+ |
EPHB1 | up-regulates activity
phosphorylation
|
NRCAM |
0.423 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262862 |
Tyr1276 |
DGSFIGQySGKKEKE |
Homo sapiens |
HEK-293 Cell |
pmid |
sentence |
24023801 |
EphB receptors were found to induce phosphorylation of NrCAM on the tyrosine residue within the FIGQY ankyrin binding motif, inhibiting ankyrin recruitment. Furthermore, NrCAM phospho-FIGQY levels in the SC were decreased in EphB1/3 and EphB1/2/3 null mice and increased in mutant mice overexpressing constitutively active EphB2 kinase. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
EPHB1 | up-regulates activity
phosphorylation
|
CASKIN1 |
0.287 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262860 |
Tyr296 |
TKDYCNNyDLTSLNV |
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
23181695 |
EphB1 phosphorylates Caskin1 on tyrosine 296 and 336. Tyrosine phosphorylated Caskin1 then likely promotes reorganization of the actin cytoskeleton leading to spine formation. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262861 |
Tyr336 |
TGNDRVGyFPSSLGE |
Chlorocebus aethiops |
|
pmid |
sentence |
23181695 |
EphB1 phosphorylates Caskin1 on tyrosine 296 and 336. Tyrosine phosphorylated Caskin1 then likely promotes reorganization of the actin cytoskeleton leading to spine formation. |
|
Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
+ |
EPHB1 | up-regulates activity
phosphorylation
|
EPHB1 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251122 |
Tyr594 |
GSPGMKIyIDPFTYE |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
12223469 |
Co-immunoprecipitation was used to confirm the interaction of Grb7 with the cytoplasmic domain of EphB1 as well as the full-length receptor in intact cells. This interaction is mediated by the SH2 domain of Grb7 and requires tyrosine autophosphorylation of EphB1. We also found that EphB1 could phosphorylate Grb7 and mutation of either Tyr-928 or Tyr-594 to Phe decreased this activity. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-251123 |
Tyr928 |
SAIKMVQyRDSFLTA |
Cricetulus griseus |
CHO Cell |
pmid |
sentence |
12223469 |
Co-immunoprecipitation was used to confirm the interaction of Grb7 with the cytoplasmic domain of EphB1 as well as the full-length receptor in intact cells. This interaction is mediated by the SH2 domain of Grb7 and requires tyrosine autophosphorylation of EphB1. We also found that EphB1 could phosphorylate Grb7 and mutation of either Tyr-928 or Tyr-594 to Phe decreased this activity. |
|
Publications: |
2 |
Organism: |
Cricetulus Griseus |
+ |
EPHB1 | up-regulates activity
relocalization
|
MAP2K4 |
0.2 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275922 |
|
|
|
|
pmid |
sentence |
26319181 |
The phosphorylated CNK1 interacts with ephrinB1. The binding of ephrinB1 to CNK1 connects RhoA and p115RhoGEF with ephrinB1-associated MKK4, promoting JNK activation and cell migration. |
|
Publications: |
1 |
+ |
CNKSR1 | up-regulates activity
binding
|
EPHB1 |
0.297 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-275921 |
|
|
|
|
pmid |
sentence |
26319181 |
The phosphorylated CNK1 interacts with ephrinB1. The binding of ephrinB1 to CNK1 connects RhoA and p115RhoGEF with ephrinB1-associated MKK4, promoting JNK activation and cell migration. |
|
Publications: |
1 |
+ |
EFNB1 | up-regulates
binding
|
EPHB1 |
0.822 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-111851 |
|
|
Homo sapiens |
|
pmid |
sentence |
11713248 |
We show here that despite its lack of kinase activity, ephb6 undergoes inducible tyrosine phosphorylation upon stimulation with the eph-b receptor subfamily ligand ephrin-b1. Overexpression of a catalytically active member of the eph-b subfamily, ephb1, resulted in increased ephb6 phosphorylation. Ephb1-induced ephb6 phosphorylation was ligand-dependent and required the functional catalytic activity of ephb1. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |