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Protein

ERO1-like protein beta

Gene

ERO1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Oxidoreductase involved in disulfide bond formation in the endoplasmic reticulum. Efficiently reoxidizes P4HB/PDI, the enzyme catalyzing protein disulfide formation, in order to allow P4HB to sustain additional rounds of disulfide formation. Other protein disulfide isomerase family members can also be reoxidized, but at lower rates compared to P4HB, including PDIA2 (50% of P4HB reoxidation rate), as well as PDIA3, PDIA4, PDIA6 and NXNDC12 (<10%). Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. May be involved in oxidative proinsulin folding in pancreatic cells, hence may play a role in glucose homeostasis.2 Publications

Cofactori

FAD1 Publication

Activity regulationi

Glutathione may be required to regulate its activity in the endoplasmic reticulum.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei186FADBy similarity1
Binding sitei188FADBy similarity1
Binding sitei199FADBy similarity1
Binding sitei251FADBy similarity1
Binding sitei254FADBy similarity1
Binding sitei286FADBy similarity1
Binding sitei299FADBy similarity1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionOxidoreductase
Biological processElectron transport, Transport
LigandFAD, Flavoprotein

Enzyme and pathway databases

ReactomeiR-HSA-264876 Insulin processing

Names & Taxonomyi

Protein namesi
Recommended name:
ERO1-like protein beta (EC:1.8.4.-)
Short name:
ERO1-L-beta
Alternative name(s):
Endoplasmic reticulum oxidoreductase betaImported
Endoplasmic reticulum oxidoreductin-1-like protein B
Oxidoreductin-1-L-beta
Gene namesi
Name:ERO1BImported
Synonyms:ERO1LB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

EuPathDBiHostDB:ENSG00000086619.13
HGNCiHGNC:14355 ERO1B
MIMi615437 gene
neXtProtiNX_Q86YB8

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi90C → A: No effect on catalytic activity when DTT is used as an electron donor; when associated with A-95. Loss of catalytic activity when P4HB is used as an electron donor; when associated with A-95. 1 Publication1
Mutagenesisi95C → A: No effect on catalytic activity when DTT is used as an electron donor; when associated with A-90. Loss of catalytic activity when P4HB is used as an electron donor; when associated with A-90. 1 Publication1
Mutagenesisi100C → A: Slightly decrease in activity. Significant increased activity; when associated with A-130. 1 Publication1
Mutagenesisi130C → A: Small increase in activity. Significant increased activity; when associated with A-130. 1 Publication1
Mutagenesisi390C → A: Strong decrease in P4HB-binding. Efficient homodimerization with both wild-type and A-390 mutated protein. 1 Publication1
Mutagenesisi393C → A: Some decrease in P4HB-binding. Efficient homodimerization with wild-type protein. Loss of catalytic activity when DTT or P4HB are used as an electron donor; when associated with A-396. 2 Publications1
Mutagenesisi396C → A: Some decrease in P4HB-binding. Efficient homodimerization with wild-type protein, but loss of homodimerization with A-396 mutated protein. Loss of catalytic activity when DTT or P4HB are used as an electron donor; when associated with A-393. 2 Publications1

Organism-specific databases

DisGeNETi56605
OpenTargetsiENSG00000086619
PharmGKBiPA134918597

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide

Polymorphism and mutation databases

BioMutaiERO1LB
DMDMi116241353

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 33Sequence analysisAdd BLAST33
ChainiPRO_000000841834 – 467ERO1-like protein betaAdd BLAST434

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi81 ↔ 3901 Publication
Disulfide bondi90 ↔ 130Alternate1 Publication
Disulfide bondi90 ↔ 95Redox-active; alternate1 Publication
Disulfide bondi100 ↔ 2621 Publication
Glycosylationi122N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi140N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi145N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi207 ↔ 2401 Publication
Glycosylationi383N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi393 ↔ 396Redox-active1 Publication

Post-translational modificationi

N-glycosylated.2 Publications
The Cys-90/Cys-95 and Cys-393/Cys-396 disulfide bonds constitute the redox-active center. The Cys-90/Cys-95 disulfide bond accepts electron from P4HB and funnel them to the active site disulfide Cys-393/Cys-396. The Cys-81/Cys-390 disulfide bond may be critical for structural stability. Two long-range disulfide bonds participate in loose feedback regulation. The Cys-90/Cys-130 disulfide bond may be the predominant regulatory switch to modulate the catalytic activity, while the Cys-100/Cys-262 disulfide bond may play an auxiliary regulatory role.1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

EPDiQ86YB8
MaxQBiQ86YB8
PaxDbiQ86YB8
PeptideAtlasiQ86YB8
PRIDEiQ86YB8
ProteomicsDBi70394

PTM databases

GlyConnecti1226
iPTMnetiQ86YB8
PhosphoSitePlusiQ86YB8

Expressioni

Tissue specificityi

Highly expressed in the digestive tract, including the duodenum and lower digestive tract. In the stomach, highly expressed in enzyme-producing chief cells (at protein level). In the pancreas, expressed in islets of Langerhans and, at lower levels, in enzyme-secreting cells (at protein level). Detected at low level in many other tissues.2 Publications

Inductioni

Up-regulated by inducers of the unfolded protein response (UPR).2 Publications

Gene expression databases

BgeeiENSG00000086619 Expressed in 186 organ(s), highest expression level in body of pancreas
CleanExiHS_ERO1LB
ExpressionAtlasiQ86YB8 baseline and differential
GenevisibleiQ86YB8 HS

Organism-specific databases

HPAiHPA028085

Interactioni

Subunit structurei

Homodimer; disulfide-linked. Heterodimer with ERO1A; disulfide-linked. Also detected as monomer. Homodimers may be somewhat less active than monomers. Interacts with P4HB. Interacts with ERP44.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PDIA3P301012EBI-2806988,EBI-979862

GO - Molecular functioni

Protein-protein interaction databases

BioGridi121155, 29 interactors
IntActiQ86YB8, 6 interactors
MINTiQ86YB8
STRINGi9606.ENSP00000346635

Structurei

3D structure databases

ProteinModelPortaliQ86YB8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the EROs family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiKOG2608 Eukaryota
COG5061 LUCA
GeneTreeiENSGT00390000007753
HOGENOMiHOG000012778
HOVERGENiHBG051507
InParanoidiQ86YB8
KOiK10976
OMAiSISTHIC
OrthoDBiEOG091G04ZQ
PhylomeDBiQ86YB8
TreeFamiTF314471

Family and domain databases

InterProiView protein in InterPro
IPR007266 Ero1
IPR037192 ERO1-like_sf
PANTHERiPTHR12613 PTHR12613, 1 hit
PfamiView protein in Pfam
PF04137 ERO1, 1 hit
PIRSFiPIRSF017205 ERO1, 1 hit
SUPFAMiSSF110019 SSF110019, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 2 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: Q86YB8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MSQGVRRAGA GQGVAAAVQL LVTLSFLRSV VEAQVTGVLD DCLCDIDSID
60 70 80 90 100
NFNTYKIFPK IKKLQERDYF RYYKVNLKRP CPFWAEDGHC SIKDCHVEPC
110 120 130 140 150
PESKIPVGIK AGHSNKYLKM ANNTKELEDC EQANKLGAIN STLSNQSKEA
160 170 180 190 200
FIDWARYDDS RDHFCELDDE RSPAAQYVDL LLNPERYTGY KGTSAWRVWN
210 220 230 240 250
SIYEENCFKP RSVYRPLNPL APSRGEDDGE SFYTWLEGLC LEKRVFYKLI
260 270 280 290 300
SGLHASINLH LCANYLLEET WGKPSWGPNI KEFKHRFDPV ETKGEGPRRL
310 320 330 340 350
KNLYFLYLIE LRALSKVAPY FERSIVDLYT GNAEEDADTK TLLLNIFQDT
360 370 380 390 400
KSFPMHFDEK SMFAGDKKGA KSLKEEFRLH FKNISRIMDC VGCDKCRLWG
410 420 430 440 450
KLQTQGLGTA LKILFSEKEI QKLPENSPSK GFQLTRQEIV ALLNAFGRLS
460
TSIRDLQNFK VLLQHSR
Length:467
Mass (Da):53,543
Last modified:October 17, 2006 - v2
Checksum:i4DA8753DDEE15314
GO
Isoform 2 (identifier: Q86YB8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     144-466: Missing.

Note: No experimental confirmation available.
Show »
Length:144
Mass (Da):16,096
Checksum:i05408D9D015C85D8
GO

Computationally mapped potential isoform sequencesi

There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q5TAE8Q5TAE8_HUMAN
ERO1-like protein beta
ERO1B
173Annotation score:
Q5T1H5Q5T1H5_HUMAN
ERO1-like protein beta
ERO1B
71Annotation score:

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_028012129D → V1 PublicationCorresponds to variant dbSNP:rs2477599Ensembl.1
Natural variantiVAR_019492465H → Q1 PublicationCorresponds to variant dbSNP:rs1055851Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056988144 – 466Missing in isoform 2. 1 PublicationAdd BLAST323

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252538 mRNA Translation: AAF97547.1
AK293941 mRNA Translation: BAG57318.1
AL139162 Genomic DNA No translation available.
AL450309 Genomic DNA No translation available.
BC032823 mRNA Translation: AAH32823.2
BC044573 mRNA Translation: AAH44573.1
CCDSiCCDS31064.1 [Q86YB8-1]
RefSeqiNP_063944.3, NM_019891.3 [Q86YB8-1]
UniGeneiHs.558519

Genome annotation databases

EnsembliENST00000354619; ENSP00000346635; ENSG00000086619 [Q86YB8-1]
GeneIDi56605
KEGGihsa:56605
UCSCiuc001hxt.4 human [Q86YB8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252538 mRNA Translation: AAF97547.1
AK293941 mRNA Translation: BAG57318.1
AL139162 Genomic DNA No translation available.
AL450309 Genomic DNA No translation available.
BC032823 mRNA Translation: AAH32823.2
BC044573 mRNA Translation: AAH44573.1
CCDSiCCDS31064.1 [Q86YB8-1]
RefSeqiNP_063944.3, NM_019891.3 [Q86YB8-1]
UniGeneiHs.558519

3D structure databases

ProteinModelPortaliQ86YB8
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121155, 29 interactors
IntActiQ86YB8, 6 interactors
MINTiQ86YB8
STRINGi9606.ENSP00000346635

Chemistry databases

DrugBankiDB03147 Flavin adenine dinucleotide

PTM databases

GlyConnecti1226
iPTMnetiQ86YB8
PhosphoSitePlusiQ86YB8

Polymorphism and mutation databases

BioMutaiERO1LB
DMDMi116241353

Proteomic databases

EPDiQ86YB8
MaxQBiQ86YB8
PaxDbiQ86YB8
PeptideAtlasiQ86YB8
PRIDEiQ86YB8
ProteomicsDBi70394

Protocols and materials databases

DNASUi56605
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354619; ENSP00000346635; ENSG00000086619 [Q86YB8-1]
GeneIDi56605
KEGGihsa:56605
UCSCiuc001hxt.4 human [Q86YB8-1]

Organism-specific databases

CTDi56605
DisGeNETi56605
EuPathDBiHostDB:ENSG00000086619.13
GeneCardsiERO1B
H-InvDBiHIX0001722
HGNCiHGNC:14355 ERO1B
HPAiHPA028085
MIMi615437 gene
neXtProtiNX_Q86YB8
OpenTargetsiENSG00000086619
PharmGKBiPA134918597
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2608 Eukaryota
COG5061 LUCA
GeneTreeiENSGT00390000007753
HOGENOMiHOG000012778
HOVERGENiHBG051507
InParanoidiQ86YB8
KOiK10976
OMAiSISTHIC
OrthoDBiEOG091G04ZQ
PhylomeDBiQ86YB8
TreeFamiTF314471

Enzyme and pathway databases

ReactomeiR-HSA-264876 Insulin processing

Miscellaneous databases

ChiTaRSiERO1B human
GeneWikiiERO1LB
GenomeRNAii56605
PROiPR:Q86YB8
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000086619 Expressed in 186 organ(s), highest expression level in body of pancreas
CleanExiHS_ERO1LB
ExpressionAtlasiQ86YB8 baseline and differential
GenevisibleiQ86YB8 HS

Family and domain databases

InterProiView protein in InterPro
IPR007266 Ero1
IPR037192 ERO1-like_sf
PANTHERiPTHR12613 PTHR12613, 1 hit
PfamiView protein in Pfam
PF04137 ERO1, 1 hit
PIRSFiPIRSF017205 ERO1, 1 hit
SUPFAMiSSF110019 SSF110019, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiERO1B_HUMAN
AccessioniPrimary (citable) accession number: Q86YB8
Secondary accession number(s): B4DF57
, Q5T1H4, Q8IZ11, Q9NR62
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 17, 2006
Last modified: November 7, 2018
This is version 140 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  3. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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