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SEC9 protein (Saccharomyces cerevisiae) - STRING interaction network
"SEC9" - t-SNARE protein important for fusion of secretory vesicles with the plasma membrane in Saccharomyces cerevisiae
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second shell of interactors
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
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textmining
co-expression
protein homology
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SEC9t-SNARE protein important for fusion of secretory vesicles with the plasma membrane; similar to but not functionally redundant with Spo20p; SNAP-25 homolog; Component of a SNARE complex that may be the effector of SEC4 function in exocytosis (651 aa)    
Predicted Functional Partners:
SSO1
Plasma membrane t-SNARE involved in fusion of secretory vesicles at the plasma membrane and in vesicle fusion during sporulation; forms a complex with Sec9p that binds v-SNARE Snc2p; syntaxin homolog; functionally redundant with Sso2p; Required for vesicle fusion with the plasma membrane (290 aa)
       
  0.999
SNC1
Vesicle membrane receptor protein (v-SNARE) involved in the fusion between Golgi-derived secretory vesicles with the plasma membrane; proposed to be involved in endocytosis; member of the synaptobrevin/VAMP family of R-type v-SNARE proteins; SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion (117 aa)
       
  0.999
SNC2
Vesicle membrane receptor protein (v-SNARE) involved in the fusion between Golgi-derived secretory vesicles with the plasma membrane; member of the synaptobrevin/VAMP family of R-type v-SNARE proteins; SNC1 and SNC2 are vesicle-targeting proteins essential for normal secretory traffic between the Golgi and the plasma membrane. They may also be involved in vesicle fusion (115 aa)
       
  0.996
SSO2
Plasma membrane t-SNARE involved in fusion of secretory vesicles at the plasma membrane; syntaxin homolog that is functionally redundant with Sso1p; Required for vesicle fusion with the plasma membrane (295 aa)
       
  0.994
SEC22
R-SNARE protein; assembles into SNARE complex with Bet1p, Bos1p and Sed5p; cycles between the ER and Golgi complex; involved in anterograde and retrograde transport between the ER and Golgi; synaptobrevin homolog; Nonessential SNARE involved in targeting and fusion of ER-derived transport vesicles with the Golgi complex as well as Golgi-derived retrograde transport vesicles with the ER (214 aa)
       
  0.992
MSO1
Probable component of the secretory vesicle docking complex, acts at a late step in secretion; shows genetic and physical interactions with Sec1p; required for prospore membrane formation during sporulation; Involved in secretion. Component of the secretory vesicle docking complex (210 aa)
       
  0.986
BOS1
v-SNARE (vesicle specific SNAP receptor), localized to the endoplasmic reticulum membrane and necessary for vesicular transport from the ER to the Golgi; SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex (244 aa)
         
  0.978
SEC4
Rab family GTPase essential for vesicle-mediated exocytic secretion and autophagy; associates with the exocyst component Sec15p and may regulate polarized delivery of transport vesicles to the exocyst at the plasma membrane; Involved in exocytosis. Maybe by regulating the binding and fusion of secretory vesicles with the cell surface. The GTP- bound form of SEC4 may interact with an effector, thereby stimulating its activity and leading to exocytotic fusion. SEC4 may be an upstream activator of the 19.5S SEC8/SEC15 particle. SEC4 probably interacts directly with SEC8; it could serve as [...] (215 aa)
       
 
  0.974
SED5
cis-Golgi t-SNARE syntaxin required for vesicular transport between the ER and the Golgi complex, binds at least 9 SNARE proteins; Required for vesicular transport between the endoplasmic reticulum and the Golgi complex. Acts as a target organelle soluble NSF attachment protein receptor (t-SNARE) (340 aa)
     
 
  0.969
SPO20
Meiosis-specific subunit of the t-SNARE complex, required for prospore membrane formation during sporulation; similar to but not functionally redundant with Sec9p; SNAP-25 homolog; Required to maintain the prospore membrane to the nucleus during sporulation in order to capture the daughter nuclei and form the spores. Mediates the fusion of exocytic vesicles with the plasma membrane during sporulation through its interactions with the t-SNARE SSO1 and v-SNARE SNC2 (397 aa)
       
0.966
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: Candida robusta, Pachytichospora, S. cerevisiae, Saccharomyces, Saccharomyces capensis, Saccharomyces cerevisiae, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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