Activating Compound | Comment | Organism | Structure |
---|---|---|---|
anionic phospholipids | APLs, the enzymatic activity of nSMase2 is dependent on anionic phospholipids, structural requirements for APL-selective binding of nSMase2, overview. nSMase2 interacts specifically and directly with several APLs, including phosphatidylserine and phosphatidic acid. Identification of two discrete APL binding domains in the N terminus of nSMase2, the nSMase2 N-terminal domain is essential for nSMase interaction with APLs | Mus musculus |
Cloned (Comment) | Organism |
---|---|
expression of (E)GFP-fused wild-type nSMase2 and of several (E)GFP-fused truncated mutant nSMase2s possessing additional V5- or FLAG-tags in HEK-293 or MCF-7 cells | Mus musculus |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
plasma membrane | associated via anionic phospholipids binding sites at the enzyme's N-terminus | Mus musculus | 5886 | - |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Mus musculus | - |
- |
- |
Synonyms | Comment | Organism |
---|---|---|
neutral sphingomyelinase 2 | - |
Mus musculus |
nSMase2 | - |
Mus musculus |
General Information | Comment | Organism |
---|---|---|
physiological function | APLs, the enzymatic activity of nSMase2 is dependent on anionic phospholipids, structural requirements for APL-selective binding of nSMase2, overview. nSMase2 interacts specifically and directly with several APLs, including phosphatidylserine and phosphatidic acid. Identification of two discrete APL binding domains in the N terminus of nSMase2, the nSMase2 N-terminal domain is essential for nSMase interaction with APLs. APL binding domains are important for nSMase2 to localize at the plasma membrane | Mus musculus |