| Type |
Details |
Score |
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
244
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Abdeen HH |
| Year: |
1999 |
| Journal: |
Mol Biochem Parasitol |
| Title: |
Molecular cloning and characterization of the polypeptide backbone of Schistosoma mansoni circulating cathodic antigen. |
| Volume: |
101 |
| Issue: |
1-2 |
| Pages: |
149-59 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Huang J |
| Year: |
2005 |
| Journal: |
EMBO J |
| Title: |
SIKE is an IKK epsilon/TBK1-associated suppressor of TLR3- and virus-triggered IRF-3 activation pathways. |
| Volume: |
24 |
| Issue: |
23 |
| Pages: |
4018-28 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Sukotjo C |
| Year: |
2003 |
| Journal: |
J Biol Chem |
| Title: |
Oral fibroblast expression of wound-inducible transcript 3.0 (wit3.0) accelerates the collagen gel contraction in vitro. |
| Volume: |
278 |
| Issue: |
51 |
| Pages: |
51527-34 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Van Dam GJ |
| Year: |
1994 |
| Journal: |
Eur J Biochem |
| Title: |
The immunologically reactive O-linked polysaccharide chains derived from circulating cathodic antigen isolated from the human blood fluke Schistosoma mansoni have Lewis x as repeating unit. |
| Volume: |
225 |
| Issue: |
1 |
| Pages: |
467-82 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Chang CH |
| Year: |
2015 |
| Journal: |
Oncotarget |
| Title: |
Gab1 is essential for membrane translocation, activity and integrity of mTORCs after EGF stimulation in urothelial cell carcinoma. |
| Volume: |
6 |
| Issue: |
3 |
| Pages: |
1478-89 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
This entry represents GRB2-associated-binding proteins 1-4 (Gab1-4) and similar proteins from animals. Proteins in this family contain one PH domain. GAB1 from humans and its orthologues dos and soc-1 from Drosophila and C. elegans [], respectively, function as adapter proteins that modulate intracellular signalling cascades triggered by activated receptor-type kinases. Gab1 from human plays a role in FGFR1 signalling, is involved in the MET/HGF-signalling pathway and functions as an important upstream regulator in EGF-mediated activation of mTORCs [, ]. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Suppressor of IKBKE 1 (SIKE) is a physiological suppressor of IKK-epsilon and TBK1 []. IKKepsilon and TBK1 are two IKK-related kinases critically involved in virus- and TLR3-triggered activation of interferon regulatory factor 3 (IRF-3).Other members of this family are circulating cathodic antigen (CCA), found in Schistosoma mansoni (Blood fluke) [, ], and FGFR1 oncogene partner 2, which may be involved in wound healing pathway []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Rochester JR |
| Year: |
2012 |
| Journal: |
Am J Physiol Endocrinol Metab |
| Title: |
Opposite-sex housing reactivates the declining GnRH system in aged transgenic male mice with FGF signaling deficiency. |
| Volume: |
303 |
| Issue: |
12 |
| Pages: |
E1428-39 |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Pbsn-FGFR1*K656E)#Wmck/? Tg(Pbsn-FGFR2_iiib*)#Ng/? |
| Background: |
involves: FVB |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Genotype |
| Symbol: |
Tg(Myh6-rtTA)8585Jam/? Tg(tetO-Fgfr3*R248C/Fgfr1)#Dor/? |
| Background: |
involves: 129 * C57BL/6 * FVB/N * FVB/NTac |
| Zygosity: |
cx |
| Has Mutant Allele: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
1302
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
913
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Neuroplastin and basigin are members of the immunoglobulin (Ig) superfamily. They have two Ig domains that project into the extracellular space. They are also present as isoforms containing an additional N-terminal Ig domain. They contain a glutamate (E) at exactly the same position in the transmembrane domain, which may be important for molecular interactions within the membrane region [].Neuroplastin is a probable homophilic and heterophilic cell adhesion molecule involved in long term potentiation at hippocampal excitatory synapses through activation of p38MAPK []. It may also regulate neurite outgrowth by activating the FGFR1 signaling pathway []. It may play a role in synaptic plasticity []. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Hecht D |
| Year: |
1995 |
| Journal: |
Growth Factors |
| Title: |
Identification of fibroblast growth factor 9 (FGF9) as a high affinity, heparin dependent ligand for FGF receptors 3 and 2 but not for FGF receptors 1 and 4. |
| Volume: |
12 |
| Issue: |
3 |
| Pages: |
223-33 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Cao Z |
| Year: |
2014 |
| Journal: |
Cancer Cell |
| Title: |
Angiocrine factors deployed by tumor vascular niche induce B cell lymphoma invasiveness and chemoresistance. |
| Volume: |
25 |
| Issue: |
3 |
| Pages: |
350-65 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Zhang B |
| Year: |
2024 |
| Journal: |
J Clin Invest |
| Title: |
Interruption of KLF5 acetylation promotes PTEN-deficient prostate cancer progression by reprogramming cancer-associated fibroblasts. |
| Volume: |
134 |
| Issue: |
14 |
|
|
•
•
•
•
•
|
| Publication |
| First Author: |
Oberkersch RE |
| Year: |
2022 |
| Journal: |
Dev Cell |
| Title: |
Aspartate metabolism in endothelial cells activates the mTORC1 pathway to initiate translation during angiogenesis. |
| Volume: |
57 |
| Issue: |
10 |
| Pages: |
1241-1256.e8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Saarimäki-Vire J |
| Year: |
2011 |
| Journal: |
Dev Dyn |
| Title: |
Analysis of Cdh22 expression and function in the developing mouse brain. |
| Volume: |
240 |
| Issue: |
8 |
| Pages: |
1989-2001 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Geng L |
| Year: |
2019 |
| Journal: |
Cell Rep |
| Title: |
Exercise Alleviates Obesity-Induced Metabolic Dysfunction via Enhancing FGF21 Sensitivity in Adipose Tissues. |
| Volume: |
26 |
| Issue: |
10 |
| Pages: |
2738-2752.e4 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Fu Z |
| Year: |
2021 |
| Journal: |
iScience |
| Title: |
Retinal glial remodeling by FGF21 preserves retinal function during photoreceptor degeneration. |
| Volume: |
24 |
| Issue: |
4 |
| Pages: |
102376 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Pizette S |
| Year: |
1996 |
| Journal: |
Exp Cell Res |
| Title: |
FGF6 modulates the expression of fibroblast growth factor receptors and myogenic genes in muscle cells. |
| Volume: |
224 |
| Issue: |
1 |
| Pages: |
143-51 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Browaeys-Poly E |
| Year: |
2010 |
| Journal: |
FEBS Lett |
| Title: |
Grb14 inhibits FGF receptor signaling through the regulation of PLCγ recruitment and activation. |
| Volume: |
584 |
| Issue: |
21 |
| Pages: |
4383-8 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Peifer M |
| Year: |
2012 |
| Journal: |
Nat Genet |
| Title: |
Integrative genome analyses identify key somatic driver mutations of small-cell lung cancer. |
| Volume: |
44 |
| Issue: |
10 |
| Pages: |
1104-10 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Eichner LJ |
| Year: |
2023 |
| Journal: |
Sci Adv |
| Title: |
HDAC3 is critical in tumor development and therapeutic resistance in Kras-mutant non-small cell lung cancer. |
| Volume: |
9 |
| Issue: |
11 |
| Pages: |
eadd3243 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Yu Y |
| Year: |
2017 |
| Journal: |
Nat Commun |
| Title: |
Genome-wide analyses of non-syndromic cleft lip with palate identify 14 novel loci and genetic heterogeneity. |
| Volume: |
8 |
|
| Pages: |
14364 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Riazuddin S |
| Year: |
2011 |
| Journal: |
BMC Med Genet |
| Title: |
Variable expressivity of FGF3 mutations associated with deafness and LAMM syndrome. |
| Volume: |
12 |
|
| Pages: |
21 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Publication |
| 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 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 5 (FGF5). This protein plays an important role in the regulation of cell proliferation and cell differentiation. It is required for normal regulation of the hair growth cycle, as it functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen, the apoptosis-induced regression phase [, ]. FGF5 has a high affinity for FGFR1 and FGFR2 []. |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Family |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].This entry represents fibroblast growth factor 3 (FGF3), also known as heparin-binding growth factor 3 and INT-2 proto-oncogene protein. The protein plays an important role in the regulation of embryonic development, cell proliferation and differentiation, and is required for normal ear development [, ]. FGF3 has a high affinity for FGFR3 and FGFR2, but a low affinity for FGFR1 []. |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
508
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
424
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
245
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
156
 |
| Fragment?: |
true |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
264
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein Coding Gene |
| Type: |
protein_coding_gene |
| Organism: |
mouse, laboratory |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
189
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
189
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
189
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Protein |
| Organism: |
Mus musculus/domesticus |
| Length: |
593
 |
| Fragment?: |
false |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Ong SH |
| Year: |
2000 |
| Journal: |
Mol Cell Biol |
| Title: |
FRS2 proteins recruit intracellular signaling pathways by binding to diverse targets on fibroblast growth factor and nerve growth factor receptors. |
| Volume: |
20 |
| Issue: |
3 |
| Pages: |
979-89 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Karlsson T |
| Year: |
1995 |
| Journal: |
Oncogene |
| Title: |
Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, tyrosine kinase receptors and Src homology 3 domain proteins. |
| Volume: |
10 |
| Issue: |
8 |
| Pages: |
1475-83 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Smalla KH |
| Year: |
2000 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
The synaptic glycoprotein neuroplastin is involved in long-term potentiation at hippocampal CA1 synapses. |
| Volume: |
97 |
| Issue: |
8 |
| Pages: |
4327-32 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Empson RM |
| Year: |
2006 |
| Journal: |
J Neurochem |
| Title: |
The cell adhesion molecule neuroplastin-65 inhibits hippocampal long-term potentiation via a mitogen-activated protein kinase p38-dependent reduction in surface expression of GluR1-containing glutamate receptors. |
| Volume: |
99 |
| Issue: |
3 |
| Pages: |
850-60 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Owczarek S |
| Year: |
2010 |
| Journal: |
FASEB J |
| Title: |
Neuroplastin-55 binds to and signals through the fibroblast growth factor receptor. |
| Volume: |
24 |
| Issue: |
4 |
| Pages: |
1139-50 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Schlessinger J |
| Year: |
2000 |
| Journal: |
Mol Cell |
| Title: |
Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization. |
| Volume: |
6 |
| Issue: |
3 |
| Pages: |
743-50 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Itoh N |
| Year: |
1990 |
| Journal: |
Biochem Biophys Res Commun |
| Title: |
The complete amino acid sequence of the shorter form of human basic fibroblast growth factor receptor deduced from its cDNA. |
| Volume: |
169 |
| Issue: |
2 |
| Pages: |
680-5 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Riley BM |
| Year: |
2007 |
| Journal: |
Proc Natl Acad Sci U S A |
| Title: |
Impaired FGF signaling contributes to cleft lip and palate. |
| Volume: |
104 |
| Issue: |
11 |
| Pages: |
4512-7 |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Dixon MJ |
| Year: |
2011 |
| Journal: |
Nat Rev Genet |
| Title: |
Cleft lip and palate: understanding genetic and environmental influences. |
| Volume: |
12 |
| Issue: |
3 |
| Pages: |
167-78 |
|
•
•
•
•
•
|
| Protein Domain |
| Type: |
Domain |
| Description: |
Fibroblast growth factors (FGFs) [, ]are a family of multifunctional proteins, often referred to as 'promiscuous growth factors' due to their diverse actions on multiple cell types [, ]. FGFs are mitogens, which stimulate growth or differentiation of cells of mesodermal or neuroectodermal origin. The function of FGFs in developmental processes include mesoderm induction, anterior-posterior patterning, limb development, and neural induction and development. In mature tissues, they are involved in diverse processes including keratinocyte organisation and wound healing [, , , , , ]. FGF involvement is critical during normal development of both vertebrates and invertebrates, and irregularities in their function leads to a range of developmental defects [, , , ]. Fibroblast growth factors are heparin-binding proteins and interactions with cell-surface-associated heparan sulfate proteoglycans have been shown to be essential for FGF signal transduction. FGFs have internal pseudo-threefold symmetry (β-trefoil topology) []. There are currently over 20 different FGF family members that have been identified in mammals, all of which are structurally related signaling molecules [, ]. They exert their effects through four distinct membrane fibroblast growth factor receptors (FGFRs), FGFR1 to FGFR4 [], which belong to the tyrosine kinase superfamily. Upon binding to FGF, the receptors dimerize and their intracellular tyrosine kinase domains become active [].The FGFRs consist of an extracellular ligand-binding domain composed of three immunoglobulin-like domains (D1-D3), a single transmembrane helix domain, and an intracellular domain with tyrosine kinase activity []. The three immunoglobin(Ig)-like domains, D1, D2, and D3, present a stretch of acidic amino acids (known as the acid box) between D1 and D2. This acid box can participate in the regulation of FGF binding to the FGFR. Immunoglobulin-like domains D2 and D3 are sufficient for FGF binding. FGFR family members differ from one another in their ligandaffinities and tissue distribution [, ]. Most FGFs can bind to several different FGFR subtypes. Indeed, FGF1 is sometimes referred to as the universal ligand, as it is capable of activating all of the different FGFRs []. However, there are some exceptions. For example, FGF7 only interacts with FGFR2 []and FGF18 was recently shown to only activate FGFR3 []. Fibroblast growth factor receptor 1 (FGFR1) binds both acidic and basic fibroblast growth factors and is involved in limb induction []. FGFR1 has been shown to be associated with Pfeiffer syndrome [], and cleft lip and/or palate [, ]. Fibroblast growth factor receptor 1 has been shown to interact with growth factor receptor-bound protein 14 (GRB14) [], Src homology 2 domain containing adaptor protein B (SHB) [], fibroblast growth factor receptor substrate 2 (FRS2)[]and fibroblast growth factor 1 (FGF1) [, ].This entry represents the catalytic domain of FGFR1. |
|
•
•
•
•
•
|
| Publication |
| First Author: |
Still IH |
| Year: |
1999 |
| Journal: |
Genomics |
| Title: |
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