ERO1LB

Protein-coding gene in the species Homo sapiens
ERO1B
Identifiers
AliasesERO1B, ERO1LB, Ero1beta, endoplasmic reticulum oxidoreductase beta, endoplasmic reticulum oxidoreductase 1 beta
External IDsOMIM: 615437; MGI: 1914725; HomoloGene: 8740; GeneCards: ERO1B; OMA:ERO1B - orthologs
Gene location (Human)
Chromosome 1 (human)
Chr.Chromosome 1 (human)[1]
Chromosome 1 (human)
Genomic location for ERO1B
Genomic location for ERO1B
Band1q42.3Start236,214,681 bp[1]
End236,282,019 bp[1]
Gene location (Mouse)
Chromosome 13 (mouse)
Chr.Chromosome 13 (mouse)[2]
Chromosome 13 (mouse)
Genomic location for ERO1B
Genomic location for ERO1B
Band13|13 A1Start12,580,755 bp[2]
End12,626,285 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • body of pancreas

  • islet of Langerhans

  • secondary oocyte

  • body of stomach

  • corpus epididymis

  • endothelial cell

  • fundus

  • right lobe of liver

  • right lobe of thyroid gland

  • left lobe of thyroid gland
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
SpeciesHumanMouse
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 MbChr 13: 12.58 – 12.63 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/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. ^ a b c GRCh38: Ensembl release 89: ENSG00000086619 – Ensembl, May 2017
  2. ^ a b c 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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