| + |
PRKCA |
phosphorylation
|
SNAP25 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249178 |
Ser187 |
RIMEKADsNKTRIDE |
Homo sapiens |
|
| pmid |
sentence |
| 12459461 |
This study establishes that SNAP-25 is differentially phosphorylated by protein kinase C and protein kinase A in neuroendocrine PC12 cells. Using phosphopeptide mapping and site-directed mutagenesis we identified both Thr138 and Ser187 as the targets of SNAP-25 phosphorylation by protein kinase C |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-249179 |
Thr138 |
GGFIRRVtNDARENE |
Homo sapiens |
|
| pmid |
sentence |
| 12459461 |
This study establishes that SNAP-25 is differentially phosphorylated by protein kinase C and protein kinase A in neuroendocrine PC12 cells. Using phosphopeptide mapping and site-directed mutagenesis we identified both Thr138 and Ser187 as the targets of SNAP-25 phosphorylation by protein kinase C |
|
| Publications: |
2 |
Organism: |
Homo Sapiens |
| + |
PRKCA | up-regulates 
phosphorylation
|
SNAP25 |
0.353 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-160313 |
Ser187 |
RIMEKADsNKTRIDE |
Homo sapiens |
Neuron |
| pmid |
sentence |
| 18171919 |
Phosphorylation of snap-25 at ser187 mediates enhancement of exocytosis by a phorbol ester in ins-1 cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
PRKACA |
phosphorylation
|
SNAP25 |
0.326 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-250052 |
Thr138 |
GGFIRRVtNDARENE |
Rattus norvegicus |
PC-12 Cell |
| pmid |
sentence |
| 12459461 |
Thr138 as the exclusive site of SNAP-25 phosphorylation by protein kinase A in vivo. PMA or forskolin treatment alone resulted in dramatic phosphorylation of SNAP-25 Ser187 and/or Thr138 without appreciable neurotransmitter release. |
|
| Publications: |
1 |
Organism: |
Rattus Norvegicus |
| + |
CADPS2 | up-regulates activity
binding
|
SNAP25 |
0.267 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264339 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24363652 |
CAPS interacted independently with either syntaxin-1 or SNAP-25 suggesting that CAPS might promote QaQbc-SNARE heterodimer formation. CAPS binding to syntaxin-1 was mediated by the membrane-proximal C-terminal SNARE motif (H3) and membrane linker domain sequences of syntaxin-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
OPTN | up-regulates quantity by expression 
transcriptional regulation
|
SNAP25 |
0.2 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-259880 |
|
|
Mus musculus |
|
| pmid |
sentence |
| 22194658 |
SiRNA effectively downregulated optineurin expression in RGC-5 and PC12 stable transfected cells. Optineurin siRNA significantly inhibited cell growth and increased apoptosis in RGC-5 and PC12 cells. Microarray analysis identified 112 differentially expressed genes in optineurin siRNA transfected RGC-5 cells. Quantitative real-time PCR and western blot confirmed that the expression of brain-derived neurotrophic factor (Bdnf), neurotrophin-3(Ntf3), synaptosomal-associated protein 25(Snap25), and neurofilament, light polypeptide(Nefl) was significantly downregulated in RGC-5 and PC12 cells transfected with optineurin siRNA. |
|
| Publications: |
1 |
Organism: |
Mus Musculus |
| + |
CADPS | up-regulates activity
binding
|
SNAP25 |
0.37 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-264338 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 24363652 |
CAPS interacted independently with either syntaxin-1 or SNAP-25 suggesting that CAPS might promote QaQbc-SNARE heterodimer formation. CAPS binding to syntaxin-1 was mediated by the membrane-proximal C-terminal SNARE motif (H3) and membrane linker domain sequences of syntaxin-1 |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SNAPIN | up-regulates activity
binding
|
SNAP25 |
0.587 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-261171 |
|
|
Homo sapiens |
SH-SY5Y Cell |
| pmid |
sentence |
| 18167355 |
In the present study, we used yeast two-hybrid analysis to identify a new binding partner of torsinA, the SNARE-associated protein snapin. We have reported that snapin shows a robust interaction with wild type and mutant torsinA. we have demonstrated that this portion of torsinA and/or the adjacent linker region has the additional role of recruiting snapin. we found that snapin, which binds SNAP-25 (synaptosome-associated protein of 25,000 Da) and enhances the association of the SNARE complex with synaptotagmin, is an interacting partner for both wild type and mutant torsinA. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
NSF | down-regulates activity 
binding
|
SNAP25 |
0.727 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263974 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16679567 |
NSF is an important regulator of SNARE assembly/disassembly. NSF binds to SNAP-25, while in complex with other SNAREs, and hydrolyzes adenosine triphosphate to disassemble the SNARE complex down to monomers |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| + |
SYT1 | up-regulates activity
binding
|
SNAP25 |
0.95 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263975 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 16679567 |
Because synaptotagmins bind SNAP-25 and Ca2+, SNAP-25 has also been linked to the Ca2+ dependence of exocytosis (42). One model suggests that synaptotagmin blocks full SNARE fusion pore formation by binding to t-SNAREs.This interaction prevents fusion from occurring in the absence of calcium. When Ca2+ is present, synaptotagmin releases the t-SNAREs so they can fully zipper with the v-SNARE, leading to fusion |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
| + |
SNAP25 | form complex 
binding
|
SNARE_complex |
0.958 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-263967 |
|
|
Homo sapiens |
Neuron |
| pmid |
sentence |
| 30267828 |
The best-studied SNARE-complex is the one formed between three proteins, VAMP2/synaptobrevin-2, syntaxin-1, and SNAP-25, that mediate fast exocytosis in neuronal cells. |
|
| Publications: |
1 |
Organism: |
Homo Sapiens |
| Pathways: | Neurotransmitters release |
3.0
SNAP25
- 
- 