| + |
EPHA2 | down-regulates activity 
phosphorylation
|
CLDN4 |
0.494 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262859 |
Tyr208 |
RSAAASNyV |
Chlorocebus aethiops |
|
| pmid |
sentence |
| 16236711 |
EphA2 associates with claudin-4 via their extracellular domains. This association, in turn, leads to phosphorylation of the cytoplasmic carboxyl terminus of claudin-4 at Tyr-208. The tyrosine phosphorylation of claudin-4 attenuates association of claudin-4 with ZO-1, decreasing integration of claudin-4 into sites of cell-cell contact and enhancing paracellular permeability. These results indicate that EphA2 moderates the function of tight junctions via phosphorylation of claudin-4. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
ACP1 | down-regulates activity
dephosphorylation
|
EPHA2 |
0.644 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246031 |
Tyr575 |
RQSPEDVyFSKSEQL |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246035 |
Tyr588 |
QLKPLKTyVDPHTYE |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246039 |
Tyr594 |
TYVDPHTyEDPNQAV |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246027 |
Tyr772 |
EDDPEATyTTSGGKI |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246023 |
Tyr960 |
GHQKRIAySLLGLKD |
in vitro |
|
| pmid |
sentence |
| 21538645 |
The SAM domain tyrosine Y960 which has been implicated in downstream PI3K signaling is dephosphorylated exclusively by HCPTP-B. The activation loop tyrosine (Y772) which directly controls kinase activity is dephosphorylated about six times faster by HCPTP-A. In contrast, the juxtamembrane tyrosines (Y575, Y588 and Y594) which are implicated in both control of kinase activity and downstream signaling are dephosphorylated by both variants with similar rates |
|
| Publications: |
5 |
Organism: |
In Vitro |
| + |
EPHA2 | up-regulates 
phosphorylation
|
EPHA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178169 |
Tyr588 |
QLKPLKTyVDPHTYE |
Homo sapiens |
|
| pmid |
sentence |
| 18387945 |
The binding of ephrin ligands to eph receptors induces the transphosphorylation of the cytoplasmic domains and initiates kinase activity.Taken together, these results suggest that tyr587, tyr593, tyr771, and tyr734 are likely to be autophospho-rylated in vascular endothelial cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178177 |
Tyr735 |
KYLANMNyVHRDLAA |
Homo sapiens |
|
| pmid |
sentence |
| 18387945 |
The binding of ephrin ligands to eph receptors induces the transphosphorylation of the cytoplasmic domains and initiates kinase activity.Taken together, these results suggest that tyr587, tyr593, tyr771, and tyr734 are likely to be autophospho-rylated in vascular endothelial cells. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178181 |
Tyr772 |
EDDPEATyTTSGGKI |
Homo sapiens |
|
| pmid |
sentence |
| 18387945 |
The binding of ephrin ligands to eph receptors induces the transphosphorylation of the cytoplasmic domains and initiates kinase activity.Taken together, these results suggest that tyr587, tyr593, tyr771, and tyr734 are likely to be autophospho-rylated in vascular endothelial cells. |
|
| Publications: |
3 |
Organism: |
Homo Sapiens |
| + |
SRC | up-regulates activity
phosphorylation
|
EPHA2 |
0.426 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-246104 |
Tyr594 |
TYVDPHTyEDPNQAV |
Homo sapiens |
|
| pmid |
sentence |
| 24457997 |
SRC phosphorylates EPHA2 on Tyr594|. It is therefore likely that this phosphorylation site is included in the binding motif of an additional signalling molecule required for cell transformation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHA2 | up-regulates activity
phosphorylation
|
EPHA2 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-178173 |
Tyr594 |
TYVDPHTyEDPNQAV |
Homo sapiens |
|
| pmid |
sentence |
| 18387945 |
The binding of ephrin ligands to eph receptors induces the transphosphorylation of the cytoplasmic domains and initiates kinase activity.Taken together, these results suggest that tyr587, tyr593, tyr771, and tyr734 are likely to be autophospho-rylated in vascular endothelial cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHA2 | up-regulates 
|
PIK3R2 |
0.371 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-35418 |
|
|
Homo sapiens |
T-lymphocyte |
| pmid |
sentence |
| 7982920 |
In keeping with the above observations, activation of eck by its ligand, b61, increased phosphatidylinositol 3-kinase activity |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHB6 | down-regulates activity
binding
|
EPHA2 |
0.392 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-273853 |
|
|
Homo sapiens |
MCF-7 Cell |
| pmid |
sentence |
| 25239188 |
EphB6 is frequently silenced in invasive and metastatic cancers; however, its role in cancer progression is poorly understood. Here we show that EphB6 interacts with EphA2 and suppresses EphA2-mediated promotion of anoikis resistance in MCF7 breast cancer cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
MTA1 | down-regulates quantity by repression 
transcriptional regulation
|
EPHA2 |
0.293 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254242 |
|
|
Homo sapiens |
Breast Epithelial Cell |
| pmid |
sentence |
| 22184117 |
The receptor tyrosine kinase EphA2 is a direct target gene of hypermethylated in cancer 1 (HIC1). we observe that inactivation of endogenous HIC1 through RNA interference in normal breast epithelial cells results in the up-regulation of EphA2 and is correlated with increased cellular migration. chromatin immunoprecipitation (ChIP) and sequential ChIP experiments demonstrate that endogenous HIC1 proteins are bound, together with the MTA1 corepressor, to the EphA2 promoter in WI38 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
CBL | down-regulates quantity by destabilization
binding
|
EPHA2 |
0.618 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-272590 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12496371 |
In our present study, we demonstrate that ligand-mediated stimulation causes EphA2 to be internalized and degraded. The mechanism of this response involves ligand-mediated autophosphorylation of EphA2, which promotes an association between EphA2 and the c-Cbl adaptor protein. We also show that c-Cbl promotes stimulation-dependent EphA2 degradation. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFNA1 | up-regulates
binding
|
EPHA2 |
0.935 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-56901 |
|
|
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 |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-51939 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9330863 |
Receptors of the epha group preferentially interact with glycosylphosphatidylinositol (gpi)-linked ligands (of the ephrin-a subclass, which comprises five ligands), while receptors of the ephb group preferentially interact with transmembrane ligands (of the ephrin-b subclass, which comprises three ligands) (table 1). In either case, binding of a ligand results in eph receptor autophosphorylation on tyrosine residues and activation of the kinase activity of the eph receptor |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
EFNA5 | up-regulates
binding
|
EPHA2 |
0.919 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52467 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9330863 |
Members of the epha subfamily of receptor tyrosine kinases and their ephrin-a ligands have been implicated in the guidance of retinal axons along the anterior-posterior axis of the chick optic tectum. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SLA | down-regulates quantity by destabilization
binding
|
EPHA2 |
0.425 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-262964 |
|
|
Homo sapiens |
JURKAT Cell |
| pmid |
sentence |
| 24457997 |
These data are consistent with a model where SLAP induces Ephrin-independent EPHA2 degradation. | This activity is independent from CBL but requires SLAP SH3 interaction with the ubiquitination factor UBE4A and SLAP SH2 interaction with pTyr594-EPHA2. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
regorafenib | down-regulates activity
chemical inhibition
|
EPHA2 |
0.8 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259210 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 24756792 |
In biochemical in vitro or cell-based assays, Regorafenib or its major human active metabolites M-2 and M-5 inhibited the activity of RET,VEGFR 1-3, KIT, PDGFR-alpha, PDGFR-beta, FGFR1, FGFR2, TIE2, DDR2, TrkA, Eph2A, RAF-1, BRAF, BRAFV600E, SAPK2, PTK5, and Abl at concentrations that can be achieved clinically. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
HIC1 | down-regulates quantity by repression
transcriptional regulation
|
EPHA2 |
0.321 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-254241 |
|
|
Homo sapiens |
Breast Epithelial Cell |
| pmid |
sentence |
| 22184117 |
The receptor tyrosine kinase EphA2 is a direct target gene of hypermethylated in cancer 1 (HIC1). we observe that inactivation of endogenous HIC1 through RNA interference in normal breast epithelial cells results in the up-regulation of EphA2 and is correlated with increased cellular migration. chromatin immunoprecipitation (ChIP) and sequential ChIP experiments demonstrate that endogenous HIC1 proteins are bound, together with the MTA1 corepressor, to the EphA2 promoter in WI38 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFNA2 | up-regulates
binding
|
EPHA2 |
0.81 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-65413 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 10072375 |
Ephrin-a ligands (named ephrin-a1_ephrin-a5) are anchored in the plasma membrane through a gpi-linkage, and each can bind any of the epha subclass of receptors (epha1_epha8) |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EFNA3 | up-regulates
binding
|
EPHA2 |
0.807 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-52309 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 9330863 |
The eph family of receptors. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
EPHA2 | up-regulates
binding
|
SHC1 |
0.594 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-94804 |
|
|
Homo sapiens |
|
| pmid |
sentence |
| 12400011 |
We also show that the interaction of epha2 with grb2 is indirect and mediated by shc and that this complex is necessary for epha2-mediated activation of erk kinases. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
3.0
EPHA2
- 
- 