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P34913

- HYES_HUMAN

UniProt

P34913 - HYES_HUMAN

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Protein
Bifunctional epoxide hydrolase 2
Gene
EPHX2
Organism
Homo sapiens (Human)
Status
Reviewed - 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 phospate.2 Publications

Catalytic activityi

An epoxide + H2O = a glycol.4 Publications
(9S,10S)-10-hydroxy-9-(phosphonooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphate.4 Publications

Cofactori

Magnesium.1 Publication

Kineticsi

  1. KM=21 µM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
  2. KM=1.1 mM for p-nitrophenyl phosphate

Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid

Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi9 – 91Magnesium
Metal bindingi11 – 111Magnesium
Metal bindingi185 – 1851Magnesium
Active sitei335 – 3351Nucleophile
Binding sitei383 – 3831Substrate
Active sitei466 – 4661Proton donor
Active sitei524 – 5241Proton acceptor

GO - Molecular functioni

  1. 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
  2. epoxide hydrolase activity Source: UniProtKB
  3. lipid phosphatase activity Source: UniProtKB
  4. magnesium ion binding Source: UniProtKB
  5. phosphatase activity Source: UniProtKB
  6. protein homodimerization activity Source: UniProtKB
  7. receptor binding Source: UniProtKB
  8. toxic substance binding Source: UniProtKB

GO - Biological processi

  1. arachidonic acid metabolic process Source: Reactome
  2. cellular calcium ion homeostasis Source: UniProtKB
  3. cholesterol homeostasis Source: UniProtKB
  4. dephosphorylation Source: UniProtKB
  5. drug metabolic process Source: UniProtKB
  6. epoxygenase P450 pathway Source: Reactome
  7. inflammatory response Source: UniProtKB
  8. phospholipid dephosphorylation Source: UniProtKB
  9. positive regulation of gene expression Source: UniProtKB
  10. positive regulation of vasodilation Source: UniProtKB
  11. reactive oxygen species metabolic process Source: UniProtKB
  12. regulation of blood pressure Source: UniProtKB
  13. regulation of cholesterol metabolic process Source: UniProtKB
  14. response to toxic substance Source: UniProtKB
  15. small molecule metabolic process Source: Reactome
  16. stilbene catabolic process Source: UniProtKB
  17. 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

ReactomeiREACT_150417. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
SABIO-RKP34913.

Protein family/group databases

MEROPSiS33.973.

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
ProteomesiUP000005640: Chromosome 8

Organism-specific databases

HGNCiHGNC:3402. EPHX2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. extracellular vesicular exosome Source: UniProt
  3. peroxisome Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Peroxisome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91D → A: Loss of phosphatase activity. 1 Publication
Mutagenesisi522 – 5221C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. 1 Publication

Organism-specific databases

PharmGKBiPA27830.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 555555Bifunctional epoxide hydrolase 2
PRO_0000084111Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei43 – 431N6-acetyllysine1 Publication
Modified residuei55 – 551N6-succinyllysine By similarity
Modified residuei191 – 1911N6-acetyllysine By similarity
Modified residuei215 – 2151N6-acetyllysine By similarity
Modified residuei370 – 3701Phosphoserine By similarity
Modified residuei421 – 4211N6-succinyllysine By similarity
Modified residuei455 – 4551N6-succinyllysine By similarity
Lipidationi522 – 5221S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine Inferred
Modified residuei554 – 5541N6-succinyllysine By similarity

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 Inferred.

Keywords - PTMi

Acetylation, Lipoprotein, Phosphoprotein

Proteomic databases

MaxQBiP34913.
PaxDbiP34913.
PeptideAtlasiP34913.
PRIDEiP34913.

PTM databases

PhosphoSiteiP34913.

Expressioni

Inductioni

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

Gene expression databases

ArrayExpressiP34913.
BgeeiP34913.
CleanExiHS_EPHX2.
GenevestigatoriP34913.

Organism-specific databases

HPAiCAB009808.
HPA023094.
HPA023660.
HPA023779.

Interactioni

Subunit structurei

Homodimer.

Protein-protein interaction databases

BioGridi108367. 5 interactions.
IntActiP34913. 3 interactions.
MINTiMINT-1385532.
STRINGi9606.ENSP00000369843.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi5 – 84
Turni12 – 143
Beta strandi15 – 173
Helixi20 – 2910
Helixi36 – 427
Helixi45 – 473
Helixi49 – 546
Beta strandi57 – 593
Helixi60 – 7718
Helixi88 – 9811
Helixi103 – 11412
Beta strandi118 – 1236
Turni131 – 1333
Helixi134 – 14411
Beta strandi147 – 1526
Helixi153 – 1564
Helixi163 – 17311
Helixi177 – 1793
Beta strandi180 – 1856
Helixi187 – 19610
Beta strandi199 – 2024
Helixi206 – 21712
Helixi234 – 2363
Beta strandi237 – 2459
Beta strandi248 – 2558
Beta strandi257 – 2648
Helixi271 – 2744
Helixi277 – 2837
Beta strandi287 – 2915
Helixi305 – 3084
Helixi310 – 32415
Beta strandi329 – 3346
Helixi336 – 34712
Helixi349 – 3513
Beta strandi352 – 3598
Beta strandi367 – 3693
Helixi371 – 3766
Helixi379 – 3813
Helixi382 – 3887
Helixi392 – 3998
Helixi401 – 4088
Helixi412 – 4143
Helixi419 – 4213
Helixi422 – 4254
Beta strandi427 – 4293
Beta strandi440 – 4423
Helixi444 – 45411
Turni455 – 4595
Helixi460 – 4645
Helixi465 – 4673
Helixi469 – 4779
Turni478 – 4814
Beta strandi488 – 4936
Beta strandi497 – 4993
Helixi501 – 5044
Helixi507 – 5093
Beta strandi515 – 5195
Helixi526 – 5294
Helixi531 – 54515

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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[»]
4HAIX-ray2.55A1-555[»]
4J03X-ray2.92A1-555[»]
4JNCX-ray1.96A238-549[»]
ProteinModelPortaliP34913.
SMRiP34913. Positions 2-548.

Miscellaneous databases

EvolutionaryTraceiP34913.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 224224Phosphatase
Add
BLAST
Regioni123 – 1242Phosphate binding
Regioni235 – 555321Epoxide hydrolase
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi553 – 5553Microbody targeting signal Reviewed prediction

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0596.
HOGENOMiHOG000028073.
HOVERGENiHBG006095.
InParanoidiP34913.
KOiK08726.
OMAiGHWTQMD.
OrthoDBiEOG72VH5T.
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. Align

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

MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT    50
TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK 100
INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL 150
IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT 200
ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL 250
HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS 300
APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE 350
RVRAVASLNT PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN 400
LSRTFKSLFR ASDESVLSMH KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY 450
VQQFKKSGFR GPLNWYRNME RNWKWACKSL GRKILIPALM VTAEKDFVLV 500
PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK WLDSDARNPP 550
VVSKM 555
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

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti21 – 211G → A.1 Publication
VAR_055392
Natural varianti52 – 521R → Q.1 Publication
Corresponds to variant rs72475803 [ dbSNP | Ensembl ].
VAR_055393
Natural varianti55 – 551K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 Publications
Corresponds to variant rs41507953 [ dbSNP | Ensembl ].
VAR_051059
Natural varianti103 – 1031R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 Publications
Corresponds to variant rs17057255 [ dbSNP | Ensembl ].
VAR_033991
Natural varianti154 – 1541C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 Publications
Corresponds to variant rs57699806 [ dbSNP | Ensembl ].
VAR_055394
Natural varianti225 – 2251P → L.1 Publication
VAR_055395
Natural varianti287 – 2871R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 Publications
Corresponds to variant rs751141 [ dbSNP | Ensembl ].
VAR_014852
Natural varianti369 – 3691M → V.1 Publication
Corresponds to variant rs72475894 [ dbSNP | Ensembl ].
VAR_055396
Natural varianti403 – 4031R → RR.2 Publications
VAR_022613
Natural varianti470 – 4701E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 Publications
Corresponds to variant rs68053459 [ dbSNP | Ensembl ].
VAR_055397

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6666Missing in isoform 3.
VSP_045597Add
BLAST
Alternative sequencei1 – 5353Missing in isoform 2.
VSP_045598Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → G in AAA02756. 1 Publication
Sequence conflicti257 – 2582SG → W in AAA02756. 1 Publication
Sequence conflicti409 – 4091F → L in BAG53362. 1 Publication
Sequence conflicti473 – 4731W → R in BAG53362. 1 Publication
Sequence conflicti494 – 4941E → G in BAG53362. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.4. human. [P34913-1]

Polymorphism databases

DMDMi67476665.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS59097.1. [P34913-2 ]
CCDS59098.1. [P34913-3 ]
CCDS6060.1. [P34913-1 ]
PIRi JC4711.
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 ]
UniGenei Hs.212088.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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 [» ]
4HAI X-ray 2.55 A 1-555 [» ]
4J03 X-ray 2.92 A 1-555 [» ]
4JNC X-ray 1.96 A 238-549 [» ]
ProteinModelPortali P34913.
SMRi P34913. Positions 2-548.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108367. 5 interactions.
IntActi P34913. 3 interactions.
MINTi MINT-1385532.
STRINGi 9606.ENSP00000369843.

Chemistry

BindingDBi P34913.
ChEMBLi CHEMBL2409.
DrugBanki DB00675. Tamoxifen.

Protein family/group databases

MEROPSi S33.973.

PTM databases

PhosphoSitei P34913.

Polymorphism databases

DMDMi 67476665.

Proteomic databases

MaxQBi P34913.
PaxDbi P34913.
PeptideAtlasi P34913.
PRIDEi P34913.

Protocols and materials databases

DNASUi 2053.
Structural Biology Knowledgebase Search...

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.4. human. [P34913-1 ]

Organism-specific databases

CTDi 2053.
GeneCardsi GC08P027348.
HGNCi HGNC:3402. EPHX2.
HPAi CAB009808.
HPA023094.
HPA023660.
HPA023779.
MIMi 132811. gene.
neXtProti NX_P34913.
PharmGKBi PA27830.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0596.
HOGENOMi HOG000028073.
HOVERGENi HBG006095.
InParanoidi P34913.
KOi K08726.
OMAi GHWTQMD.
OrthoDBi EOG72VH5T.
PhylomeDBi P34913.
TreeFami TF315395.

Enzyme and pathway databases

Reactomei REACT_150417. Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET).
SABIO-RK P34913.

Miscellaneous databases

EvolutionaryTracei P34913.
GeneWikii Epoxide_hydrolase_2.
GenomeRNAii 2053.
NextBioi 35535129.
PROi P34913.
SOURCEi Search...

Gene expression databases

ArrayExpressi P34913.
Bgeei P34913.
CleanExi HS_EPHX2.
Genevestigatori P34913.

Family and domain databases

Gene3Di 1.10.150.240. 1 hit.
3.40.50.1000. 1 hit.
3.40.50.1820. 1 hit.
InterProi IPR029058. 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 ]
Pfami PF00561. Abhydrolase_1. 1 hit.
PF13419. HAD_2. 1 hit.
[Graphical view ]
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.
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Publicationsi

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  1. "cDNA cloning and expression of a soluble epoxide hydrolase from human liver."
    Beetham J.K., Tian T., Hammock B.D.
    Arch. Biochem. Biophys. 305:197-201(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, VARIANT GLN-287.
    Tissue: Liver.
  2. "Structural characterization of the human soluble epoxide hydrolase gene (EPHX2)."
    Sandberg M., Meijer J.
    Biochem. Biophys. Res. Commun. 221:333-339(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Placenta.
  3. "Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms."
    Sandberg M., Hassett C., Adman E.T., Meijer J., Omiecinski C.J.
    J. Biol. Chem. 275:28873-28881(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLN-287 AND ARG-403 INS.
    Tissue: Liver.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), VARIANT ARG-403 INS.
    Tissue: Kidney and Prostate.
  6. NIEHS SNPs program
    Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ALA-21; GLN-52; ARG-55; CYS-103; TYR-154; LEU-225; GLN-287; VAL-369 AND GLY-470.
  7. "DNA sequence and analysis of human chromosome 8."
    Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., Asakawa T.
    , Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., Lander E.S.
    Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: B-cell and Lung.
  10. Cited for: CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
  11. "The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
    Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
    Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9.
  12. "The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
    Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES.
  13. "Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure."
    Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.
    Arch. Biochem. Biophys. 427:164-169(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
  14. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-43, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "Redox regulation of soluble epoxide hydrolase by 15-deoxy-delta-prostaglandin J2 controls coronary hypoxic vasodilation."
    Charles R.L., Burgoyne J.R., Mayr M., Weldon S.M., Hubner N., Dong H., Morisseau C., Hammock B.D., Landar A., Eaton P.
    Circ. Res. 108:324-334(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: LIPIDATION AT CYS-522, MUTAGENESIS OF CYS-522.
  17. "Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis."
    Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.
    Biochemistry 43:4716-4723(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE; MAGNESIUM AND EPOXIDE HYDROLASE INHIBITOR.
  18. "Human soluble epoxide hydrolase: structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids."
    Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.
    Protein Sci. 15:58-64(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH DIALKYLUREA INHIBITORS AND MAGNESIUM.
  19. "Structure-based optimization of arylamides as inhibitors of soluble epoxide hydrolase."
    Eldrup A.B., Soleymanzadeh F., Taylor S.J., Muegge I., Farrow N.A., Joseph D., McKellop K., Man C.C., Kukulka A., De Lombaert S.
    J. Med. Chem. 52:5880-5895(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEXES WITH ARYLAMIDE INHIBITORS.
  20. "Optimization of piperidyl-ureas as inhibitors of soluble epoxide hydrolase."
    Eldrup A.B., Soleymanzadeh F., Farrow N.A., Kukulka A., De Lombaert S.
    Bioorg. Med. Chem. Lett. 20:571-575(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.
  21. "Substituted pyrazoles as novel sEH antagonist: investigation of key binding interactions within the catalytic domain."
    Lo H.Y., Man C.C., Fleck R.W., Farrow N.A., Ingraham R.H., Kukulka A., Proudfoot J.R., Betageri R., Kirrane T., Patel U., Sharma R., Hoermann M.A., Kabcenell A., Lombaert S.D.
    Bioorg. Med. Chem. Lett. 20:6379-6383(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR.

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: September 3, 2014
This is version 149 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

External Data

Dasty 3

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