| + |
SRC | up-regulates
phosphorylation
|
FLT4 |
0.533 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165035 |
Tyr1063 |
FGLARDIyKDPDYVR |
Homo sapiens |
|
| pmid |
sentence |
| 20431062 |
Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337 vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165039 |
Tyr1333 |
ARGGQVFyNSEYGEL |
Homo sapiens |
|
| pmid |
sentence |
| 20431062 |
Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337, demonstrating that integrin-mediated receptor phosphorylation induces a phosphorylation pattern that is distinct from that induced by growth factors. Furthermore, pull-down assays show that integrin-mediated vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165043 |
Tyr1337 |
QVFYNSEyGELSEPS |
Homo sapiens |
|
| pmid |
sentence |
| 20431062 |
Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337, demonstrating that integrin-mediated receptor phosphorylation induces a phosphorylation pattern that is distinct from that induced by growth factors. Furthermore, pull-down assays show that integrin-mediated vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165047 |
Tyr830 |
PLEEQCEyLSYDASQ |
Homo sapiens |
|
| pmid |
sentence |
| 20431062 |
Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337 vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165051 |
Tyr833 |
EQCEYLSyDASQWEF |
Homo sapiens |
|
| pmid |
sentence |
| 20431062 |
Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337, demonstrating that integrin-mediated receptor phosphorylation induces a phosphorylation pattern that is distinct from that induced by growth factors. Furthermore, pull-down assays show that integrin-mediated vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-165055 |
Tyr853 |
HLGRVLGyGAFGKVV |
Homo sapiens |
|
| pmid |
sentence |
| 20431062 |
Vegfr-3 is a direct c-src target and mass spectrometry analysis identified the sites phosphorylated by c-src as tyrosine 830, 833, 853, 1063, 1333, and 1337 vegfr-3 phosphorylation activates the recruitment to the receptor of the adaptor proteins crki/ii and shc inducing activation of jnk. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
FLT4 | up-regulates activity
phosphorylation
|
FLT4 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104072 |
Tyr1230 |
RHSLAARyYNWVSFP |
Homo sapiens |
Aorta Endothelium |
| pmid |
sentence |
| 12881528 |
Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the vegfr-3 carboxyl-terminal tail. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104076 |
Tyr1231 |
HSLAARYyNWVSFPG |
Homo sapiens |
|
| pmid |
sentence |
| 12881528 |
Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the vegfr-3 carboxyl-terminal tail. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104080 |
Tyr1265 |
FPMTPTTyKGSVDNQ |
Homo sapiens |
Aorta Endothelium |
| pmid |
sentence |
| 12881528 |
Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the vegfr-3 carboxyl-terminal tail. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104084 |
Tyr1333 |
ARGGQVFyNSEYGEL |
Homo sapiens |
Aorta Endothelium |
| pmid |
sentence |
| 12881528 |
Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the vegfr-3 carboxyl-terminal tail. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104088 |
Tyr1337 |
QVFYNSEyGELSEPS |
Homo sapiens |
Aorta Endothelium |
| pmid |
sentence |
| 12881528 |
Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the vegfr-3 carboxyl-terminal tail. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-104092 |
Tyr1363 |
TFFTDNSy |
Homo sapiens |
Aorta Endothelium |
| pmid |
sentence |
| 12881528 |
Trans-phosphorylation of activated, dimerized receptor tyrosine kinases is known to be critical for the regulation of kinase activity and for receptor interaction with signal transduction molecules. In this study, we have identified five tyrosyl phosphorylation sites in the vegfr-3 carboxyl-terminal tail. |
|
| Publications: |
6 |
Organism: |
Homo Sapiens |
| + |
FLT4 | up-regulates activity
phosphorylation
|
GLO1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-276180 |
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 |
| + |
FLT4 |
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#0 /home/prisca/signor/relation_result.php(2084): implode()
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