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Entry version 167 (18 Sep 2019)
Sequence version 2 (19 Jul 2004)
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Protein

ERO1-like protein alpha

Gene

ERO1A

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

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

FAD2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity 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)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei187FADCombined sources1 Publication1
Binding sitei189FADCombined sources1 Publication1
Binding sitei200FADCombined sources1 Publication1
Binding sitei252FADCombined sources1 Publication1
Binding sitei255FADCombined sources1 Publication1
Binding sitei287FADCombined sources1 Publication1
Binding sitei300FADCombined sources1 Publication1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionOxidoreductase
Biological processApoptosis, Electron transport, Transport
LigandFAD, Flavoprotein

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-HSA-264876 Insulin processing
R-HSA-3299685 Detoxification of Reactive Oxygen Species

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>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
Endoplasmic reticulum oxidoreductase alphaImported
Oxidoreductin-1-L-alpha
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:ERO1AImported
Synonyms:ERO1L
ORF Names:UNQ434/PRO865
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 14

Organism-specific databases

Human Gene Nomenclature Database

More...
HGNCi
HGNC:13280 ERO1A

Online Mendelian Inheritance in Man (OMIM)

More...
MIMi
615435 gene

neXtProt; the human protein knowledge platform

More...
neXtProti
NX_Q96HE7

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Endoplasmic reticulum, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi85C → A: Alters protein folding and stability. Loss of regulatory disulfide bond formation and increased activity towards P4HB; when associated with A-131. 2 Publications1
Mutagenesisi85C → S: Induces a decrease in activity. 2 Publications1
Mutagenesisi94C → 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 Publications1
Mutagenesisi99C → 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 Publications1
Mutagenesisi104C → A: No effect. Strongly increased activity towards P4HB and UPR induction, but no broad oxidative injury; when associated with A-131. 3 Publications1
Mutagenesisi104C → S: No effect. 3 Publications1
Mutagenesisi131C → 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 Publications1
Mutagenesisi166C → A: No effect. 2 Publications1
Mutagenesisi208C → A or S: No effect. 2 Publications1
Mutagenesisi241C → A or S: No effect. 2 Publications1
Mutagenesisi280N → A: No effect on activity. 1 Publication1
Mutagenesisi384N → A: No effect on activity. 1 Publication1
Mutagenesisi391C → A: Alters protein folding. Prevents formation of regulatory disulfide bond and down-regulation of activity. Decreases association with P4HB. 3 Publications1
Mutagenesisi394C → A: Retains activity towards P4HB. Does not act as a dominant negative mutant. Induces defects in folding. Remains associated with P4HB. 5 Publications1
Mutagenesisi395F → D: Increased catalytical activity. 1 Publication1
Mutagenesisi397C → A: Acts as a dominant negative mutant; does not induce defects in folding; remains associated with P4HB. 3 Publications1

Organism-specific databases

DisGeNET

More...
DisGeNETi
30001

Open Targets

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OpenTargetsi
ENSG00000197930

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...
PharmGKBi
PA27862

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
Q96HE7

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...
ChEMBLi
CHEMBL1671609

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...
BioMutai
ERO1A

Domain mapping of disease mutations (DMDM)

More...
DMDMi
50400608

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 231 PublicationAdd BLAST23
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000841524 – 468ERO1-like protein alphaAdd BLAST445

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi35 ↔ 48Combined sources1 Publication
Disulfide bondi37 ↔ 46Combined sources1 Publication
Disulfide bondi85 ↔ 391Combined sources1 Publication
Disulfide bondi94 ↔ 131AlternateCombined sources1 Publication
Disulfide bondi94 ↔ 99Redox-active; alternate2 Publications
Disulfide bondi99 ↔ 104AlternateCurated
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei106PhosphoserineCombined sources1
Modified residuei143PhosphoserineCombined sources1
Disulfide bondi208 ↔ 241Combined sources1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi280N-linked (GlcNAc...) asparagine1 Publication1
Glycosylationi384N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi394 ↔ 397Redox-activeCombined sources1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>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

Encyclopedia of Proteome Dynamics

More...
EPDi
Q96HE7

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q96HE7

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
Q96HE7

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q96HE7

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q96HE7

PeptideAtlas

More...
PeptideAtlasi
Q96HE7

PRoteomics IDEntifications database

More...
PRIDEi
Q96HE7

ProteomicsDB: a multi-organism proteome resource

More...
ProteomicsDBi
76737

PTM databases

GlyConnect protein glycosylation platform

More...
GlyConnecti
1225

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q96HE7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q96HE7

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q96HE7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>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

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSG00000197930 Expressed in 218 organ(s), highest expression level in esophagus squamous epithelium

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
Q96HE7 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
Q96HE7 HS

Organism-specific databases

Human Protein Atlas

More...
HPAi
CAB034294
HPA026653
HPA030053

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Predominantly monomer. May function both as a monomer and a homodimer.

Interacts with PDILT.

3 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section%27">Interaction</a> section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
119025, 28 interactors

Protein interaction database and analysis system

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IntActi
Q96HE7, 17 interactors

Molecular INTeraction database

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MINTi
Q96HE7

STRING: functional protein association networks

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STRINGi
9606.ENSP00000379042

Chemistry databases

BindingDB database of measured binding affinities

More...
BindingDBi
Q96HE7

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1468
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q96HE7

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

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EvolutionaryTracei
Q96HE7

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the EROs family.Curated

Keywords - Domaini

Redox-active center, Signal

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG2608 Eukaryota
COG5061 LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00390000007753

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000012778

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
Q96HE7

KEGG Orthology (KO)

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KOi
K10950

Identification of Orthologs from Complete Genome Data

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OMAi
SDSFCEA

Database of Orthologous Groups

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OrthoDBi
1181226at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
Q96HE7

TreeFam database of animal gene trees

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TreeFami
TF314471

Family and domain databases

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR007266 Ero1
IPR037192 ERO1-like_sf

The PANTHER Classification System

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PANTHERi
PTHR12613 PTHR12613, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF04137 ERO1, 1 hit

PIRSF; a whole-protein classification database

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PIRSFi
PIRSF017205 ERO1, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF110019 SSF110019, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

This entry has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

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
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i92ECE6531C9CCA33
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V5B3G3V5B3_HUMAN
ERO1-like protein alpha
ERO1A
169Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V3E6G3V3E6_HUMAN
ERO1-like protein alpha
ERO1A
257Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V503G3V503_HUMAN
ERO1-like protein alpha
ERO1A
125Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
G3V2H0G3V2H0_HUMAN
ERO1-like protein alpha
ERO1A
75Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti456E → K in AAH08674 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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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

The Consensus CDS (CCDS) project

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CCDSi
CCDS9709.1

NCBI Reference Sequences

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RefSeqi
NP_055399.1, NM_014584.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

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Ensembli
ENST00000395686; ENSP00000379042; ENSG00000197930

Database of genes from NCBI RefSeq genomes

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GeneIDi
30001

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
hsa:30001

UCSC genome browser

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UCSCi
uc001wzv.4 human

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>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

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

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PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3AHQX-ray2.35A22-468[»]
3AHRX-ray3.07A22-468[»]
SMRiQ96HE7
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi119025, 28 interactors
IntActiQ96HE7, 17 interactors
MINTiQ96HE7
STRINGi9606.ENSP00000379042

Chemistry databases

BindingDBiQ96HE7
ChEMBLiCHEMBL1671609

PTM databases

GlyConnecti1225
iPTMnetiQ96HE7
PhosphoSitePlusiQ96HE7
SwissPalmiQ96HE7

Polymorphism and mutation databases

BioMutaiERO1A
DMDMi50400608

Proteomic databases

EPDiQ96HE7
jPOSTiQ96HE7
MassIVEiQ96HE7
MaxQBiQ96HE7
PaxDbiQ96HE7
PeptideAtlasiQ96HE7
PRIDEiQ96HE7
ProteomicsDBi76737

Protocols and materials databases

The DNASU plasmid repository

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DNASUi
30001

Genome annotation databases

EnsembliENST00000395686; ENSP00000379042; ENSG00000197930
GeneIDi30001
KEGGihsa:30001
UCSCiuc001wzv.4 human

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
30001
DisGeNETi30001

GeneCards: human genes, protein and diseases

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GeneCardsi
ERO1A
HGNCiHGNC:13280 ERO1A
HPAiCAB034294
HPA026653
HPA030053
MIMi615435 gene
neXtProtiNX_Q96HE7
OpenTargetsiENSG00000197930
PharmGKBiPA27862

GenAtlas: human gene database

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GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG2608 Eukaryota
COG5061 LUCA
GeneTreeiENSGT00390000007753
HOGENOMiHOG000012778
InParanoidiQ96HE7
KOiK10950
OMAiSDSFCEA
OrthoDBi1181226at2759
PhylomeDBiQ96HE7
TreeFamiTF314471

Enzyme and pathway databases

ReactomeiR-HSA-264876 Insulin processing
R-HSA-3299685 Detoxification of Reactive Oxygen Species

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

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ChiTaRSi
ERO1A human
EvolutionaryTraceiQ96HE7

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
ERO1L

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

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GenomeRNAii
30001
PharosiQ96HE7

Protein Ontology

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PROi
PR:Q96HE7

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000197930 Expressed in 218 organ(s), highest expression level in esophagus squamous epithelium
ExpressionAtlasiQ96HE7 baseline and differential
GenevisibleiQ96HE7 HS

Family and domain databases

InterProiView protein in InterPro
IPR007266 Ero1
IPR037192 ERO1-like_sf
PANTHERiPTHR12613 PTHR12613, 1 hit
PfamiView protein in Pfam
PF04137 ERO1, 1 hit
PIRSFiPIRSF017205 ERO1, 1 hit
SUPFAMiSSF110019 SSF110019, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiERO1A_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q96HE7
Secondary accession number(s): A8K9X4
, A8MYW1, Q7LD45, Q9P1Q9, Q9UKV6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: July 19, 2004
Last modified: September 18, 2019
This is version 167 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

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

Documents

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