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UniProtKB - P34913 (HYES_HUMAN)

Entry version 201 (07 Apr 2021)
Sequence version 2 (07 Jun 2005)
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Protein

Bifunctional epoxide hydrolase 2

Gene

EPHX2

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

Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12869654, PubMed:12574510, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12869654, PubMed:12574510, PubMed:22798687, PubMed:21217101).By similarity5 Publications
Bifunctional enzyme (PubMed:12574510). 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 (PubMed:12574510). Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (PubMed:22217705, PubMed:22387545).3 Publications

<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+3 Publications

<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). Phosphatase activity is inhibited by dodecyl-phosphate, phospholipids such as phospho-lysophosphatidic acids and fatty acids such as palmitic acid and lauric acid (PubMed:22217705, PubMed:22387545).4 Publications

<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

kcat are 14 sec(-1), 354 sec(-1), 167 sec(-1), 125 sec(-1), 177 sec(-1), 250 sec(-1), 18 sec(-1) and 136 sec(-1) for farnesyl pyro-phosphate, 1-myristoyl-2-hydroxy-3-glycerophosphate, 1-palmityl-2-hydroxy-3-glycerophosphate, 1-stearyl-2-hydroxy-3-glycerophosphate, 1-oleoyl-2-hydroxy-3-glycerophosphate, 1-arachidonoyl-2-hydroxy-3-glycerophosphate, shingosine-1-phosphate and N-acetyl-ceramide-phosphate, respectively.1 Publication
  1. KM=21 µM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. KM=1.7 µM for 8,9-EET1 Publication
  3. KM=3.4 µM for 11,12-EET1 Publication
  4. KM=15 µM for 14,15-EET1 Publication
  5. KM=1.5 µM for leukotoxin1 Publication
  6. KM=1.1 mM for p-nitrophenyl phosphate3 Publications
  7. KM=7.3 µM for 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate1 Publication
  8. KM=10.8 µM for 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate1 Publication
  9. KM=3 µM for palmitoyl-lysophosphatidic acid1 Publication
  10. KM=6.4 µM for stearoyl-lysophosphatidic acid1 Publication
  11. KM=6.2 µM for oleoyl-lysophosphatidic acid1 Publication
  12. KM=5.9 µM for arachidonoyl-lysophosphatidic acid1 Publication
  13. KM=5.3 µM for arachidoyl-lysophosphatidic acid1 Publication
  14. KM=23.5 µM for 1-alkyl lysophosphatidic acid (C18:0)1 Publication
  15. KM=14.8 µM for sphingosine-1-phosphate1 Publication
  16. KM=20.9 µM for geranylgeranyl pyrophosphate1 Publication
  17. KM=10 µM for farnesyl pyro-phosphate1 Publication
  18. KM=5.1 µM for 1-myristoyl-2-hydroxy-3-glycerophosphate1 Publication
  19. KM=23 µM for 1-palmityl-2-hydroxy-3-glycerophosphate1 Publication
  20. KM=4.2 µM for 1-stearyl-2-hydroxy-3-glycerophosphate1 Publication
  21. KM=6.9 µM for 1-oleoyl-2-hydroxy-3-glycerophosphate1 Publication
  22. KM=13 µM for 1-arachidonoyl-2-hydroxy-3-glycerophosphate1 Publication
  23. KM=31 µM for shingosine-1-phosphate1 Publication
  24. KM=67 µM for N-acetyl-ceramide-phosphate1 Publication
  1. Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. Vmax=0.9 µmol/min/mg enzyme with 8,9-EET as substrate1 Publication
  3. Vmax=4.5 µmol/min/mg enzyme with 11,12-EET as substrate1 Publication
  4. Vmax=7 µmol/min/mg enzyme with 14,15-EET as substrate1 Publication
  5. Vmax=0.55 µmol/min/mg enzyme with leukotoxin as substrate1 Publication
  6. Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate3 Publications
  7. Vmax=385 nmol/min/mg enzyme with 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate as substrate1 Publication
  8. Vmax=95 nmol/min/mg enzyme with 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate as substrate1 Publication
  9. Vmax=150.4 nmol/min/mg enzyme with palmitoyl-lysophosphatidic acid as substrate1 Publication
  10. Vmax=193.5 nmol/min/mg enzyme with stearoyl-lysophosphatidic acid as substrate1 Publication
  11. Vmax=191.6 nmol/min/mg enzyme with oleoyl-lysophosphatidic acid as substrate1 Publication
  12. Vmax=157.9 nmol/min/mg enzyme with arachidonoyl-lysophosphatidic acid as substrate1 Publication
  13. Vmax=26.8 nmol/min/mg enzyme with arachidoyl-lysophosphatidic acid as substrate1 Publication
  14. Vmax=171.1 nmol/min/mg enzyme with 1-alkyl lysophosphatidic acid (C18:0) as substrate1 Publication
  15. Vmax=60.6 nmol/min/mg enzyme with sphingosine-1-phosphate as substrate1 Publication
  16. Vmax=101.3 nmol/min/mg enzyme with geranylgeranyl pyrophosphate 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 bindingi9Magnesium1 Publication1
Metal bindingi11Magnesium1 Publication1
Metal bindingi185Magnesium1 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 sitei335Nucleophile5 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 sitei383Substrate5 Publications1
Active sitei466Proton donor5 Publications1
Active sitei524Proton acceptor5 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, 2681

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P34913

Reactome - a knowledgebase of biological pathways and processes

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

SABIO-RK: Biochemical Reaction Kinetics Database

More...SABIO-RKi		P34913

Protein family/group databases

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

More...ESTHERi		human-EPHX2, Epoxide_hydrolase

MEROPS protease database

More...MEROPSi		S33.973

Chemistry databases

SwissLipids knowledge resource for lipid biology

More...SwissLipidsi		SLP:000001105

<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:3.3.2.104 Publications)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase2 Publications
Short name:
SEH2 Publications
Lipid-phosphate phosphatase (EC:3.1.3.762 Publications)
<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
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 8

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:3402, EPHX2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		132811, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P34913

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000120915.13

<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

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>Mutagenesisi9D → A: Loss of phosphatase activity. 2 Publications1
Mutagenesisi522C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		2053

MalaCards human disease database

More...MalaCardsi		EPHX2

Open Targets

More...OpenTargetsi		ENSG00000120915

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA27830

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P34913, Tchem

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2409

Drug and drug target database

More...DrugBanki		DB08257, 4-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}BUTANOIC ACID
DB08258, 6-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEXANOIC ACID
DB08259, 7-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEPTANOIC ACID
DB06345, AR-9281
DB12610, Ebselen
DB08256, N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE
DB02029, N-Cyclohexyl-N'-(4-Iodophenyl)Urea
DB04213, N-Cyclohexyl-N'-(Propyl)Phenyl Urea
DB03677, N-Cyclohexyl-N'-Decylurea

DrugCentral

More...DrugCentrali		P34913

IUPHAR/BPS Guide to PHARMACOLOGY

More...GuidetoPHARMACOLOGYi		2970

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		EPHX2

Domain mapping of disease mutations (DMDM)

More...DMDMi		67476665

<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_00000841111 – 555Bifunctional epoxide hydrolase 2Add BLAST555

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 residuei43N6-acetyllysineCombined sources1
Modified residuei55N6-succinyllysineBy similarity1
Modified residuei191N6-acetyllysineBy similarity1
Modified residuei215N6-acetyllysineBy similarity1
Modified residuei370PhosphoserineBy similarity1
Modified residuei421N6-succinyllysineBy similarity1
Modified residuei455N6-succinyllysineBy similarity1
<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>Lipidationi522S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine1 Publication1
Modified residuei554N6-succinyllysineBy similarity1

<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 (Probable).Curated

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P34913

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P34913

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P34913

MaxQB - The MaxQuant DataBase

More...MaxQBi		P34913

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

More...PaxDbi		P34913

PeptideAtlas

More...PeptideAtlasi		P34913

PRoteomics IDEntifications database

More...PRIDEi		P34913

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		32244
54953 [P34913-1]

PTM databases

DEPOD human dephosphorylation database

More...DEPODi		EPHX2

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P34913

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

More...PhosphoSitePlusi		P34913

<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 compounds that cause peroxisome proliferation such as clofibrate, tiadenol and fenofibrate.

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000120915, Expressed in right lobe of liver and 181 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P34913, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P34913, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000120915, Tissue enhanced (intestine, liver)

<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.

3 Publications

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		108367, 16 interactors

Protein interaction database and analysis system

More...IntActi		P34913, 5 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000430269

Chemistry databases

BindingDB database of measured binding affinities

More...BindingDBi		P34913

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P34913, 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

1555
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		P34913

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		P34913

<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>Domaini259 – 531AB hydrolase-1Sequence analysisAdd BLAST273

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 binding1 Publication2
Regioni235 – 555Epoxide hydrolaseAdd BLAST321

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>Motifi553 – 555Microbody 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		P34913

Identification of Orthologs from Complete Genome Data

More...OMAi		ANHWLDD

Database of Orthologous Groups

More...OrthoDBi		616687at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P34913

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
IPR011945, HAD-SF_ppase_IA/epoxid_hydro_N
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		TIGR02247, HAD-1A3-hyp, 1 hit
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 (3+)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 3 <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. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 4 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P34913-1) [UniParc]FASTAAdd to basket

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
MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT 
        60         70         80         90        100
TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK 
       110        120        130        140        150
INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL 
       160        170        180        190        200
IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT 
       210        220        230        240        250
ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL 
       260        270        280        290        300
HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS 
       310        320        330        340        350
APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE 
       360        370        380        390        400
RVRAVASLNT PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN 
       410        420        430        440        450
LSRTFKSLFR ASDESVLSMH KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY 
       460        470        480        490        500
VQQFKKSGFR GPLNWYRNME RNWKWACKSL GRKILIPALM VTAEKDFVLV 
       510        520        530        540        550
PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK WLDSDARNPP 

VVSKM
Length:555
Mass (Da):62,616
Last modified:June 7, 2005 - 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:i1B5ACE7F80F9A26C
GO
Isoform 2 (identifier: P34913-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-53: Missing.

Show »
Length:502
Mass (Da):57,123
Checksum:iCB56A36CDF4F2FFF
GO
Isoform 3 (identifier: P34913-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-66: Missing.

Show »
Length:489
Mass (Da):55,626
Checksum:i7188F0A08408CD29
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
E5RFU2E5RFU2_HUMAN
Bifunctional epoxide hydrolase 2
EPHX2
523Annotation 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>
E5RFH6E5RFH6_HUMAN
Bifunctional epoxide hydrolase 2
EPHX2
372Annotation 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>
H0YAW7H0YAW7_HUMAN
Bifunctional epoxide hydrolase 2
EPHX2
312Annotation 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>
E5RI53E5RI53_HUMAN
Bifunctional epoxide hydrolase 2
EPHX2
158Annotation 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 conflicti5A → G in AAA02756 (PubMed:8342951).Curated1
Sequence conflicti257 – 258SG → W in AAA02756 (PubMed:8342951).Curated2
Sequence conflicti409F → L in BAG53362 (PubMed:14702039).Curated1
Sequence conflicti473W → R in BAG53362 (PubMed:14702039).Curated1
Sequence conflicti494E → G in BAG53362 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_05539221G → A1 PublicationCorresponds to variant dbSNP:rs72473930Ensembl.1
Natural variantiVAR_05539352R → Q1 PublicationCorresponds to variant dbSNP:rs72475803EnsemblClinVar.1
Natural variantiVAR_05105955K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs41507953Ensembl.1
Natural variantiVAR_033991103R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs17057255Ensembl.1
Natural variantiVAR_055394154C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs57699806Ensembl.1
Natural variantiVAR_055395225P → L1 PublicationCorresponds to variant dbSNP:rs72475821Ensembl.1
Natural variantiVAR_014852287R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 PublicationsCorresponds to variant dbSNP:rs751141EnsemblClinVar.1
Natural variantiVAR_055396369M → V1 PublicationCorresponds to variant dbSNP:rs72475894Ensembl.1
Natural variantiVAR_022613403R → RR2 Publications1
Natural variantiVAR_055397470E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs68053459Ensembl.1

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_0455971 – 66Missing in isoform 3. 1 PublicationAdd BLAST66
Alternative sequenceiVSP_0455981 – 53Missing in isoform 2. 1 PublicationAdd BLAST53

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
L05779 mRNA Translation: AAA02756.1
X97024 X97038 Genomic DNA Translation: CAA65751.1
AF233334 mRNA Translation: AAG14966.1
AF233335 mRNA Translation: AAG14967.1
AF233336 mRNA Translation: AAG14968.1
BT006885 mRNA Translation: AAP35531.1
AK096089 mRNA Translation: BAG53210.1
AK096770 mRNA Translation: BAG53362.1
EU584434 Genomic DNA Translation: ACD11487.1
AF311103 Genomic DNA No translation available.
CH471080 Genomic DNA Translation: EAW63548.1
CH471080 Genomic DNA Translation: EAW63549.1
CH471080 Genomic DNA Translation: EAW63551.1
BC007708 mRNA Translation: AAH07708.1
BC011628 mRNA Translation: AAH11628.1
BC013874 mRNA Translation: AAH13874.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS59097.1 [P34913-2]
CCDS59098.1 [P34913-3]
CCDS6060.1 [P34913-1]

Protein sequence database of the Protein Information Resource

More...PIRi		JC4711

NCBI Reference Sequences

More...RefSeqi		NP_001243411.1, NM_001256482.1 [P34913-2]
NP_001243412.1, NM_001256483.1 [P34913-3]
NP_001243413.1, NM_001256484.1 [P34913-2]
NP_001970.2, NM_001979.5 [P34913-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2]
ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1]
ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		2053

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:2053

UCSC genome browser

More...UCSCi		uc003xfu.5, human [P34913-1]

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

<p>This subsection of the <a href="http://www.uniprot.org/manual/cross%5Freferences%5Fsection">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05779 mRNA Translation: AAA02756.1
X97024 X97038 Genomic DNA Translation: CAA65751.1
AF233334 mRNA Translation: AAG14966.1
AF233335 mRNA Translation: AAG14967.1
AF233336 mRNA Translation: AAG14968.1
BT006885 mRNA Translation: AAP35531.1
AK096089 mRNA Translation: BAG53210.1
AK096770 mRNA Translation: BAG53362.1
EU584434 Genomic DNA Translation: ACD11487.1
AF311103 Genomic DNA No translation available.
CH471080 Genomic DNA Translation: EAW63548.1
CH471080 Genomic DNA Translation: EAW63549.1
CH471080 Genomic DNA Translation: EAW63551.1
BC007708 mRNA Translation: AAH07708.1
BC011628 mRNA Translation: AAH11628.1
BC013874 mRNA Translation: AAH13874.1
CCDSiCCDS59097.1 [P34913-2]
CCDS59098.1 [P34913-3]
CCDS6060.1 [P34913-1]
PIRiJC4711
RefSeqiNP_001243411.1, NM_001256482.1 [P34913-2]
NP_001243412.1, NM_001256483.1 [P34913-3]
NP_001243413.1, NM_001256484.1 [P34913-2]
NP_001970.2, NM_001979.5 [P34913-1]

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
1S8OX-ray2.60A1-555[»]
1VJ5X-ray2.35A1-555[»]
1ZD2X-ray3.00P1-555[»]
1ZD3X-ray2.30A1-555[»]
1ZD4X-ray2.70A1-555[»]
1ZD5X-ray2.60A1-555[»]
3ANSX-ray1.98A/B230-555[»]
3ANTX-ray2.40A/B230-555[»]
3I1YX-ray2.47A1-555[»]
3I28X-ray1.95A1-555[»]
3KOOX-ray2.79A1-555[»]
3OTQX-ray3.00A1-555[»]
3PDCX-ray2.60A/B226-548[»]
3WK4X-ray2.11A1-555[»]
3WK5X-ray2.77A1-555[»]
3WK6X-ray2.10A1-555[»]
3WK7X-ray2.20A1-555[»]
3WK8X-ray2.20A1-555[»]
3WK9X-ray2.20A1-555[»]
3WKAX-ray2.01A1-555[»]
3WKBX-ray2.20A1-555[»]
3WKCX-ray2.20A1-555[»]
3WKDX-ray2.48A1-555[»]
3WKEX-ray2.75A1-555[»]
4C4XX-ray2.17A/B230-555[»]
4C4YX-ray2.41A230-555[»]
4C4ZX-ray2.06A/B230-555[»]
4HAIX-ray2.55A1-555[»]
4J03X-ray2.92A1-555[»]
4JNCX-ray1.96A238-549[»]
4OCZX-ray2.94A1-555[»]
4OD0X-ray2.92A1-555[»]
4X6XX-ray1.80A/B230-555[»]
4X6YX-ray2.10A/B230-555[»]
4Y2JX-ray2.15A1-555[»]
4Y2PX-ray2.05A1-555[»]
4Y2QX-ray2.40A1-555[»]
4Y2RX-ray2.45A1-555[»]
4Y2SX-ray2.30A1-555[»]
4Y2TX-ray2.40A1-555[»]
4Y2UX-ray2.75A1-555[»]
4Y2VX-ray2.40A1-555[»]
4Y2XX-ray2.50A1-555[»]
4Y2YX-ray2.30A1-555[»]
5AHXX-ray2.00A1-548[»]
5AI0X-ray1.75A1-548[»]
5AI4X-ray1.93A1-548[»]
5AI5X-ray2.28A1-548[»]
5AI6X-ray2.30A1-548[»]
5AI8X-ray1.85A1-548[»]
5AI9X-ray1.80A1-548[»]
5AIAX-ray2.26A1-548[»]
5AIBX-ray1.95A1-548[»]
5AICX-ray1.89A1-548[»]
5AK3X-ray2.28A1-548[»]
5AK4X-ray1.79A1-548[»]
5AK5X-ray2.22A1-548[»]
5AK6X-ray2.15A1-548[»]
5AKEX-ray2.26A1-548[»]
5AKGX-ray2.51A1-548[»]
5AKHX-ray2.10A1-548[»]
5AKIX-ray1.81A1-548[»]
5AKJX-ray2.03A1-548[»]
5AKKX-ray1.90A1-548[»]
5AKLX-ray2.00A1-548[»]
5AKXX-ray2.09A1-548[»]
5AKYX-ray2.18A1-548[»]
5AKZX-ray2.18A1-548[»]
5ALDX-ray2.26A1-548[»]
5ALEX-ray1.95A1-548[»]
5ALFX-ray2.32A1-548[»]
5ALGX-ray2.40A1-548[»]
5ALHX-ray1.90A1-548[»]
5ALIX-ray1.85A1-548[»]
5ALJX-ray2.10A1-548[»]
5ALKX-ray2.33A1-548[»]
5ALLX-ray2.20A1-548[»]
5ALMX-ray2.00A1-548[»]
5ALNX-ray2.00A1-548[»]
5ALOX-ray2.00A1-548[»]
5ALPX-ray2.06A1-548[»]
5ALQX-ray2.78A1-548[»]
5ALRX-ray2.60A1-548[»]
5ALSX-ray2.57A1-548[»]
5ALTX-ray2.15A1-548[»]
5ALUX-ray1.87A1-548[»]
5ALVX-ray1.80A1-548[»]
5ALWX-ray2.20A1-548[»]
5ALXX-ray2.23A1-548[»]
5ALYX-ray1.90A1-548[»]
5ALZX-ray2.30A1-548[»]
5AM0X-ray1.88A1-548[»]
5AM1X-ray2.15A1-548[»]
5AM2X-ray1.70A1-548[»]
5AM3X-ray2.20A1-548[»]
5AM4X-ray1.87A1-548[»]
5AM5X-ray2.26A1-548[»]
5FP0X-ray2.35A1-548[»]
5MWAX-ray1.55A2-224[»]
6AUMX-ray2.95A1-555[»]
6I5EX-ray2.60A/B230-555[»]
6I5GX-ray2.00A/B230-555[»]
SMRiP34913
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi108367, 16 interactors
IntActiP34913, 5 interactors
STRINGi9606.ENSP00000430269

Chemistry databases

BindingDBiP34913
ChEMBLiCHEMBL2409
DrugBankiDB08257, 4-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}BUTANOIC ACID
DB08258, 6-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEXANOIC ACID
DB08259, 7-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEPTANOIC ACID
DB06345, AR-9281
DB12610, Ebselen
DB08256, N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE
DB02029, N-Cyclohexyl-N'-(4-Iodophenyl)Urea
DB04213, N-Cyclohexyl-N'-(Propyl)Phenyl Urea
DB03677, N-Cyclohexyl-N'-Decylurea
DrugCentraliP34913
GuidetoPHARMACOLOGYi2970
SwissLipidsiSLP:000001105

Protein family/group databases

ESTHERihuman-EPHX2, Epoxide_hydrolase
MEROPSiS33.973

PTM databases

DEPODiEPHX2
iPTMnetiP34913
PhosphoSitePlusiP34913

Genetic variation databases

BioMutaiEPHX2
DMDMi67476665

Proteomic databases

EPDiP34913
jPOSTiP34913
MassIVEiP34913
MaxQBiP34913
PaxDbiP34913
PeptideAtlasiP34913
PRIDEiP34913
ProteomicsDBi32244
54953 [P34913-1]

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		4070, 405 antibodies

The DNASU plasmid repository

More...DNASUi		2053

Genome annotation databases

EnsembliENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2]
ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1]
ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3]
GeneIDi2053
KEGGihsa:2053
UCSCiuc003xfu.5, human [P34913-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		2053
DisGeNETi2053

GeneCards: human genes, protein and diseases

More...GeneCardsi		EPHX2
HGNCiHGNC:3402, EPHX2
HPAiENSG00000120915, Tissue enhanced (intestine, liver)
MalaCardsiEPHX2
MIMi132811, gene
neXtProtiNX_P34913
OpenTargetsiENSG00000120915
PharmGKBiPA27830
VEuPathDBiHostDB:ENSG00000120915.13

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG3085, Eukaryota
KOG4178, Eukaryota
GeneTreeiENSGT00940000158614
HOGENOMiCLU_036085_1_1_1
InParanoidiP34913
OMAiANHWLDD
OrthoDBi616687at2759
PhylomeDBiP34913
TreeFamiTF315395

Enzyme and pathway databases

BRENDAi3.3.2.10, 2681
PathwayCommonsiP34913
ReactomeiR-HSA-2142670, Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET)
R-HSA-9018682, Biosynthesis of maresins
R-HSA-9033241, Peroxisomal protein import
SABIO-RKiP34913

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		2053, 5 hits in 997 CRISPR screens

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

More...ChiTaRSi		EPHX2, human
EvolutionaryTraceiP34913

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		Epoxide_hydrolase_2

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

More...GenomeRNAii		2053
PharosiP34913, Tchem

Protein Ontology

More...PROi		PR:P34913
RNActiP34913, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000120915, Expressed in right lobe of liver and 181 other tissues
ExpressionAtlasiP34913, baseline and differential
GenevisibleiP34913, HS

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
IPR011945, HAD-SF_ppase_IA/epoxid_hydro_N
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
TIGRFAMsiTIGR02247, HAD-1A3-hyp, 1 hit
TIGR01509, HAD-SF-IA-v3, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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MobiDB: a database of protein disorder and mobility annotations

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<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_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: P34913
Secondary accession number(s): B2Z3B1
, B3KTU8, B3KUA0, G3V134, J3KPH7, Q16764, Q9HBJ1, Q9HBJ2
<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: June 7, 2005
Last modified: April 7, 2021
This is version 201 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. Human variants curated from literature reports
    Index of human variants curated from literature reports
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families
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