Ephx2
entrez
13850
canonical
uniprot
P34914
canonical
ensembl
ENSMUSG00000022040
resolver
ensp
ENSMUSP00000069209
resolver
ensp
ENSMUSP00000152894
resolver
ensp
ENSMUSP00000153161
resolver
enst
ENSMUST00000225309
resolver
genesymbol
Ephx2
resolver
genesymbol_syn
Eph2
resolver
uniprot
A0A286YCA9
resolver
uniprot
A8JYK8
resolver
uniprot
Q3UQ71
resolver
uniprot
Q8CGV0
resolver
uniprot_entry
A0A286YCA9_MOUSE
resolver
uniprot_entry
A8JYK8_MOUSE
resolver
uniprot_entry
HYES_MOUSE
resolver
uniprot_entry
Q3UQ71_MOUSE
resolver
uniprot_sec
Q8CGV0
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) (By similarity). Phosphatase activity is inhibited by dodecyl-phosphate, phospholipids such as phospho-lysophosphatidic acids and fatty acids such as palmitic acid and lauric acid (PubMed:21217101). {ECO:0000250|UniProtKB:P34913, ECO:0000269|PubMed:21217101}.
uniprot
proteins
amino_acid_sequence
MALRVAAFDLDGVLALPSIAGAFRRSEEALALPRDFLLGAYQTEFPEGPTEQLMKGKITFSQWVPLMDESYRKSSKACGANLPENFSISQIFSQAMAARSINRPMLQAAIALKKKGFTTCIVTNNWLDDGDKRDSLAQMMCELSQHFDFLIESCQVGMIKPEPQIYNFLLDTLKAKPNEVVFLDDFGSNLKPARDMGMVTILVHNTASALRELEKVTGTQFPEAPLPVPCNPNDVSHGYVTVKPGIRLHFVEMGSGPALCLCHGFPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEEYAMELLCKEMVTFLDKLGIPQAVFIGHDWAGVMVWNMALFYPERVRAVASLNTPFMPPDPDVSPMKVIRSIPVFNYQLYFQEPGVAEAELEKNMSRTFKSFFRASDETGFIAVHKATEIGGILVNTPEDPNLSKITTEEEIEFYIQQFKKTGFRGPLNWYRNTERNWKWSCKGLGRKILVPALMVTAEKDIVLRPEMSKNMEKWIPFLKRGHIEDCGHWTQIEKPTEVNQILIKWLQTEVQNPSVTSKI
uniprot
proteins
ec_number
3.1.3.76
uniprot
proteins
ec_number
3.3.2.10
uniprot
proteins
function
FUNCTION: Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:21217101, PubMed:7840649). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (By similarity). {ECO:0000250|UniProtKB:P34913, ECO:0000250|UniProtKB:P80299, ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:7840649}.; FUNCTION: Bifunctional enzyme. 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 (By similarity). Has phosphatase activity toward lyso-glycerophospholipids with also some lower activity toward lysolipids of sphingolipid and isoprenoid phosphates (By similarity). {ECO:0000250|UniProtKB:P34913}.
uniprot
proteins
mass_dalton
62515
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 (By similarity). {ECO:0000250}.
uniprot
proteins
protein_family
AB hydrolase superfamily
uniprot
proteins
protein_family
Epoxide hydrolase family
uniprot
proteins
pubmed
10485878
uniprot
proteins
pubmed
10747889
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15601917
uniprot
proteins
pubmed
17242355
uniprot
proteins
pubmed
21183079
uniprot
proteins
pubmed
21217101
uniprot
proteins
pubmed
23576753
uniprot
proteins
pubmed
23806337
uniprot
proteins
pubmed
7840649
uniprot
proteins
pubmed
8349642
uniprot
proteins
pubmed
8750907
uniprot
proteins
sequence_length
554
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21217101, ECO:0000269|PubMed:7840649}. Peroxisome.
uniprot
proteins