+ |
LRRK2 | up-regulates activity
phosphorylation
|
NSF |
0.375 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-277196 |
Thr645 |
RKLLIIGtTSRKDVL |
Homo sapiens |
HEK-293T Cell |
pmid |
sentence |
26758690 |
LRRK2 phosphorylates full-length NSF at threonine 645 in the ATP binding pocket of D2 domain. Functionally, NSF phosphorylated by LRRK2 displays enhanced ATPase activity and increased rate of SNARE complex disassembling. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
PTPN9 | down-regulates
dephosphorylation
|
NSF |
0.422 |
Identifier |
Residue |
Sequence |
Organism |
Cell Line |
SIGNOR-128348 |
Tyr83 |
QEIEVSLyTFDKAKQ |
Homo sapiens |
|
pmid |
sentence |
15322554 |
Our results suggest that the molecular mechanism by which ptp-meg2 promotes secretory vesicle fusion involves the local release of nsf from a tyrosine-phosphorylated, inactive state. |
|
Publications: |
1 |
Organism: |
Homo Sapiens |
+ |
NSF | down-regulates activity
binding
|
SNAP25 |
0.746 |
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 |