Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteprivacy & cookiesCuration ProcessContact
logos LINCs Logo Mt Sinai Logo NIH Logo NCI Logo
Protein Page:
ERO1L (human)

Overview
ERO1L Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for the release of the unfolded cholera toxin from reduced P4HB/PDI in case of infection by V.cholerae, thereby playing a role in retrotranslocation of the toxin. Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Enzyme activity is tightly regulated to prevent the accumulation of reactive oxygen species in the endoplasmic reticulum. Reversibly down-regulated by the formation of disulfide bonds between the active site Cys-94 and Cys-131, and between Cys- 99 and Cys-104. Glutathione may be required to regulate its activity in the endoplasmic reticulum. Belongs to the EROs family. Note: This description may include information from UniProtKB.
Protein type: EC 1.8.4.-; Oxidoreductase; Secreted; Secreted, signal peptide
Chromosomal Location of Human Ortholog: 14q22.1
Cellular Component: endoplasmic reticulum; endoplasmic reticulum lumen; endoplasmic reticulum membrane; intracellular membrane-bound organelle; membrane
Molecular Function: disulfide oxidoreductase activity; oxidoreductase activity; protein binding; protein disulfide isomerase activity; protein disulfide oxidoreductase activity
Biological Process: chaperone cofactor-dependent protein folding; protein folding; protein modification process; release of sequestered calcium ion into cytosol; response to reactive oxygen species; response to temperature stimulus
Reference #:  Q96HE7 (UniProtKB)
Alt. Names/Synonyms: Endoplasmic oxidoreductin-1-like protein; ERO1-alpha; ERO1-L; ERO1-L-alpha; ERO1-like (S. cerevisiae); ERO1-like protein alpha; ERO1A; ERO1L; Oxidoreductin-1-L-alpha
Gene Symbols: ERO1A
Molecular weight: 54,393 Da
Basal Isoelectric point: 5.48  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

ERO1L

Protein Structure Not Found.
Download PyMol Script
Download ChimeraX Script


STRING  |  cBioPortal  |  Wikipedia  |  Reactome  |  neXtProt  |  Protein Atlas  |  BioGPS  |  Scansite  |  Pfam  |  RCSB PDB  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene  |  InnateDB