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Protein

ERO1-like protein beta

Gene

ERO1B

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

Enzyme regulationi

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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei186 – 1861FADBy similarity
Binding sitei188 – 1881FADBy similarity
Binding sitei199 – 1991FADBy similarity
Binding sitei251 – 2511FADBy similarity
Binding sitei254 – 2541FADBy similarity
Binding sitei286 – 2861FADBy similarity
Binding sitei299 – 2991FADBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Electron transport, Transport

Keywords - Ligandi

FAD, 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

HGNCiHGNC:14355. ERO1B.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901C → 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 Publication
Mutagenesisi95 – 951C → 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 Publication
Mutagenesisi100 – 1001C → A: Slightly decrease in activity. Significant increased activity; when associated with A-130. 1 Publication
Mutagenesisi130 – 1301C → A: Small increase in activity. Significant increased activity; when associated with A-130. 1 Publication
Mutagenesisi390 – 3901C → A: Strong decrease in P4HB-binding. Efficient homodimerization with both wild-type and A-390 mutated protein. 1 Publication
Mutagenesisi393 – 3931C → 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 Publications
Mutagenesisi396 – 3961C → 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 Publications

Organism-specific databases

PharmGKBiPA134918597.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

Polymorphism and mutation databases

BioMutaiERO1LB.
DMDMi116241353.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3333Sequence analysisAdd
BLAST
Chaini34 – 467434ERO1-like protein betaPRO_0000008418Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi81 ↔ 3901 Publication
Disulfide bondi90 ↔ 130Alternate1 Publication
Disulfide bondi90 ↔ 95Redox-active; alternate1 Publication
Disulfide bondi100 ↔ 2621 Publication
Glycosylationi122 – 1221N-linked (GlcNAc...)Sequence analysis
Glycosylationi140 – 1401N-linked (GlcNAc...)1 Publication
Glycosylationi145 – 1451N-linked (GlcNAc...)Sequence analysis
Disulfide bondi207 ↔ 2401 Publication
Glycosylationi383 – 3831N-linked (GlcNAc...)Sequence analysis
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.
PRIDEiQ86YB8.

PTM databases

PhosphoSiteiQ86YB8.

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

BgeeiQ86YB8.
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

  • unfolded protein binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121155. 22 interactions.
IntActiQ86YB8. 6 interactions.
STRINGi9606.ENSP00000346635.

Structurei

3D structure databases

ProteinModelPortaliQ86YB8.
SMRiQ86YB8. Positions 34-464.
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.
OMAiDAMDHHD.
OrthoDBiEOG7PP579.
PhylomeDBiQ86YB8.
TreeFamiTF314471.

Family and domain databases

InterProiIPR007266. Ero1.
[Graphical view]
PANTHERiPTHR12613. PTHR12613. 1 hit.
PfamiPF04137. ERO1. 1 hit.
[Graphical view]
PIRSFiPIRSF017205. ERO1. 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

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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti129 – 1291D → V.1 Publication
Corresponds to variant rs2477599 [ dbSNP | Ensembl ].
VAR_028012
Natural varianti465 – 4651H → Q.1 Publication
Corresponds to variant rs1055851 [ dbSNP | Ensembl ].
VAR_019492

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei144 – 466323Missing in isoform 2. 1 PublicationVSP_056988Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252538 mRNA. Translation: AAF97547.1.
AK293941 mRNA. Translation: BAG57318.1.
AL139162, AL450309 Genomic DNA. Translation: CAI23525.1.
AL450309, AL139162 Genomic DNA. Translation: CAI14420.1.
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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF252538 mRNA. Translation: AAF97547.1.
AK293941 mRNA. Translation: BAG57318.1.
AL139162, AL450309 Genomic DNA. Translation: CAI23525.1.
AL450309, AL139162 Genomic DNA. Translation: CAI14420.1.
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.
SMRiQ86YB8. Positions 34-464.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121155. 22 interactions.
IntActiQ86YB8. 6 interactions.
STRINGi9606.ENSP00000346635.

Chemistry

DrugBankiDB03147. Flavin adenine dinucleotide.

PTM databases

PhosphoSiteiQ86YB8.

Polymorphism and mutation databases

BioMutaiERO1LB.
DMDMi116241353.

Proteomic databases

EPDiQ86YB8.
MaxQBiQ86YB8.
PaxDbiQ86YB8.
PRIDEiQ86YB8.

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.
GeneCardsiERO1LB.
H-InvDBHIX0001722.
HGNCiHGNC:14355. ERO1B.
HPAiHPA028085.
MIMi615437. gene.
neXtProtiNX_Q86YB8.
PharmGKBiPA134918597.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2608. Eukaryota.
COG5061. LUCA.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000012778.
HOVERGENiHBG051507.
InParanoidiQ86YB8.
KOiK10976.
OMAiDAMDHHD.
OrthoDBiEOG7PP579.
PhylomeDBiQ86YB8.
TreeFamiTF314471.

Enzyme and pathway databases

ReactomeiR-HSA-264876. Insulin processing.

Miscellaneous databases

GeneWikiiERO1LB.
GenomeRNAii56605.
NextBioi35471410.
PROiQ86YB8.
SOURCEiSearch...

Gene expression databases

BgeeiQ86YB8.
CleanExiHS_ERO1LB.
ExpressionAtlasiQ86YB8. baseline and differential.
GenevisibleiQ86YB8. HS.

Family and domain databases

InterProiIPR007266. Ero1.
[Graphical view]
PANTHERiPTHR12613. PTHR12613. 1 hit.
PfamiPF04137. ERO1. 1 hit.
[Graphical view]
PIRSFiPIRSF017205. ERO1. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Endoplasmic reticulum oxidoreductin 1-lbeta (ERO1-Lbeta), a human gene induced in the course of the unfolded protein response."
    Pagani M., Fabbri M., Benedetti C., Fassio A., Pilati S., Bulleid N.J., Cabibbo A., Sitia R.
    J. Biol. Chem. 275:23685-23692(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION, INDUCTION, VARIANT GLN-465.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Cerebellum.
  3. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT VAL-129.
    Tissue: Testis.
  5. "Manipulation of oxidative protein folding and PDI redox state in mammalian cells."
    Mezghrani A., Fassio A., Benham A., Simmen T., Braakman I., Sitia R.
    EMBO J. 20:6288-6296(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, POSSIBLE HOMODIMERIZATION, ASSOCIATION WITH P4HB.
  6. "ERp44, a novel endoplasmic reticulum folding assistant of the thioredoxin family."
    Anelli T., Alessio M., Mezghrani A., Simmen T., Talamo F., Bachi A., Sitia R.
    EMBO J. 21:835-844(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERP44.
  7. "The cellular oxygen tension regulates expression of the endoplasmic oxidoreductase ERO1-Lalpha."
    Gess B., Hofbauer K.H., Wenger R.H., Lohaus C., Meyer H.E., Kurtz A.
    Eur. J. Biochem. 270:2228-2235(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  8. "Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum."
    Nerini Molteni S., Fassio A., Ciriolo M.R., Filomeni G., Pasqualetto E., Fagioli C., Sitia R.
    J. Biol. Chem. 279:32667-32673(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  9. "Tissue-specific expression and dimerization of the endoplasmic reticulum oxidoreductase Ero1beta."
    Dias-Gunasekara S., Gubbens J., van Lith M., Dunne C., Williams J.A., Kataky R., Scoones D., Lapthorn A., Bulleid N.J., Benham A.M.
    J. Biol. Chem. 280:33066-33075(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH ERO1L AND P4HB, HOMODIMERIZATION, TISSUE SPECIFICITY, MUTAGENESIS OF CYS-390; CYS-393 AND CYS-396.
  10. "Elucidation of N-glycosylation sites on human platelet proteins: a glycoproteomic approach."
    Lewandrowski U., Moebius J., Walter U., Sickmann A.
    Mol. Cell. Proteomics 5:226-233(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-140.
    Tissue: Platelet.
  11. "The endoplasmic reticulum sulfhydryl oxidase Ero1beta drives efficient oxidative protein folding with loose regulation."
    Wang L., Zhu L., Wang C.C.
    Biochem. J. 434:113-121(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, COFACTOR, HOMODIMERIZATION, DISULFIDE BONDS, MUTAGENESIS OF CYS-90; CYS-95; CYS-100; CYS-130; CYS-393 AND CYS-396.

Entry informationi

Entry nameiERO1B_HUMAN
AccessioniPrimary (citable) accession number: Q86YB8
Secondary accession number(s): B4DF57
, Q5T1H4, Q8IZ11, Q9NR62
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 17, 2006
Last modified: March 16, 2016
This is version 122 of the entry and version 2 of the sequence. [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. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.