| + |
SYNJ1 | up-regulates activity 
binding
|
MYO1E |
0.44 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-265423 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 17257598 |
We describe binding of two PRD-containing endocytic proteins, dynamin and synaptojanin-1, to the SH3 domain of Myo1E. This interaction was detected both in vitro, using pull-downs of purified proteins, and in vivo, using immunoprecipitation of protein complexes from synapse-enriched brain extract and immunolocalization of Myo1E and dynamin. Our observation of the interaction between human Myo1E and endocytic proteins suggests that this longtailed myosin may play a role in clathrin-dependent endocytosis.Interaction between Myo1E SH3 domain and PRD-containing endocytic proteins may promote recruitment of Myo1E to clathrin-coated structures since an inactivating mutation in the SH3 domain reduced Myo1E localization to clathrin-containing puncta. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Tissue: |
Brain |
| + |
EPHB2 | down-regulates 
phosphorylation
|
SYNJ1 |
0.544 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-135274 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 15821731 |
Ephb2 causes tyrosine phosphorylation in the proline-rich domain of synaptojanin 1, and inhibits both the interaction with endophilin and the 5'-phosphatase activity of synaptojanin 1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PAK5 | up-regulates activity
phosphorylation
|
SYNJ1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263026 |
|
|
in vitro |
|
| pmid |
sentence |
| 22371566 |
We identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
AP-2 complex | up-regulates activity
binding
|
SYNJ1 |
0.495 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-260396 |
|
|
Rattus norvegicus |
|
| pmid |
sentence |
| 15496985 |
Some of the more minor interactors are very strongly enriched (AAK, auxilin, Dab2, eps15, epsin1 and synaptojanin170). All these enriched proteins have multiple copies of short alpha‐appendage interaction motifs |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PAK6 | up-regulates activity
phosphorylation
|
SYNJ1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263022 |
|
|
in vitro |
|
| pmid |
sentence |
| 22371566 |
We identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
| + |
PAK4 | up-regulates activity
phosphorylation
|
SYNJ1 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263024 |
|
|
in vitro |
|
| pmid |
sentence |
| 22371566 |
We identified two novel Pak5 substrates, Pacsin1 and Synaptojanin1, proteins that directly interact with one another to regulate synaptic vesicle endocytosis and recycling. Pacsin1 and Synaptojanin1 were phosphorylated by Pak5 and the other group II Paks in vitro, and Pak5 phosphorylation promoted Pacsin1-Synaptojanin1 binding both in vitro and in vivo. |
|
| Publications: |
1 |
Organism: |
In Vitro |
3.0
SYNJ1
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