ERO1LB

ERO1-like beta (S. cerevisiae)

Identifiers

ERO1LB ; DKFZp779C1042; DKFZp779I0141; FLJ11003

External IDs

OMIM: 615437 MGI: 1914725 HomoloGene: 8740 GeneCards: ERO1LB Gene

Gene ontology
Molecular function	• protein disulfide isomerase activity • protein binding • oxidoreductase activity • oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor • unfolded protein binding
Cellular component	• endoplasmic reticulum • endoplasmic reticulum membrane
Biological process	• protein folding • oxidation-reduction process
Sources: Amigo / QuickGO

RNA expression pattern

More reference expression data

Orthologs

Species

Human

Mouse

ENSG00000086619

ENSMUSG00000057069

RefSeq (mRNA)

RefSeq (protein)

Location (UCSC)

Chr 1:
236.38 – 236.45 Mb

Chr 13:
12.57 – 12.61 Mb

PubMed search

ERO1-like protein beta is a protein that in humans is encoded by the ERO1LB gene.^[1]^[2]

Interactions

ERO1LB has been shown to interact with P4HB.^[3]^[4]

References

↑ Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R (Sep 2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response". J Biol Chem 275 (31): 23685–92. doi:10.1074/jbc.M003061200. PMID 10818100.
↑ "Entrez Gene: ERO1LB ERO1-like beta (S. cerevisiae)".
↑ Anelli, Tiziana; Alessio Massimo; Mezghrani Alexandre; Simmen Thomas; Talamo Fabio; Bachi Angela; Sitia Roberto (Feb 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. (England) 21 (4): 835–44. doi:10.1093/emboj/21.4.835. ISSN 0261-4189. PMC 125352. PMID 11847130.
↑ Mezghrani, A; Fassio A; Benham A; Simmen T; Braakman I; Sitia R (Nov 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. (England) 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. ISSN 0261-4189. PMC 125306. PMID 11707400.

Further reading

Mezghrani A, Fassio A, Benham A et al. (2002). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". EMBO J. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.
Anelli T, Alessio M, Mezghrani A et al. (2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". EMBO J. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Gess B, Hofbauer KH, Wenger RH et al. (2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha". Eur. J. Biochem. 270 (10): 2228–35. doi:10.1046/j.1432-1033.2003.03590.x. PMID 12752442.
Molteni SN, Fassio A, Ciriolo MR et al. (2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum". J. Biol. Chem. 279 (31): 32667–73. doi:10.1074/jbc.M404992200. PMID 15161913.
Gerhard DS, Wagner L, Feingold EA et al. (2004). "The Status, Quality, and Expansion of the NIH Full-Length cDNA Project: The Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
Dias-Gunasekara S, Gubbens J, van Lith M et al. (2005). "Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta". J. Biol. Chem. 280 (38): 33066–75. doi:10.1074/jbc.M505023200. PMID 16012172.
Lewandrowski U, Moebius J, Walter U, Sickmann A (2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach". Mol. Cell Proteomics 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID 16263699.
Otsu M, Bertoli G, Fagioli C et al. (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxid. Redox Signal. 8 (3–4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.
Dias-Gunasekara S, van Lith M, Williams JA et al. (2006). "Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta". J. Biol. Chem. 281 (35): 25018–25. doi:10.1074/jbc.M602354200. PMID 16822866.