EPHX2
entrez
2053
canonical
uniprot
P34913
canonical
ensembl
ENSG00000120915
resolver
ensp
ENSP00000369843
resolver
ensp
ENSP00000427956
resolver
ensp
ENSP00000430269
resolver
ensp
ENSP00000430302
resolver
ensp
ENSP00000543014
resolver
ensp
ENSP00000779100
resolver
ensp
ENSP00000786801
resolver
ensp
ENSP00000786802
resolver
ensp
ENSP00000796928
resolver
enst
ENST00000518379
resolver
genesymbol
EPHX2
resolver
hgnc
HGNC:3402
resolver
uniprot
B2Z3B1
resolver
uniprot
B3KTU8
resolver
uniprot
B3KUA0
resolver
uniprot
E5RFU2
resolver
uniprot
G3V134
resolver
uniprot
J3KPH7
resolver
uniprot
Q16764
resolver
uniprot
Q9HBJ1
resolver
uniprot
Q9HBJ2
resolver
uniprot_entry
E5RFU2_HUMAN
resolver
uniprot_entry
HYES_HUMAN
resolver
uniprot_sec
B2Z3B1
resolver
uniprot_sec
B3KTU8
resolver
uniprot_sec
B3KUA0
resolver
uniprot_sec
G3V134
resolver
uniprot_sec
J3KPH7
resolver
uniprot_sec
Q16764
resolver
uniprot_sec
Q9HBJ1
resolver
uniprot_sec
Q9HBJ2
resolver
activity_regulation
ACTIVITY REGULATION: 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). {ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:22217705, ECO:0000269|PubMed:22387545, ECO:0000269|PubMed:22798687}.
uniprot
proteins
amino_acid_sequence
MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM
uniprot
proteins
ec_number
3.1.3.76
uniprot
proteins
ec_number
3.3.2.10
uniprot
proteins
function
FUNCTION: Bifunctional enzyme (PubMed:12574510). The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:12574510, PubMed:12869654, PubMed:22798687). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (PubMed:12574510, PubMed:12869654, PubMed:21217101, PubMed:22798687). {ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:12869654, ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:22798687}.; FUNCTION: 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). {ECO:0000269|PubMed:12574510, ECO:0000269|PubMed:22217705, ECO:0000269|PubMed:22387545}.
uniprot
proteins
mass_dalton
62616
uniprot
proteins
mutagenesis
MUTAGEN 9; /note="D->A: Loss of phosphatase activity."; /evidence="ECO:0000269|PubMed:12574508, ECO:0000269|PubMed:22217705"; MUTAGEN 522; /note="C->S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity."; /evidence="ECO:0000269|PubMed:21164107
uniprot
proteins
post_translational_modification
PTM: The N-terminus is blocked.; PTM: 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). {ECO:0000305}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Epoxide hydrolase family
uniprot
proteins
pubmed
10862610
uniprot
proteins
pubmed
12574508
uniprot
proteins
pubmed
12574510
uniprot
proteins
pubmed
12869654
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15096040
uniprot
proteins
pubmed
15196990
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16322563
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19746975
uniprot
proteins
pubmed
19969453
uniprot
proteins
pubmed
20934334
uniprot
proteins
pubmed
21164107
uniprot
proteins
pubmed
21217101
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22217705
uniprot
proteins
pubmed
22387545
uniprot
proteins
pubmed
22798687
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
8342951
uniprot
proteins
pubmed
8619856
uniprot
proteins
sequence_length
555
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm. Peroxisome.
uniprot
proteins