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0VTI1B_HUMAN*   SwissProt (?) | Description Local Annotation Link Reference
General Information
DescriptionVesicle transport through interaction with t-snares homolog 1b (vesicle transport v-snare protein vti1-like 1) (vti1-rp1).
SpeciesHomo sapiens (NCBI taxonomy ID: 9606)
GO0008283 cell proliferation (TAS)
0006944 membrane fusion (TAS)
0006904 vesicle docking during exocytosis (TAS)
0016192 vesicle-mediated transport (TAS)

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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:
A crucial step in membrane fusion is the formation of the SNARE complex in which conserved regions.alled SNARE motifs.rom individual SNAREs associate and twist to form the core complex.hich is an all-parallel coiled coil. The neuronal SNARE complex is a heterotrimer of vesicular (v-) SNARE VAMP-2 and the two target plasma membrane (t-) SNAREssyntaxin 1A and SNAP-25. It has been proposed that SNARE core complex formation proceeds like a zipper.eginning at themembrane-distal region and propagating toward themembrane-proximal end. SNARE complex formation is an energy-releasing process that may supply the required freeenergy for membrane fusion .This family includes the Golgi SNAP receptor (SNARE) complex protein.hich is involved in transport from the endoplasmic reticulum to the golgi apparatus and intra-golgi transport.nd the vesicle transport v-SNARE protein.hat mediates vesicle transport pathways through interaction with T-SNAREs on the target membrane.
  IPR007705:Vesicle transport v-SNARE
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
InterPro domains unassigned to SynO:
The fusion glycoproteins from this family are found in ssRNA negative-strand viruses.This protein directs fusion of viral and cellular membranes.esulting in viral penetration.nd can direct fusion of infected cells with adjoining cells.esulting in the formation ofsyncytia. The mature form is a dimer of polypeptides F1 and F2 linked by a disulphidebond .
  IPR000776:Fusion glycoprotein F0
Muscle contraction is caused by sliding between the thick and thin filaments of the myofibril. Myosin is a major component of thick filaments and exists as a hexamer of 2 heavy chains . alkali light chains.nd 2 regulatory light chains. The heavy chain can be subdivided into the N-terminal globular head and the C-terminal coiled-coil rod-like tail.lthough some forms have a globular region in their C-terminal. There are many cell-specific isoforms of myosin heavy chains.oded for by a multi-gene family . Myosin interacts with actin to convert chemical energy.n the form of ATP.o mechanical energy . The 3-D structure of the head portion of myosin has been determined and a model for actin-myosin complex has been constructed .This family consists of the coiled-coil myosin heavy chain tail region.The coiled-coil is composed of the tail from two molecules of myosin.These can then assemble into the macromolecular thick filament .The coiled-coil region provides the structural backbone of the thick filament .
  IPR002928:Myosin tail
SequencesProtein: VTI1B_HUMAN (232 aa)
mRNA: NM_006370
Local Annotation
Synapse Ontology
endosome of the presynaptic compartment. A cellular structure that is involved in the transport of proteins in the neuron after the proteins are endocytosed from the outside to the inside of the cell.
sdb:0088 endosome  (Evidence:keywords,domains)
Typical ecretory organelles, some 50 nm in diameter, of presynaptic nerve terminals; accumulate high concentrations of nonpeptide neurotransmitters and secrete these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane.
sdb:0094 typical synaptic vesicle  (Evidence:keywords,domains)
Various stages of the synaptic vesicle cycle, including attachment, prefusion, triggering, recycling and reloading of the vesicles with transmitter.
sdb:0098 synaptic vesicle cycling  (Evidence:keywords,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: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: 112 residues, 67187618-67187951Exon2: 22 residues, 67189906-67189968Exon3: 60 residues, 67192885-67193059Exon4: 66 residues, 67196200-67196392Exon5: 21 residues, 67198946-67199005Exon6: 154 residues, 67210844-67211301Exon7: 2 residues, -Jump to VTI1B_HUMAN  
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Loci Cluster (Details)Loci: 2850 67156331-67188187 ~-32K 11338(ARG2)(+)Loci: 4135 67187618-67211301 ~-24K 11340(VTI1B)(-)Loci: 4136 67213270-67232213 ~-19K 11341(RDH11)(-)Loci: 2849 66777773-66872288 ~-95K 11329(MPP5)(+)Link out to UCSC