| + |
EPHA3 | up-regulates activity 
phosphorylation
|
PAK1 |
0.278 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-278398 |
Tyr153 |
TDKSAEDyNSSNALN |
Homo sapiens |
|
| pmid |
sentence |
| 26944939 |
Etk kinase directly phosphorylates and activates PAK1 in response to estrogen.|We demonstrated that estrogen-activated Etk directly phosphorylated PAK1 on Tyr153. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHA3 | up-regulates activity
phosphorylation
|
AR |
0.273 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279370 |
Tyr535 |
MDSYSGPyGDMRLET |
Homo sapiens |
|
| pmid |
sentence |
| 20570899 |
Src and Etk share some common substrates due to the high degree of homology of their kinase domains, thus we examined whether the increased Etk expression could also contribute to AR Y534 phosphorylation.|This is supported by our observations that the association between Etk and AR is increased after castration and Etk induces tyrosine phosphorylation of AR, leading an increase in AR stability and transcriptional activity under androgen depleted conditions. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-279371 |
Tyr552 |
DHVLPIDyYFPPQKT |
Homo sapiens |
|
| pmid |
sentence |
| 20570899 |
These data suggest that Etk may be able to phosphorylate AR at Y534 and Y551/552, and the interaction between the Etk SH2 domain and phosphorylated ARY551/552 may promote their association.|This is supported by our observations that the association between Etk and AR is increased after castration and Etk induces tyrosine phosphorylation of AR, leading an increase in AR stability and transcriptional activity under androgen depleted conditions. |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EPHA3 | up-regulates activity
phosphorylation
|
EPHA3 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251115 |
Tyr596 |
KLPGLRTyVDPHTYE |
Homo sapiens |
|
| pmid |
sentence |
| 11870224 |
Eph receptor activation leads to tyrosine phosphorylation of three major autophosphorylation sites. these residues function to regulate kinase activity, their phosphorylation being required for full intrinsic enzyme activity. these tyrosines (EphA3 Y596, Y602 and Y779) as the prominent autophosphorylation sites of EphA3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251116 |
Tyr602 |
TYVDPHTyEDPTQAV |
Homo sapiens |
|
| pmid |
sentence |
| 11870224 |
Eph receptor activation leads to tyrosine phosphorylation of three major autophosphorylation sites. these residues function to regulate kinase activity, their phosphorylation being required for full intrinsic enzyme activity. these tyrosines (EphA3 Y596, Y602 and Y779) as the prominent autophosphorylation sites of EphA3 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-251117 |
Tyr779 |
EDDPEAAyTTRGGKI |
Homo sapiens |
|
| pmid |
sentence |
| 11870224 |
Eph receptor activation leads to tyrosine phosphorylation of three major autophosphorylation sites. these residues function to regulate kinase activity, their phosphorylation being required for full intrinsic enzyme activity. these tyrosines (EphA3 Y596, Y602 and Y779) as the prominent autophosphorylation sites of EphA3 |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
PTPN1 | down-regulates activity 
dephosphorylation
|
EPHA3 |
0.417 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-248426 |
Tyr779 |
EDDPEAAyTTRGGKI |
Homo sapiens |
|
| pmid |
sentence |
| 21135139 |
Nevertheless, the finding that phosphorylation of the activation loop tyrosine (EphA3-Y779), a recently identified PTP1B substrate (Mertins et al., 2008), is essential for ligand-induced endocytosis (Janes et al., 2009) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHA3 | up-regulates
binding
|
CRK |
0.625 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-115335 |
|
|
Homo sapiens |
HEK-293 Cell |
| pmid |
sentence |
| 11870224 |
Our results suggest that recruitment of crkii and activation of rho signalling are responsible for epha3-mediated cell rounding, blebbing and de-adhesion, and that ephrin-a5-mediated receptor clustering and epha3 tyrosine kinase activity are essential for this response |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFNA1 | up-regulates
binding
|
EPHA3 |
0.816 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52005 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9330863 |
Transmembrane ligands for eph receptors also exhibit properties of signal transducing molecules, suggesting that bidirectional signaling occurs when receptor-expressing cells contact ligand-expressing cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56904 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9576626 |
Ephrin-a1 binds and activates the tyrosine kinase activity of eph-a2, and has a dissociation constant of 20_30 nm. ephrin-a1 interacts with all the other epha subclass receptors as well, although with different affinity |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EPHA3 | up-regulates
binding
|
SRC |
0.527 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-58139 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 9632142 |
We propose src kinase as a downstream effector that mediates the neuron's response to eph receptor activation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFNA5 | up-regulates
binding
|
EPHA3 |
0.943 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52470 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9330863 |
Highly promiscuous for ephrin-a ligands it binds preferentially efna5 and became active. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFNA3 | up-regulates
binding
|
EPHA3 |
0.803 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52312 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9330863 |
The activation of eph receptors by their ligands, which are membrane-anchored molecules, involves a cell-cell recognition event that often causes cell repulsion. transmembrane ligands for eph receptors also exhibit properties of signal transducing molecules, suggesting that bidirectional signaling occurs when receptor-expressing cells contact ligand-expressing cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
4.0
EPHA3
- 
- 