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Q96HE7

- ERO1A_HUMAN

UniProt

Q96HE7 - ERO1A_HUMAN

Protein

ERO1-like protein alpha

Gene

ERO1L

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 124 (01 Oct 2014)
      Sequence version 2 (19 Jul 2004)
      Previous versions | rss
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    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

    FAD.2 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

    1. oxidoreductase activity Source: UniProtKB
    2. oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Source: InterPro
    3. protein binding Source: IntAct
    4. protein disulfide isomerase activity Source: InterPro

    GO - Biological processi

    1. brown fat cell differentiation Source: Ensembl
    2. cellular protein metabolic process Source: Reactome
    3. cellular protein modification process Source: ProtInc
    4. chaperone mediated protein folding requiring cofactor Source: UniProtKB
    5. endoplasmic reticulum unfolded protein response Source: Ensembl
    6. intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Source: UniProtKB
    7. protein folding Source: ProtInc
    8. release of sequestered calcium ion into cytosol Source: UniProtKB
    9. response to endoplasmic reticulum stress Source: UniProtKB
    10. response to temperature stimulus Source: ProtInc

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Apoptosis, Electron transport, Transport

    Keywords - Ligandi

    FAD, Flavoprotein

    Enzyme and pathway databases

    ReactomeiREACT_15550. Insulin processing.
    REACT_172715. 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: Chromosome 14

    Organism-specific databases

    HGNCiHGNC:13280. ERO1L.

    Subcellular locationi

    Endoplasmic reticulum membrane 2 Publications; Peripheral membrane protein 2 Publications; Lumenal side 2 Publications
    Note: The association with ERP44 is essential for its retention in the endoplasmic reticulum.

    GO - Cellular componenti

    1. endoplasmic reticulum Source: UniProtKB
    2. endoplasmic reticulum lumen Source: Reactome
    3. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    4. intracellular membrane-bounded organelle Source: ProtInc
    5. membrane Source: UniProtKB

    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.

    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 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

    ArrayExpressiQ96HE7.
    BgeeiQ96HE7.
    CleanExiHS_ERO1L.
    GenevestigatoriQ96HE7.

    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
    P4HBP072372EBI-2564539,EBI-395883
    PDIA3P301013EBI-2564539,EBI-979862

    Protein-protein interaction databases

    BioGridi119025. 20 interactions.
    IntActiQ96HE7. 7 interactions.
    MINTiMINT-144080.
    STRINGi9606.ENSP00000379042.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000012778.
    HOVERGENiHBG051507.
    KOiK10950.
    OMAiEADDIHS.
    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

    MGRGWGFLFG LLGAVWLLSS GHGEEQPPET AAQRCFCQVS GYLDDCTCDV    50
    ETIDRFNNYR LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA 100
    VKPCQSDEVP DGIKSASYKY SEEANNLIEE CEQAERLGAV DESLSEETQK 150
    AVLQWTKHDD SSDNFCEADD IQSPEAEYVD LLLNPERYTG YKGPDAWKIW 200
    NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL CVEKRAFYRL 250
    ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR 300
    LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE 350
    IKSFPLHFDE NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW 400
    GKLQTQGLGT ALKILFSEKL IANMPESGPS YEFHLTRQEI VSLFNAFGRI 450
    STSVKELENF RNLLQNIH 468
    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:
    EMBL
    GenBank
    DDBJ
    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_014584.1.
    UniGeneiHs.592304.

    Genome annotation databases

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

    Polymorphism databases

    DMDMi50400608.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9709.1.
    RefSeqi NP_055399.1. NM_014584.1.
    UniGenei Hs.592304.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3AHQ X-ray 2.35 A 22-468 [» ]
    3AHR X-ray 3.07 A 22-468 [» ]
    ProteinModelPortali Q96HE7.
    SMRi Q96HE7. Positions 34-465.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119025. 20 interactions.
    IntActi Q96HE7. 7 interactions.
    MINTi MINT-144080.
    STRINGi 9606.ENSP00000379042.

    Chemistry

    BindingDBi Q96HE7.
    ChEMBLi CHEMBL1671609.

    PTM databases

    PhosphoSitei Q96HE7.

    Polymorphism databases

    DMDMi 50400608.

    Proteomic databases

    MaxQBi Q96HE7.
    PaxDbi Q96HE7.
    PeptideAtlasi Q96HE7.
    PRIDEi Q96HE7.

    Protocols and materials databases

    DNASUi 30001.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395686 ; ENSP00000379042 ; ENSG00000197930 .
    GeneIDi 30001.
    KEGGi hsa:30001.
    UCSCi uc001wzv.3. human.

    Organism-specific databases

    CTDi 30001.
    GeneCardsi GC14M053106.
    HGNCi HGNC:13280. ERO1L.
    HPAi CAB034294.
    HPA026653.
    HPA030053.
    MIMi 615435. gene.
    neXtProti NX_Q96HE7.
    PharmGKBi PA27862.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5061.
    HOGENOMi HOG000012778.
    HOVERGENi HBG051507.
    KOi K10950.
    OMAi EADDIHS.
    OrthoDBi EOG7PP579.
    PhylomeDBi Q96HE7.
    TreeFami TF314471.

    Enzyme and pathway databases

    Reactomei REACT_15550. Insulin processing.
    REACT_172715. Detoxification of Reactive Oxygen Species.

    Miscellaneous databases

    EvolutionaryTracei Q96HE7.
    GeneWikii ERO1L.
    GenomeRNAii 30001.
    NextBioi 52816.
    PROi Q96HE7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96HE7.
    Bgeei Q96HE7.
    CleanExi HS_ERO1L.
    Genevestigatori Q96HE7.

    Family and domain databases

    InterProi IPR007266. Ero1.
    [Graphical view ]
    PANTHERi PTHR12613. PTHR12613. 1 hit.
    Pfami PF04137. ERO1. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF017205. ERO1. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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. "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: October 1, 2014
    This is version 124 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