STRING protein interaction network
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:
some 3D structure is known or predicted
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
protein homology
Your Input:
Gene Fusion
SNC1Synaptobrevin 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 (117 aa)    
Predicted Functional Partners:
Essential t-SNARE that mediates fusion of vesicles with the late Golgi; forms a complex with Tlg2p and Vti1p; mediates fusion of endosome-derived vesicles with the late Golgi; binds the docking complex VFT (Vps fifty-three) through interaction with Vps51p; Belongs to the syntaxin family
t-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
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
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
t-SNARE affecting a late Golgi compartment protein 2; Syntaxin-like t-SNARE; forms a complex with Tlg1p and Vti1p and mediates fusion of endosome-derived vesicles with the late Golgi; required along with VPS45 for an early step of the constitutive CVT pathway; interactions with Vps45 prevents Tlg2p degradation, and facilitates t-SNARE complex formation; homologous to mammalian SNARE protein syntaxin 16 (Sx16)
Sporulation-specific protein 20; Meiosis-specific subunit of the t-SNARE complex; required for prospore membrane formation during sporulation; similar to but not functionally redundant with Sec9p; binds to phosphatidic acid; SNAP-25 homolog
t-SNARE VTI1; Protein involved in cis-Golgi membrane traffic; v-SNARE that interacts with two t-SNARES, Sed5p and Pep12p; required for multiple vacuolar sorting pathways; human homolog VTI1A can complement yeast null mutant; Belongs to the VTI1 family
Synaptobrevin homolog YKT6; Vesicle membrane protein (v-SNARE) with acyltransferase activity; involved in trafficking to and within the Golgi, endocytic trafficking to the vacuole, and vacuolar fusion; membrane localization due to prenylation at the carboxy-terminus; human homolog YKT6 can complement yeast ykt6 mutant; Belongs to the synaptobrevin family
Integral membrane protein SED5; cis-Golgi t-SNARE syntaxin; required for vesicular transport between the ER and the Golgi complex; binds at least 9 SNARE proteins
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
Your Current Organism:
Saccharomyces cerevisiae
NCBI taxonomy Id: 4932
Other names: ATCC 18824, Candida robusta, NRRL Y-12632, S. cerevisiae, Saccharomyces capensis, Saccharomyces italicus, Saccharomyces oviformis, Saccharomyces uvarum var. melibiosus, lager beer yeast, yeast
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