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SNAP25 Protein, Antibody, ELISA Kit, cDNA Clone

SNAP25 Related Areas

SNAP25 Related Pathways

SNAP25 Related Product

    SNAP25 Summary & Protein Information

    SNAP25 Background

    Gene Summary: Synaptic vesicle membrane docking and fusion is mediated by SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors) located on the vesicle membrane (v-SNAREs) and the target membrane (t-SNAREs). The assembled v-SNARE/t-SNARE complex consists of a bundle of four helices, one of which is supplied by v-SNARE and the other three by t-SNARE. For t-SNAREs on the plasma membrane, the protein syntaxin supplies one helix and the protein encoded by this gene contributes the other two. Therefore, this gene product is a presynaptic plasma membrane protein involved in the regulation of neurotransmitter release. Two alternative transcript variants encoding different protein isoforms have been described for SNAP25 gene. [provided by RefSeq, Jul 2008]
    General information above from NCBI
    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 (By similarity). Associates with the BLOC-1 complex. Isoform 1 and isoform 2 interact with BLOC1S6. Interacts with EQTN (By similarity).
    Subcellular location: Cytoplasm, perinuclear region (By similarity). Cell membrane; Lipid-anchor. Cell junction, synapse, synaptosome. Note=Membrane association requires palmitoylation. Expressed throughout cytoplasm, concentrating at the perinuclear region (By similarity).
    Tissue specificity: Neurons of the neocortex, hippocampus, piriform cortex, anterior thalamic nuclei, pontine nuclei, and granule cells of the cerebellum.
    Post-translational: Palmitoylated. Cys-85 appears to be the main site, and palmitoylation is required for membrane association (By similarity).
    Sequence similarity: Belongs to the SNAP-25 family.
    Contains 2 t-SNARE coiled-coil homology domains.C
    General information above from UniProt

    Synaptosomal-associated protein 25, also known as Super protein, Synaptosomal-associated 25 kDa protein, SNAP25 and SNAP, is a cytoplasm and cell membrane protein which belongs to the SNAP-25 family. SNAP25 / SUP contains 2 t-SNARE coiled-coil homology domains. SNAP25 / SUP is a membrane bound protein anchored to the cytosolic face of membranes via palmitoyl side chains in the middle of the molecule. SNAP25 / SUP protein is a component of the SNARE complex, which is proposed to account for the specificity of membrane fusion and to directly execute fusion by forming a tight complex that brings the synaptic vesicle and plasma membranes together. SNAP25 / SUP is a Q-SNARE protein contributing two α-helices in the formation of the exocytotic fusion complex in neurons where it assembles with syntaxin-1 and synaptobrevin. SNAP25 / SUP is involved in the molecular regulation of neurotransmitter release. It may play an important role in the synaptic function of specific neuronal systems. SNAP25 / SUP associates with proteins involved in vesicle docking and membrane fusion. SNAP25 / SUP regulates plasma membrane recycling through its interaction with CENPF. SNAP25 / SUP inhibits P/Q- and L-type voltage-gated calcium channels located presynaptically and interacts with the synaptotagmin C2B domain in Ca2+-independent fashion. In glutamatergic synapses SNAP25 / SUP decreases the Ca2+ responsiveness, while it is naturally absent in GABAergic synapses.

    SNAP25 Alternative Name

    bA416N4.2,dJ1068F16.2,FLJ23079,RIC4,RIC-4,SEC9,SNAP,SNAP25,SNAP-25, [human]
    Bdr,RP23-142F14.2,Snap25,SNAP-25,sp, [mouse]

    SNAP25 Related Studies

  • Hodel A ,et al.,1998, Int. J. Biochem. Cell Biol. 30 (10): 1069-73.
  • Sudhof TC, et al.,2002, Nat Rev Neurosci 3 (8): 641-653.
  • Chapman ER et al.,2002, Nat. Rev. Mol. Cell Biol. 3(7): 498-508.
  • Chen X., et al., 2002, Neuron 33:397-409.
  • Huang Q., et al., 2008, FEBS Lett. 582:1431-1436.
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