Hmdb loader
You are using an unsupported browser. Please upgrade your browser to a newer version to get the best experience on Human Metabolome Database.
Identification
HMDB Protein ID HMDBP08270
Secondary Accession Numbers
  • 13982
Name ERO1-like protein beta
Synonyms
  1. ERO1-L-beta
  2. Endoplasmic oxidoreductin-1-like protein B
  3. Oxidoreductin-1-L-beta
Gene Name ERO1LB
Protein Type Unknown
Biological Properties
General Function Involved in protein binding
Specific Function 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 being a source of oxidative stress. Required for the folding of cell, thereby being a source of oxidative stress
Pathways Not Available
Reactions Not Available
GO Classification
Component
membrane
cell part
endoplasmic reticulum membrane
organelle membrane
Function
oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor
binding
catalytic activity
nucleoside binding
purine nucleoside binding
adenyl nucleotide binding
protein binding
oxidoreductase activity, acting on a sulfur group of donors
oxidoreductase activity
fad or fadh2 binding
Process
metabolic process
macromolecule metabolic process
cellular protein metabolic process
protein thiol-disulfide exchange
protein folding
oxidation reduction
protein metabolic process
Cellular Location
  1. Peripheral membrane protein
  2. Endoplasmic reticulum membrane
  3. Lumenal side
Gene Properties
Chromosome Location Chromosome:1
Locus 1q42.2-q43
SNPs ERO1LB
Gene Sequence
>1404 bp
ATGAGCCAAGGGGTCCGCCGGGCAGGCGCTGGGCAGGGGGTAGCGGCCGCGGTGCAGCTG
CTGGTCACCCTGAGCTTCCTGCGGAGCGTCGTCGAGGCGCAGGTCACTGGAGTTCTGGAT
GATTGCTTGTGTGATATTGACAGCATCGATAACTTCAATACCTACAAAATCTTCCCCAAA
ATAAAAAAATTGCAAGAGAGAGACTATTTTCGTTATTACAAGGTTAATCTGAAGCGACCT
TGTCCTTTCTGGGCAGAAGATGGCCACTGTTCAATAAAAGACTGTCATGTGGAGCCCTGT
CCAGAGAGTAAAATTCCGGTTGGAATAAAAGCTGGGCATTCTAATAAGTACTTGAAAATG
GCAAACAATACCAAAGAATTAGAAGATTGTGAGCAAGCTAATAAACTGGGAGCAATTAAC
AGCACATTAAGTAATCAAAGCAAAGAAGCTTTCATTGACTGGGCAAGATATGATGATTCA
CGGGATCACTTTTGTGAACTTGATGATGAGAGATCTCCAGCTGCTCAGTATGTAGACCTA
TTGCTGAACCCAGAGCGTTACACTGGCTATAAAGGGACCTCTGCATGGAGAGTGTGGAAC
AGCATCTATGAAGAGAACTGTTTCAAGCCTCGATCTGTTTATCGTCCTTTAAATCCTCTG
GCGCCTAGCCGAGGCGAAGATGATGGAGAATCATTCTACACATGGCTAGAAGGTTTGTGT
CTGGAGAAAAGAGTCTTCTATAAGCTTATATCGGGACTTCATGCTAGCATCAATTTACAT
CTATGCGCAAATTATCTTTTGGAAGAAACCTGGGGTAAGCCCAGTTGGGGACCTAATATT
AAAGAATTCAAACACCGCTTTGACCCTGTGGAAACCAAGGGAGAAGGTCCAAGAAGGCTC
AAGAATCTTTACTTTTTATACTTGATTGAGCTTCGAGCTTTGTCAAAGGTGGCTCCATAT
TTTGAGCGCTCAATTGTCGATCTTTACACTGGAAATGCAGAAGAAGATGCTGACACAAAA
ACTCTTCTACTGAATATCTTTCAAGATACAAAGTCCTTTCCCATGCACTTTGATGAGAAA
TCCATGTTTGCAGGTGACAAAAAAGGGGCCAAGTCACTAAAGGAGGAATTCCGATTACAT
TTCAAGAATATCTCCCGTATAATGGACTGTGTTGGATGTGACAAATGCAGATTATGGGGA
AAATTACAGACTCAGGGTTTAGGAACTGCCCTGAAGATATTATTCTCTGAAAAAGAAATC
CAAAAGCTTCCAGAGAATAGTCCATCTAAAGGCTTCCAACTCACCCGACAGGAAATAGTT
GCTCTTTTAAATGCTTTTGGAAGGCTTTCTACAAGTATAAGAGACTTACAGAATTTTAAA
GTCTTATTACAACAGAGTAGGTAA
Protein Properties
Number of Residues 467
Molecular Weight 53542.6
Theoretical pI 8.07
Pfam Domain Function
Signals
  • 1-33
Transmembrane Regions
  • None
Protein Sequence
>ERO1-like protein beta
MSQGVRRAGAGQGVAAAVQLLVTLSFLRSVVEAQVTGVLDDCLCDIDSIDNFNTYKIFPK
IKKLQERDYFRYYKVNLKRPCPFWAEDGHCSIKDCHVEPCPESKIPVGIKAGHSNKYLKM
ANNTKELEDCEQANKLGAINSTLSNQSKEAFIDWARYDDSRDHFCELDDERSPAAQYVDL
LLNPERYTGYKGTSAWRVWNSIYEENCFKPRSVYRPLNPLAPSRGEDDGESFYTWLEGLC
LEKRVFYKLISGLHASINLHLCANYLLEETWGKPSWGPNIKEFKHRFDPVETKGEGPRRL
KNLYFLYLIELRALSKVAPYFERSIVDLYTGNAEEDADTKTLLLNIFQDTKSFPMHFDEK
SMFAGDKKGAKSLKEEFRLHFKNISRIMDCVGCDKCRLWGKLQTQGLGTALKILFSEKEI
QKLPENSPSKGFQLTRQEIVALLNAFGRLSTSIRDLQNFKVLLQHSR
GenBank ID Protein 9716557
UniProtKB/Swiss-Prot ID Q86YB8
UniProtKB/Swiss-Prot Entry Name ERO1B_HUMAN
PDB IDs Not Available
GenBank Gene ID AF252538
GeneCard ID ERO1LB
GenAtlas ID ERO1LB
HGNC ID HGNC:14355
References
General References
  1. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  2. Gregory SG, Barlow KF, McLay KE, Kaul R, Swarbreck D, Dunham A, Scott CE, Howe KL, Woodfine K, Spencer CC, Jones MC, Gillson C, Searle S, Zhou Y, Kokocinski F, McDonald L, Evans R, Phillips K, Atkinson A, Cooper R, Jones C, Hall RE, Andrews TD, Lloyd C, Ainscough R, Almeida JP, Ambrose KD, Anderson F, Andrew RW, Ashwell RI, Aubin K, Babbage AK, Bagguley CL, Bailey J, Beasley H, Bethel G, Bird CP, Bray-Allen S, Brown JY, Brown AJ, Buckley D, Burton J, Bye J, Carder C, Chapman JC, Clark SY, Clarke G, Clee C, Cobley V, Collier RE, Corby N, Coville GJ, Davies J, Deadman R, Dunn M, Earthrowl M, Ellington AG, Errington H, Frankish A, Frankland J, French L, Garner P, Garnett J, Gay L, Ghori MR, Gibson R, Gilby LM, Gillett W, Glithero RJ, Grafham DV, Griffiths C, Griffiths-Jones S, Grocock R, Hammond S, Harrison ES, Hart E, Haugen E, Heath PD, Holmes S, Holt K, Howden PJ, Hunt AR, Hunt SE, Hunter G, Isherwood J, James R, Johnson C, Johnson D, Joy A, Kay M, Kershaw JK, Kibukawa M, Kimberley AM, King A, Knights AJ, Lad H, Laird G, Lawlor S, Leongamornlert DA, Lloyd DM, Loveland J, Lovell J, Lush MJ, Lyne R, Martin S, Mashreghi-Mohammadi M, Matthews L, Matthews NS, McLaren S, Milne S, Mistry S, Moore MJ, Nickerson T, O'Dell CN, Oliver K, Palmeiri A, Palmer SA, Parker A, Patel D, Pearce AV, Peck AI, Pelan S, Phelps K, Phillimore BJ, Plumb R, Rajan J, Raymond C, Rouse G, Saenphimmachak C, Sehra HK, Sheridan E, Shownkeen R, Sims S, Skuce CD, Smith M, Steward C, Subramanian S, Sycamore N, Tracey A, Tromans A, Van Helmond Z, Wall M, Wallis JM, White S, Whitehead SL, Wilkinson JE, Willey DL, Williams H, Wilming L, Wray PW, Wu Z, Coulson A, Vaudin M, Sulston JE, Durbin R, Hubbard T, Wooster R, Dunham I, Carter NP, McVean G, Ross MT, Harrow J, Olson MV, Beck S, Rogers J, Bentley DR, Banerjee R, Bryant SP, Burford DC, Burrill WD, Clegg SM, Dhami P, Dovey O, Faulkner LM, Gribble SM, Langford CF, Pandian RD, Porter KM, Prigmore E: The DNA sequence and biological annotation of human chromosome 1. Nature. 2006 May 18;441(7091):315-21. [PubMed:16710414 ]
  3. Lewandrowski U, Moebius J, Walter U, Sickmann A: Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach. Mol Cell Proteomics. 2006 Feb;5(2):226-33. Epub 2005 Oct 31. [PubMed:16263699 ]
  4. Anelli T, Alessio M, Mezghrani A, Simmen T, Talamo F, Bachi A, Sitia R: ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family. EMBO J. 2002 Feb 15;21(4):835-44. [PubMed:11847130 ]
  5. Pagani M, Fabbri M, Benedetti C, Fassio A, Pilati S, Bulleid NJ, Cabibbo A, Sitia R: Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response. J Biol Chem. 2000 Aug 4;275(31):23685-92. [PubMed:10818100 ]
  6. Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, Sitia R: Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J. 2001 Nov 15;20(22):6288-96. [PubMed:11707400 ]
  7. Gess B, Hofbauer KH, Wenger RH, Lohaus C, Meyer HE, Kurtz A: The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha. Eur J Biochem. 2003 May;270(10):2228-35. [PubMed:12752442 ]
  8. Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, Sitia R: Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum. J Biol Chem. 2004 Jul 30;279(31):32667-73. Epub 2004 May 25. [PubMed:15161913 ]