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ERV41 protein (Saccharomyces cerevisiae) - STRING interaction network
"ERV41" - Protein localized to COPII-coated vesicles, forms a complex with Erv46p in Saccharomyces cerevisiae
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Predicted Interactions
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ERV41Protein localized to COPII-coated vesicles, forms a complex with Erv46p; involved in the membrane fusion stage of transport; has homology to human ERGIC2 (PTX1) protein; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Ile-Leu motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (352 aa)    
Predicted Functional Partners:
ERV46
Protein localized to COPII-coated vesicles, forms a complex with Erv41p; involved in the membrane fusion stage of transport; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal Phe-Tyr motif is required for exit from the endoplasmic reticulum. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (415 aa)
     
 
0.925
DER1
Endoplasmic reticulum membrane protein, required for ER-associated protein degradation of misfolded or unassembled proteins; N- and C- termini protrude into the cytoplasm, has similarity to Dfm1p; Component of the endoplasmic reticulum-associated degradation (ERAD) pathway. Specifically required for the ERAD-L pathway which mediates the degradation of proteins with misfolded lumenal domains within the endoplasmic reticulum (211 aa)
     
 
  0.873
HRD3
ER membrane protein that plays a central role in ERAD; forms HRD complex with Hrd1p and ER-associated protein degradation (ERAD) determinants that engages in lumen to cytosol communication and coordination of ERAD events; Component of the endoplasmic reticulum quality control (ERQC) system involved in ubiquitin-dependent degradation of missfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane proteins with misfolded lumenal domains (ERAD [...] (833 aa)
       
 
  0.872
USA1
Scaffold subunit of the Hrd1p ubiquitin ligase; also promotes ligase oligomerization; involved in ER-associated protein degradation (ERAD); interacts with the U1 snRNP-specific protein, Snp1p; Scaffold protein of the endoplasmic reticulum-associated degradation (ERAD) (also known as endoplasmic reticulum quality control, ERQC) pathway involved in ubiquitin-dependent degradation of misfolded endoplasmic reticulum proteins. Component of the HRD1 ubiquitin ligase complex, which is part of the ERAD-L and ERAD-M pathways responsible for the rapid degradation of soluble lumenal and membrane [...] (838 aa)
       
      0.868
SPC1
Subunit of the signal peptidase complex (SPC), which cleaves the signal sequence from proteins targeted to the endoplasmic reticulum (ER), homolog of the SPC12 subunit of mammalian signal peptidase complex; Nonessential component of the signal peptidase complex (SPC), which catalyzes the cleavage of N-terminal signal sequences of proteins targeted to the endoplasmic reticulum. Signal peptide cleavage occurs during the translocation (cotranslationally or post-translationally) through the translocon pore into the endoplasmic reticulum. SPC3 is not required for signal peptidase activity (94 aa)
       
 
  0.824
ERV29
Protein localized to COPII-coated vesicles, involved in vesicle formation and incorporation of specific secretory cargo; Constituent of COPII-coated endoplasmic reticulum- derived transport vesicles. Required for efficient transport of a subset of secretory proteins to the Golgi. The C-terminal di- lysine motif is required for exit from the endoplasmic reticulum. Required directly for packaging glycosylated pro-alpha-factor into COPII vesicles. Facilitates retrograde transport from the Golgi to the endoplasmic reticulum (310 aa)
     
 
  0.795
SEC28
Epsilon-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)
     
 
  0.795
ROT2
Glucosidase II catalytic subunit required for normal cell wall synthesis; mutations in rot2 suppress tor2 mutations, and are synthetically lethal with rot1 mutations; Catalytic subunit of glucosidase 2, which cleaves sequentially the 2 innermost alpha-1,3-linked glucose residues from the Glc(2)Man(9)GlcNAc(2) oligosaccharide precursor of immature glycoproteins (954 aa)
       
 
  0.793
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)
     
      0.777
SVP26
Integral membrane protein of the early Golgi apparatus and ER; involved in COP II vesicle transport; may also function to promote retention of proteins in the early Golgi compartment; Plays a role in retention of a subset of membrane proteins in the early Golgi compartments. Facilitates endoplasmic reticulum to Golgi transport of mannosyltransferases MNN2 and MNN5 (228 aa)
       
 
  0.762
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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