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Protein

ERO1-like protein alpha

Gene

ERO1L

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. Following P4HB reoxidation, passes its electrons to molecular oxygen via FAD, leading to the production of reactive oxygen species (ROS) in the cell. Required for the proper folding of immunoglobulins. Involved in 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 IP3R1.7 Publications

Cofactori

FAD2 Publications

Enzyme regulationi

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.3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei187 – 1871FAD
Binding sitei189 – 1891FAD
Binding sitei200 – 2001FAD
Binding sitei252 – 2521FAD
Binding sitei255 – 2551FAD
Binding sitei287 – 2871FAD
Binding sitei300 – 3001FAD

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Apoptosis, Electron transport, Transport

Keywords - Ligandi

FAD, Flavoprotein

Enzyme and pathway databases

ReactomeiREACT_15550. Insulin processing.
REACT_264249. Detoxification of Reactive Oxygen Species.

Names & Taxonomyi

Protein namesi
Recommended name:
ERO1-like protein alpha (EC:1.8.4.-)
Short name:
ERO1-L
Short name:
ERO1-L-alpha
Alternative name(s):
Endoplasmic oxidoreductin-1-like protein
Oxidoreductin-1-L-alpha
Gene namesi
Name:ERO1L
ORF Names:UNQ434/PRO865
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:13280. ERO1L.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • endoplasmic reticulum membrane Source: UniProtKB-SubCell
  • intracellular membrane-bounded organelle Source: ProtInc
  • membrane Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi85 – 851C → A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards P4HB; when associated with A-131. 2 Publications
Mutagenesisi85 – 851C → S: Induces a decrease in activity. 2 Publications
Mutagenesisi94 – 941C → S: Induces a decrease in activity towards thioredoxin. Loss of activity towards thioredoxin and loss of regulatory disulfide bond formation; when associated with A-99. 2 Publications
Mutagenesisi99 – 991C → A: Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94. 2 Publications
Mutagenesisi104 – 1041C → A: No effect. Strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-131. 3 Publications
Mutagenesisi104 – 1041C → S: No effect. 3 Publications
Mutagenesisi131 – 1311C → A: Loss of regulatory disulfide bond formation and increased activity towards P4HB. Loss of regulatory disulfide bond formation and strongly increased activity towards P4HB; when associated with A-85. Loss of regulatory disulfide bond formation, strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-104. 4 Publications
Mutagenesisi166 – 1661C → A: No effect. 2 Publications
Mutagenesisi208 – 2081C → A or S: No effect. 2 Publications
Mutagenesisi241 – 2411C → A or S: No effect. 2 Publications
Mutagenesisi280 – 2801N → A: No effect on activity. 1 Publication
Mutagenesisi384 – 3841N → A: No effect on activity. 1 Publication
Mutagenesisi391 – 3911C → A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB. 3 Publications
Mutagenesisi394 – 3941C → A: Retains activity towards P4HB. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB. 5 Publications
Mutagenesisi395 – 3951F → D: Increased catalytical activity. 1 Publication
Mutagenesisi397 – 3971C → A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB. 3 Publications

Organism-specific databases

PharmGKBiPA27862.

Polymorphism and mutation databases

BioMutaiERO1L.
DMDMi50400608.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 23231 PublicationAdd
BLAST
Chaini24 – 468445ERO1-like protein alphaPRO_0000008415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi35 ↔ 48
Disulfide bondi37 ↔ 46
Disulfide bondi85 ↔ 391
Disulfide bondi94 ↔ 131Alternate
Disulfide bondi94 ↔ 99Redox-active; alternate
Disulfide bondi99 ↔ 104Alternate
Modified residuei106 – 1061Phosphoserine1 Publication
Modified residuei143 – 1431Phosphoserine1 Publication
Disulfide bondi208 ↔ 241
Glycosylationi280 – 2801N-linked (GlcNAc...)1 Publication
Glycosylationi384 – 3841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi394 ↔ 397Redox-active

Post-translational modificationi

N-glycosylated.3 Publications
The Cys-94/Cys-99 and Cys-394/Cys-397 disulfide bonds constitute the redox-active center. The Cys-94/Cys-99 disulfide bond may accept electron from P4HB and funnel them to the active site disulfide Cys-394/Cys-397 (By similarity). The regulatory Cys-99/Cys-104 disulfide bond stabilizes the other regulatory bond Cys-94/Cys-131 (PubMed:23027870).By similarity1 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiQ96HE7.
PaxDbiQ96HE7.
PeptideAtlasiQ96HE7.
PRIDEiQ96HE7.

PTM databases

PhosphoSiteiQ96HE7.

Expressioni

Tissue specificityi

Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum.1 Publication

Inductioni

Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway.1 Publication

Gene expression databases

BgeeiQ96HE7.
CleanExiHS_ERO1L.
ExpressionAtlasiQ96HE7. baseline and differential.
GenevisibleiQ96HE7. HS.

Organism-specific databases

HPAiCAB034294.
HPA026653.
HPA030053.

Interactioni

Subunit structurei

Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-2564539,EBI-743771
P4HBP072372EBI-2564539,EBI-395883
PDIA3P301013EBI-2564539,EBI-979862

Protein-protein interaction databases

BioGridi119025. 22 interactions.
IntActiQ96HE7. 8 interactions.
MINTiMINT-144080.
STRINGi9606.ENSP00000379042.

Structurei

Secondary structure

1
468
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi35 – 384Combined sources
Beta strandi40 – 434Combined sources
Beta strandi45 – 473Combined sources
Helixi50 – 5910Combined sources
Helixi62 – 709Combined sources
Helixi72 – 754Combined sources
Beta strandi76 – 794Combined sources
Helixi134 – 1385Combined sources
Helixi146 – 16116Combined sources
Beta strandi177 – 1804Combined sources
Helixi181 – 1833Combined sources
Helixi193 – 20412Combined sources
Helixi245 – 26420Combined sources
Beta strandi266 – 2705Combined sources
Beta strandi275 – 2784Combined sources
Helixi281 – 2888Combined sources
Helixi290 – 2934Combined sources
Helixi296 – 31722Combined sources
Helixi319 – 3235Combined sources
Helixi336 – 35318Combined sources
Beta strandi356 – 3583Combined sources
Helixi369 – 38921Combined sources
Helixi395 – 41521Combined sources
Helixi418 – 4225Combined sources
Beta strandi426 – 4283Combined sources
Beta strandi431 – 4333Combined sources
Helixi437 – 46327Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AHQX-ray2.35A22-468[»]
3AHRX-ray3.07A22-468[»]
ProteinModelPortaliQ96HE7.
SMRiQ96HE7. Positions 34-465.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ96HE7.

Family & Domainsi

Sequence similaritiesi

Belongs to the EROs family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

eggNOGiCOG5061.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000012778.
HOVERGENiHBG051507.
InParanoidiQ96HE7.
KOiK10950.
OMAiCHSDEVP.
OrthoDBiEOG7PP579.
PhylomeDBiQ96HE7.
TreeFamiTF314471.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

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

Q96HE7-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGRGWGFLFG LLGAVWLLSS GHGEEQPPET AAQRCFCQVS GYLDDCTCDV
60 70 80 90 100
ETIDRFNNYR LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA
110 120 130 140 150
VKPCQSDEVP DGIKSASYKY SEEANNLIEE CEQAERLGAV DESLSEETQK
160 170 180 190 200
AVLQWTKHDD SSDNFCEADD IQSPEAEYVD LLLNPERYTG YKGPDAWKIW
210 220 230 240 250
NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL CVEKRAFYRL
260 270 280 290 300
ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR
310 320 330 340 350
LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE
360 370 380 390 400
IKSFPLHFDE NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW
410 420 430 440 450
GKLQTQGLGT ALKILFSEKL IANMPESGPS YEFHLTRQEI VSLFNAFGRI
460
STSVKELENF RNLLQNIH
Length:468
Mass (Da):54,393
Last modified:July 19, 2004 - v2
Checksum:i92ECE6531C9CCA33
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti456 – 4561E → K in AAH08674 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081886 mRNA. Translation: AAF35260.1.
AF123887 mRNA. Translation: AAF06104.1.
AY358463 mRNA. Translation: AAQ88828.1.
AK292839 mRNA. Translation: BAF85528.1.
AL133453 Genomic DNA. No translation available.
BC008674 mRNA. Translation: AAH08674.1.
BC012941 mRNA. Translation: AAH12941.1.
CCDSiCCDS9709.1.
RefSeqiNP_055399.1. NM_014584.2.
UniGeneiHs.525339.
Hs.592304.

Genome annotation databases

EnsembliENST00000395686; ENSP00000379042; ENSG00000197930.
GeneIDi30001.
KEGGihsa:30001.
UCSCiuc001wzv.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF081886 mRNA. Translation: AAF35260.1.
AF123887 mRNA. Translation: AAF06104.1.
AY358463 mRNA. Translation: AAQ88828.1.
AK292839 mRNA. Translation: BAF85528.1.
AL133453 Genomic DNA. No translation available.
BC008674 mRNA. Translation: AAH08674.1.
BC012941 mRNA. Translation: AAH12941.1.
CCDSiCCDS9709.1.
RefSeqiNP_055399.1. NM_014584.2.
UniGeneiHs.525339.
Hs.592304.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AHQX-ray2.35A22-468[»]
3AHRX-ray3.07A22-468[»]
ProteinModelPortaliQ96HE7.
SMRiQ96HE7. Positions 34-465.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119025. 22 interactions.
IntActiQ96HE7. 8 interactions.
MINTiMINT-144080.
STRINGi9606.ENSP00000379042.

Chemistry

BindingDBiQ96HE7.
ChEMBLiCHEMBL1671609.

PTM databases

PhosphoSiteiQ96HE7.

Polymorphism and mutation databases

BioMutaiERO1L.
DMDMi50400608.

Proteomic databases

MaxQBiQ96HE7.
PaxDbiQ96HE7.
PeptideAtlasiQ96HE7.
PRIDEiQ96HE7.

Protocols and materials databases

DNASUi30001.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000395686; ENSP00000379042; ENSG00000197930.
GeneIDi30001.
KEGGihsa:30001.
UCSCiuc001wzv.3. human.

Organism-specific databases

CTDi30001.
GeneCardsiGC14M053106.
HGNCiHGNC:13280. ERO1L.
HPAiCAB034294.
HPA026653.
HPA030053.
MIMi615435. gene.
neXtProtiNX_Q96HE7.
PharmGKBiPA27862.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5061.
GeneTreeiENSGT00390000007753.
HOGENOMiHOG000012778.
HOVERGENiHBG051507.
InParanoidiQ96HE7.
KOiK10950.
OMAiCHSDEVP.
OrthoDBiEOG7PP579.
PhylomeDBiQ96HE7.
TreeFamiTF314471.

Enzyme and pathway databases

ReactomeiREACT_15550. Insulin processing.
REACT_264249. Detoxification of Reactive Oxygen Species.

Miscellaneous databases

ChiTaRSiERO1L. human.
EvolutionaryTraceiQ96HE7.
GeneWikiiERO1L.
GenomeRNAii30001.
NextBioi52816.
PROiQ96HE7.
SOURCEiSearch...

Gene expression databases

BgeeiQ96HE7.
CleanExiHS_ERO1L.
ExpressionAtlasiQ96HE7. baseline and differential.
GenevisibleiQ96HE7. 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. "ERO1-L, a human protein that favors disulfide bond formation in the endoplasmic reticulum."
    Cabibbo A., Pagani M., Fabbri M., Rocchi M., Farmery M.R., Bulleid N.J., Sitia R.
    J. Biol. Chem. 275:4827-4833(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF CYS-391 AND CYS-394.
    Tissue: Embryonic carcinoma.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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].
    Tissue: Trachea.
  4. "The DNA sequence and analysis of human chromosome 14."
    Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H.
    , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
    Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Tissue: Eye.
  6. "The C-terminal domain of yeast Ero1p mediates membrane localization and is essential for function."
    Pagani M., Pilati S., Bertoli G., Valsasina B., Sitia R.
    FEBS Lett. 508:117-120(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, IDENTIFICATION BY MASS SPECTROMETRY.
  7. "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: PROTEIN SEQUENCE OF 68-75; 288-299 AND 420-437, INTERACTION WITH ERP44, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "The CXXCXXC motif determines the folding, structure and stability of human Ero1-Lalpha."
    Benham A.M., Cabibbo A., Fassio A., Bulleid N., Sitia R., Braakman I.
    EMBO J. 19:4493-4502(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, GLYCOSYLATION, MUTAGENESIS OF CYS-391; CYS-394 AND CYS-397.
  9. "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: TISSUE SPECIFICITY.
  10. "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, POTENTIAL HOMODIMERIZATION, ASSOCIATION WITH P4HB, LACK OF ASSOCIATION WITH GRP58, MUTAGENESIS OF CYS-394 AND CYS-397.
  11. "Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1."
    Tsai B., Rapoport T.A.
    J. Cell Biol. 159:207-216(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "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.
  13. "Thiol-mediated protein retention in the endoplasmic reticulum: the role of ERp44."
    Anelli T., Alessio M., Bachi A., Bergamelli L., Bertoli G., Camerini S., Mezghrani A., Ruffato E., Simmen T., Sitia R.
    EMBO J. 22:5015-5022(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  14. "Two conserved cysteine triads in human Ero1alpha cooperate forefficient disulfide bond formation in the ER."
    Bertoli G., Simmen T., Anelli T., Nerini Molteni S., Fesce R., Sitia R.
    J. Biol. Chem. 279:30047-30052(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-85; CYS-94; CYS-99; CYS-104; CYS-131; CYS-166; CYS-208; CYS-241; ASN-280; ASN-384; CYS-391; CYS-394 AND CYS-397.
  15. "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.
  16. "PDILT, a divergent testis-specific protein disulfide isomerase with a non-classical SXXC motif that engages in disulfide-dependent interactions in the endoplasmic reticulum."
    van Lith M., Hartigan N., Hatch J., Benham A.M.
    J. Biol. Chem. 280:1376-1383(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDILT.
  17. "A novel disulphide switch mechanism in Ero1alpha balances ER oxidation in human cells."
    Appenzeller-Herzog C., Riemer J., Christensen B., Soerensen E.S., Ellgaard L.
    EMBO J. 27:2977-2987(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, DISULFIDE BONDS, MUTAGENESIS OF CYS-131 AND CYS-394, IDENTIFICATION BY MASS SPECTROMETRY.
  18. "Low reduction potential of Ero1alpha regulatory disulphides ensures tight control of substrate oxidation."
    Baker K.M., Chakravarthi S., Langton K.P., Sheppard A.M., Lu H., Bulleid N.J.
    EMBO J. 27:2988-2997(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, ENZYME REGULATION, COFACTOR, SUBUNIT, DISULFIDE BONDS, MUTAGENESIS OF CYS-85; CYS-94; CYS-99; CYS-104; CYS-131; CYS-166; CYS-208 AND CYS-241.
  19. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-280.
    Tissue: Liver.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-143, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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: MUTAGENESIS OF PHE-395.
  23. "Hyperactivity of the Ero1alpha oxidase elicits endoplasmic reticulum stress but no broad antioxidant response."
    Hansen H.G., Schmidt J.D., Soltoft C.L., Ramming T., Geertz-Hansen H.M., Christensen B., Sorensen E.S., Juncker A.S., Appenzeller-Herzog C., Ellgaard L.
    J. Biol. Chem. 287:39513-39523(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISULFIDE BONDS, MUTAGENESIS OF CYS-104 AND CYS-131.
  24. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-106, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  25. "Crystal structures of human Ero1alpha reveal the mechanisms of regulated and targeted oxidation of PDI."
    Inaba K., Masui S., Iida H., Vavassori S., Sitia R., Suzuki M.
    EMBO J. 29:3330-3343(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) OF 22-468, COFACTOR BINDING SITES, DISULFIDE BONDS.

Entry informationi

Entry nameiERO1A_HUMAN
AccessioniPrimary (citable) accession number: Q96HE7
Secondary accession number(s): A8K9X4
, A8MYW1, Q7LD45, Q9P1Q9, Q9UKV6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: June 24, 2015
This is version 132 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.