UniProtKB - P34913 (HYES_HUMAN)
Protein
Bifunctional epoxide hydrolase 2
Gene
EPHX2
Organism
Homo sapiens (Human)
Status
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
Catalytic activityi
- EC:3.3.2.103 Publications
- (9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate3 PublicationsEC:3.1.3.763 Publications
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy-(5Z,11Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = 14,15-dihydroxy-(5Z,8Z,11Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward1 Publication direction.
- 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate + H2O = (8,11R,12S)-trihydroxy-(5Z,9E,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate + H2O = (10,11S,12R)-trihydroxy-(5Z,8Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- 1-tetradecanoyl-sn-glycerol 3-phosphate + H2O = 1-tetradecanoyl-sn-glycerol + phosphate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forward2 Publications direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + phosphate2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- This reaction proceeds in the forward2 Publications direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphate2 PublicationsThis reaction proceeds in the forward2 Publications direction.
- (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8S,9S)-dihydroxy-(5Z,11Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14S,15S)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8R,9R)-dihydroxy-(5Z,11Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Mg2+3 Publications
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
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
- KM=21 µM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
- KM=1.7 µM for 8,9-EET1 Publication
- KM=3.4 µM for 11,12-EET1 Publication
- KM=15 µM for 14,15-EET1 Publication
- KM=1.5 µM for leukotoxin1 Publication
- KM=1.1 mM for p-nitrophenyl phosphate3 Publications
- KM=7.3 µM for 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate1 Publication
- KM=10.8 µM for 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate1 Publication
- KM=3 µM for palmitoyl-lysophosphatidic acid1 Publication
- KM=6.4 µM for stearoyl-lysophosphatidic acid1 Publication
- KM=6.2 µM for oleoyl-lysophosphatidic acid1 Publication
- KM=5.9 µM for arachidonoyl-lysophosphatidic acid1 Publication
- KM=5.3 µM for arachidoyl-lysophosphatidic acid1 Publication
- KM=23.5 µM for 1-alkyl lysophosphatidic acid (C18:0)1 Publication
- KM=14.8 µM for sphingosine-1-phosphate1 Publication
- KM=20.9 µM for geranylgeranyl pyrophosphate1 Publication
- KM=10 µM for farnesyl pyro-phosphate1 Publication
- KM=5.1 µM for 1-myristoyl-2-hydroxy-3-glycerophosphate1 Publication
- KM=23 µM for 1-palmityl-2-hydroxy-3-glycerophosphate1 Publication
- KM=4.2 µM for 1-stearyl-2-hydroxy-3-glycerophosphate1 Publication
- KM=6.9 µM for 1-oleoyl-2-hydroxy-3-glycerophosphate1 Publication
- KM=13 µM for 1-arachidonoyl-2-hydroxy-3-glycerophosphate1 Publication
- KM=31 µM for shingosine-1-phosphate1 Publication
- KM=67 µM for N-acetyl-ceramide-phosphate1 Publication
- Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
- Vmax=0.9 µmol/min/mg enzyme with 8,9-EET as substrate1 Publication
- Vmax=4.5 µmol/min/mg enzyme with 11,12-EET as substrate1 Publication
- Vmax=7 µmol/min/mg enzyme with 14,15-EET as substrate1 Publication
- Vmax=0.55 µmol/min/mg enzyme with leukotoxin as substrate1 Publication
- Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate3 Publications
- Vmax=385 nmol/min/mg enzyme with 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate as substrate1 Publication
- Vmax=95 nmol/min/mg enzyme with 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate as substrate1 Publication
- Vmax=150.4 nmol/min/mg enzyme with palmitoyl-lysophosphatidic acid as substrate1 Publication
- Vmax=193.5 nmol/min/mg enzyme with stearoyl-lysophosphatidic acid as substrate1 Publication
- Vmax=191.6 nmol/min/mg enzyme with oleoyl-lysophosphatidic acid as substrate1 Publication
- Vmax=157.9 nmol/min/mg enzyme with arachidonoyl-lysophosphatidic acid as substrate1 Publication
- Vmax=26.8 nmol/min/mg enzyme with arachidoyl-lysophosphatidic acid as substrate1 Publication
- Vmax=171.1 nmol/min/mg enzyme with 1-alkyl lysophosphatidic acid (C18:0) as substrate1 Publication
- Vmax=60.6 nmol/min/mg enzyme with sphingosine-1-phosphate as substrate1 Publication
- Vmax=101.3 nmol/min/mg enzyme with geranylgeranyl pyrophosphate as substrate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 9 | Magnesium1 Publication | 1 | |
Metal bindingi | 11 | Magnesium1 Publication | 1 | |
Metal bindingi | 185 | Magnesium1 Publication | 1 | |
Active sitei | 335 | Nucleophile5 Publications | 1 | |
Binding sitei | 383 | Substrate5 Publications | 1 | |
Active sitei | 466 | Proton donor5 Publications | 1 | |
Active sitei | 524 | Proton acceptor5 Publications | 1 |
GO - Molecular functioni
- 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
- epoxide hydrolase activity Source: UniProtKB
- hydrolase activity Source: GO_Central
- lipid phosphatase activity Source: UniProtKB
- lysophosphatidic acid phosphatase activity Source: UniProtKB
- magnesium ion binding Source: UniProtKB
- phosphatase activity Source: UniProtKB
- protein homodimerization activity Source: UniProtKB
- toxic substance binding Source: UniProtKB
GO - Biological processi
- cholesterol homeostasis Source: UniProtKB
- dephosphorylation Source: UniProtKB
- epoxide metabolic process Source: UniProtKB
- epoxygenase P450 pathway Source: Reactome
- long-chain fatty acid biosynthetic process Source: Reactome
- phospholipid dephosphorylation Source: UniProtKB
- positive regulation of gene expression Source: UniProtKB
- protein localization Source: Reactome
- regulation of cholesterol metabolic process Source: UniProtKB
- response to toxic substance Source: UniProtKB-KW
- stilbene catabolic process Source: UniProtKB
Keywordsi
Molecular function | Hydrolase, Multifunctional enzyme |
Biological process | Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism |
Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BRENDAi | 3.3.2.10, 2681 |
PathwayCommonsi | P34913 |
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-RKi | P34913 |
Protein family/group databases
ESTHERi | human-EPHX2, Epoxide_hydrolase |
MEROPSi | S33.973 |
Chemistry databases
SwissLipidsi | SLP:000001105 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional epoxide hydrolase 2CuratedIncluding the following 2 domains: |
Gene namesi | Name:EPHX2Imported |
Organismi | Homo sapiens (Human) |
Taxonomic identifieri | 9606 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Proteomesi |
|
Organism-specific databases
HGNCi | HGNC:3402, EPHX2 |
MIMi | 132811, gene |
neXtProti | NX_P34913 |
VEuPathDBi | HostDB:ENSG00000120915.13 |
Subcellular locationi
Cytoplasm and Cytosol
Peroxisome
Cytosol
- cytosol Source: UniProtKB
Extracellular region or secreted
- extracellular exosome Source: UniProtKB
Peroxisome
- peroxisomal matrix Source: Reactome
- peroxisome Source: UniProtKB
Keywords - Cellular componenti
Cytoplasm, PeroxisomePathology & Biotechi
Mutagenesis
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Mutagenesisi | 9 | D → A: Loss of phosphatase activity. 2 Publications | 1 | |
Mutagenesisi | 522 | C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. 1 Publication | 1 |
Organism-specific databases
DisGeNETi | 2053 |
MalaCardsi | EPHX2 |
OpenTargetsi | ENSG00000120915 |
PharmGKBi | PA27830 |
Miscellaneous databases
Pharosi | P34913, Tchem |
Chemistry databases
ChEMBLi | CHEMBL2409 |
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 |
DrugCentrali | P34913 |
GuidetoPHARMACOLOGYi | 2970 |
Genetic variation databases
BioMutai | EPHX2 |
DMDMi | 67476665 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000084111 | 1 – 555 | Bifunctional epoxide hydrolase 2Add BLAST | 555 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 43 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 55 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 191 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 215 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 370 | PhosphoserineBy similarity | 1 | |
Modified residuei | 421 | N6-succinyllysineBy similarity | 1 | |
Modified residuei | 455 | N6-succinyllysineBy similarity | 1 | |
Lipidationi | 522 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine1 Publication | 1 | |
Modified residuei | 554 | N6-succinyllysineBy similarity | 1 |
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, PhosphoproteinProteomic databases
EPDi | P34913 |
jPOSTi | P34913 |
MassIVEi | P34913 |
MaxQBi | P34913 |
PaxDbi | P34913 |
PeptideAtlasi | P34913 |
PRIDEi | P34913 |
ProteomicsDBi | 32244 54953 [P34913-1] |
PTM databases
DEPODi | EPHX2 |
iPTMneti | P34913 |
PhosphoSitePlusi | P34913 |
Expressioni
Inductioni
By compounds that cause peroxisome proliferation such as clofibrate, tiadenol and fenofibrate.
Gene expression databases
Bgeei | ENSG00000120915, Expressed in right lobe of liver and 181 other tissues |
ExpressionAtlasi | P34913, baseline and differential |
Genevisiblei | P34913, HS |
Organism-specific databases
HPAi | ENSG00000120915, Tissue enhanced (intestine, liver) |
Interactioni
Subunit structurei
Homodimer.
3 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: UniProtKB
Protein-protein interaction databases
BioGRIDi | 108367, 16 interactors |
IntActi | P34913, 5 interactors |
STRINGi | 9606.ENSP00000430269 |
Chemistry databases
BindingDBi | P34913 |
Miscellaneous databases
RNActi | P34913, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P34913 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P34913 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 259 – 531 | AB hydrolase-1Sequence analysisAdd BLAST | 273 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 224 | PhosphataseAdd BLAST | 224 | |
Regioni | 123 – 124 | Phosphate binding1 Publication | 2 | |
Regioni | 235 – 555 | Epoxide hydrolaseAdd BLAST | 321 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 553 – 555 | Microbody targeting signalSequence analysis | 3 |
Domaini
The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.
Sequence similaritiesi
Phylogenomic databases
eggNOGi | KOG3085, Eukaryota KOG4178, Eukaryota |
GeneTreei | ENSGT00940000158614 |
HOGENOMi | CLU_036085_1_1_1 |
InParanoidi | P34913 |
OMAi | ANHWLDD |
OrthoDBi | 616687at2759 |
PhylomeDBi | P34913 |
TreeFami | TF315395 |
Family and domain databases
Gene3Di | 1.10.150.240, 1 hit 3.40.50.1000, 1 hit 3.40.50.1820, 1 hit |
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 |
Pfami | View protein in Pfam PF00561, Abhydrolase_1, 1 hit PF13419, HAD_2, 1 hit |
PRINTSi | PR00111, ABHYDROLASE PR00412, EPOXHYDRLASE |
SUPFAMi | SSF53474, SSF53474, 1 hit SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR02247, HAD-1A3-hyp, 1 hit TIGR01509, HAD-SF-IA-v3, 1 hit |
s (3+)i Sequence
Sequence statusi: Complete.
This entry describes 3 produced by isoformsialternative splicing. AlignAdd to basketThis 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 sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. canonicali
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
Computationally mapped potential isoform sequencesi
There are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketE5RFU2 | E5RFU2_HUMAN | Bifunctional epoxide hydrolase 2 | EPHX2 | 523 | Annotation score: | ||
E5RFH6 | E5RFH6_HUMAN | Bifunctional epoxide hydrolase 2 | EPHX2 | 372 | Annotation score: | ||
H0YAW7 | H0YAW7_HUMAN | Bifunctional epoxide hydrolase 2 | EPHX2 | 312 | Annotation score: | ||
E5RI53 | E5RI53_HUMAN | Bifunctional epoxide hydrolase 2 | EPHX2 | 158 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 5 | A → G in AAA02756 (PubMed:8342951).Curated | 1 | |
Sequence conflicti | 257 – 258 | SG → W in AAA02756 (PubMed:8342951).Curated | 2 | |
Sequence conflicti | 409 | F → L in BAG53362 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 473 | W → R in BAG53362 (PubMed:14702039).Curated | 1 | |
Sequence conflicti | 494 | E → G in BAG53362 (PubMed:14702039).Curated | 1 |
Natural variant
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Natural variantiVAR_055392 | 21 | G → A1 PublicationCorresponds to variant dbSNP:rs72473930Ensembl. | 1 | |
Natural variantiVAR_055393 | 52 | R → Q1 PublicationCorresponds to variant dbSNP:rs72475803EnsemblClinVar. | 1 | |
Natural variantiVAR_051059 | 55 | K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs41507953Ensembl. | 1 | |
Natural variantiVAR_033991 | 103 | R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs17057255Ensembl. | 1 | |
Natural variantiVAR_055394 | 154 | C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs57699806Ensembl. | 1 | |
Natural variantiVAR_055395 | 225 | P → L1 PublicationCorresponds to variant dbSNP:rs72475821Ensembl. | 1 | |
Natural variantiVAR_014852 | 287 | R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 PublicationsCorresponds to variant dbSNP:rs751141EnsemblClinVar. | 1 | |
Natural variantiVAR_055396 | 369 | M → V1 PublicationCorresponds to variant dbSNP:rs72475894Ensembl. | 1 | |
Natural variantiVAR_022613 | 403 | R → RR2 Publications | 1 | |
Natural variantiVAR_055397 | 470 | E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 PublicationsCorresponds to variant dbSNP:rs68053459Ensembl. | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_045597 | 1 – 66 | Missing in isoform 3. 1 PublicationAdd BLAST | 66 | |
Alternative sequenceiVSP_045598 | 1 – 53 | Missing in isoform 2. 1 PublicationAdd BLAST | 53 |
Sequence databases
Genome annotation databases
Ensembli | ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2] ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1] ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3] |
GeneIDi | 2053 |
KEGGi | hsa:2053 |
UCSCi | uc003xfu.5, human [P34913-1] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Web resourcesi
NIEHS-SNPs |
Sequence databases
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1S8O | X-ray | 2.60 | A | 1-555 | [»] | |
1VJ5 | X-ray | 2.35 | A | 1-555 | [»] | |
1ZD2 | X-ray | 3.00 | P | 1-555 | [»] | |
1ZD3 | X-ray | 2.30 | A | 1-555 | [»] | |
1ZD4 | X-ray | 2.70 | A | 1-555 | [»] | |
1ZD5 | X-ray | 2.60 | A | 1-555 | [»] | |
3ANS | X-ray | 1.98 | A/B | 230-555 | [»] | |
3ANT | X-ray | 2.40 | A/B | 230-555 | [»] | |
3I1Y | X-ray | 2.47 | A | 1-555 | [»] | |
3I28 | X-ray | 1.95 | A | 1-555 | [»] | |
3KOO | X-ray | 2.79 | A | 1-555 | [»] | |
3OTQ | X-ray | 3.00 | A | 1-555 | [»] | |
3PDC | X-ray | 2.60 | A/B | 226-548 | [»] | |
3WK4 | X-ray | 2.11 | A | 1-555 | [»] | |
3WK5 | X-ray | 2.77 | A | 1-555 | [»] | |
3WK6 | X-ray | 2.10 | A | 1-555 | [»] | |
3WK7 | X-ray | 2.20 | A | 1-555 | [»] | |
3WK8 | X-ray | 2.20 | A | 1-555 | [»] | |
3WK9 | X-ray | 2.20 | A | 1-555 | [»] | |
3WKA | X-ray | 2.01 | A | 1-555 | [»] | |
3WKB | X-ray | 2.20 | A | 1-555 | [»] | |
3WKC | X-ray | 2.20 | A | 1-555 | [»] | |
3WKD | X-ray | 2.48 | A | 1-555 | [»] | |
3WKE | X-ray | 2.75 | A | 1-555 | [»] | |
4C4X | X-ray | 2.17 | A/B | 230-555 | [»] | |
4C4Y | X-ray | 2.41 | A | 230-555 | [»] | |
4C4Z | X-ray | 2.06 | A/B | 230-555 | [»] | |
4HAI | X-ray | 2.55 | A | 1-555 | [»] | |
4J03 | X-ray | 2.92 | A | 1-555 | [»] | |
4JNC | X-ray | 1.96 | A | 238-549 | [»] | |
4OCZ | X-ray | 2.94 | A | 1-555 | [»] | |
4OD0 | X-ray | 2.92 | A | 1-555 | [»] | |
4X6X | X-ray | 1.80 | A/B | 230-555 | [»] | |
4X6Y | X-ray | 2.10 | A/B | 230-555 | [»] | |
4Y2J | X-ray | 2.15 | A | 1-555 | [»] | |
4Y2P | X-ray | 2.05 | A | 1-555 | [»] | |
4Y2Q | X-ray | 2.40 | A | 1-555 | [»] | |
4Y2R | X-ray | 2.45 | A | 1-555 | [»] | |
4Y2S | X-ray | 2.30 | A | 1-555 | [»] | |
4Y2T | X-ray | 2.40 | A | 1-555 | [»] | |
4Y2U | X-ray | 2.75 | A | 1-555 | [»] | |
4Y2V | X-ray | 2.40 | A | 1-555 | [»] | |
4Y2X | X-ray | 2.50 | A | 1-555 | [»] | |
4Y2Y | X-ray | 2.30 | A | 1-555 | [»] | |
5AHX | X-ray | 2.00 | A | 1-548 | [»] | |
5AI0 | X-ray | 1.75 | A | 1-548 | [»] | |
5AI4 | X-ray | 1.93 | A | 1-548 | [»] | |
5AI5 | X-ray | 2.28 | A | 1-548 | [»] | |
5AI6 | X-ray | 2.30 | A | 1-548 | [»] | |
5AI8 | X-ray | 1.85 | A | 1-548 | [»] | |
5AI9 | X-ray | 1.80 | A | 1-548 | [»] | |
5AIA | X-ray | 2.26 | A | 1-548 | [»] | |
5AIB | X-ray | 1.95 | A | 1-548 | [»] | |
5AIC | X-ray | 1.89 | A | 1-548 | [»] | |
5AK3 | X-ray | 2.28 | A | 1-548 | [»] | |
5AK4 | X-ray | 1.79 | A | 1-548 | [»] | |
5AK5 | X-ray | 2.22 | A | 1-548 | [»] | |
5AK6 | X-ray | 2.15 | A | 1-548 | [»] | |
5AKE | X-ray | 2.26 | A | 1-548 | [»] | |
5AKG | X-ray | 2.51 | A | 1-548 | [»] | |
5AKH | X-ray | 2.10 | A | 1-548 | [»] | |
5AKI | X-ray | 1.81 | A | 1-548 | [»] | |
5AKJ | X-ray | 2.03 | A | 1-548 | [»] | |
5AKK | X-ray | 1.90 | A | 1-548 | [»] | |
5AKL | X-ray | 2.00 | A | 1-548 | [»] | |
5AKX | X-ray | 2.09 | A | 1-548 | [»] | |
5AKY | X-ray | 2.18 | A | 1-548 | [»] | |
5AKZ | X-ray | 2.18 | A | 1-548 | [»] | |
5ALD | X-ray | 2.26 | A | 1-548 | [»] | |
5ALE | X-ray | 1.95 | A | 1-548 | [»] | |
5ALF | X-ray | 2.32 | A | 1-548 | [»] | |
5ALG | X-ray | 2.40 | A | 1-548 | [»] | |
5ALH | X-ray | 1.90 | A | 1-548 | [»] | |
5ALI | X-ray | 1.85 | A | 1-548 | [»] | |
5ALJ | X-ray | 2.10 | A | 1-548 | [»] | |
5ALK | X-ray | 2.33 | A | 1-548 | [»] | |
5ALL | X-ray | 2.20 | A | 1-548 | [»] | |
5ALM | X-ray | 2.00 | A | 1-548 | [»] | |
5ALN | X-ray | 2.00 | A | 1-548 | [»] | |
5ALO | X-ray | 2.00 | A | 1-548 | [»] | |
5ALP | X-ray | 2.06 | A | 1-548 | [»] | |
5ALQ | X-ray | 2.78 | A | 1-548 | [»] | |
5ALR | X-ray | 2.60 | A | 1-548 | [»] | |
5ALS | X-ray | 2.57 | A | 1-548 | [»] | |
5ALT | X-ray | 2.15 | A | 1-548 | [»] | |
5ALU | X-ray | 1.87 | A | 1-548 | [»] | |
5ALV | X-ray | 1.80 | A | 1-548 | [»] | |
5ALW | X-ray | 2.20 | A | 1-548 | [»] | |
5ALX | X-ray | 2.23 | A | 1-548 | [»] | |
5ALY | X-ray | 1.90 | A | 1-548 | [»] | |
5ALZ | X-ray | 2.30 | A | 1-548 | [»] | |
5AM0 | X-ray | 1.88 | A | 1-548 | [»] | |
5AM1 | X-ray | 2.15 | A | 1-548 | [»] | |
5AM2 | X-ray | 1.70 | A | 1-548 | [»] | |
5AM3 | X-ray | 2.20 | A | 1-548 | [»] | |
5AM4 | X-ray | 1.87 | A | 1-548 | [»] | |
5AM5 | X-ray | 2.26 | A | 1-548 | [»] | |
5FP0 | X-ray | 2.35 | A | 1-548 | [»] | |
5MWA | X-ray | 1.55 | A | 2-224 | [»] | |
6AUM | X-ray | 2.95 | A | 1-555 | [»] | |
6I5E | X-ray | 2.60 | A/B | 230-555 | [»] | |
6I5G | X-ray | 2.00 | A/B | 230-555 | [»] | |
SMRi | P34913 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 108367, 16 interactors |
IntActi | P34913, 5 interactors |
STRINGi | 9606.ENSP00000430269 |
Chemistry databases
BindingDBi | P34913 |
ChEMBLi | CHEMBL2409 |
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 |
DrugCentrali | P34913 |
GuidetoPHARMACOLOGYi | 2970 |
SwissLipidsi | SLP:000001105 |
Protein family/group databases
ESTHERi | human-EPHX2, Epoxide_hydrolase |
MEROPSi | S33.973 |
PTM databases
DEPODi | EPHX2 |
iPTMneti | P34913 |
PhosphoSitePlusi | P34913 |
Genetic variation databases
BioMutai | EPHX2 |
DMDMi | 67476665 |
Proteomic databases
EPDi | P34913 |
jPOSTi | P34913 |
MassIVEi | P34913 |
MaxQBi | P34913 |
PaxDbi | P34913 |
PeptideAtlasi | P34913 |
PRIDEi | P34913 |
ProteomicsDBi | 32244 54953 [P34913-1] |
Protocols and materials databases
Antibodypediai | 4070, 405 antibodies |
DNASUi | 2053 |
Genome annotation databases
Ensembli | ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2] ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1] ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3] |
GeneIDi | 2053 |
KEGGi | hsa:2053 |
UCSCi | uc003xfu.5, human [P34913-1] |
Organism-specific databases
CTDi | 2053 |
DisGeNETi | 2053 |
GeneCardsi | EPHX2 |
HGNCi | HGNC:3402, EPHX2 |
HPAi | ENSG00000120915, Tissue enhanced (intestine, liver) |
MalaCardsi | EPHX2 |
MIMi | 132811, gene |
neXtProti | NX_P34913 |
OpenTargetsi | ENSG00000120915 |
PharmGKBi | PA27830 |
VEuPathDBi | HostDB:ENSG00000120915.13 |
GenAtlasi | Search... |
Phylogenomic databases
eggNOGi | KOG3085, Eukaryota KOG4178, Eukaryota |
GeneTreei | ENSGT00940000158614 |
HOGENOMi | CLU_036085_1_1_1 |
InParanoidi | P34913 |
OMAi | ANHWLDD |
OrthoDBi | 616687at2759 |
PhylomeDBi | P34913 |
TreeFami | TF315395 |
Enzyme and pathway databases
BRENDAi | 3.3.2.10, 2681 |
PathwayCommonsi | P34913 |
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-RKi | P34913 |
Miscellaneous databases
BioGRID-ORCSi | 2053, 5 hits in 997 CRISPR screens |
ChiTaRSi | EPHX2, human |
EvolutionaryTracei | P34913 |
GeneWikii | Epoxide_hydrolase_2 |
GenomeRNAii | 2053 |
Pharosi | P34913, Tchem |
PROi | PR:P34913 |
RNActi | P34913, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSG00000120915, Expressed in right lobe of liver and 181 other tissues |
ExpressionAtlasi | P34913, baseline and differential |
Genevisiblei | P34913, HS |
Family and domain databases
Gene3Di | 1.10.150.240, 1 hit 3.40.50.1000, 1 hit 3.40.50.1820, 1 hit |
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 |
Pfami | View protein in Pfam PF00561, Abhydrolase_1, 1 hit PF13419, HAD_2, 1 hit |
PRINTSi | PR00111, ABHYDROLASE PR00412, EPOXHYDRLASE |
SUPFAMi | SSF53474, SSF53474, 1 hit SSF56784, SSF56784, 1 hit |
TIGRFAMsi | TIGR02247, HAD-1A3-hyp, 1 hit TIGR01509, HAD-SF-IA-v3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HYES_HUMAN | |
Accessioni | P34913Primary (citable) accession number: P34913 Secondary accession number(s): B2Z3B1 Q9HBJ2 | |
Entry historyi | Integrated 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. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program | |
Disclaimer | Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM - Human entries with genetic variants
List of human entries with genetic variants - Human variants curated from literature reports
Index of human variants curated from literature reports - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families