ERO1LB

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
Enzyme activity
Gene location (Human)
Chr.	Chromosome 1 (human)
End	236,282,019 bp
Gene location (Mouse)
Chr.	Chromosome 13 (mouse)
End	12,626,285 bp
RNA expression pattern
	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
	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
	56605
	67475
	ENSG00000086619
	ENSMUSG00000057069
	Q86YB8
	Q8R2E9
	NM_019891
	NM_026184
	NP_063944
	NP_080460
	Wikidata
View/Edit Human	View/Edit Mouse

ERO1-like protein beta is a protein that in humans is encoded by the ERO1LB gene.^[5]^[6]

Interactions

ERO1LB has been shown to interact with P4HB.^[7]^[8]

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000086619 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000057069 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ 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.
↑ "Entrez Gene: ERO1LB ERO1-like beta (S. cerevisiae)".
↑ 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.
↑ 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.

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.

This article on a gene on human chromosome 1 is a stub. You can help Wikipedia by adding missing information.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000086619 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 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.

[pmid10818100-5] 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.

[entrez-6] "Entrez Gene: ERO1LB ERO1-like beta (S. cerevisiae)".

[pmid11847130-7] 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.

[pmid11707400-8] 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.

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ERO1LB

Interactions

References

Further reading