+ |
MAPK14 | up-regulates activity
phosphorylation
|
EEA1 |
0.47 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140082 |
Thr1392 |
CSAKNALtPSSKKPV |
Mus musculus |
MEF Cell |
pmid |
sentence |
16138080 |
We found that p38alpha can phosphorylate the rab5 effectors eea1 and rabenosyn-5 on thr-1392 and ser-215, respectively, and these phosphorylation events regulate the recruitment of eea1 and rabenosyn-5 to membranes |
|
Publications: |
1 |
Organism: |
Mus Musculus |
+ |
MAPK14 | up-regulates
phosphorylation
|
EEA1 |
0.47 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-140085 |
|
|
Homo sapiens |
|
pmid |
sentence |
16138080 |
We found that p38alpha can phosphorylate the rab5 effectors eea1 and rabenosyn-5 on thr-1392 and ser-215, respectively, and these phosphorylation events regulate the recruitment of eea1 and rabenosyn-5 to membranes. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
RAB5C | up-regulates activity
binding
|
EEA1 |
0.826 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261266 |
|
|
in vitro |
|
pmid |
sentence |
12493736 |
The Rab5 effector early endosome antigen 1 (EEA1) is a parallel coiled coil homodimer with an N-terminal C(2)H(2) Zn(2+) finger and a C-terminal FYVE domain. Rab5 binds to independent sites at the N and C terminus of EEA1.|The results demonstrate that the C(2)H(2) Zn(2+) finger is both essential and sufficient for the N-terminal interaction with Rab5. |
|
Publications: |
1 |
Organism: |
In Vitro |
+ |
EEA1 | form complex
binding
|
Early Endosome |
0.536 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-260623 |
|
|
Homo sapiens |
|
pmid |
sentence |
19924646 |
Early endosomal antigen-1 (EEA1) is a well-characterized effector of Rab5 and one of the most widely used markers for EE due to its specific localization to this compartment. EEA1, in coordination with members of the SNARE family, is essential for EE fusion in vivo |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PLEKHF2 | up-regulates activity
binding
|
EEA1 |
0.251 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261276 |
|
|
in vitro |
|
pmid |
sentence |
22816767 |
In yeast two-hybrid analysis we identified Phafin2 as a novel interactor of the endosomal-tethering protein EEA1, and Phafin2 colocalized strongly with EEA1 in microdomains of the endosome membrane. Our results suggest that Phafin2 controls receptor trafficking and fluid-phase transport through early endosomes by facilitating endosome fusion in concert with EEA1. |
|
Publications: |
1 |
Organism: |
In Vitro |