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Entry version 169 (07 Apr 2021)
Sequence version 1 (01 Nov 1997)
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Protein

Endoplasmic oxidoreductin-1

Gene

ERO1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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

Essential oxidoreductase that oxidizes proteins in the endoplasmic reticulum to produce disulfide bonds. Acts by oxidizing directly PDI1 isomerase through a direct disulfide exchange. Does not act as a direct oxidant of folding substrate, but relies on PDI1 to transfer oxidizing equivalent. Also able to oxidize directly the PDI related protein MPD2. Does not oxidize all PDI related proteins, suggesting that it can discriminate between PDI1 and related proteins. Reoxidation of ERO1 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.5 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

FAD1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 Cys-150 and Cys-295.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">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 sitei187FAD1 Publication1
Binding sitei189FAD1 Publication1
Binding sitei200FAD1 Publication1
Binding sitei228FAD1 Publication1
Binding sitei231FAD1 Publication1
Binding sitei260FAD1 Publication1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei352Nucleophile1 Publication1
Active sitei3551 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 processElectron transport, Transport
LigandFAD, Flavoprotein

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...
BioCyci
MetaCyc:G3O-32708-MONOMER

<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%5Fand%5Ftaxonomy%5Fsection">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:
Endoplasmic oxidoreductin-1 (EC:1.8.4.-)
Alternative name(s):
Endoplasmic reticulum oxidoreductase protein 1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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:ERO1
Ordered Locus Names:YML130C
ORF Names:YM4987.05C
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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>OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 identifieri559292 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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 lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">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
  • UP000002311 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">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 XIII

Organism-specific databases

Saccharomyces Genome Database

More...
SGDi
S000004599, ERO1

Eukaryotic Pathogen, Vector and Host Database Resources

More...
VEuPathDBi
FungiDB:YML130C

<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

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%5Fand%5Fbiotech%5Fsection">'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>Mutagenesisi90C → A: No effect. 2 Publications1
Mutagenesisi100C → A: Impairs the capture of mixed-disulfide with PDI1 thereby blocking its function. Loss of activity; when associated with A-105. 2 Publications1
Mutagenesisi105C → A: Loss of activity. 2 Publications1
Mutagenesisi143C → A: No effect; when associated with A-166. 1 Publication1
Mutagenesisi150C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-295. 1 Publication1
Mutagenesisi166C → A: No effect; when associated with A-143. 1 Publication1
Mutagenesisi208C → A: No effect. 1 Publication1
Mutagenesisi229G → S in ERO1-1; induces defective folding of disulfide proteins. 1 Publication1
Mutagenesisi231H → Y in ERO1-2; induces defective folding of disulfide proteins. 1 Publication1
Mutagenesisi295C → A: Loss of regulatory disulfide bond and strongly increased activity towards PDI; when associated with A-150. 1 Publication1
Mutagenesisi349C → A: Does not affect activity but increases by twofold the amount of protein found in mixed disulfide with PDI1 or MPD2. 1 Publication1
Mutagenesisi352C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications1
Mutagenesisi355C → A: Loss of activity. Prevents its reoxidation thereby blocking its function. 2 Publications1

<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 – 18Sequence analysisAdd BLAST18
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000842919 – 563Endoplasmic oxidoreductin-1Add BLAST545

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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>Glycosylationi21N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi35N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi53N-linked (GlcNAc...) asparagineSequence analysis1
<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 bondi90 ↔ 349Combined sources1 Publication
Disulfide bondi100 ↔ 105Redox-activeCombined sources1 Publication
Glycosylationi130N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi143 ↔ 166Combined sources1 Publication
Disulfide bondi150 ↔ 295Combined sources1 Publication
Glycosylationi342N-linked (GlcNAc...) asparagineSequence analysis1
Disulfide bondi352 ↔ 355Redox-activeCombined sources1 Publication
Glycosylationi425N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi458N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi468N-linked (GlcNAc...) asparagineSequence analysis1
Glycosylationi491N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">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

The Cys-100/Cys-105 and Cys-352/Cys-355 disulfide bonds constitute the redox-active center. The Cys-100/Cys-105 disulfide bond may accept electron from PDI1 and funnel them to the active site disulfide Cys-352/Cys-355.
N-glycosylated.2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q03103

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

More...
PaxDbi
Q03103

PRoteomics IDEntifications database

More...
PRIDEi
Q03103

<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 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

By unfolded protein response (UPR).2 Publications

<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%5Fsection">'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%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

May function both as a monomer and a homodimer.

1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
35075, 356 interactors

Database of interacting proteins

More...
DIPi
DIP-4515N

Protein interaction database and analysis system

More...
IntActi
Q03103, 11 interactors

STRING: functional protein association networks

More...
STRINGi
4932.YML130C

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...
RNActi
Q03103, protein

<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

1563
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

More...
SMRi
Q03103

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
Q03103

<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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The C-terminal part (437-563) is required for the association with the endoplasmic reticulum lumen membrane.1 Publication

<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

More...
eggNOGi
KOG2608, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT00390000007753

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_023061_1_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q03103

Identification of Orthologs from Complete Genome Data

More...
OMAi
YRENCFQ

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR007266, Ero1
IPR037192, ERO1-like_sf

The PANTHER Classification System

More...
PANTHERi
PTHR12613, PTHR12613, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF04137, ERO1, 1 hit

PIRSF; a whole-protein classification database

More...
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%5Flength">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>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">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.

Q03103-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLRTAIATL CLTAFTSATS NNSYIATDQT QNAFNDTHFC KVDRNDHVSP
60 70 80 90 100
SCNVTFNELN AINENIRDDL SALLKSDFFK YFRLDLYKQC SFWDANDGLC
110 120 130 140 150
LNRACSVDVV EDWDTLPEYW QPEILGSFNN DTMKEADDSD DECKFLDQLC
160 170 180 190 200
QTSKKPVDIE DTINYCDVND FNGKNAVLID LTANPERFTG YGGKQAGQIW
210 220 230 240 250
STIYQDNCFT IGETGESLAK DAFYRLVSGF HASIGTHLSK EYLNTKTGKW
260 270 280 290 300
EPNLDLFMAR IGNFPDRVTN MYFNYAVVAK ALWKIQPYLP EFSFCDLVNK
310 320 330 340 350
EIKNKMDNVI SQLDTKIFNE DLVFANDLSL TLKDEFRSRF KNVTKIMDCV
360 370 380 390 400
QCDRCRLWGK IQTTGYATAL KILFEINDAD EFTKQHIVGK LTKYELIALL
410 420 430 440 450
QTFGRLSESI ESVNMFEKMY GKRLNGSENR LSSFFQNNFF NILKEAGKSI
460 470 480 490 500
RYTIENINST KEGKKKTNNS QSHVFDDLKM PKAEIVPRPS NGTVNKWKKA
510 520 530 540 550
WNTEVNNVLE AFRFIYRSYL DLPRNIWELS LMKVYKFWNK FIGVADYVSE
560
ETREPISYKL DIQ
Length:563
Mass (Da):65,033
Last modified:November 1, 1997 - v1
<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:i928CE700AE6137EF
GO

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 conflicti555P → L in AAT93069 (PubMed:17322287).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
Z50178 Genomic DNA Translation: CAA90553.1
AY693050 Genomic DNA Translation: AAT93069.1
BK006946 Genomic DNA Translation: DAA09769.1

Protein sequence database of the Protein Information Resource

More...
PIRi
S58198

NCBI Reference Sequences

More...
RefSeqi
NP_013576.1, NM_001182493.1

Genome annotation databases

Ensembl fungal genome annotation project

More...
EnsemblFungii
YML130C_mRNA; YML130C; YML130C

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
854909

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
sce:YML130C

<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
Z50178 Genomic DNA Translation: CAA90553.1
AY693050 Genomic DNA Translation: AAT93069.1
BK006946 Genomic DNA Translation: DAA09769.1
PIRiS58198
RefSeqiNP_013576.1, NM_001182493.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RP4X-ray2.20A56-424[»]
1RQ1X-ray2.80A56-424[»]
3M31X-ray1.85A56-424[»]
3NVJX-ray3.20A56-424[»]
SMRiQ03103
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi35075, 356 interactors
DIPiDIP-4515N
IntActiQ03103, 11 interactors
STRINGi4932.YML130C

Proteomic databases

MaxQBiQ03103
PaxDbiQ03103
PRIDEiQ03103

Genome annotation databases

EnsemblFungiiYML130C_mRNA; YML130C; YML130C
GeneIDi854909
KEGGisce:YML130C

Organism-specific databases

SGDiS000004599, ERO1
VEuPathDBiFungiDB:YML130C

Phylogenomic databases

eggNOGiKOG2608, Eukaryota
GeneTreeiENSGT00390000007753
HOGENOMiCLU_023061_1_0_1
InParanoidiQ03103
OMAiYRENCFQ

Enzyme and pathway databases

BioCyciMetaCyc:G3O-32708-MONOMER

Miscellaneous databases

EvolutionaryTraceiQ03103

Protein Ontology

More...
PROi
PR:Q03103
RNActiQ03103, protein

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

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
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 nameiERO1_YEAST
<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: Q03103
Secondary accession number(s): D6W0F5, E9P913
<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%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: April 7, 2021
This is version 169 of the entry and version 1 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 programFungal Protein Annotation Program

<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, Reference proteome

Documents

  1. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  2. Yeast chromosome XIII
    Yeast (Saccharomyces cerevisiae) chromosome XIII: entries and gene names
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
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