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0SNAG_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
NameNAPG
DescriptionGamma-soluble nsf attachment protein (snap-gamma) (n-ethylmaleimide- sensitive factor attachment protein, gamma).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0005624 membrane fraction (NAS)
0005739 mitochondrion (IDA)
0005515 protein binding (IPI)
0006891 intra-Golgi transport (TAS)
0006944 membrane fusion (TAS)
0006461 protein complex assembly (NAS)
0050821 protein stabilization (NAS)

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schematic display of those terms with internal associations, click the node and browse the corresponding GO term
Domain Architecture (Details)
InterPro domains assigned to SynO:
Regulated exocytosis of neurotransmitters and hormones.s well as intracellular traffic.equires fusion of two lipid bilayers. SNARE proteins are thought to form a protein bridge.he SNARE complex.etween an incoming vesicle and the acceptor compartment. SNARE proteins contribute to the specificity of membrane fusion.mplying that the mechanisms by which SNAREs are targeted to subcellular compartments are important for specific docking and fusion of vesicles. This mechanism involves a family of conserved proteins.embers of which appear to function at all sites of constitutive and regulated secretion in eukaryotes . Among them are 2 types of cytosolic protein.SF (N-ethyl-maleimide-sensitive protein) and the SNAPs (alpha-.eta- and gamma-soluble NSF attachment proteins). The yeast vesicular fusion protein.ec17. cytoplasmic peripheral membrane protein involved in vesicular transport between theendoplasmic reticulum and the golgi apparatus.hows a high degree of sequence similarity to the alpha-SNAP family. SNAP-25 and its non-neuronal homologue Syndet/SNAP-23 are synthesized as soluble proteins in the cytosol. Both SNAP-25 and Syndet/SNAP-23 are palmitoylated at cysteine residues clustered in a loopbetween two N- and C-terminal coils and palmitoylation is essential for membrane binding and plasma membrane targeting. The C-terminal and the N-terminal helices of SNAP-25.re each targeted to the plasma membrane by two distinct cysteine-rich domains and appear to regulate the availability of SNAP to form complexes with SNARE .
  IPR000744:NSF attachment protein
InterPro domains unassigned to SynO:
This domain consists of a multi-helical fold comprised of two curved layers of alpha helices arranged in a regular right-handed superhelix.here the repeats that make up this structure are arranged about a common axis . These superhelical structures present an extensive solvent-accessible surface that is well suited to binding large substrates such as proteins and nucleic acids. This topology has been found with a number of repeats and domains.ncluding the tetratricopeptide repeat (TPR) (found in kinesin light chains.NAP regulatory proteins.lathrin heavy chains and bacterial aspartyl-phosphate phosphatases).nd the pentatricopeptide repeat (PPR) (RNA-processing proteins). The TRP is likely to be an ancient repeat.ince it is found in eukaryotes.acteria and archaea.hereas the PPR repeat is found predominantly in higher plants. The superhelix formed from these repeats can bind ligands at a number of different regions.nd has the ability to acquire multiple functional roles .
  IPR011990:Tetratricopeptide-like helical
IPR000744:NSF 
Evalue:-0.481486052274704 
Location:74-85IPR000744:NSFATTACHMNT 
Evalue:0 
Location:224-244IPR000744:NSFATTACHMNT 
Evalue:0 
Location:30-49
SequencesProtein: SNAG_HUMAN (312 aa)
mRNA: NM_003826
Local Annotation
Synapse Ontology
mitochondria are frequently observed in the vicinity of the synaptic vesicle clusters, in agreement with the ATP requirement of several steps of the vesicle cycle.
sdb:0118 mitochondria  (Evidence:keywords,domains)
attachment of the vesicle filled with transmitters involves a specific interaction between the vesicle membrane and the presynaptic active zone.
sdb:0148 docking  (Evidence:keywords,domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 42 residues, 10516030-10516155Exon2: 24 residues, 10520766-10520834Exon3: 30 residues, 10522707-10522792Exon4: 8 residues, 10523532-10523550Exon5: 12 residues, 10524462-10524493Exon6: 38 residues, 10529758-10529868Exon7: 24 residues, 10529984-10530051Exon8: 25 residues, 10530325-10530396Exon9: 28 residues, 10536322-10536401Exon10: 28 residues, 10538295-10538375Exon11: 45 residues, 10538963-10539093Exon12: 101 residues, 10540073-10540371Exon13: 2 residues, -Jump to SNAG_HUMAN  
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