NP_001028036.1
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
NCBI Official Full Name
synaptosomal-associated protein 25
NCBI Official Synonym Symbols
NCBI Protein Information
synaptosomal-associated protein 25; synaptosomal-associated 25 kDa protein; synaptosomal-associated protein 25 isoform SNAP25B
UniProt Protein Name
Synaptosomal-associated protein 25
UniProt Synonym Protein Names
Synaptosomal-associated 25 kDa protein
UniProt Synonym Gene Names
UniProt Entry Name
SNP25_MACMU
UniProt Comments for SNAP25
Function: t-SNARE involved in the molecular regulation of neurotransmitter release. May play an important role in the synaptic function of specific neuronal systems. Associates with proteins involved in vesicle docking and membrane fusion. Regulates plasma membrane recycling through its interaction with CENPF
By similarity.
Subunit structure: Part of the SNARE core complex containing SNAP25, VAMP2 and STX1A. This complex binds CPLX1. Interacts with CENPF, TRIM9, RIMS1, SNAPIN, OTOF and HGS. Binds STXBP6. Found in a ternary complex with STX1A and VAMP8. Found in a complex containing SYT1, SV2B and syntaxin-1. Associates with the BLOC-1 complex. Interacts with BLOC1S6
By similarity. Interacts with EQTN
By similarity.
Subcellular location: Cytoplasm › perinuclear region
By similarity. Cell membrane; Lipid-anchor
By similarity. Cell junction › synapse › synaptosome
By similarity. Note: Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region
By similarity.
Post-translational modification: Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association
By similarity.
Sequence similarities: Belongs to the SNAP-25 family.Contains 2 t-SNARE coiled-coil homology domains.
Research Articles on SNAP25
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Pathways associated with SNAP25 recombinant protein
Diseases associated with SNAP25 recombinant protein
Organs/Tissues associated with SNAP25 recombinant protein
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