CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-019308
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 ERO1-like protein alpha 
Protein Synonyms/Alias
 ERO1-L; ERO1-L-alpha; Endoplasmic oxidoreductin-1-like protein; Oxidoreductin-1-L-alpha 
Gene Name
 ERO1L 
Gene Synonyms/Alias
 UNQ434/PRO865 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
67RLFPRLQKLLESDYFubiquitination[1]
150SLSEETQKAVLQWTKubiquitination[2]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983] 
Functional Description
 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. Plays an important role in ER stress-induced, CHOP- dependent apoptosis by activating the inositol 1,4,5-trisphosphate receptor IP3R1. 
Sequence Annotation
 BINDING 187 187 FAD.
 BINDING 189 189 FAD.
 BINDING 200 200 FAD.
 BINDING 252 252 FAD.
 BINDING 255 255 FAD.
 BINDING 287 287 FAD.
 BINDING 300 300 FAD.
 MOD_RES 143 143 Phosphoserine.
 CARBOHYD 280 280 N-linked (GlcNAc...).
 CARBOHYD 384 384 N-linked (GlcNAc...) (Potential).
 DISULFID 35 48
 DISULFID 37 46
 DISULFID 85 391
 DISULFID 94 131 Alternate.
 DISULFID 94 99 Redox-active; alternate.
 DISULFID 99 104 Alternate.
 DISULFID 208 241
 DISULFID 394 397 Redox-active.  
Keyword
 3D-structure; Apoptosis; Complete proteome; Direct protein sequencing; Disulfide bond; Electron transport; Endoplasmic reticulum; FAD; Flavoprotein; Glycoprotein; Membrane; Oxidoreductase; Phosphoprotein; Redox-active center; Reference proteome; Signal; Transport. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 468 AA 
Protein Sequence
MGRGWGFLFG LLGAVWLLSS GHGEEQPPET AAQRCFCQVS GYLDDCTCDV ETIDRFNNYR 60
LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA VKPCQSDEVP DGIKSASYKY 120
SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEADD IQSPEAEYVD 180
LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL 240
CVEKRAFYRL ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR 300
LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE IKSFPLHFDE 360
NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW GKLQTQGLGT ALKILFSEKL 420
IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH 468 
Gene Ontology
 GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
 GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
 GO:0016020; C:membrane; TAS:ProtInc.
 GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
 GO:0016491; F:oxidoreductase activity; IDA:UniProtKB.
 GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IEA:InterPro.
 GO:0003756; F:protein disulfide isomerase activity; IEA:InterPro.
 GO:0050873; P:brown fat cell differentiation; IEA:Compara.
 GO:0006464; P:cellular protein modification process; TAS:ProtInc.
 GO:0051085; P:chaperone mediated protein folding requiring cofactor; IDA:UniProtKB.
 GO:0022900; P:electron transport chain; IEA:UniProtKB-KW.
 GO:0030968; P:endoplasmic reticulum unfolded protein response; IEA:Compara.
 GO:0070059; P:intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress; ISS:UniProtKB.
 GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
 GO:0009266; P:response to temperature stimulus; TAS:ProtInc. 
Interpro
 IPR007266; ER_oxidoreductin-1. 
Pfam
 PF04137; ERO1 
SMART
  
PROSITE
  
PRINTS