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:
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Gene Fusion
Cooccurrence
Coexpression
Experiments
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Textmining
[Homology]
Score
SEC9t-SNARE protein required for secretory vesicle-plasma membrane fusion; similar to but not functionally redundant with Spo20p; interacts non-exocyst bound Sec6p; SNAP-25 homolog. (651 aa)    
Predicted Functional Partners:
SNC1
Synaptobrevin homolog 1; 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 has a paralog, SNC2, that arose from the whole genome duplication.
   
 0.999
SEC6
Essential 88kDa subunit of the exocyst complex; the exocyst mediates polarized targeting and tethering of post-Golgi secretory vesicles to active sites of exocytosis at the plasma membrane prior to SNARE-mediated fusion; anchors the assembled complex to sites of secretion; interacts with SM-like protein and SNARE regulator Sec1p and may recruit it to sites of secretion; binds to SNARE complexes binteracting with Sec9p.
   
 
 0.999
SNC2
Synaptobrevin homolog 2; Vesicle membrane receptor protein (v-SNARE); involved in the fusion between Golgi-derived secretory vesicles with the plasma membrane; Snc2p levels regulated by Vps45p; member of the synaptobrevin/VAMP family of R-type v-SNARE proteins; SNC2 has a paralog, SNC1, that arose from the whole genome duplication.
   
 0.999
SSO1
Protein 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; SSO1 has a paralog, SSO2, that arose from the whole genome duplication.
   
 0.999
SRO7
Lethal(2) giant larvae protein homolog SRO7; Effector of Rab GTPase Sec4p; forms a complex with Sec4p and t-SNARE Sec9p; involved in exocytosis and docking and fusion of post-Golgi vesicles with plasma membrane; regulates cell proliferation and colony development via the Rho1-Tor1 pathway; homolog of Drosophila lgl tumor suppressor; SRO7 has a paralog, SRO77, that arose from the whole genome duplication; Belongs to the WD repeat L(2)GL family.
   
 
 0.999
SSO2
Protein SSO2; Plasma membrane t-SNARE; involved in fusion of secretory vesicles at the plasma membrane; syntaxin homolog that is functionally redundant with Sso1p; SSO2 has a paralog, SSO1, that arose from the whole genome duplication.
   
 0.998
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.
    
 0.996
MSO1
Protein MSO1; Lipid-interacting protein in SNARE complex assembly machinery; acts at late step in secretion; interacts with membranes through two distinct binding sites; shows genetic and physical interactions with Sec1p; required for prospore membrane formation during sporulation; N-terminus closely associates with plasma membrane, C-terminus colocalizes with Sec4p on intracellular membranes; relocalizes from bud neck to nucleus upon DNA replication stress.
    
 0.995
SEC1
Sm-like protein involved in docking and fusion of exocytic vesicles; binds to assembled SNARE complexes at the membrane and stimulates membrane fusion; localization to sites of secretion (bud neck and bud tip) is dependent on SNARE function; interacts directly with essential exocyst subunit Sec6p.
   
 
 0.994
SEC17
Alpha-soluble NSF attachment protein; Alpha-SNAP cochaperone; SNARE-complex adaptor for Sec18 (NSF) during the disassembly of postfusion cis-SNARE complexes; stimulates the ATPase activity of Sec18p; peripheral membrane protein required for vesicular transport between ER and Golgi, the 'priming' step in homotypic vacuole fusion, and autophagy; similar to mammalian alpha-SNAP.
   
 0.993
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, Mycoderma cerevisiae, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, yeast
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