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.

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.

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.

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.

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.

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 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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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 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.

Syntaxin UFE1; t-SNARE protein required for retrograde vesicular traffic; involved in Sey1p-independent homotypic ER fusion; required for efficient nuclear fusion during mating; forms a complex with the SNAREs Sec22p, Sec20p and Use1p to mediate fusion of Golgi-derived vesicles at the ER; Belongs to the syntaxin family.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

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.

Syntaxin UFE1; t-SNARE protein required for retrograde vesicular traffic; involved in Sey1p-independent homotypic ER fusion; required for efficient nuclear fusion during mating; forms a complex with the SNAREs Sec22p, Sec20p and Use1p to mediate fusion of Golgi-derived vesicles at the ER; Belongs to the syntaxin family.