+ |
PRKACA | up-regulates activity
phosphorylation
|
SNAPIN |
0.311 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-250053 |
Ser50 |
HVHAVREsQVELREQ |
|
|
pmid |
sentence |
11283605 |
PKA-phosphorylation of Snapin significantly increases its binding to synaptosomal-associated protein-25 (SNAP-25). Mutation of Snapin serine 50 to aspartic acid (S50D) mimics this effect of PKA phosphorylation |
|
Publications: |
1 |
+ |
LRRK2 | down-regulates
phosphorylation
|
SNAPIN |
0.53 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-202436 |
Thr117 |
NHSVAKEtARRRAML |
Homo sapiens |
Neuron |
pmid |
sentence |
23949442 |
Lrrk2 phosphorylates snapin and inhibits interaction of snapin with snap-25. these data suggest that lrrk2 may regulate neurotransmitter release via control of snapin function by inhibitory phosphorylation. hreonine 117 of snapin is one of the sites phosphorylated by lrrk2 |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
Tissue: |
Brain |
+ |
RNF13 | up-regulates activity
polyubiquitination
|
SNAPIN |
0.537 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-272044 |
|
|
Chlorocebus aethiops |
COS-7 Cell |
pmid |
sentence |
22890573 |
RNF13 directly interacted with snapin, a SNAP-25-interacting protein. Interestingly, snapin was ubiquitinated by RNF13 via the lysine-29 conjugated polyubiquitin chain, which in turn promoted the association of snapin with SNAP-25. Consistently, we found an attenuated interaction between snapin and SNAP-25 in the RNF13-null mice. Therefore, these results suggest that RNF13 is involved in the regulation of the SNARE complex, which thereby controls synaptic function. |
|
Publications: |
1 |
Organism: |
Chlorocebus Aethiops |
+ |
SNAPIN | form complex
binding
|
BLOC-1 |
0.713 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-265935 |
|
|
Homo sapiens |
|
pmid |
sentence |
22203680 |
We show that BLOC-1 is an elongated complex that contains one copy each of the eight subunits pallidin, Cappuccino, dysbindin, Snapin, Muted, BLOS1, BLOS2, and BLOS3. The complex appears as a linear chain of eight globular domains, ∼300 A long and ∼30 A in diameter. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
TOR1A | up-regulates activity
binding
|
SNAPIN |
0.434 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-261170 |
|
|
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 |
+ |
SNAPIN | up-regulates activity
binding
|
SNAP25 |
0.601 |
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 |