ERO1LB

From Wikipedia, the free encyclopedia

ERO1-like beta (S. cerevisiae)

Identifiers

External IDs

MGI: 1914725 HomoloGene: 8740

Gene ontology
Molecular Function:	• oxidoreductase activity • unfolded protein binding
Cellular Component:	• endoplasmic reticulum • membrane
Biological Process:	• electron transport • protein folding • transport

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_019891 (mRNA)
NP_063944 (protein)

XM_001006075 (mRNA)
XP_001006075 (protein)

Location

Chr 1: 234.45 - 234.51 Mb

Chr 13: 12.63 - 12.66 Mb

Pubmed search

[1]

[2]

ERO1-like beta (S. cerevisiae), also known as ERO1LB, is a human gene.^[1]

[edit] References

^ Entrez Gene: ERO1LB ERO1-like beta (S. cerevisiae).

[edit] Further reading

Pagani M, Fabbri M, Benedetti C, et al. (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.
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. 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. 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. 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. 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. 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.