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UniProtKB - P34914 (HYES_MOUSE)

Entry version 186 (02 Jun 2021)
Sequence version 2 (01 Oct 1996)
Previous versions | rss
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Protein

Bifunctional epoxide hydrolase 2

Gene

Ephx2

Organism
Mus musculus (Mouse)
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

Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:7840649, PubMed:21217101).

Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity).

Also determines steady-state levels of physiological mediators (By similarity).

By similarity2 Publications

Bifunctional enzyme. The N-terminal domain has lipid phosphatase activity, with the highest activity towards threo-9,10-phosphonooxy-hydroxy-octadecanoic acid, followed by erythro-9,10-phosphonooxy-hydroxy-octadecanoic acid, 12-phosphonooxy-octadec-9Z-enoic acid and 12-phosphonooxy-octadec-9E-enoic acid (By similarity).

Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (By similarity).

By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<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

Mg2+By similarity

<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

Inhibited by 1-(1-acetylpiperidin-4-yl)-3-(4-(trifl uoromethoxy)phenyl)urea (TPAU), 1-cyclohexyl-3-dodecylurea (CDU), 12-(3-adamantan-1-yl-ureido)-dodecanoic acid (AUDA), 1-((3S, 5S, 7S)-adamantan-1-yl)-3-(5-(2-(2-ethoxyethoxy) ethoxy)pentyl)urea (AEPU), N-adamantyl-N[']-cyclohexyl urea (ACU), 4-(((1S, 4S)-4-(3-((3S, 5S, 7S)-adamantan-1-yl) ureido)cyclohexyl)oxy)benzoic acid (c-AUCB), 4-(((1R, 4R)-4-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido)cyclohexyl)oxy)benzoic acid (t-AUCB), 4-(((1R, 4R)-4-(3-(4(trifluoromethoxy)phenyl)ureido)cyclohexyl)oxy)benzoic acid (t-TAUCB) and to a lesser extent by 8-(3-((3S, 5S, 7S)-adamantan-1-yl)ureido) octanoic acid (AUOA) (By similarity). Phosphatase activity is inhibited by dodecyl-phosphate, phospholipids such as phospho-lysophosphatidic acids and fatty acids such as palmitic acid and lauric acid (PubMed:21217101).By similarity1 Publication

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=4 µM for 14(R),15(S)-EET1 Publication
  2. KM=5 µM for 14(S),15(R)-EET1 Publication
  3. KM=3 µM for 11(R),12(R)-EET1 Publication
  4. KM=4 µM for 11(S),12(R)-EET1 Publication
  5. KM=41 µM for 8(R),9(S)-EET1 Publication
  6. KM=5 µM for 8(S),9(R)-EET1 Publication
  1. Vmax=9.03 µmol/min/mg enzyme with 14(R),15(S)-EET as substrate1 Publication
  2. Vmax=1.36 µmol/min/mg enzyme with 14(S),15(R)-EET as substrate1 Publication
  3. Vmax=0.82 µmol/min/mg enzyme with 11(R),12(R)-EET as substrate1 Publication
  4. Vmax=3.02 µmol/min/mg enzyme with 11(S),12(R)-EET as substrate1 Publication
  5. Vmax=0.83 µmol/min/mg enzyme with 8(R),9(S)-EET as substrate1 Publication
  6. Vmax=3.10 µmol/min/mg enzyme with 8(S),9(R)-EET as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi9MagnesiumBy similarity1
Metal bindingi11MagnesiumBy similarity1
Metal bindingi185MagnesiumBy similarity1
<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 sitei333Nucleophile2 Publications1
<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 sitei381SubstrateBy similarity1
Active sitei465Proton donor2 Publications1
Active sitei523Proton acceptor2 Publications1

<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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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 functionHydrolase, Multifunctional enzyme
Biological processAromatic hydrocarbons catabolism, Detoxification, Lipid metabolism
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.3.2.10, 3474

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-2142670, Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
R-MMU-9018682, Biosynthesis of maresins
R-MMU-9033241, Peroxisomal protein import

Protein family/group databases

ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins

More...ESTHERi		mouse-hyes, Epoxide_hydrolase

MEROPS protease database

More...MEROPSi		S33.973

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001106

<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:
Bifunctional epoxide hydrolase 2Curated
Including the following 2 domains:
Cytosolic epoxide hydrolase 2 (EC:3.3.2.101 Publication)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase1 Publication
Short name:
SEH1 Publication
Lipid-phosphate phosphatase (EC:3.1.3.76By similarity)
<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:Ephx2Imported
Synonyms:Eph2
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 14

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:99500, Ephx2

<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

Cytoplasm, Peroxisome

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

In knockout mice, hepoxilin turnover to trioxilins is greatly abolished (PubMed:21217101). In livers, the activity toward HxA3 (8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate) and HxB3 (10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate) is greatly reduced compared with the WT mice (PubMed:21217101).1 Publication

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL4140

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2970

<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 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_00000841121 – 554Bifunctional epoxide hydrolase 2Add BLAST554

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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 residuei55N6-succinyllysineCombined sources1
Modified residuei176N6-acetyllysine; alternateCombined sources1
Modified residuei176N6-succinyllysine; alternateCombined sources1
Modified residuei191N6-acetyllysineCombined sources1
Modified residuei215N6-acetyllysineCombined sources1
Modified residuei368PhosphoserineCombined sources1
Modified residuei371N6-succinyllysineCombined sources1
Modified residuei420N6-succinyllysineCombined sources1
Modified residuei454N6-succinyllysineCombined sources1
Modified residuei504N6-succinyllysineCombined sources1
Modified residuei508N6-acetyllysine; alternateCombined sources1
Modified residuei508N6-succinyllysine; alternateCombined sources1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi521S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteineBy similarity1
Modified residuei553N6-succinyllysineCombined sources1

<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 N-terminus is blocked.
The covalent modification of cysteine by 15-deoxy-Delta12,14-prostaglandin-J2 is autocatalytic and reversible. It may occur as an alternative to other cysteine modifications, such as S-nitrosylation and S-palmitoylation (By similarity).By similarity

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P34914

MaxQB - The MaxQuant DataBase

More...MaxQBi		P34914

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

More...PaxDbi		P34914

PeptideAtlas

More...PeptideAtlasi		P34914

PRoteomics IDEntifications database

More...PRIDEi		P34914

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		267029 [P34914-1]
267030 [P34914-2]

2D gel databases

Two-dimensional polyacrylamide gel electrophoresis database from the Geneva University Hospital

More...SWISS-2DPAGEi		P34914

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P34914

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P34914

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

More...PhosphoSitePlusi		P34914

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P34914

<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

Detected in liver, intestine, ovary and kidney. Detected at low levels in heart and muscle.4 Publications

<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

Up-regulated during the luteal phase of the stimulated estrus cycle and by compounds that cause peroxisome proliferation, such as clofibrate, tiadenol and fenofibrate.3 Publications

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSMUSG00000022040, Expressed in cumulus cell and 282 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P34914, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P34914, MM

<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

Homodimer.

2 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		199481, 3 interactors

Protein interaction database and analysis system

More...IntActi		P34914, 8 interactors

Molecular INTeraction database

More...MINTi		P34914

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000069209

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P34914

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P34914, 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

1554
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		P34914

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		P34914

<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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini257 – 530AB hydrolase-1Sequence analysisAdd BLAST274

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni1 – 224PhosphataseAdd BLAST224
Regioni123 – 124Phosphate bindingBy similarity2
Regioni233 – 554Epoxide hydrolaseAdd BLAST322

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi552 – 554Microbody targeting signalSequence analysis3

<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 N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.

<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 AB hydrolase superfamily. Epoxide hydrolase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG3085, Eukaryota
KOG4178, Eukaryota

Ensembl GeneTree

More...GeneTreei		ENSGT00940000158614

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_036085_1_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P34914

Database for complete collections of gene phylogenies

More...PhylomeDBi		P34914

TreeFam database of animal gene trees

More...TreeFami		TF315395

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		1.10.150.240, 1 hit
3.40.50.1000, 1 hit
3.40.50.1820, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR029058, AB_hydrolase
IPR000073, AB_hydrolase_1
IPR000639, Epox_hydrolase-like
IPR036412, HAD-like_sf
IPR006439, HAD-SF_hydro_IA
IPR041492, HAD_2
IPR023214, HAD_sf
IPR023198, PGP-like_dom2

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00561, Abhydrolase_1, 1 hit
PF13419, HAD_2, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00111, ABHYDROLASE
PR00412, EPOXHYDRLASE

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53474, SSF53474, 1 hit
SSF56784, SSF56784, 1 hit

TIGRFAMs; a protein family database

More...TIGRFAMsi		TIGR01509, HAD-SF-IA-v3, 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>Sequences (2+)i

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P34914-1) [UniParc]FASTAAdd to basket
Also known as: Ephx2A

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide
        10         20         30         40         50
MALRVAAFDL DGVLALPSIA GAFRRSEEAL ALPRDFLLGA YQTEFPEGPT 
        60         70         80         90        100
EQLMKGKITF SQWVPLMDES YRKSSKACGA NLPENFSISQ IFSQAMAARS 
       110        120        130        140        150
INRPMLQAAI ALKKKGFTTC IVTNNWLDDG DKRDSLAQMM CELSQHFDFL 
       160        170        180        190        200
IESCQVGMIK PEPQIYNFLL DTLKAKPNEV VFLDDFGSNL KPARDMGMVT 
       210        220        230        240        250
ILVHNTASAL RELEKVTGTQ FPEAPLPVPC NPNDVSHGYV TVKPGIRLHF 
       260        270        280        290        300
VEMGSGPALC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP 
       310        320        330        340        350
PEIEEYAMEL LCKEMVTFLD KLGIPQAVFI GHDWAGVMVW NMALFYPERV 
       360        370        380        390        400
RAVASLNTPF MPPDPDVSPM KVIRSIPVFN YQLYFQEPGV AEAELEKNMS 
       410        420        430        440        450
RTFKSFFRAS DETGFIAVHK ATEIGGILVN TPEDPNLSKI TTEEEIEFYI 
       460        470        480        490        500
QQFKKTGFRG PLNWYRNTER NWKWSCKGLG RKILVPALMV TAEKDIVLRP 
       510        520        530        540        550
EMSKNMEKWI PFLKRGHIED CGHWTQIEKP TEVNQILIKW LQTEVQNPSV 

TSKI
Length:554
Mass (Da):62,515
Last modified:October 1, 1996 - 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:i2F3A3F7DACE47C93
GO
Isoform 2 (identifier: P34914-2) [UniParc]FASTAAdd to basket
Also known as: Ephx2B

The sequence of this isoform differs from the canonical sequence as follows:
     1-62: MALRVAAFDL...LMKGKITFSQ → MRFAAMAAFS...EDTDTIHTSE

Show »
Length:536
Mass (Da):60,613
Checksum:iD9BD995CB9347551
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 is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A8JYK8A8JYK8_MOUSE
Bifunctional epoxide hydrolase 2
Ephx2
488Annotation 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 conflicti77A → T in CAA85471 (PubMed:8750907).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0139041 – 62MALRV…ITFSQ → MRFAAMAAFSVFFVSKGLLM NSNIWCVGQEGPSQEDTDTI HTSE in isoform 2. 1 PublicationAdd BLAST62

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
L05781 mRNA Translation: AAA37555.1
Z37107 mRNA Translation: CAA85471.1
AY098585 mRNA Translation: AAM28238.1
BC015087 mRNA Translation: AAH15087.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS27218.1 [P34914-1]
CCDS88694.1 [P34914-2]

Protein sequence database of the Protein Information Resource

More...PIRi		A47504

NCBI Reference Sequences

More...RefSeqi		NP_001258332.1, NM_001271403.1 [P34914-2]
NP_031966.2, NM_007940.4 [P34914-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000070515; ENSMUSP00000069209; ENSMUSG00000022040 [P34914-1]
ENSMUST00000224698; ENSMUSP00000153161; ENSMUSG00000022040 [P34914-2]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		13850

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:13850

UCSC genome browser

More...UCSCi		uc007ujv.2, mouse [P34914-1]
uc033grp.1, mouse [P34914-2]

Keywords - Coding sequence diversityi

Alternative splicing

<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
L05781 mRNA Translation: AAA37555.1
Z37107 mRNA Translation: CAA85471.1
AY098585 mRNA Translation: AAM28238.1
BC015087 mRNA Translation: AAH15087.1
CCDSiCCDS27218.1 [P34914-1]
CCDS88694.1 [P34914-2]
PIRiA47504
RefSeqiNP_001258332.1, NM_001271403.1 [P34914-2]
NP_031966.2, NM_007940.4 [P34914-1]

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
1CQZX-ray2.80A/B1-554[»]
1CR6X-ray2.80A/B1-554[»]
1EK1X-ray3.10A/B1-554[»]
1EK2X-ray3.00A/B1-554[»]
SMRiP34914
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi199481, 3 interactors
IntActiP34914, 8 interactors
MINTiP34914
STRINGi10090.ENSMUSP00000069209

Chemistry databases

BindingDBiP34914
ChEMBLiCHEMBL4140
GuidetoPHARMACOLOGYi2970
SwissLipidsiSLP:000001106

Protein family/group databases

ESTHERimouse-hyes, Epoxide_hydrolase
MEROPSiS33.973

PTM databases

iPTMnetiP34914
MetOSiteiP34914
PhosphoSitePlusiP34914
SwissPalmiP34914

2D gel databases

SWISS-2DPAGEiP34914

Proteomic databases

jPOSTiP34914
MaxQBiP34914
PaxDbiP34914
PeptideAtlasiP34914
PRIDEiP34914
ProteomicsDBi267029 [P34914-1]
267030 [P34914-2]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		4070, 405 antibodies

The DNASU plasmid repository

More...DNASUi		13850

Genome annotation databases

EnsembliENSMUST00000070515; ENSMUSP00000069209; ENSMUSG00000022040 [P34914-1]
ENSMUST00000224698; ENSMUSP00000153161; ENSMUSG00000022040 [P34914-2]
GeneIDi13850
KEGGimmu:13850
UCSCiuc007ujv.2, mouse [P34914-1]
uc033grp.1, mouse [P34914-2]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2053
MGIiMGI:99500, Ephx2

Phylogenomic databases

eggNOGiKOG3085, Eukaryota
KOG4178, Eukaryota
GeneTreeiENSGT00940000158614
HOGENOMiCLU_036085_1_1_1
InParanoidiP34914
PhylomeDBiP34914
TreeFamiTF315395

Enzyme and pathway databases

BRENDAi3.3.2.10, 3474
ReactomeiR-MMU-2142670, Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
R-MMU-9018682, Biosynthesis of maresins
R-MMU-9033241, Peroxisomal protein import

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		13850, 0 hits in 52 CRISPR screens

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

More...ChiTaRSi		Ephx2, mouse
EvolutionaryTraceiP34914

Protein Ontology

More...PROi		PR:P34914
RNActiP34914, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000022040, Expressed in cumulus cell and 282 other tissues
ExpressionAtlasiP34914, baseline and differential
GenevisibleiP34914, MM

Family and domain databases

Gene3Di1.10.150.240, 1 hit
3.40.50.1000, 1 hit
3.40.50.1820, 1 hit
InterProiView protein in InterPro
IPR029058, AB_hydrolase
IPR000073, AB_hydrolase_1
IPR000639, Epox_hydrolase-like
IPR036412, HAD-like_sf
IPR006439, HAD-SF_hydro_IA
IPR041492, HAD_2
IPR023214, HAD_sf
IPR023198, PGP-like_dom2
PfamiView protein in Pfam
PF00561, Abhydrolase_1, 1 hit
PF13419, HAD_2, 1 hit
PRINTSiPR00111, ABHYDROLASE
PR00412, EPOXHYDRLASE
SUPFAMiSSF53474, SSF53474, 1 hit
SSF56784, SSF56784, 1 hit
TIGRFAMsiTIGR01509, HAD-SF-IA-v3, 1 hit

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 nameiHYES_MOUSE
<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: P34914
Secondary accession number(s): Q8CGV0
<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: February 1, 1994
Last sequence update: October 1, 1996
Last modified: June 2, 2021
This is version 186 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

<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, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
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