| + |
FGR | up-regulates activity 
phosphorylation
|
KCND3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276394 |
Tyr108 |
GKLHYPRyECISAYD |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 22198508 |
These results indicate that Y108 (for Src-family kinases) and Y136 (for EGFR kinase) are involved in the tyrosine phosphorylation of hKv4.3 channels. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGR | up-regulates activity
phosphorylation
|
GLO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276188 |
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 |
| + |
FGR |
phosphorylation
|
HCLS1 |
0.447 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251144 |
Tyr222 |
MEAPTTAyKKTTPIE |
in vitro |
|
| pmid |
sentence |
| 10066823 |
We have now identified tyrosine 222 as the HS1 residue phosphorylated by the Src family protein kinases c-Fgr and Lyn. this interaction is weakened by phosphorylation of Tyr-222, through an allosteric mechanism that ultimately causes the detachment of fully phosphorylated HS1 from c-Fgr. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FGR | down-regulates activity 
phosphorylation
|
TBK1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276725 |
Tyr354 |
SSNQELIyEGRRLVL |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 28618271 |
The Src family kinases (SFKs) Lck, Hck, and Fgr directly phosphorylate TBK1 at Tyr354/394, to prevent TBK1 dimerization and activation. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276722 |
Tyr394 |
LNTIGLIyEKISLPK |
Homo sapiens |
HEK-293T Cell |
| pmid |
sentence |
| 28618271 |
The Src family kinases (SFKs) Lck, Hck, and Fgr directly phosphorylate TBK1 at Tyr354/394, to prevent TBK1 dimerization and activation. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
FGR | down-regulates activity
phosphorylation
|
IKBKG |
0.332 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276368 |
Tyr374 |
PLPPAPAyLSSPLAL |
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 23131831 |
Either IKKγ/NEMO WT or the Y374F mutant was coexpressed with each member of the Src family protein tyrosine kinases (SF-PTKs) in HEK 293T cells. Our study thus demonstrates that the Y374 or S377 residue located at the C-terminal proline-rich domain of human IKKγ/NEMO undergoes phosphorylation upon TNF-α treatment or KvFLIP expression, respectively, resulting in the suppression of IKKγ/NEMO activity to induce NF-κB activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
FGR | up-regulates activity
phosphorylation
|
FGR |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251143 |
Tyr412 |
RLIKDDEyNPCQGSK |
in vitro |
|
| pmid |
sentence |
| 8612628 |
Autophosphorylation of c-Fgr under basal conditions involves Tyr-400 (homologous of c-Src Tyr-416) but not, to any appreciable extent, Tyr-511. Both Tyr-511 and Tyr-400, however, incorporate phosphate if autophosphorylation is performed in the presence of polycationic peptides, such as polylysine, histones H1 and protamines. Such a double phosphorylation induced by polylysine gives rise to an upshifted form of c-Fgr on SDS-PAGE and correlates with a stimulation of catalytic activity instead of a down-regulation |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
CSK | down-regulates activity
phosphorylation
|
FGR |
0.516 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250779 |
Tyr523 |
FTSAEPQyQPGDQT |
in vitro |
|
| pmid |
sentence |
| 7515063 |
CSK catalyzed phosphorylation affects Tyr-511 of c-Fgr, homologous to Tyr-527 of c-Src and it prevents the autophosphorylation normally occurring at c-Fgr Tyr-400, homologous to c-Src Tyr-416. | Once phosphorylated at Tyr-511 and down-regulated by CSK, c-Fgr is no more susceptible to polylysine stimulation. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FGR |
phosphorylation
|
SRC |
0.63 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251145 |
Tyr530 |
FTSTEPQyQPGENL |
in vitro |
|
| pmid |
sentence |
| 9208935 |
An eicosapeptide encompassing the C-terminal tail of c-Src (Tyr527) which is conserved in most Src-related protein kinases, is phosphorylated by C-terminal Src kinase (CSK) and by the two Src-related protein kinases c-Fgr and Lyn, with similar kinetic constants. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
FGR |
phosphorylation
|
SDHA |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262872 |
Tyr543 |
CGKISKLyGDLKHLK |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262873 |
Tyr604 |
YKVRIDEyDYSKPIQ |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Publications: |
2 |
Organism: |
In Vitro |
| + |
FGR |
phosphorylation
|
ACO2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262869 |
Tyr544 |
FDPGQDTyQHPPKDS |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262870 |
Tyr665 |
VVIGDENyGEGSSRE |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262871 |
Tyr71 |
TLSEKIVyGHLDDPA |
in vitro |
|
| pmid |
sentence |
| 17997986 |
Here, we provide evidence that the flavoprotein of succinate dehydrogenase and aconitase are "in vitro" substrates of Fgr tyrosine kinase. Fgr phosphorylates flavoprotein of succinate dehydrogenase at Y535 and Y596 and aconitase at Y71, Y544 and Y665. Further experiments will be necessary to verify if Fgr is the tyrosine kinase responsible for the tyrosine phosphorylation of these proteins in vivo and to elucidate the role of these phosphorylations. |
|
| Publications: |
3 |
Organism: |
In Vitro |
| + |
FGR | up-regulates
phosphorylation
|
PTK2 |
0.532 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94405 |
Tyr925 |
DRSNDKVyENVTGLV |
Homo sapiens |
|
| pmid |
sentence |
| 12387730 |
Phosphorylated on tyrosine residues upon activation. Phosphorylation at tyr-925 is important for interaction with grb2 and depends on the complex formation between fak and the src-kinase fgr. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
midostaurin | down-regulates activity
chemical inhibition
|
FGR |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261976 |
|
|
in vitro |
|
| pmid |
sentence |
| 30069632 |
Midostaurin (PKC412, Rydapt®) is an oral multiple tyrosine kinase inhibitor. Main targets are the kinase domain receptor, vascular endothelial-, platelet derived-, and fibroblast growth factor receptor, stem cell factor receptor c-KIT, as well as mutated and wild-type FLT3 kinase |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
FGR
- 
- 