UniProtKB - P34914 (HYES_MOUSE)
Protein
Bifunctional epoxide hydrolase 2
Gene
Ephx2
Organism
Mus musculus (Mouse)
Status
Functioni
Bifunctional enzyme. The C-terminal domain has epoxide hydrolase activity and acts on epoxides (alkene oxides, oxiranes) and arene oxides (PubMed:7840649, PubMed:21217101). Plays a role in xenobiotic metabolism by degrading potentially toxic epoxides (By similarity). Also determines steady-state levels of physiological mediators (By similarity).By similarity2 Publications
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).By similarity
Catalytic activityi
- EC:3.3.2.10By similarity
- (9S,10S)-10-hydroxy-9-(phosphooxy)octadecanoate + H2O = (9S,10S)-9,10-dihydroxyoctadecanoate + phosphateBy similarityEC:3.1.3.76By similarity
- 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.
- (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8S,9S)-dihydroxy-(5Z,11Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14S,15S)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8R,9R)-dihydroxy-(5Z,11Z,14Z)-eicosatrienoate1 PublicationThis reaction proceeds in the forward1 Publication direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy-(5Z,11Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = 14,15-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 1-tetradecanoyl-sn-glycerol 3-phosphate + H2O = 1-tetradecanoyl-sn-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
- This reaction proceeds in the forwardBy similarity direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphateBy similarityThis reaction proceeds in the forwardBy similarity direction.
Cofactori
Mg2+By similarity
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) (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).By similarity1 Publication
Kineticsi
- KM=4 µM for 14(R),15(S)-EET1 Publication
- KM=5 µM for 14(S),15(R)-EET1 Publication
- KM=3 µM for 11(R),12(R)-EET1 Publication
- KM=4 µM for 11(S),12(R)-EET1 Publication
- KM=41 µM for 8(R),9(S)-EET1 Publication
- KM=5 µM for 8(S),9(R)-EET1 Publication
- Vmax=9.03 µmol/min/mg enzyme with 14(R),15(S)-EET as substrate1 Publication
- Vmax=1.36 µmol/min/mg enzyme with 14(S),15(R)-EET as substrate1 Publication
- Vmax=0.82 µmol/min/mg enzyme with 11(R),12(R)-EET as substrate1 Publication
- Vmax=3.02 µmol/min/mg enzyme with 11(S),12(R)-EET as substrate1 Publication
- Vmax=0.83 µmol/min/mg enzyme with 8(R),9(S)-EET as substrate1 Publication
- Vmax=3.10 µmol/min/mg enzyme with 8(S),9(R)-EET as substrate1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 9 | MagnesiumBy similarity | 1 | |
Metal bindingi | 11 | MagnesiumBy similarity | 1 | |
Metal bindingi | 185 | MagnesiumBy similarity | 1 | |
Active sitei | 333 | Nucleophile2 Publications | 1 | |
Binding sitei | 381 | SubstrateBy similarity | 1 | |
Active sitei | 465 | Proton donor2 Publications | 1 | |
Active sitei | 523 | Proton acceptor2 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: MGI
- protein homodimerization activity Source: MGI
- toxic substance binding Source: MGI
GO - Biological processi
- cholesterol homeostasis Source: UniProtKB
- dephosphorylation Source: UniProtKB
- epoxide metabolic process Source: UniProtKB
- inflammatory response Source: MGI
- linoleic acid metabolic process Source: MGI
- phospholipid dephosphorylation Source: UniProtKB
- positive regulation of blood pressure Source: MGI
- positive regulation of gene expression Source: UniProtKB
- prostaglandin production involved in inflammatory response Source: MGI
- regulation of cholesterol metabolic process Source: UniProtKB
- response to toxic substance Source: UniProtKB-KW
- sensory perception of pain Source: MGI
- stilbene catabolic process Source: MGI
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, 3474 |
Reactomei | R-MMU-2142670, Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) R-MMU-9018682, Biosynthesis of maresins R-MMU-9033241, Peroxisomal protein import |
Protein family/group databases
ESTHERi | mouse-hyes, Epoxide_hydrolase |
MEROPSi | S33.973 |
Chemistry databases
SwissLipidsi | SLP:000001106 |
Names & Taxonomyi
Protein namesi | Recommended name: Bifunctional epoxide hydrolase 2CuratedIncluding the following 2 domains: |
Gene namesi | |
Organismi | Mus musculus (Mouse) |
Taxonomic identifieri | 10090 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus |
Proteomesi |
|
Organism-specific databases
MGIi | MGI:99500, Ephx2 |
Subcellular locationi
Peroxisome
Other locations
- Cytoplasm 2 Publications
Cytosol
- cytosol Source: MGI
Peroxisome
- peroxisome Source: MGI
Keywords - Cellular componenti
Cytoplasm, PeroxisomePathology & Biotechi
Disruption phenotypei
In knockout mice, hepoxilin turnover to trioxilins is greatly abolished (PubMed:21217101). In livers, the activity toward HxA3 (8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate) and HxB3 (10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate) is greatly reduced compared with the WT mice (PubMed:21217101).1 Publication
Chemistry databases
ChEMBLi | CHEMBL4140 |
GuidetoPHARMACOLOGYi | 2970 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000084112 | 1 – 554 | Bifunctional epoxide hydrolase 2Add BLAST | 554 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 55 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 176 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 176 | N6-succinyllysine; alternateCombined sources | 1 | |
Modified residuei | 191 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 215 | N6-acetyllysineCombined sources | 1 | |
Modified residuei | 368 | PhosphoserineCombined sources | 1 | |
Modified residuei | 371 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 420 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 454 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 504 | N6-succinyllysineCombined sources | 1 | |
Modified residuei | 508 | N6-acetyllysine; alternateCombined sources | 1 | |
Modified residuei | 508 | N6-succinyllysine; alternateCombined sources | 1 | |
Lipidationi | 521 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteineBy similarity | 1 | |
Modified residuei | 553 | N6-succinyllysineCombined sources | 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 (By similarity).By similarity
Keywords - PTMi
Acetylation, Lipoprotein, PhosphoproteinProteomic databases
jPOSTi | P34914 |
MaxQBi | P34914 |
PaxDbi | P34914 |
PeptideAtlasi | P34914 |
PRIDEi | P34914 |
2D gel databases
SWISS-2DPAGEi | P34914 |
PTM databases
iPTMneti | P34914 |
MetOSitei | P34914 |
PhosphoSitePlusi | P34914 |
SwissPalmi | P34914 |
Expressioni
Tissue specificityi
Detected in liver, intestine, ovary and kidney. Detected at low levels in heart and muscle.4 Publications
Inductioni
Up-regulated during the luteal phase of the stimulated estrus cycle and by compounds that cause peroxisome proliferation, such as clofibrate, tiadenol and fenofibrate.3 Publications
Gene expression databases
Bgeei | ENSMUSG00000022040, Expressed in cumulus cell and 276 other tissues |
ExpressionAtlasi | P34914, baseline and differential |
Genevisiblei | P34914, MM |
Interactioni
Subunit structurei
Homodimer.
2 PublicationsGO - Molecular functioni
- protein homodimerization activity Source: MGI
Protein-protein interaction databases
BioGRIDi | 199481, 3 interactors |
IntActi | P34914, 8 interactors |
MINTi | P34914 |
STRINGi | 10090.ENSMUSP00000069209 |
Chemistry databases
BindingDBi | P34914 |
Miscellaneous databases
RNActi | P34914, protein |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | P34914 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | P34914 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 257 – 530 | AB hydrolase-1Sequence analysisAdd BLAST | 274 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 224 | PhosphataseAdd BLAST | 224 | |
Regioni | 123 – 124 | Phosphate bindingBy similarity | 2 | |
Regioni | 233 – 554 | Epoxide hydrolaseAdd BLAST | 322 |
Motif
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Motifi | 552 – 554 | 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 | P34914 |
PhylomeDBi | P34914 |
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 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 | TIGR01509, HAD-SF-IA-v3, 1 hit |
s (2+)i Sequence
Sequence statusi: Complete.
This entry describes 2 produced by isoformsialternative splicing. AlignAdd to basketThis entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All
Isoform 1 (identifier: P34914-1) [UniParc]FASTAAdd to basket
Also known as: Ephx2A
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
MALRVAAFDL DGVLALPSIA GAFRRSEEAL ALPRDFLLGA YQTEFPEGPT
60 70 80 90 100
EQLMKGKITF SQWVPLMDES YRKSSKACGA NLPENFSISQ IFSQAMAARS
110 120 130 140 150
INRPMLQAAI ALKKKGFTTC IVTNNWLDDG DKRDSLAQMM CELSQHFDFL
160 170 180 190 200
IESCQVGMIK PEPQIYNFLL DTLKAKPNEV VFLDDFGSNL KPARDMGMVT
210 220 230 240 250
ILVHNTASAL RELEKVTGTQ FPEAPLPVPC NPNDVSHGYV TVKPGIRLHF
260 270 280 290 300
VEMGSGPALC LCHGFPESWF SWRYQIPALA QAGFRVLAID MKGYGDSSSP
310 320 330 340 350
PEIEEYAMEL LCKEMVTFLD KLGIPQAVFI GHDWAGVMVW NMALFYPERV
360 370 380 390 400
RAVASLNTPF MPPDPDVSPM KVIRSIPVFN YQLYFQEPGV AEAELEKNMS
410 420 430 440 450
RTFKSFFRAS DETGFIAVHK ATEIGGILVN TPEDPNLSKI TTEEEIEFYI
460 470 480 490 500
QQFKKTGFRG PLNWYRNTER NWKWSCKGLG RKILVPALMV TAEKDIVLRP
510 520 530 540 550
EMSKNMEKWI PFLKRGHIED CGHWTQIEKP TEVNQILIKW LQTEVQNPSV
TSKI
Computationally mapped potential isoform sequencesi
There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basketA8JYK8 | A8JYK8_MOUSE | Bifunctional epoxide hydrolase 2 | Ephx2 | 488 | Annotation score: |
Experimental Info
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sequence conflicti | 77 | A → T in CAA85471 (PubMed:8750907).Curated | 1 |
Alternative sequence
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Alternative sequenceiVSP_013904 | 1 – 62 | MALRV…ITFSQ → MRFAAMAAFSVFFVSKGLLM NSNIWCVGQEGPSQEDTDTI HTSE in isoform 2. 1 PublicationAdd BLAST | 62 |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L05781 mRNA Translation: AAA37555.1 Z37107 mRNA Translation: CAA85471.1 AY098585 mRNA Translation: AAM28238.1 BC015087 mRNA Translation: AAH15087.1 |
CCDSi | CCDS27218.1 [P34914-1] CCDS88694.1 [P34914-2] |
PIRi | A47504 |
RefSeqi | NP_001258332.1, NM_001271403.1 [P34914-2] NP_031966.2, NM_007940.4 [P34914-1] |
Genome annotation databases
Ensembli | ENSMUST00000070515; ENSMUSP00000069209; ENSMUSG00000022040 [P34914-1] ENSMUST00000224698; ENSMUSP00000153161; ENSMUSG00000022040 [P34914-2] |
GeneIDi | 13850 |
KEGGi | mmu:13850 |
UCSCi | uc007ujv.2, mouse [P34914-1] uc033grp.1, mouse [P34914-2] |
Keywords - Coding sequence diversityi
Alternative splicingSimilar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | L05781 mRNA Translation: AAA37555.1 Z37107 mRNA Translation: CAA85471.1 AY098585 mRNA Translation: AAM28238.1 BC015087 mRNA Translation: AAH15087.1 |
CCDSi | CCDS27218.1 [P34914-1] CCDS88694.1 [P34914-2] |
PIRi | A47504 |
RefSeqi | NP_001258332.1, NM_001271403.1 [P34914-2] NP_031966.2, NM_007940.4 [P34914-1] |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1CQZ | X-ray | 2.80 | A/B | 1-554 | [»] | |
1CR6 | X-ray | 2.80 | A/B | 1-554 | [»] | |
1EK1 | X-ray | 3.10 | A/B | 1-554 | [»] | |
1EK2 | X-ray | 3.00 | A/B | 1-554 | [»] | |
SMRi | P34914 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
BioGRIDi | 199481, 3 interactors |
IntActi | P34914, 8 interactors |
MINTi | P34914 |
STRINGi | 10090.ENSMUSP00000069209 |
Chemistry databases
BindingDBi | P34914 |
ChEMBLi | CHEMBL4140 |
GuidetoPHARMACOLOGYi | 2970 |
SwissLipidsi | SLP:000001106 |
Protein family/group databases
ESTHERi | mouse-hyes, Epoxide_hydrolase |
MEROPSi | S33.973 |
PTM databases
iPTMneti | P34914 |
MetOSitei | P34914 |
PhosphoSitePlusi | P34914 |
SwissPalmi | P34914 |
2D gel databases
SWISS-2DPAGEi | P34914 |
Proteomic databases
jPOSTi | P34914 |
MaxQBi | P34914 |
PaxDbi | P34914 |
PeptideAtlasi | P34914 |
PRIDEi | P34914 |
Protocols and materials databases
Antibodypediai | 4070, 397 antibodies |
Genome annotation databases
Ensembli | ENSMUST00000070515; ENSMUSP00000069209; ENSMUSG00000022040 [P34914-1] ENSMUST00000224698; ENSMUSP00000153161; ENSMUSG00000022040 [P34914-2] |
GeneIDi | 13850 |
KEGGi | mmu:13850 |
UCSCi | uc007ujv.2, mouse [P34914-1] uc033grp.1, mouse [P34914-2] |
Organism-specific databases
CTDi | 2053 |
MGIi | MGI:99500, Ephx2 |
Phylogenomic databases
eggNOGi | KOG3085, Eukaryota KOG4178, Eukaryota |
GeneTreei | ENSGT00940000158614 |
HOGENOMi | CLU_036085_1_1_1 |
InParanoidi | P34914 |
PhylomeDBi | P34914 |
TreeFami | TF315395 |
Enzyme and pathway databases
BRENDAi | 3.3.2.10, 3474 |
Reactomei | R-MMU-2142670, Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) R-MMU-9018682, Biosynthesis of maresins R-MMU-9033241, Peroxisomal protein import |
Miscellaneous databases
BioGRID-ORCSi | 13850, 0 hits in 17 CRISPR screens |
ChiTaRSi | Ephx2, mouse |
EvolutionaryTracei | P34914 |
PROi | PR:P34914 |
RNActi | P34914, protein |
SOURCEi | Search... |
Gene expression databases
Bgeei | ENSMUSG00000022040, Expressed in cumulus cell and 276 other tissues |
ExpressionAtlasi | P34914, baseline and differential |
Genevisiblei | P34914, MM |
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 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 | TIGR01509, HAD-SF-IA-v3, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | HYES_MOUSE | |
Accessioni | P34914Primary (citable) accession number: P34914 Secondary accession number(s): Q8CGV0 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
Last sequence update: | October 1, 1996 | |
Last modified: | December 2, 2020 | |
This is version 183 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- MGD cross-references
Mouse Genome Database (MGD) 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