ERO1 protein (Saccharomyces cerevisiae) - STRING interaction network
"ERO1" - Thiol oxidase required for oxidative protein folding in the endoplasmic reticulum in Saccharomyces cerevisiae
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Predicted Interactions
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Gene Fusion
ERO1Thiol oxidase required for oxidative protein folding in the endoplasmic reticulum; Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 probably involves elect [...] (563 aa)    
Predicted Functional Partners:
Protein disulfide isomerase; multifunctional protein resident in the endoplasmic reticulum lumen, essential for the formation of disulfide bonds in secretory and cell-surface proteins, unscrambles non-native disulfide bonds; forms a complex with Mnl /.../t has exomannosidase activity, processing unfolded protein-bound Man8GlcNAc2 oligosaccharides to Man7GlcNAc2 which promotes degradation in the unfolded protein response; Protein disulfide isomerase of ER lumen required for formation of disulfide bonds in secretory and cell-surface proteins and which unscrambles non-native disulfide bon [...] (522 aa)
Protein disulfide isomerase of the endoplasmic reticulum lumen, function overlaps with that of Pdi1p; may interact with nascent polypeptides in the ER; Probably interacts with nascent polypeptides in the endoplasmic reticulum. It is an essential gene only in the absence of PDI. Its native disulfide isomerase activity is very low (517 aa)
Flavin-linked sulfhydryl oxidase localized to the endoplasmic reticulum lumen, involved in disulfide bond formation within the ER; FAD-dependent sulfhydryl oxidase that catalyzes disulfide bond formation in the endoplasmic reticulum lumen in parallel to ERO1 (196 aa)
Phospholipid hydroperoxide glutathione peroxidase induced by glucose starvation that protects cells from phospholipid hydroperoxides and nonphospholipid peroxides during oxidative stress; May constitute a glutathione peroxidase-like protective system against oxidative stresses (167 aa)
Thiol peroxidase that functions as a hydroperoxide receptor to sense intracellular hydroperoxide levels and transduce a redox signal to the Yap1p transcription factor; Involved in oxidative stress response and redox homeostasis. Functions as a sensor and transducer of hydroperoxide stress. In response to hydroperoxide stress it oxidizes (activates) the transcription activator YAP1, which is involved in transcription activation of genes of the oxidative stress response pathway. May also play a direct role in hydroperoxide scavenging, being the most active of three closely related S.cere [...] (163 aa)
ATPase involved in protein import into the ER, also acts as a chaperone to mediate protein folding in the ER and may play a role in ER export of soluble proteins; regulates the unfolded protein response via interaction with Ire1p; Probably plays a role in facilitating the assembly of multimeric protein complexes inside the ER. Is required for secretory polypeptide translocation. May physically associate with SEC63 protein in the endoplasmic reticulum and this interaction may be regulated by ATP hydrolysis (682 aa)
Member of the protein disulfide isomerase (PDI) family, exhibits chaperone activity; overexpression suppresses the lethality of a pdi1 deletion but does not complement all Pdi1p functions; undergoes oxidation by Ero1p; Non essential disulfide isomerase, which participates in the folding of proteins containing disulfide bonds. May be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. Able to fold proteins by being directly oxidized by ERO1 (277 aa)
Basic leucine zipper (bZIP) transcription factor (ATF/CREB1 homolog) that regulates the unfolded protein response, via UPRE binding, and membrane biogenesis; ER stress-induced splicing pathway facilitates efficient Hac1p synthesis; Transcriptional activator involved in the unfolded protein response (UPR) pathway. Recognizes and binds to the UPR element (UPRE) in the promoter of UPR-regulated genes such as KAR2, PDI1, EUG1 and FKB2. Increases the synthesis of endoplasmic reticulum-resident proteins required for protein folding as well as components of the secretory pathway (238 aa)
Serine-threonine kinase and endoribonuclease; transmembrane protein that mediates the unfolded protein response (UPR) by regulating Hac1p synthesis through HAC1 mRNA splicing; Kar2p binds inactive Ire1p and releases from it upon ER stress; Senses unfolded proteins in the lumen of the endoplasmic reticulum via its N-terminal domain which leads to enzyme auto- activation. The active endoribonuclease domain splices HAC1 precursor mRNA to produce the mature form which then induces transcription of UPR target genes (1115 aa)
ER protein with chaperone and co-chaperone activity, involved in retention of resident ER proteins; has a role in recognizing proteins targeted for ER-associated degradation (ERAD), member of the protein disulfide isomerase family; Acts as a membrane-bound chaperone in endoplasmic reticulum quality control. Probably facilitates presentation of substrate to membrane-bound components of the degradation machinery (701 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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