SEY1 protein (Saccharomyces cerevisiae) - STRING interaction network
"SEY1" - GTPase with a role in ER morphology in Saccharomyces cerevisiae
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second shell of interactors
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proteins of unknown 3D structure
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some 3D structure is known or predicted
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Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
protein homology
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Gene Fusion
SEY1GTPase with a role in ER morphology; interacts physically and genetically with Yop1p and Rtn1p; possible functional ortholog of mammalian atlastins, defects in which cause a form of hereditary spastic paraplegia; homolog of Arabidopsis RHD3; Cooperates with the reticulon proteins RTN1 and RTN2 and the tubule-shaping DP1 family protein YOP1 to generate and maintain the structure of the tubular endoplasmic reticulum network. Has GTPase activity, which is required for its function in ER organization (776 aa)    
Predicted Functional Partners:
Membrane protein that interacts with Yip1p to mediate membrane traffic; interacts with Sey1p to maintain ER morphology; overexpression leads to cell death and accumulation of internal cell membranes; Involved in membrane/vesicle trafficking (180 aa)
Putative protein of unknown function; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm and is induced in response to the DNA-damaging agent MMS; Plays a role in tubular endoplasmic reticulum network formation and maintenance. Works in conjunction with the ER shaping proteins (reticulons RTN1 and RTN2, YOP1), and in antagonism to SEY1 to maintain the network in a dynamic equilibrium. May counterbalance SEY1-directed polygon formation by promoting polygon loss through ring closure (278 aa)
Homodimeric protein that is packaged into COPII vesicles; cycles between the ER and Golgi; involved in secretory transport but not directly required for aspects of transport assayed in vitro; may influence membrane composition; Nonessential protein required for the fusion of ER- derived transport vesicles with the Golgi complex. Can be replaced by SFT2 (138 aa)
Integral endoplasmic reticulum membrane protein that stimulates Sar1p GTPase activity; involved in COPII vesicle budding through disassociation of coat proteins from membranes onto liposomes; binds Sec16p; similar to Sec12p; Putative guanine nucleotide-exchange factor (GEF) involved in the formation or budding of transport vesicles from the ER. Positive regulator of SAR1 probably through inhibition of the GTPase activation by SEC23 (1065 aa)
Protein required for inositol prototrophy, identified as an ortholog of the FIT family of proteins involved in triglyceride droplet biosynthesis; disputed role in the synthesis of inositol phospholipids from inositol; Appears to be involved in the synthesis of inositol phospholipids from inositol (380 aa)
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)
Diacylglycerol kinase, localized to the endoplasmic reticulum (ER); overproduction induces enlargement of ER-like membrane structures and suppresses a temperature-sensitive sly1 mutation; contains a CTP transferase domain; Involved in pre-tRNA splicing (By similarity). CTP- dependent diacylglycerol kinase that catalyzes the phosphorylation of diacylglycerol (DAG) to phosphatidate (PA). Controls phosphatidate levels at the nuclear envelope. Counteracts the activity of PAH1/SMP2. Involved in the resistance to nickel chloride and nalidixic acid. May be involved in vesicle trafficking betw [...] (290 aa)
ER membrane protein that interacts with Sey1p to maintain ER morphology; interacts with exocyst subunit Sec6p, with Yip3p, and with Sbh1p; null mutant has an altered ER morphology; member of the RTNLA (reticulon-like A) subfamily (295 aa)
Membrane glycoprotein v-SNARE involved in retrograde transport from the Golgi to the ER; required for N- and O-glycosylation in the Golgi but not in the ER; interacts with the Dsl1p complex through Tip20p; SNARE required for targeting and fusion of Golgi-derived retrograde transport vesicles with the ER (383 aa)
t-SNARE required for retrograde vesicular traffic and homotypic ER membrane fusion; forms a complex with the SNAREs Sec22p, Sec20p and Use1p to mediate fusion of Golgi-derived vesicles at the ER; Syntaxin required for targeting and fusion of Golgi- derived retrograde transport vesicles with the ER (346 aa)
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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