Q96HE7 (ERO1A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	468 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly P4HB/PDI isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on P4HB/PDI to transfer oxidizing equivalent. Associates with ERP44 but not with GRP54, demonstrating that it does not oxidize all PDI related proteins and can discriminate between PDI and related proteins. Its reoxidation probably involves electron transfer to molecular oxygen via FAD. Acts independently of glutathione. May be responsible for a significant proportion of reactive oxygen species (ROS) in the cell, thereby being a source of oxidative stress. Required for the folding of immunoglobulin proteins. Responsible for 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.7 Ref.9 Ref.11 Ref.17 Ref.18
Cofactor	FAD. Ref.18 Ref.22
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.9 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.8
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.7 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.
Sequence similarities	Belongs to the EROs family.

Ontologies

Keywords
Biological process	Apoptosis Electron transport Transport
Cellular component	Endoplasmic reticulum Membrane
Domain	Redox-active center Signal
Ligand	FAD Flavoprotein
Molecular function	Oxidoreductase
PTM	Disulfide bond Glycoprotein Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	brown fat cell differentiation Inferred from electronic annotation. Source: Compara cellular protein modification process Traceable author statement Ref.1. Source: ProtInc chaperone mediated protein folding requiring cofactor Inferred from direct assay Ref.9. Source: UniProtKB electron transport chain Inferred from electronic annotation. Source: UniProtKB-KW endoplasmic reticulum unfolded protein response Inferred from electronic annotation. Source: Compara intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress Inferred from sequence or structural similarity. Source: UniProtKB release of sequestered calcium ion into cytosol Inferred from sequence or structural similarity. Source: UniProtKB response to temperature stimulus Traceable author statement Ref.1. Source: ProtInc
Cellular_component	endoplasmic reticulum lumen Traceable author statement. Source: Reactome endoplasmic reticulum membrane Inferred from electronic annotation. Source: UniProtKB-SubCell membrane Traceable author statement Ref.1. Source: ProtInc
Molecular_function	flavin adenine dinucleotide binding Inferred from electronic annotation. Source: InterPro oxidoreductase activity Inferred from direct assay Ref.9. Source: UniProtKB oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor Inferred from electronic annotation. Source: InterPro protein disulfide isomerase activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 23

23

Ref.6

Chain

24 – 468

445

ERO1-like protein alpha

PRO_0000008415

Sites

Binding site

187

1

FAD

Binding site

189

1

FAD

Binding site

200

1

FAD

Binding site

252

1

FAD

Binding site

255

1

FAD

Binding site

287

1

FAD

Binding site

300

1

FAD

Amino acid modifications

Modified residue

143

1

Phosphoserine Ref.20

Glycosylation

280

1

N-linked (GlcNAc...) Ref.19

Glycosylation

384

1

N-linked (GlcNAc...) Potential

Disulfide bond

35 ↔ 48

Ref.17 Ref.18 Ref.22

Disulfide bond

37 ↔ 46

Ref.17 Ref.18 Ref.22

Disulfide bond

85 ↔ 391

Ref.17 Ref.18 Ref.22

Disulfide bond

94 ↔ 131

Alternate Ref.17 Ref.18 Ref.22

Disulfide bond

94 ↔ 99

Redox-active Ref.17 Ref.18 Ref.22

Disulfide bond

99 ↔ 104

Alternate Ref.17 Ref.18 Ref.22

Disulfide bond

208 ↔ 241

Ref.17 Ref.18 Ref.22

Disulfide bond

394 ↔ 397

Redox-active Ref.17 Ref.18 Ref.22

Experimental info

Mutagenesis

85

1

C → A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards PDI; when associated with A-131. Ref.14 Ref.18

Mutagenesis

85

1

C → S: Induces a decrease in activity. Ref.14 Ref.18

Mutagenesis

94

1

C → 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

Mutagenesis

99

1

C → 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

Mutagenesis

104

1

C → A: No effect. Strongly increased activity towards PDI; when associated with A-131. Ref.14 Ref.18

Mutagenesis

104

1

C → S: No effect. Ref.14 Ref.18

Mutagenesis

131

1

C → A: Loss of regulatory disulfide bond formation and increased activity towards PDI. Loss of regulatory disulfide bond formation and strongly increased activity towards PDI; when associated with A-85. Loss of regulatory disulfide bond formation and strongly increased activity towards PDI; when associated with A-104. Ref.14 Ref.17 Ref.18

Mutagenesis

166

1

C → A: No effect. Ref.14 Ref.18

Mutagenesis

208

1

C → A or S: No effect. Ref.14 Ref.18

Mutagenesis

241

1

C → A or S: No effect. Ref.14 Ref.18

Mutagenesis

280

1

N → A: No effect on activity. Ref.14

Mutagenesis

384

1

N → A: No effect on activity. Ref.14

Mutagenesis

391

1

C → A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB. Ref.1 Ref.7 Ref.14

Mutagenesis

394

1

C → A: Retains activity towards PDI. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB. Ref.1 Ref.7 Ref.9 Ref.14 Ref.17

Mutagenesis

397

1

C → A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB. Ref.7 Ref.9 Ref.14

Sequence conflict

456

1

E → K in AAH08674. Ref.5

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

468

Helix Strand Turn

Details...

Beta strand

35 – 38

4

Beta strand

40 – 43

4

Beta strand

45 – 47

3

Helix

50 – 59

10

Helix

62 – 70

9

Helix

72 – 75

4

Beta strand

76 – 79

4

Helix

134 – 138

5

Helix

146 – 161

16

Beta strand

177 – 180

4

Helix

181 – 183

3

Helix

193 – 204

12

Helix

245 – 264

20

Beta strand

266 – 270

5

Beta strand

275 – 278

4

Helix

281 – 288

8

Helix

290 – 293

4

Helix

296 – 317

22

Helix

319 – 323

5

Helix

336 – 353

18

Beta strand

356 – 358

3

Helix

369 – 389

21

Helix

395 – 415

21

Helix

418 – 422

5

Beta strand

426 – 428

3

Beta strand

431 – 433

3

Helix

437 – 463

27

Sequences

	Sequence		Length	Mass (Da)
	Q96HE7 [UniParc]. Last modified July 19, 2004. Version 2. Checksum: 92ECE6531C9CCA33	FASTA	468	54,393
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY.
[7]	"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.
[8]	"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.
[9]	"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.
[10]	"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.
[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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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]	"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.

IPI

IPI00386755.

RefSeq

NP_055399.1. NM_014584.1.

UniGene

Hs.592304.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
3AHQ	X-ray	2.35	A	22-468	[»]
3AHR	X-ray	3.07	A	22-468	[»]

ProteinModelPortal

Q96HE7.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q96HE7. 4 interactions.

MINT

MINT-144080.

STRING

9606.ENSP00000379042.

PTM databases

PhosphoSite

Q96HE7.

Polymorphism databases

DMDM

50400608.

Proteomic databases

PaxDb

Q96HE7.

PeptideAtlas

Q96HE7.

PRIDE

Q96HE7.

Protocols and materials databases

DNASU

30001.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000395686; ENSP00000379042; ENSG00000197930.

GeneID

30001.

KEGG

hsa:30001.

UCSC

uc001wzv.3. human.

Organism-specific databases

CTD

30001.

GeneCards

GC14M053106.

HGNC

HGNC:13280. ERO1L.

HPA

CAB034294.
HPA026653.
HPA030053.

neXtProt

NX_Q96HE7.

PharmGKB

PA27862.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5061.

HOGENOM

HOG000012778.

HOVERGEN

HBG051507.

KO

K10950.

OMA

YLLQETW.

OrthoDB

EOG4T7833.

Enzyme and pathway databases

Reactome

REACT_116125. Disease.

Gene expression databases

ArrayExpress

Q96HE7.

Bgee

Q96HE7.

CleanEx

HS_ERO1L.

Genevestigator

Q96HE7.

GermOnline

ENSG00000197930. Homo sapiens.

Family and domain databases

InterPro

IPR007266. ER_oxidoreductin-1.
[Graphical view]

PANTHER

PTHR12613. PTHR12613. 1 hit.

Pfam

PF04137. ERO1. 1 hit.
[Graphical view]

PIRSF

PIRSF017205. ERO1. 1 hit.

SUPFAM

SSF110019. ERO1. 1 hit.

ProtoNet

Search...

Other

BindingDB

Q96HE7.

ChEMBL

CHEMBL1671609.

EvolutionaryTrace

Q96HE7.

GenomeRNAi

30001.

NextBio

52816.

Entry information

Entry name

ERO1A_HUMAN

Accession

Primary (citable) accession number: Q96HE7
Secondary accession number(s): A8K9X4 , A8MYW1, Q7LD45, Q9P1Q9, Q9UKV6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2004
Last sequence update:	July 19, 2004
Last modified:	May 1, 2013
This is version 110 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.