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Gene Ontology Classifications
synaptosomal-associated protein 25

Go Annotations as Summary Text (Tabular View) (GO Graph)

GO curators for mouse genes have assigned the following annotations to the gene product of Snap25. (This text reflects annotations as of Tuesday, May 26, 2015.)
Summary from NCBI RefSeq

[Summary is not available for the mouse gene. This summary is for the human ortholog.] 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 this gene. [provided by RefSeq, Jul 2008]
Summary text based on GO annotations supported by experimental evidence in mouse
Summary text based on GO annotations supported by experimental evidence in other organisms
Summary text for additional MGI annotations
  1. Burgalossi A et al. (2010) SNARE protein recycling by alphaSNAP and betaSNAP supports synaptic vesicle priming. Neuron, 68:473-87. (PubMed:21040848)
  2. Corradini I et al. (2014) Epileptiform activity and cognitive deficits in SNAP-25(+/-) mice are normalized by antiepileptic drugs. Cereb Cortex, 24:364-76. (PubMed:23064108)
  3. Ghiani CA et al. (2010) The dysbindin-containing complex (BLOC-1) in brain: developmental regulation, interaction with SNARE proteins and role in neurite outgrowth. Mol Psychiatry, 15:115, 204-15. (PubMed:19546860)
  4. Gorini G et al. (2010) Dynamin-1 co-associates with native mouse brain BKCa channels: proteomics analysis of synaptic protein complexes. FEBS Lett, 584:845-51. (PubMed:20114047)
  5. Hu XQ et al. (2010) Acrosome formation-associated factor is involved in fertilization. Fertil Steril, 93:1482-92. (PubMed:19285662)
  6. Hui E et al. (2009) Synaptotagmin-mediated bending of the target membrane is a critical step in Ca(2+)-regulated fusion. Cell, 138:709-21. (PubMed:19703397)
  7. Jurado S et al. (2013) LTP requires a unique postsynaptic SNARE fusion machinery. Neuron, 77:542-58. (PubMed:23395379)
  8. Kaltenbach LS et al. (2007) Huntingtin interacting proteins are genetic modifiers of neurodegeneration. PLoS Genet, 3:e82. (PubMed:17500595)
  9. Pellet JB et al. (2000) Spatial, temporal and subcellular localization of islet-brain 1 (IB1), a homologue of JIP-1, in mouse brain. Eur J Neurosci, 12:621-32. (PubMed:10712642)
  10. Pooley RD et al. (2006) CytLEK1 is a regulator of plasma membrane recycling through its interaction with SNAP-25. Mol Biol Cell, 17:3176-86. (PubMed:16672379)
  11. Pooley RD et al. (2008) Murine CENPF interacts with syntaxin 4 in the regulation of vesicular transport. J Cell Sci, 121:3413-21. (PubMed:18827011)
  12. Quetglas S et al. (2002) Calmodulin and lipid binding to synaptobrevin regulates calcium-dependent exocytosis. EMBO J, 21:3970-9. (PubMed:12145198)
  13. Roux I et al. (2006) Otoferlin, defective in a human deafness form, is essential for exocytosis at the auditory ribbon synapse. Cell, 127:277-89. (PubMed:17055430)
  14. Sharma M et al. (2012) CSPalpha knockout causes neurodegeneration by impairing SNAP-25 function. EMBO J, 31:829-41. (PubMed:22187053)
  15. Washbourne P et al. (2002) Genetic ablation of the t-SNARE SNAP-25 distinguishes mechanisms of neuroexocytosis. Nat Neurosci, 5:19-26. (PubMed:11753414)
  16. Werner HB et al. (2007) Proteolipid protein is required for transport of sirtuin 2 into CNS myelin. J Neurosci, 27:7717-30. (PubMed:17634366)
  17. Wu CS et al. (2011) Type VI Adenylyl Cyclase Regulates Neurite Extension by Binding to Snapin and Snap25. Mol Cell Biol, 31:4874-86. (PubMed:21986494)
  18. Yun HJ et al. (2013) LRRK2 phosphorylates Snapin and inhibits interaction of Snapin with SNAP-25. Exp Mol Med, 45:e36. (PubMed:23949442)

Go Annotations in Tabular Form (Text View) (GO Graph)

Filter Markers by: Category  Evidence Code 


Gene Ontology Evidence Code Abbreviations:

  EXP Inferred from experiment
  IAS Inferred from ancestral sequence
  IBA Inferred from biological aspect of ancestor
  IBD Inferred from biological aspect of descendant
  IC Inferred by curator
  IDA Inferred from direct assay
  IEA Inferred from electronic annotation
  IGI Inferred from genetic interaction
  IKR Inferred from key residues
  IMP Inferred from mutant phenotype
  IMR Inferred from missing residues
  IPI Inferred from physical interaction
  IRD Inferred from rapid divergence
  ISS Inferred from sequence or structural similarity
  ISO Inferred from sequence orthology
  ISA Inferred from sequence alignment
  ISM Inferred from sequence model
  NAS Non-traceable author statement
  ND No biological data available
  RCA Reviewed computational analysis
  TAS Traceable author statement


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