Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
ERO1L (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

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: Secreted; EC 1.8.4.-; Oxidoreductase; Secreted, signal peptide
Cellular Component: endoplasmic reticulum membrane; intracellular membrane-bound organelle; membrane; endoplasmic reticulum lumen; endoplasmic reticulum
Molecular Function: protein binding; protein disulfide isomerase activity; oxidoreductase activity; oxidoreductase activity, acting on sulfur group of donors, disulfide as acceptor
Biological Process: response to temperature stimulus; cellular protein metabolic process; protein folding; chaperone cofactor-dependent protein folding; unfolded protein response; release of sequestered calcium ion into cytosol; brown fat cell differentiation; protein modification process
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: ERO1L
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


Protein Structure Not Found.

STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  ENZYME  |  InnateDB  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend

Show Multiple Sequence Alignment


SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.



Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.