| + |
PICK1 | up-regulates activity 
relocalization
|
BNC1 |
0.31 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-223414 |
|
|
Rattus norvegicus |
Neuron |
| pmid |
sentence |
| 11802773 |
we found that the PDZ domain-containing protein PICK1 (protein interacting with C kinase) interacts specifically with the C-termini of BNC1 and ASIC. Our studies showing association of recombinant PICK1 with ASIC and BNC1, and the presence of both PICK1 and ASIC in the synaptosomal fraction |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PICK1 | up-regulates activity
binding
|
AMPA |
0.802 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-270236 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 25784538 |
RAB39B directs GluA2 trafficking in neurons. GTP-bound RAB39B interacts with PICK1. In line with evidence that PICK1 can dimerize, the structural model suggests that dimerization of PICK1 is a prerequisite for simultaneous recognition of both RAB39B and GluA2 each by one of the PICK1 molecules in the PICK1 dimer (Fig. 6a–c). The existence of such complex is supported by our co-immunoprecipitation experiments shown above. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
PICK1 | up-regulates activity
relocalization
|
ASIC1 |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-223417 |
|
|
Rattus norvegicus |
Neuron |
| pmid |
sentence |
| 11802773 |
we found that the PDZ domain-containing protein PICK1 (protein interacting with C kinase) interacts specifically with the C-termini of BNC1 and ASIC. Our studies showing association of recombinant PICK1 with ASIC and BNC1, and the presence of both PICK1 and ASIC in the synaptosomal fraction |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
PICK1 | up-regulates activity
binding
|
PRKCA |
0.796 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268178 |
|
|
Rattus norvegicus |
Hippocampal Cell Line |
| pmid |
sentence |
| 16554470 |
We show that protein interacting with C-kinase 1 (PICK1) recruits activated protein kinase Cα (PKCα) to MycUNC5A at the plasma membrane, stimulating its endocytosis. We identify two PKCα phosphorylation sites at serines 408 and 587, as well as dileucine internalization motifs, which are required for this endocytosis. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Pathways: | Axon guidance |
| + |
RAB39B | up-regulates activity
binding
|
PICK1 |
0.39 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264045 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 25784538 |
GTP-bound RAB39B interacts with PICK1. In line with evidence that PICK1 can dimerize, the structural model suggests that dimerization of PICK1 is a prerequisite for simultaneous recognition of both RAB39B and GluA2 each by one of the PICK1 molecules in the PICK1 dimer (Fig. 6a–c). The existence of such complex is supported by our co-immunoprecipitation experiments shown above. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
| + |
UNC5A | up-regulates activity
binding
|
PICK1 |
0.295 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-268181 |
|
|
Rattus norvegicus |
Hippocampal Cell Line |
| pmid |
sentence |
| 16554470 |
Recently, our laboratory showed that UNC5A is coimmunoprecipitated with PICK1 and PKCα. Moreover, we demonstrated that the association of PKCα with UNC5A depends on the activation of PKCα and the ability of UNC5A to bind PICK1 |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| Pathways: | Axon guidance |
| + |
PICK1 | up-regulates activity
binding
|
GRIA2 |
0.802 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264046 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
| pmid |
sentence |
| 25784538 |
RAB39B directs GluA2 trafficking in neurons. GTP-bound RAB39B interacts with PICK1. In line with evidence that PICK1 can dimerize, the structural model suggests that dimerization of PICK1 is a prerequisite for simultaneous recognition of both RAB39B and GluA2 each by one of the PICK1 molecules in the PICK1 dimer (Fig. 6a–c). The existence of such complex is supported by our co-immunoprecipitation experiments shown above. |
|
| Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
3.0
PICK1
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