+ |
BMX | up-regulates activity
phosphorylation
|
RUFY1 |
0.619 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262678 |
Tyr389 |
TKVELETyKQTRQGL |
Chlorocebus aethiops |
|
pmid |
sentence |
11877430 |
Etk interacts with RUFY1 through its SH3 and SH2 domains. RUFY1 is tyrosine-phosphorylated and appears to be a substrate of Etk. Phosphorylation of the two tyrosine residues, Tyr-281 and Tyr-292, located in the linker region of the two coiled-coil domains by Etk seems to be critical for RUFY1 targeting to the endosomes. |
|
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-262679 |
Tyr400 |
RQGLDEMySDVWKQL |
Chlorocebus aethiops |
|
pmid |
sentence |
11877430 |
Etk interacts with RUFY1 through its SH3 and SH2 domains. RUFY1 is tyrosine-phosphorylated and appears to be a substrate of Etk. Phosphorylation of the two tyrosine residues, Tyr-281 and Tyr-292, located in the linker region of the two coiled-coil domains by Etk seems to be critical for RUFY1 targeting to the endosomes. |
|
Publications: |
2 |
Organism: |
Chlorocebus Aethiops |
+ |
RAB14 | up-regulates activity
relocalization
|
RUFY1 |
0.615 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261279 |
|
|
Homo sapiens |
HeLa Cell |
pmid |
sentence |
20534812 |
Here, we have demonstrated that Rab14 interacts with RUFY1, previously identified as a Rab4 effector, and is required for RUFY1 recruitment onto endosomes and efficient recycling of Tfn. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB4A | up-regulates activity
binding
|
RUFY1 |
0.667 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261280 |
|
|
Homo sapiens |
|
pmid |
sentence |
20534812 |
Here, we have demonstrated that Rab14 interacts with RUFY1, previously identified as a Rab4 effector, and is required for RUFY1 recruitment onto endosomes and efficient recycling of Tfn.|We also found that enlargement of early endosomes mediated by RUFY1 requires its interaction with Rab4 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |