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NYV1 protein (Saccharomyces cerevisiae) - STRING interaction network
"NYV1" - v-SNARE component of the vacuolar SNARE complex involved in vesicle fusion in Saccharomyces cerevisiae
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second shell of interactors
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proteins of unknown 3D structure
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
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NYV1v-SNARE component of the vacuolar SNARE complex involved in vesicle fusion; inhibits ATP-dependent Ca(2+) transport activity of Pmc1p in the vacuolar membrane; Vacuolar v-SNARE required for docking. Only involved in homotypic vacuole fusion. Required for Ca(2+) efflux from the vacuolar lumen, a required signal for subsequent membrane fusion events, by inhibiting vacuolar Ca(2+)-ATPase PMC1 and promoting Ca(2+) release when forming trans-SNARE assemblies during the docking step (253 aa)    
Predicted Functional Partners:
VAM3
Syntaxin-like vacuolar t-SNARE; functions with Vam7p in vacuolar protein trafficking; mediates docking/fusion of late transport intermediates with the vacuole; has an acidic di-leucine sorting signal and C-terminal transmembrane region; Required for vacuolar assembly. Provides the t-SNARE function in a late step of the vacuolar assembly. Required for homotypic vacuole membrane fusion, autophagy and fusion of biosynthetic transport vesicles with the vacuole. Required for the delivery of alpha-factor receptor-ligand complexes to the vacuole (283 aa)
     
  0.999
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; t-SNARE found in various SNARE complexes involved in multiple transport pathways. The composition of the t-SNARE complexes is specific for a limited number of v-SNAREs and therefore allows only the vesicles carrying the matching v-SNARE to fuse (217 aa)
     
  0.999
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)
     
  0.999
BET1
Type II membrane protein required for vesicular transport between the endoplasmic reticulum and Golgi complex; v-SNARE with similarity to synaptobrevins; SNARE required for targeting and fusion of ER-derived transport vesicles with the Golgi complex (142 aa)
     
  0.999
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)
     
  0.999
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)
     
  0.998
SEC17
Peripheral membrane protein required for vesicular transport between ER and Golgi, the ’priming’ step in homotypic vacuole fusion, and autophagy; stimulates the ATPase activity of Sec18p; has similarity to mammalian alpha-SNAP; SNARE complex protein that binds to cis-SNARE complexes on membranes and is required for vesicular transport between the endoplasmic reticulum and the Golgi apparatus and for homotypic vacuole fusion. During the priming step of membrane fusion, is released from cis-SNARE complexes by SEC18 to establish a pool of unpaired SNAREs, which are required for interactio [...] (292 aa)
     
  0.998
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 (200 aa)
     
  0.997
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)
     
  0.997
VAM7
Vacuolar SNARE protein that functions with Vam3p in vacuolar protein trafficking; has an N-terminal PX domain (phosphoinositide-binding module) that binds PtdIns-3-P and mediates membrane binding; SNAP-25 homolog; Essential for proper morphogenesis of the vacuole. May exist as structural reinforcement on the surface of the vacuolar membrane and be required for maintenance against rupture by osmotic pressure (316 aa)
       
  0.997
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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