reducing tau hyperphosphorylation and neuronal apoptosis.
Volume: 22
Issue: 9
Pages: e13937
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Protein Coding Gene
MGI:1206581 | Pik3ca
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:97376 | Nras
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:99511 | Ptpn11
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:96680 | Kras
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:96224 | Hras
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein
Q61411
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
P32883
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
P08556
Organism: Mus musculus/domesticus
Length: 189  
Fragment?: false
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Protein
P42337
Organism: Mus musculus/domesticus
Length: 1068  
Fragment?: false
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Protein
P35235
Organism: Mus musculus/domesticus
Length: 593  
Fragment?: false
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Publication
15806171 | J:100761
First Author: Beer HD
Year: 2005
Journal: Oncogene
Title: The fibroblast growth factor binding protein is a novel interaction partner of FGF-7, FGF-10 and FGF-22 and regulates FGF activity: implications for epithelial repair.
Volume: 24
Issue: 34
Pages: 5269-77
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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
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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
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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
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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
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Publication
7923352 | J:20551
First Author: Hébert JM
Year: 1994
Journal: Cell
Title: FGF5 as a regulator of the hair growth cycle: evidence from targeted and spontaneous mutations.
Volume: 78
Issue: 6
Pages: 1017-25
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Publication
12713572 | J:83352
First Author: Cho YM
Year: 2003
Journal: J Invest Dermatol
Title: Hair-cycle-dependent expression of parathyroid hormone-related protein and its type I receptor: evidence for regulation at the anagen to catagen transition.
Volume: 120
Issue: 5
Pages: 715-27
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Publication
16875743 | J:116006
First Author: Armand AS
Year: 2006
Journal: Biochim Biophys Acta
Title: FGF6 in myogenesis.
Volume: 1763
Issue: 8
Pages: 773-8
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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 [, ].
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Protein Domain
IPR028242 | FGF6
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 6 (FGF6). This protein plays an important role in the regulation of cell proliferation, cell differentiation, angiogenesis and myogenesis, and is required for normal muscle regeneration [, , ]. It may also regulate bone metabolism, as shown by its activity on both osteoblasts and osteoclasts []. FGF6 has a high affinity for FGFR1, FGFR2 and FGFR4 [].
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Protein Domain
IPR028240 | FGF5
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
IPR028247 | FGF7
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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Protein Domain
IPR028223 | FGF2
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
16502419 | J:108218
First Author: Connerney J
Year: 2006
Journal: Dev Dyn
Title: Twist1 dimer selection regulates cranial suture patterning and fusion.
Volume: 235
Issue: 5
Pages: 1345-57
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Publication
19515808 | J:150719
First Author: Gattineni J
Year: 2009
Journal: Am J Physiol Renal Physiol
Title: FGF23 decreases renal NaPi-2a and NaPi-2c expression and induces hypophosphatemia in vivo predominantly via FGF receptor 1.
Volume: 297
Issue: 2
Pages: F282-91
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Publication
9640329 | J:174265
First Author: Robinson ML
Year: 1998
Journal: Dev Biol
Title: Disregulation of ocular morphogenesis by lens-specific expression of FGF-3/int-2 in transgenic mice.
Volume: 198
Issue: 1
Pages: 13-31
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Publication
11287183 | J:69279
First Author: Mailleux AA
Year: 2001
Journal: Mech Dev
Title: Evidence that SPROUTY2 functions as an inhibitor of mouse embryonic lung growth and morphogenesis.
Volume: 102
Issue: 1-2
Pages: 81-94
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Publication
10196476 | J:54853
First Author: Zhang Y
Year: 1999
Journal: Gene
Title: Genomic organization of the human fibroblast growth factor receptor 2 (FGFR2) gene and comparative analysis of the human FGFR gene family.
Volume: 230
Issue: 1
Pages: 69-79
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Protein Coding Gene
MGI:97583 | Pik3r1
Type: protein_coding_gene
Organism: mouse, laboratory
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Protein Coding Gene
MGI:98354 | Sos1
Type: protein_coding_gene
Organism: mouse, laboratory
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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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