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FLASH GENE
Symbol SNAP29 contributors: mct/ - updated : 20-08-2015
HGNC name synaptosomal-associated protein, 29kDa
HGNC id 11133
PROTEIN
PHYSICAL PROPERTIES
STRUCTURE
motifs/domains
  • two soluble NSF attachment protein receptor (SNARE) domains and a asparagine-proline-phenylalanine (NPF motif) at its N terminus
    • HOMOLOGY
    interspecies ortholog to murine Snap25
    Homologene
    FAMILY
  • SNAP-25 family
    • CATEGORY regulatory , transport
    SUBCELLULAR LOCALIZATION     plasma membrane
        intracellular
    intracellular,cytoplasm,organelle,membrane
    intracellular,cytoplasm,organelle,Golgi
    intracellular,cytoplasm,cytosolic,vesicle
    intracellular,cytoplasm,cytoskeleton,microtubule,centrosome
    intracellular,nucleus
    text present at synapses
    basic FUNCTION
  • modulator of synaptic transmission by inhibiting dessassembly of the synaptic core (SNARE) complex
  • acts as a negative modulator for neurotransmitter release, probably by slowing recycling of the SNARE-based fusion machinery and synaptic vesicle turnover
  • importance of SNAP29 mediated membrane fusion in endocytic recycling and consequently, in cell motility
  • synaptosomal-associated SNARE protein
  • novel function of SNAP29 in mast cell phagocytosis, having implications in protection against bacterial infection
  • predicted to mediate vesicle fusion at the endoplasmic reticulum or Golgi membranes
  • major role of SNAP29 in autophagy and secretion
  • STX17, SNAP29, and VAMP8, are potentially essential for the fusion between autophagosomes and lysosomes
  • is a major modifier of variable expressivity in DEL22q11 patients
    • CELLULAR PROCESS
    PHYSIOLOGICAL PROCESS cellular trafficking transport
    text membrane trafficking steps
    PATHWAY
    metabolism
    signaling neurotransmission
    a component
    INTERACTION
    DNA
    RNA
    small molecule
    protein
  • directly with STX1A, competing with NAPA for binding to the SNARE complex
  • interacting with EHD3, EHD1
  • RAB3A, RAB24, and septin 4 bind to the N-terminal domain of SNAP29
  • interacts with several syntaxins and with the EH domain containing protein EHD1
  • STX17 interacts with SNAP29 and the lysosomal SNARE VAMP8, and all of these proteins are required for autophagosome-lysosome fusion
  • OGT mediates O-GlcNAcylation of the SNARE protein SNAP29 and regulates autophagy in a nutrient-dependent manner
  • interacts with SNARE proteins, localizes to multiple trafficking organelles, and is required for protein trafficking and for proper Golgi apparatus morphology
  • ATG14 binds to the SNARE core domain of STX17 through its coiled-coil domain, and stabilizes the STX17-SNAP29 binary t-SNARE complex on autophagosomes
  • ATG14-STX17-SNAP29 interaction mediates autophagosome-lysosome tethering and fusion events, thus revealing a novel function of ATG14 in the later steps of the autophagy pathway
  • ATG14 directly binds to the STX17-SNAP29 binary complex on autophagosomes and promotes STX17-SNAP29-VAMP8-mediated autophagosome fusion with lysosomes
    • cell & other
    REGULATION
    ASSOCIATED DISORDERS
    corresponding disease(s) CEDNIK
    Other morbid association(s)
    TypeGene ModificationChromosome rearrangementProtein expressionProtein Function
    constitutional germinal mutation     loss of function
    hemizygous deletions modifying phenotype in 22q11DS patients
    Susceptibility
    Variant & Polymorphism
    Candidate gene
    Marker
    Therapy target
    ANIMAL & CELL MODELS
  • abundance of Snap29 in sciatic nerves was increased during remyelination and in a rat model of Charcot-Marie-Tooth disease, two pathological situations with increased myelin membrane biogenesis