| + |
FGFR4 | up-regulates activity 
phosphorylation
|
GLO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276182 |
Tyr136 |
GIAVPDVySACKRFE |
in vitro |
|
| pmid |
sentence |
| 34838714 |
We show that Glo1 activity is promoted by phosphorylation on Tyrosine 136 via multiple kinases. Glo1 Y136 is phosphorylated by multiple different kinases including all members of the Src family. Depletion of multiple different kinases led to a partial reduction in Glo1(Y136) phosphorylation. These included members of the Src family (Src, Yes1, FGR, and the related Abl1), and of the FAK, EPHA, FGFR, and VEGFR families (Figure 2B), suggesting phosphorylation of Glo1 on Y136 by multiple different kinases. In vitro kinase assays revealed that all the members of the Src family, as well as Epha5 and VEGFR3, can efficiently phosphorylate recombinant Glo1 on Y136 (Figure 2C–D). |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FGFR4 | up-regulates
phosphorylation
|
FGFR4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179776 |
Tyr642 |
RGVHHIDyYKKTSNG |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 18670643 |
Binding of fgf to fgf receptors leads to receptor dimerization and subsequent tyrosine autophosphorylation and phosphorylation of target substrates. Autophosphorylation on tyrosine is considered to have at least two functions. One such function is the stimulation of the intrinsic protein tyrosine kinase activity by an allosteric mechanismthis antibody specifically recognizes tyr642/643 in fgfr-4. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-179780 |
Tyr643 |
GVHHIDYyKKTSNGR |
Homo sapiens |
Prostate Gland Cancer Cell |
| pmid |
sentence |
| 18670643 |
Binding of fgf to fgf receptors leads to receptor dimerization and subsequent tyrosine autophosphorylation and phosphorylation of target substrates. Autophosphorylation on tyrosine is considered to have at least two functions. One such function is the stimulation of the intrinsic protein tyrosine kinase activity by an allosteric mechanismthis antibody specifically recognizes tyr642/643 in fgfr-4. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma |
| + |
FGFR4 | up-regulates activity
phosphorylation
|
STAT1 |
0.355 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251141 |
Tyr701 |
DGPKGTGyIKTELIS |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 10918587 |
Activation of Stat1 and Stat3 by FGFR derivatives. Lysates of 293T cells transfected as indicated were analysed by Western blotting using Phospho-Stat1 (Y701) antisera (top) or Stat1 antisera (bottom). (b) The same lysates in (a) were re-examined for phosphorylated Stat3 by Western blotting with Phospho-Stat3 (Y705) (top). all three FGFR family members examined here are able to lead to Stat activation. Expression of the 'TDII-like' derivatives of FGFR1, FGFR3, and FGFR4, as well as myrR1-WT, led to phosphorylation of both Stat1 and Stat3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGFR4 | up-regulates activity
phosphorylation
|
STAT3 |
0.411 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251142 |
Tyr705 |
DPGSAAPyLKTKFIC |
Homo sapiens |
|
| pmid |
sentence |
| 10918587 |
Activation of Stat1 and Stat3 by FGFR derivatives. Lysates of 293T cells transfected as indicated were analysed by Western blotting using Phospho-Stat1 (Y701) antisera (top) or Stat1 antisera (bottom). (b) The same lysates in (a) were re-examined for phosphorylated Stat3 by Western blotting with Phospho-Stat3 (Y705) (top). all three FGFR family members examined here are able to lead to Stat activation. Expression of the 'TDII-like' derivatives of FGFR1, FGFR3, and FGFR4, as well as myrR1-WT, led to phosphorylation of both Stat1 and Stat3. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma |
| + |
FGFR4 | up-regulates activity
phosphorylation
|
FGFR4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251140 |
Tyr754 |
LLAVSEEyLDLRLTF |
in vitro |
|
| pmid |
sentence |
| 8576110 |
Analysis of the major autophosphorylation site Y754F mutant of FGFR-4 showed that binding of p85 and its serine phosphorylation were independent of receptor autophosphorylation at this site. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| Pathways: | Rhabdomyosarcoma |
| + |
FGF1 | up-regulates
binding
|
FGFR4 |
0.821 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18454 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1385111 |
Our results establish an fgf binding profile for fgfr-4 with afgf having the highest affinity, followed by k-fgf/hst-1 and bfgf. In addition, fgf-6 was found to bind to fgfr-4 in ligand competition experiments. Ligands binding to fgfr-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma |
| + |
PAX7-FOXO1 | up-regulates quantity by expression 
transcriptional regulation
|
FGFR4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251565 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
Several deregulated signalling pathways enhance cell growth by modulating cell-cycle regulatory factors in RMS. The most frequently affected signalling pathways include the insulin-like growth factor (IGF), fibroblast growth factor (FGF), hepatocyte growth factor, and platelet-derived growth factor. In ARMS, PAX-FOXO1 activates these pathways by transcriptional activation of receptor genes including IGFR1, FGFR4, MET (c-Met), and PDGFRA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGF4 | up-regulates
binding
|
FGFR4 |
0.659 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18567 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1385111 |
Our results establish an fgf binding profile for fgfr-4 with afgf having the highest affinity, followed by k-fgf/hst-1 and bfgf. In addition, fgf-6 was found to bind to fgfr-4 in ligand competition experiments. Ligands binding to fgfr-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
nintedanib | down-regulates activity 
chemical inhibition
|
FGFR4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-257803 |
|
|
in vitro |
|
| pmid |
sentence |
| 18559524 |
In this report, we describe the preclinical profile of BIBF 1120, a combined VEGFR, FGFR, and PDGFR inhibitor currently entering phase III clinical studies in non–small cell lung carcinoma and other cancers. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
BGJ-398 | down-regulates
chemical inhibition
|
FGFR4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-190272 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| Other |
|
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGFR4 | up-regulates activity
phosphorylation
|
FRS2 |
0.673 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-242661 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 9182757 |
In this report, we demonstrate that FGF stimulation induces tyrosine phosphorylation of a novel lipid anchored docking protein, termed FRS2, that forms a complex with Grb2/Sos, thus linking FGF-receptor activation to the Ras/MAPK signaling pathway. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
FGF2 | up-regulates
binding
|
FGFR4 |
0.812 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18564 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1385111 |
Our results establish an fgf binding profile for fgfr-4 with afgf having the highest affinity, followed by k-fgf/hst-1 and bfgf. In addition, fgf-6 was found to bind to fgfr-4 in ligand competition experiments. Ligands binding to fgfr-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAX3-FOXO1 | up-regulates quantity by expression
transcriptional regulation
|
FGFR4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251569 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
Several deregulated signalling pathways enhance cell growth by modulating cell-cycle regulatory factors in RMS. The most frequently affected signalling pathways include the insulin-like growth factor (IGF), fibroblast growth factor (FGF), hepatocyte growth factor, and platelet-derived growth factor. In ARMS, PAX-FOXO1 activates these pathways by transcriptional activation of receptor genes including IGFR1, FGFR4, MET (c-Met), and PDGFRA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAX3 | up-regulates quantity by expression
transcriptional regulation
|
FGFR4 |
0.374 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251572 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 25211658 |
FGFR4 is a transcriptional target of PAX3 and the PAX3-FOXO1 fusion protein found in ARMS. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Rhabdomyosarcoma |
| + |
FGF6 | up-regulates
binding
|
FGFR4 |
0.722 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-18570 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 1385111 |
Our results establish an fgf binding profile for fgfr-4 with afgf having the highest affinity, followed by k-fgf/hst-1 and bfgf. In addition, fgf-6 was found to bind to fgfr-4 in ligand competition experiments. Ligands binding to fgfr-4 induced receptor autophosphorylation and phosphorylation of a set of cellular polypeptides. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
ponatinib | down-regulates activity
chemical inhibition
|
FGFR4 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259280 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 23468082 |
Ponatinib is an oral multitargeted kinase inhibitor that potently inhibits all 4 members of the FGFR family. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
FGFR4
- 
- 