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Q96HE7 (ERO1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
ERO1-like protein alpha

Short name=ERO1-L
Short name=ERO1-L-alpha
EC=1.8.4.-
Alternative name(s):
Endoplasmic oxidoreductin-1-like protein
Oxidoreductin-1-L-alpha
Gene names
Name:ERO1L
ORF Names:UNQ434/PRO865
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.8 Ref.10 Ref.11 Ref.17 Ref.18 Ref.23

Cofactor

FAD. Ref.18 Ref.24

Enzyme regulation

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. Ref.15 Ref.17 Ref.18

Subunit structure

Predominantly monomer. May function both as a monomer and a homodimer. Interacts with PDILT. Ref.7 Ref.10 Ref.16 Ref.18

Subcellular location

Endoplasmic reticulum membrane; Peripheral membrane protein; Lumenal side. Note: The association with ERP44 is essential for its retention in the endoplasmic reticulum. Ref.1 Ref.13

Tissue specificity

Widely expressed at low level. Expressed at high level in upper digestive tract. Highly expressed in esophagus. Weakly expressed in stomach and duodenum. Ref.9

Induction

Stimulated by hypoxia; suggesting that it is regulated via the HIF-pathway. Ref.12 Ref.15 Ref.17 Ref.18

Post-translational modification

N-glycosylated. Ref.1 Ref.8

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 (Ref.23).

Sequence similarities

Belongs to the EROs family.

Ontologies

Keywords
   Biological processApoptosis
Electron transport
Transport
   Cellular componentEndoplasmic reticulum
Membrane
   DomainRedox-active center
Signal
   LigandFAD
Flavoprotein
   Molecular functionOxidoreductase
   PTMDisulfide bond
Glycoprotein
Phosphoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processbrown fat cell differentiation

Inferred from electronic annotation. Source: Ensembl

cellular protein metabolic process

Traceable author statement. Source: Reactome

cellular protein modification process

Traceable author statement Ref.1. Source: ProtInc

chaperone mediated protein folding requiring cofactor

Inferred from direct assay Ref.10. Source: UniProtKB

endoplasmic reticulum unfolded protein response

Inferred from electronic annotation. Source: Ensembl

intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

protein folding

Traceable author statement Ref.1. Source: ProtInc

release of sequestered calcium ion into cytosol

Inferred from sequence or structural similarity. Source: UniProtKB

response to endoplasmic reticulum stress

Inferred from sequence or structural similarity. Source: UniProtKB

response to temperature stimulus

Traceable author statement Ref.1. Source: ProtInc

   Cellular_componentendoplasmic reticulum

Inferred from direct assay Ref.1. Source: UniProtKB

endoplasmic reticulum lumen

Traceable author statement. Source: Reactome

endoplasmic reticulum membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

intracellular membrane-bounded organelle

Traceable author statement Ref.1. Source: ProtInc

membrane

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionoxidoreductase activity

Inferred from direct assay Ref.10. Source: UniProtKB

oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor

Inferred from electronic annotation. Source: InterPro

protein binding

Inferred from physical interaction PubMed 17170699PubMed 20802462. Source: IntAct

protein disulfide isomerase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Ref.6
Chain24 – 468445ERO1-like protein alpha
PRO_0000008415

Sites

Binding site1871FAD
Binding site1891FAD
Binding site2001FAD
Binding site2521FAD
Binding site2551FAD
Binding site2871FAD
Binding site3001FAD

Amino acid modifications

Modified residue1431Phosphoserine Ref.20
Glycosylation2801N-linked (GlcNAc...) Ref.19
Glycosylation3841N-linked (GlcNAc...) Potential
Disulfide bond35 ↔ 48 Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond37 ↔ 46 Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond85 ↔ 391 Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond94 ↔ 131Alternate Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond94 ↔ 99Redox-active; alternate Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond99 ↔ 104Alternate Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond208 ↔ 241 Ref.17 Ref.18 Ref.23 Ref.24
Disulfide bond394 ↔ 397Redox-active Ref.17 Ref.18 Ref.23 Ref.24

Experimental info

Mutagenesis851C → A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards P4HB; when associated with A-131. Ref.14 Ref.18
Mutagenesis851C → S: Induces a decrease in activity. Ref.14 Ref.18
Mutagenesis941C → 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. Ref.14 Ref.18
Mutagenesis991C → A: Acts as a weak dominant-negative mutant. Loss of activity towards thioredoxin. Loss of regulatory disulfide bond formation; when associated with A-94. Ref.14 Ref.18
Mutagenesis1041C → A: No effect. Strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-131. Ref.14 Ref.18 Ref.23
Mutagenesis1041C → S: No effect. Ref.14 Ref.18 Ref.23
Mutagenesis1311C → 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. Ref.14 Ref.17 Ref.18 Ref.23
Mutagenesis1661C → A: No effect. Ref.14 Ref.18
Mutagenesis2081C → A or S: No effect. Ref.14 Ref.18
Mutagenesis2411C → A or S: No effect. Ref.14 Ref.18
Mutagenesis2801N → A: No effect on activity. Ref.14
Mutagenesis3841N → A: No effect on activity. Ref.14
Mutagenesis3911C → A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB. Ref.1 Ref.8 Ref.14
Mutagenesis3941C → A: Retains activity towards P4HB. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB. Ref.1 Ref.8 Ref.10 Ref.14 Ref.17
Mutagenesis3951F → D: Increased catalytical activity. Ref.22
Mutagenesis3971C → A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB. Ref.8 Ref.10 Ref.14
Sequence conflict4561E → K in AAH08674. Ref.5

Secondary structure

..................................................... 468
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q96HE7 [UniParc].

Last modified July 19, 2004. Version 2.
Checksum: 92ECE6531C9CCA33

FASTA46854,393
        10         20         30         40         50         60 
MGRGWGFLFG LLGAVWLLSS GHGEEQPPET AAQRCFCQVS GYLDDCTCDV ETIDRFNNYR 

        70         80         90        100        110        120 
LFPRLQKLLE SDYFRYYKVN LKRPCPFWND ISQCGRRDCA VKPCQSDEVP DGIKSASYKY 

       130        140        150        160        170        180 
SEEANNLIEE CEQAERLGAV DESLSEETQK AVLQWTKHDD SSDNFCEADD IQSPEAEYVD 

       190        200        210        220        230        240 
LLLNPERYTG YKGPDAWKIW NVIYEENCFK PQTIKRPLNP LASGQGTSEE NTFYSWLEGL 

       250        260        270        280        290        300 
CVEKRAFYRL ISGLHASINV HLSARYLLQE TWLEKKWGHN ITEFQQRFDG ILTEGEGPRR 

       310        320        330        340        350        360 
LKNLYFLYLI ELRALSKVLP FFERPDFQLF TGNKIQDEEN KMLLLEILHE IKSFPLHFDE 

       370        380        390        400        410        420 
NSFFAGDKKE AHKLKEDFRL HFRNISRIMD CVGCFKCRLW GKLQTQGLGT ALKILFSEKL 

       430        440        450        460 
IANMPESGPS YEFHLTRQEI VSLFNAFGRI STSVKELENF RNLLQNIH 

« Hide

References

« Hide 'large scale' references
[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]"The secreted protein discovery initiative (SPDI), a large-scale effort to identify novel human secreted and transmembrane proteins: a bioinformatics assessment."
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E. expand/collapse author list , Heldens S., Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.
Genome Res. 13:2265-2270(2003) [PubMed] [Europe PMC] [Abstract]
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. expand/collapse author list , 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. expand/collapse author list , 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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS9709.1.
RefSeqNP_055399.1. NM_014584.1.
UniGeneHs.592304.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AHQX-ray2.35A22-468[»]
3AHRX-ray3.07A22-468[»]
ProteinModelPortalQ96HE7.
SMRQ96HE7. Positions 34-465.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119025. 20 interactions.
IntActQ96HE7. 7 interactions.
MINTMINT-144080.
STRING9606.ENSP00000379042.

Chemistry

BindingDBQ96HE7.
ChEMBLCHEMBL1671609.

PTM databases

PhosphoSiteQ96HE7.

Polymorphism databases

DMDM50400608.

Proteomic databases

MaxQBQ96HE7.
PaxDbQ96HE7.
PeptideAtlasQ96HE7.
PRIDEQ96HE7.

Protocols and materials databases

DNASU30001.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000395686; ENSP00000379042; ENSG00000197930.
GeneID30001.
KEGGhsa:30001.
UCSCuc001wzv.3. human.

Organism-specific databases

CTD30001.
GeneCardsGC14M053106.
HGNCHGNC:13280. ERO1L.
HPACAB034294.
HPA026653.
HPA030053.
MIM615435. gene.
neXtProtNX_Q96HE7.
PharmGKBPA27862.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5061.
HOGENOMHOG000012778.
HOVERGENHBG051507.
KOK10950.
OMAEADDIHS.
OrthoDBEOG7PP579.
PhylomeDBQ96HE7.
TreeFamTF314471.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_17015. Metabolism of proteins.

Gene expression databases

ArrayExpressQ96HE7.
BgeeQ96HE7.
CleanExHS_ERO1L.
GenevestigatorQ96HE7.

Family and domain databases

InterProIPR007266. Ero1.
[Graphical view]
PANTHERPTHR12613. PTHR12613. 1 hit.
PfamPF04137. ERO1. 1 hit.
[Graphical view]
PIRSFPIRSF017205. ERO1. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ96HE7.
GeneWikiERO1L.
GenomeRNAi30001.
NextBio52816.
PROQ96HE7.
SOURCESearch...

Entry information

Entry nameERO1A_HUMAN
AccessionPrimary (citable) accession number: Q96HE7
Secondary accession number(s): A8K9X4 expand/collapse secondary AC list , A8MYW1, Q7LD45, Q9P1Q9, Q9UKV6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: July 9, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM