STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
aex-4t-SNARE protein aex-4; t-SNARE protein which regulates the secretion of aex-5 from intestinal cells. Involved in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds; Belongs to the SNAP-25 family. (234 aa)    
Predicted Functional Partners:
syx-3
Putative syntaxin-3; Potentially involved in docking of synaptic vesicles at presynaptic active zones (By similarity). Acts in the intestine to regulate anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP).
   
 0.915
snap-1
SNAP (Soluble NSF Attachment Protein) homolog.
   
 0.900
syx-6
Putative syntaxin 6; Potentially involved in docking of synaptic vesicles at presynaptic active zones; Belongs to the syntaxin family.
    
 0.843
syx-17
t-SNARE coiled-coil homology domain-containing protein.
   
 0.832
aex-1
C2 domain-containing protein aex-1; Involved in retrograde signaling from post-synaptic cells to pre-synaptic neurons, probably by regulating vesicle exocytosis in post-synaptic cells. Acts in muscles, to regulate the localization of synaptic vesicle fusion protein unc-13 likely during vesicle exocytosis and thus regulate retrograde signaling at the neuromuscular junction (NMJ). Regulates anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP). Probably by regulating DMP, plays a homeostatic role in the uptake of triglycerides. Regulat [...]
   
  
 0.817
sec-22
Yeast SEC homolog; Belongs to the synaptobrevin family.
    
 0.816
syx-4
Putative syntaxin-4; Potentially involved in docking of synaptic vesicles at presynaptic active zones.
   
 0.815
aex-5
Endoprotease aex-5; Probable serine endoprotease which cleaves preproteins at paired basic amino acids. May process FMRFamide-like (flp) and neuropeptide-like protein (nlp) neuropeptides. In muscles, involved in neuronal retrograde signaling by regulating presynaptic activity and localization of synaptic vesicle fusion protein unc-13 at the neuromuscular junction (NMJ). Acts in the intestine to regulate anterior body muscle contractions (aBOC) and the expulsion steps during the defecation motor program (DMP). Probably by regulating DMP, required for fatty acid uptake by intestinal cell [...]
   
  
 0.810
aex-2
G-protein coupled receptor aex-2; G-protein coupled receptor for the nlp-40 neuropeptide. The activity of this receptor is mediated by G proteins which activate adenylyl cyclase. Plays a role in the defecation motor program, which is a coordinated series of three muscle contractions that occurs every 45 seconds. Specifically, acts in GABAergic neurons, such as AVL and DVB, to control the expulsion step of defecation. Required for fatty acid uptake and metabolism by intestinal cells and therefore regulates the levels of triglycerides in the intestine.
      
 0.809
syx-7
t-SNARE coiled-coil homology domain-containing protein; Belongs to the syntaxin family.
   
 0.795
Your Current Organism:
Caenorhabditis elegans
NCBI taxonomy Id: 6239
Other names: C. elegans, Rhabditis elegans, roundworm
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