| Annotated protein: | Synaptosomal-associated protein 25 (SNAP-25) (Super protein) (SUP) (Synaptosomal-associated 25 kDa protein). Gene symbol: SNAP25. Taxonomy: Rattus norvegicus (Rat). Uniprot ID: P60881 |
| antibody wiki: | |
| SynGO gene info: | SynGO data @ SNAP25 |
| Ontology domain: | Cellular Component |
| SynGO term: | anchored component of presynaptic membrane (GO:0099026) |
| Synapse type(s): | hippocampus |
| Annotated paper: | Garcia EP, et al. "rbSec1A and B colocalize with syntaxin 1 and SNAP-25 throughout the axon, but are not in a stable complex with syntaxin" J Cell Biol. 1995 Apr;129(1):105-20 PMID:7698978 |
| Figure(s): | Fig. 3 - Fig. 4 |
| Annotation description: | In this study, Garcia et al. performed electron microscopy on fragmented neurons obtained from rat brain and performed immunoelectron microscopy for SNAP-25. They observed labeling of the cytoplasmic surfaces of plasma membranes and found that SNAP-25 is widely distributed along the axonal and synaptic plasmalemma and it is not enriched on the synaptic vesicle membrane (Fig. 3). Moreover, they performed sub-cellular fractionation of rat brain and found that the distribution of SNAP-25 resembles that of syntaxin and the bona-fide membrane marker Na+/K+ ATPase (Fig. 4). 5/2/2018 Pim "SNAP-25 is annotated as anchored protein because it has a palmitoylation site. Upon palmitoylation, SNAP25 is targeted to plasma mebrane and binds to it more stabley (see Gonzalo et al. (1998) Mol Biol Cell. Mar; 9(3): 585-597. (PMID: 9487128)." |
| Evidence tracking, Biological System: | Intact tissue |
| Evidence tracking, Protein Targeting: | Antibody (detection) |
| Evidence tracking, Experiment Assay: | Electron Microscopy Western blot Biochemical fractionation (generic) |
| Annotator(s): | Momchil Ninov (ORCID:0000-0002-0808-7003) Mahdokht Kohansalnodehi (ORCID:0000-0002-3898-5197) Reinhard Jahn (ORCID:0000-0003-1542-3498) |
| Lab: | Department of Neurobiology, Max Planck Institute for Biophysical Chemistry, 37077 Göttingen, Germany |
| Additional literature: | In this paper, using 3H-palmitic acid labeling revealed that SNAP-25 is modified by covalent addition of fatty acid. It was suggested that long-chain fatty acylation of SNAP-25 contributes to its membrane association. @ PMID:1281490 In this study, Prescott et al found that differential splicing of SNAP25 results in two splice variants, SNAP25a and SNAP25b that are different by 9 amino acids. Three of non-conserved residues occur within the cysteine-rich domain. Therefore, it was suggested that this can alter the configuration of the palmitoylated cysteines and consequently modified the subcellular licalization of SNAP-25. @ PMID:21526988 In this paper, the combination of EM imaging and the subcellular fraction was used to investigate the localization of SNAP-25. Using subcellular fractionation, it was shown that 3% of the total pool of SNAP-25 binds to coated and uncoated SVs (Fig. 1-2 and 5). @ PMID:7860636 |
| SynGO annotation ID: | 274 |
| Dataset release (version): | 20231201 |
| View annotation as GO-CAM model: |  |