ERO1LB

ERO1B

Identifiers

ERO1B, ERO1LB, Ero1beta, endoplasmic reticulum oxidoreductase beta, endoplasmic reticulum oxidoreductase 1 beta

External IDs

OMIM: 615437; MGI: 1914725; GeneCards: ERO1B

Enzyme activity
EC #	BRENDA	ExPASy	KEGG	MetaCyc
1.8.3.2	↗	↗	↗	↗

Gene location (Human)

Chr.	Chromosome 1 (human)

Band	1q42.3	Start	236,214,681 bp
Band	1q42.3	End	236,282,019 bp

Gene location (Mouse)

Chr.	Chromosome 13 (mouse)

Band	13\|13 A1	Start	12,580,755 bp
Band	13\|13 A1	End	12,626,285 bp

RNA expression pattern

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


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

Databases

NCBI: entry; OMA: entry

Species

Human

Mouse


56605


67475


ENSG00000086619


ENSMUSG00000057069


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

View/Edit Human

View/Edit Mouse

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 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.

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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