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SEC28 protein (Saccharomyces cerevisiae) - STRING interaction network
"SEC28" - Epsilon-COP subunit of the coatomer in Saccharomyces cerevisiae
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SEC28Epsilon-COP subunit of the coatomer; regulates retrograde Golgi-to-ER protein traffic; stabilizes Cop1p, the alpha-COP and the coatomer complex; non-essential for cell growth; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. The coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (296 aa)    
Predicted Functional Partners:
COP1
Alpha subunit of COPI vesicle coatomer complex, which surrounds transport vesicles in the early secretory pathway; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (1201 aa)
     
  0.999
SEC27
Essential beta’-coat protein of the COPI coatomer, involved in ER-to-Golgi and Golgi-to-ER transport; contains WD40 domains that mediate cargo selective interactions; 45% sequence identity to mammalian beta’-COP; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of di [...] (889 aa)
     
  0.998
SEC26
Essential beta-coat protein of the COPI coatomer, involved in ER-to-Golgi protein trafficking and maintenance of normal ER morphology; shares 43% sequence identity with mammalian beta-coat protein (beta-COP); The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysi [...] (973 aa)
     
  0.998
RET3
Zeta subunit of the coatomer complex (COPI); COPI coats Golgi-derived transport vesicles; involved in retrograde transport between Golgi and ER; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (189 aa)
     
  0.998
RET2
Delta subunit of the coatomer complex (COPI); COPI coats Golgi-derived transport vesicles; involved in retrograde transport between Golgi and ER; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (By similarity) (546 aa)
     
  0.997
SEC21
Gamma subunit of coatomer, a heptameric protein complex that together with Arf1p forms the COPI coat; involved in ER to Golgi transport of selective cargo; The coatomer is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non- clathrin-coated vesicles, which further mediate biosynthetic protein transport from the ER, via the Golgi up to the trans Golgi network. Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins (935 aa)
     
  0.996
VID24
Peripheral membrane protein located at Vid (vacuole import and degradation) vesicles; regulates fructose-1,6-bisphosphatase (FBPase) targeting to the vacuole; promotes proteasome-dependent catabolite degradation of FBPase; Has a role in the negative regulation of gluconeogenesis. Required for both proteasome-dependent and vacuolar catabolite degradation of fructose-1,6-bisphosphatase (FBPase). Probably regulates FBPase targeting from the FBPase- containing vesicles to the vacuole (362 aa)
       
 
  0.898
APL2
Beta-adaptin, large subunit of the clathrin-associated protein (AP-1) complex; binds clathrin; involved in clathrin-dependent Golgi protein sorting; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. The AP-1 complex interacts directly with clathrin (726 aa)
     
  0.887
APL1
Beta-adaptin, large subunit of the clathrin associated protein complex (AP-2); involved in vesicle mediated transport; similar to mammalian beta-chain of the clathrin associated protein complex; Adaptins are components of the adaptor complexes which link clathrin to receptors in coated vesicles. Clathrin-associated protein complexes are believed to interact with the cytoplasmic tails of membrane proteins, leading to their selection and concentration. Beta adaptin is a subunit of the plasma membrane adaptor (700 aa)
     
  0.887
SEC13
Component of the Nup84 nuclear pore sub-complex, the Sec13p-Sec31p complex of the COPII vesicle coat, and the SEA (Seh1-associated) complex; required for vesicle formation in ER to Golgi transport and nuclear pore complex organization; the Nup84 sub /.../x has a role in transcription elongation; Functions as a component of the nuclear pore complex (NPC) and the COPII coat. It is one of 5 proteins constituting the COPII coat, which is involved in anterograde (ER to Golgi) double- membrane transport vesicle formation. First the small GTPase SAR1, activated by and binding to the integral [...] (297 aa)
     
 
  0.860
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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