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ERO1B
Identifiers
Aliases	ERO1B, ERO1LB, Ero1beta, endoplasmic reticulum oxidoreductase beta, endoplasmic reticulum oxidoreductase 1 beta
External IDs	OMIM: 615437; MGI: 1914725; HomoloGene: 8740; GeneCards: ERO1B; OMA:ERO1B - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q42.3 Start 236,214,681 bp End 236,282,019 bp
Gene location (Mouse) Chr. Chromosome 13 (mouse) Band 13|13 A1 Start 12,580,755 bp End 12,626,285 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in body of pancreas islet of Langerhans secondary oocyte body of stomach corpus epididymis beta cell endothelial cell fundus testicle right lobe of liver Top expressed in islet of Langerhans lacrimal gland seminal vesicula spermatocyte spermatid salivary gland pyloric antrum submandibular gland parotid gland left lobe of liver More reference expression data BioGPS More reference expression data
Gene ontology Molecular function unfolded protein binding oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor oxidoreductase activity protein binding protein-disulfide reductase activity protein disulfide isomerase activity Cellular component endoplasmic reticulum membrane endoplasmic reticulum membrane Biological process insulin processing 4-hydroxyproline metabolic process extracellular matrix organization protein folding protein maturation by protein folding glucose homeostasis cell redox homeostasis protein folding in endoplasmic reticulum Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 56605 67475 Ensembl ENSG00000086619 ENSMUSG00000057069 UniProt Q86YB8 Q8R2E9 RefSeq (mRNA) NM_019891 NM_026184 RefSeq (protein) NP_063944 NP_080460 Location (UCSC) Chr 1: 236.21 – 236.28 Mb Chr 13: 12.58 – 12.63 Mb PubMed search
Wikidata
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ERO1-like protein beta is a protein that in humans is encoded by the ERO1LB gene.

Interactions

ERO1LB has been shown to interact with P4HB.

References

1. ^ GRCh38: Ensembl release 89: ENSG00000086619 – Ensembl, May 2017
2. ^ GRCm38: Ensembl release 89: ENSMUSG00000057069 – Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R (August 2000). "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response". The Journal of Biological Chemistry. 275 (31): 23685–92. doi:10.1074/jbc.M003061200. PMID 10818100.
6. "Entrez Gene: ERO1LB ERO1-like beta (S. cerevisiae)".
7. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (February 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". The EMBO Journal. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
8. Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (November 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". The EMBO Journal. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.

Further reading

• Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R (November 2001). "Manipulation of oxidative protein folding and PDI redox state in mammalian cells". The EMBO Journal. 20 (22): 6288–96. doi:10.1093/emboj/20.22.6288. PMC 125306. PMID 11707400.
• Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R (February 2002). "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family". The EMBO Journal. 21 (4): 835–44. doi:10.1093/emboj/21.4.835. PMC 125352. PMID 11847130.
• Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, Kurtz A (May 2003). "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha" (PDF). European Journal of Biochemistry. 270 (10): 2228–35. doi:10.1046/j.1432-1033.2003.03590.x. PMID 12752442. Archived from the original (PDF) on 2021-10-16. Retrieved 2020-09-07.
• Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, Sitia R (July 2004). "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum" (PDF). The Journal of Biological Chemistry. 279 (31): 32667–73. doi:10.1074/jbc.M404992200. PMID 15161913. S2CID 3919247.
• Dias-Gunasekara S, Gubbens J, van Lith M, Dunne C, Williams JA, Kataky R, Scoones D, Lapthorn A, Bulleid NJ, Benham AM (September 2005). "Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta". The Journal of Biological Chemistry. 280 (38): 33066–75. doi:10.1074/jbc.M505023200. PMID 16012172.
• Lewandrowski U, Moebius J, Walter U, Sickmann A (February 2006). "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach". Molecular & Cellular Proteomics. 5 (2): 226–33. doi:10.1074/mcp.M500324-MCP200. PMID 16263699.
• Otsu M, Bertoli G, Fagioli C, Guerini-Rocco E, Nerini-Molteni S, Ruffato E, Sitia R (2006). "Dynamic retention of Ero1alpha and Ero1beta in the endoplasmic reticulum by interactions with PDI and ERp44". Antioxidants & Redox Signaling. 8 (3–4): 274–82. doi:10.1089/ars.2006.8.274. PMID 16677073.
• Dias-Gunasekara S, van Lith M, Williams JA, Kataky R, Benham AM (September 2006). "Mutations in the FAD binding domain cause stress-induced misoxidation of the endoplasmic reticulum oxidoreductase Ero1beta". The Journal of Biological Chemistry. 281 (35): 25018–25. doi:10.1074/jbc.M602354200. PMID 16822866.

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