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1Q8N4C7_HUMAN*   Trembl (?) | Description Local Annotation Link Reference
General Information
DescriptionSimilar to mouse a030009b12rik protein.
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0016020 membrane (IEA)
0008565 protein transporter activity (IEA)
0006886 intracellular protein transport (IEA)

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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:
The process of vesicular fusion with target membranes depends on a set of SNAREs (SNAP-Receptors).hich are associated with the fusing membranes . Target SNAREs (t-SNAREs) are localised on the target membrane and belong to two different families.he syntaxin-like family and the SNAP-25 like family. One member of each family.ogether with av-SNARE localised on the vesicular required for fusion. The Syntaxins are type-I transmembrane proteins that contain several regions with coiled-coil propensity in their cytosolic part.he SNARE motif. SNAP-25 () is a protein consisting of two coiled-coil regions.hich is associated with the membrane by lipid anchors. SNARE motifs assemble into parallel four helix bundles stabilised by the burial of these hydrophobic helix faces in the bundle core. Monomeric SNARE motifs are disordered so this assembly reaction is accompanied by a dramatic increase in alpha-helical secondary structure . The parallel arrangement of SNARE motifs within complexes bring the transmembrane anchors.nd the two membranes.nto close proximity. Recently.t was shown that the two coiled-coil regions of SNAP-25 andone of the coiled-coil regions of the syntaxins are related . This domain is found in both Syntaxin and SNAP-25 families as well as in other proteins.
  IPR000727:Target SNARE coiled-coil region
Soluble N-ethylmaleimide attachment protein receptor (SNARE) proteins are a family of membrane-associated proteins characterised by an alpha-helical coiled-coil domain called the SNARE motif . These proteins are classified as v-SNAREs and t-SNAREs based on their localisation on vesicle or target membrane; another classification scheme defines R-SNAREs and Q-SNAREs.s based on the conserved arginine or glutamine residue in the centre of the SNARE motif. SNAREs are localised to distinct membrane compartments of the secretory and endocytic trafficking pathways.nd contribute to the specificity of intracellular membrane fusion processes.The t-SNARE domain consists of a 4-helical bundle with a coiled-coil twist. The SNARE motif contributes to the fusion of two membranes. SNARE motifs fall into four classes: homologues of syntaxin 1a (t-SNARE).AMP-2 (v-SNARE).nd the N- and C-terminal SNARE motifs of SNAP-25. It is thought that one member from each class interacts to form a SNARE complex.The SNARE motif represented in this entry is found in the N-terminal domains of certain syntaxin family members: syntaxin 1a.hich is required for neurotransmitter release.yntaxin 6.hich is found in endosomal transport vesicles .east Sso1p .nd Vam3p. yeast syntaxin essential for vacuolar fusion . The SNARE motifs in these proteins share structural similarity.espite having a low level of sequence similarity.
InterPro domains unassigned to SynO:
Syntaxins A and B are nervous system-specific proteins implicated in the docking of synaptic vesicles with the presynaptic plasma membrane. Syntaxins are a family of receptors for intracellular transport vesicles. Each target membrane may be identified by a specific member of the syntaxin family .Members of the syntaxin family .ave a size ranging from30 Kd to 40 Kd; a C-terminal extremity which is highly hydrophobic and anchors the protein on the cytoplasmic surface of cellular membranes; a central.ellconserved region.hich seems to be in a coiled-coil conformation.
  IPR006011:Syntaxin, N-terminal
SequencesProtein: Q8N4C7_HUMAN (294 aa)
mRNA: NM_001001850
Local Annotation
Synapse Ontology
Fusion of intracellular membrane-bound vesicles with the pre-synaptic membrane of the neuronal cell resulting in release of neurotransmitter into the synaptic cleft.
sdb:0049 synaptic vesicle fusion  (Evidence:domains)
priming for exocytosis prepares the calcium-dependent release and may involve partial fusion process. The vesicles are primed and become responsive to calcium.
sdb:0120 priming  (Evidence: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:domains)
sdb:0328 transmitters release and endocytosis  (Evidence:domains)
KO assignmentNot mapped to KEGG
Loci Structure (Details)Loci index, Chromosomal location, Length, Possible relational loci clusterExon1: 305 residues, 95215904-95216816Exon2: 83 residues, 95229900-95230144Exon3: 2 residues, -Jump to Q8N4C7_HUMAN  
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Loci Cluster (Details)Loci: 4621 95215904-95230144 ~-14K 26058(-)Loci: 4620 95075718-95175600 ~-100K 26054(PROS1)(-)Link out to UCSC