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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-Experimental evidence at protein leveli

Functioni

Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides. Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides. Also determines steady-state levels of physiological mediators. 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, 12-phosphonooxy-octadec-9E-enoic acid, and p-nitrophenyl phosphate.2 Publications

Catalytic activityi

An epoxide + H2O = a glycol.
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.

Cofactori

Mg2+1 Publication

Kineticsi

  1. KM=21 µM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. KM=1.1 mM for p-nitrophenyl phosphate3 Publications
  1. Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi9Magnesium1 Publication1
Metal bindingi11Magnesium1 Publication1
Metal bindingi185Magnesium1 Publication1
Active sitei335Nucleophile1
Binding sitei383Substrate1
Active sitei466Proton donor1
Active sitei524Proton acceptor1

GO - Molecular functioni

  • 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
  • epoxide hydrolase activity Source: UniProtKB
  • lipid phosphatase activity Source: UniProtKB
  • magnesium ion binding Source: UniProtKB
  • phosphatase activity Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB
  • toxic substance binding Source: UniProtKB

GO - Biological processi

  • cellular calcium ion homeostasis Source: UniProtKB
  • cholesterol homeostasis Source: UniProtKB
  • dephosphorylation Source: UniProtKB
  • drug metabolic process Source: UniProtKB
  • epoxygenase P450 pathway Source: Reactome
  • inflammatory response Source: UniProtKB
  • phospholipid dephosphorylation Source: UniProtKB
  • positive regulation of gene expression Source: UniProtKB
  • positive regulation of vasodilation Source: UniProtKB
  • reactive oxygen species metabolic process Source: UniProtKB
  • regulation of blood pressure Source: UniProtKB
  • regulation of cholesterol metabolic process Source: UniProtKB
  • response to toxic substance Source: UniProtKB
  • stilbene catabolic process Source: UniProtKB
  • xenobiotic metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism

Keywords - Ligandi

Magnesium, Metal-binding

Enzyme and pathway databases

BioCyciZFISH:HS04452-MONOMER.
BRENDAi3.3.2.10. 2681.
ReactomeiR-HSA-2142670. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
SABIO-RKP34913.

Protein family/group databases

ESTHERihuman-EPHX2. Epoxide_hydrolase.
MEROPSiS33.973.

Chemistry databases

SwissLipidsiSLP:000001105.

Names & Taxonomyi

Protein namesi
Recommended name:
Bifunctional epoxide hydrolase 2
Including the following 2 domains:
Cytosolic epoxide hydrolase 2 (EC:3.3.2.10)
Short name:
CEH
Alternative name(s):
Epoxide hydratase
Soluble epoxide hydrolase
Short name:
SEH
Lipid-phosphate phosphatase (EC:3.1.3.76)
Gene namesi
Name:EPHX2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:3402. EPHX2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9D → A: Loss of phosphatase activity. 1 Publication1
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

DisGeNETi2053.
MalaCardsiEPHX2.
OpenTargetsiENSG00000120915.
PharmGKBiPA27830.

Chemistry databases

ChEMBLiCHEMBL2409.

Polymorphism and mutation databases

BioMutaiEPHX2.
DMDMi67476665.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000841111 – 555Bifunctional epoxide hydrolase 2Add BLAST555

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Lipidationi522S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine1 Publication1
Modified residuei554N6-succinyllysineBy similarity1

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

EPDiP34913.
MaxQBiP34913.
PaxDbiP34913.
PeptideAtlasiP34913.
PRIDEiP34913.

PTM databases

DEPODiP34913.
iPTMnetiP34913.
PhosphoSitePlusiP34913.

Expressioni

Inductioni

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

Gene expression databases

BgeeiENSG00000120915.
CleanExiHS_EPHX2.
ExpressionAtlasiP34913. baseline and differential.
GenevisibleiP34913. HS.

Organism-specific databases

HPAiCAB009808.
HPA023094.
HPA023660.
HPA023779.

Interactioni

Subunit structurei

Homodimer.3 Publications

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB
  • receptor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi108367. 5 interactors.
IntActiP34913. 4 interactors.
MINTiMINT-1385532.
STRINGi9606.ENSP00000430269.

Chemistry databases

BindingDBiP34913.

Structurei

Secondary structure

1555
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Turni12 – 14Combined sources3
Beta strandi15 – 17Combined sources3
Helixi19 – 21Combined sources3
Helixi23 – 29Combined sources7
Helixi36 – 42Combined sources7
Helixi45 – 47Combined sources3
Helixi49 – 54Combined sources6
Beta strandi57 – 59Combined sources3
Helixi60 – 78Combined sources19
Helixi88 – 98Combined sources11
Helixi103 – 114Combined sources12
Beta strandi118 – 123Combined sources6
Turni131 – 133Combined sources3
Helixi134 – 144Combined sources11
Beta strandi147 – 152Combined sources6
Helixi153 – 156Combined sources4
Beta strandi160 – 162Combined sources3
Helixi163 – 173Combined sources11
Helixi177 – 179Combined sources3
Beta strandi180 – 185Combined sources6
Helixi187 – 196Combined sources10
Beta strandi199 – 202Combined sources4
Helixi206 – 217Combined sources12
Helixi234 – 236Combined sources3
Beta strandi237 – 245Combined sources9
Beta strandi248 – 255Combined sources8
Beta strandi257 – 264Combined sources8
Helixi271 – 274Combined sources4
Turni275 – 277Combined sources3
Helixi278 – 283Combined sources6
Beta strandi287 – 291Combined sources5
Helixi305 – 308Combined sources4
Helixi310 – 324Combined sources15
Beta strandi329 – 334Combined sources6
Helixi336 – 347Combined sources12
Helixi349 – 351Combined sources3
Beta strandi352 – 359Combined sources8
Beta strandi367 – 369Combined sources3
Helixi371 – 376Combined sources6
Helixi379 – 382Combined sources4
Helixi383 – 386Combined sources4
Helixi392 – 398Combined sources7
Helixi401 – 408Combined sources8
Helixi412 – 414Combined sources3
Helixi419 – 421Combined sources3
Turni424 – 426Combined sources3
Turni428 – 431Combined sources4
Beta strandi440 – 442Combined sources3
Helixi444 – 455Combined sources12
Turni456 – 459Combined sources4
Helixi460 – 464Combined sources5
Turni465 – 468Combined sources4
Helixi469 – 477Combined sources9
Turni478 – 481Combined sources4
Beta strandi488 – 493Combined sources6
Beta strandi497 – 499Combined sources3
Helixi501 – 504Combined sources4
Helixi507 – 509Combined sources3
Beta strandi515 – 519Combined sources5
Helixi526 – 529Combined sources4
Helixi531 – 545Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP34913.
SMRiP34913.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP34913.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini259 – 531AB hydrolase-1Sequence analysisAdd BLAST273

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 224PhosphataseAdd BLAST224
Regioni123 – 124Phosphate binding2
Regioni235 – 555Epoxide hydrolaseAdd BLAST321

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi553 – 555Microbody targeting signalSequence analysis3

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
KOG4178. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00530000063213.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiP34913.
KOiK08726.
OMAiGHWTQMD.
OrthoDBiEOG091G078G.
PhylomeDBiP34913.
TreeFamiTF315395.

Family and domain databases

Gene3Di1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.1820. 1 hit.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF13419. HAD_2. 1 hit.
[Graphical view]
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.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

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

This isoform has been chosen as the 'canonical' 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
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.

Note: No experimental confirmation available.
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.

Note: No experimental confirmation available.
Show »
Length:489
Mass (Da):55,626
Checksum:i7188F0A08408CD29
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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
Natural variantiVAR_05539221G → A.1 PublicationCorresponds to variant rs72473930dbSNPEnsembl.1
Natural variantiVAR_05539352R → Q.1 PublicationCorresponds to variant rs72475803dbSNPEnsembl.1
Natural variantiVAR_05105955K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant rs41507953dbSNPEnsembl.1
Natural variantiVAR_033991103R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant rs17057255dbSNPEnsembl.1
Natural variantiVAR_055394154C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 PublicationsCorresponds to variant rs57699806dbSNPEnsembl.1
Natural variantiVAR_055395225P → L.1 PublicationCorresponds to variant rs72475821dbSNPEnsembl.1
Natural variantiVAR_014852287R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 PublicationsCorresponds to variant rs751141dbSNPEnsembl.1
Natural variantiVAR_055396369M → V.1 PublicationCorresponds to variant rs72475894dbSNPEnsembl.1
Natural variantiVAR_022613403R → RR.2 Publications1
Natural variantiVAR_055397470E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 PublicationsCorresponds to variant rs68053459dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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:
EMBLi
GenBanki
DDBJi
Links Updated
L05779 mRNA. Translation: AAA02756.1.
X97024
, X97025, X97026, X97027, X97028, X97029, X97030, X97031, X97032, X97033, X97034, X97035, X97036, X97037, 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]
UniGeneiHs.212088.

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]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L05779 mRNA. Translation: AAA02756.1.
X97024
, X97025, X97026, X97027, X97028, X97029, X97030, X97031, X97032, X97033, X97034, X97035, X97036, X97037, 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]
UniGeneiHs.212088.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
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[»]
ProteinModelPortaliP34913.
SMRiP34913.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi108367. 5 interactors.
IntActiP34913. 4 interactors.
MINTiMINT-1385532.
STRINGi9606.ENSP00000430269.

Chemistry databases

BindingDBiP34913.
ChEMBLiCHEMBL2409.
SwissLipidsiSLP:000001105.

Protein family/group databases

ESTHERihuman-EPHX2. Epoxide_hydrolase.
MEROPSiS33.973.

PTM databases

DEPODiP34913.
iPTMnetiP34913.
PhosphoSitePlusiP34913.

Polymorphism and mutation databases

BioMutaiEPHX2.
DMDMi67476665.

Proteomic databases

EPDiP34913.
MaxQBiP34913.
PaxDbiP34913.
PeptideAtlasiP34913.
PRIDEiP34913.

Protocols and materials databases

DNASUi2053.
Structural Biology KnowledgebaseSearch...

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

CTDi2053.
DisGeNETi2053.
GeneCardsiEPHX2.
HGNCiHGNC:3402. EPHX2.
HPAiCAB009808.
HPA023094.
HPA023660.
HPA023779.
MalaCardsiEPHX2.
MIMi132811. gene.
neXtProtiNX_P34913.
OpenTargetsiENSG00000120915.
PharmGKBiPA27830.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3085. Eukaryota.
KOG4178. Eukaryota.
COG1011. LUCA.
GeneTreeiENSGT00530000063213.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiP34913.
KOiK08726.
OMAiGHWTQMD.
OrthoDBiEOG091G078G.
PhylomeDBiP34913.
TreeFamiTF315395.

Enzyme and pathway databases

BioCyciZFISH:HS04452-MONOMER.
BRENDAi3.3.2.10. 2681.
ReactomeiR-HSA-2142670. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
SABIO-RKP34913.

Miscellaneous databases

EvolutionaryTraceiP34913.
GeneWikiiEpoxide_hydrolase_2.
GenomeRNAii2053.
PROiP34913.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000120915.
CleanExiHS_EPHX2.
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.
InterProiIPR029058. AB_hydrolase.
IPR000073. AB_hydrolase_1.
IPR000639. Epox_hydrolase-like.
IPR023214. HAD-like_dom.
IPR006439. HAD-SF_hydro_IA.
IPR011945. HAD-SF_ppase_IA/epoxid_hydro_N.
IPR023198. PGP_dom2.
[Graphical view]
PfamiPF00561. Abhydrolase_1. 1 hit.
PF13419. HAD_2. 1 hit.
[Graphical view]
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.
ProtoNetiSearch...

Entry informationi

Entry nameiHYES_HUMAN
AccessioniPrimary (citable) accession number: P34913
Secondary accession number(s): B2Z3B1
, B3KTU8, B3KUA0, G3V134, J3KPH7, Q16764, Q9HBJ1, Q9HBJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: June 7, 2005
Last modified: November 2, 2016
This is version 172 of the entry and version 2 of the sequence. [Complete history]
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.

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. Human chromosome 8
    Human chromosome 8: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.