P34913 · HYES_HUMAN
- ProteinBifunctional epoxide hydrolase 2
- GeneEPHX2
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids555 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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).
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).
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).
Catalytic activity
- an epoxide + H2O = an ethanediol
- 12-phosphooxy-(9Z)-octadecenoate + H2O = 12-hydroxy-(9Z)-octadecenoate + phosphateThis reaction proceeds in the forward direction.
- 12-phosphooxy-(9E)-octadecenoate + H2O = 12-hydroxy-(9E)-octadecenoate + phosphateThis reaction proceeds in the forward direction.
- 12-(phosphooxy)octadecanoate + H2O = 12-hydroxyoctadecanoate + phosphateThis reaction proceeds in the forward direction.
- 8,9-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = 8,9-dihydroxy-(5Z,11Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- 11,12-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = 11,12-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- 14,15-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = 14,15-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- 9,10-epoxy-(12Z)-octadecenoate + H2O = 9,10-dihydroxy-(12Z)-octadecenoateThis reaction proceeds in the forward direction.
- 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate + H2O = (8,11R,12S)-trihydroxy-(5Z,9E,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate + H2O = (10,11S,12R)-trihydroxy-(5Z,8Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- 1-tetradecanoyl-sn-glycerol 3-phosphate + H2O = 1-tetradecanoyl-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1-octadecanoyl-sn-glycero-3-phosphate + H2O = 1-octadecanoyl-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycero-3-phosphate + H2O = 1-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1-hexadecanoyl-sn-glycero-3-phosphate + H2O = 1-hexadecanoyl-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- 1-(9Z-octadecenoyl)-sn-glycero-3-phosphate + H2O = 1-(9Z-octadecenoyl)-sn-glycerol + phosphateThis reaction proceeds in the forward direction.
- (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8S,9S)-dihydroxy-(5Z,11Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (11S,12R)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14S,15R)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14S,15S)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11S,12S)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (11R,12S)-epoxy-(5Z,8Z,14Z)-eicosatrienoate + H2O = (11R,12R)-dihydroxy-(5Z,8Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (8S,9R)-epoxy-(5Z,11Z,14Z)-eicosatrienoate + H2O = (8R,9R)-dihydroxy-(5Z,11Z,14Z)-eicosatrienoateThis reaction proceeds in the forward direction.
- (14R,15S)-epoxy-(5Z,8Z,11Z)-eicosatrienoate + H2O = (14R,15R)-dihydroxy-(5Z,8Z,11Z)-eicosatrienoateThis reaction proceeds in the forward direction.
Cofactor
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).
Kinetics
KM | SUBSTRATE | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|---|
21 μM | threo-9,10-phosphonooxy-hydroxy-octadecanoic acid | |||||
1.7 μM | 8,9-EET | |||||
3.4 μM | 11,12-EET | |||||
15 μM | 14,15-EET | |||||
1.5 μM | leukotoxin | |||||
1.1 mM | p-nitrophenyl phosphate | |||||
7.3 μM | 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate | |||||
10.8 μM | 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z) | |||||
3 μM | palmitoyl-lysophosphatidic acid | |||||
6.4 μM | stearoyl-lysophosphatidic acid | |||||
6.2 μM | oleoyl-lysophosphatidic acid | |||||
5.9 μM | arachidonoyl-lysophosphatidic acid | |||||
5.3 μM | arachidoyl-lysophosphatidic acid | |||||
23.5 μM | 1-alkyl lysophosphatidic acid (C18:0) | |||||
14.8 μM | sphingosine-1-phosphate | |||||
20.9 μM | geranylgeranyl pyrophosphate | |||||
10 μM | farnesyl pyro-phosphate | |||||
5.1 μM | 1-myristoyl-2-hydroxy-3-glycerophosphate | |||||
23 μM | 1-palmityl-2-hydroxy-3-glycerophosphate | |||||
4.2 μM | 1-stearyl-2-hydroxy-3-glycerophosphate | |||||
6.9 μM | 1-oleoyl-2-hydroxy-3-glycerophosphate | |||||
13 μM | 1-arachidonoyl-2-hydroxy-3-glycerophosphate | |||||
31 μM | sphingosine-1-phosphate | |||||
67 μM | N-acetyl-ceramide-phosphate |
Vmax | pH | TEMPERATURE[C] | NOTES | EVIDENCE | |
---|---|---|---|---|---|
338 nmol/min/mg | with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid | ||||
0.9 μmol/min/mg | with 8,9-EET as substrate | ||||
4.5 μmol/min/mg | with 11,12-EET as substrate | ||||
7 μmol/min/mg | with 14,15-EET as substrate | ||||
0.55 μmol/min/mg | with leukotoxin as substrate | ||||
5.8 nmol/min/mg | with p-nitrophenyl phosphate | ||||
385 nmol/min/mg | with 8-hydroxy-(11S,12S)-epoxy-(5Z,9E,14Z)-eicosatrienoate as substrate | ||||
95 nmol/min/mg | with 10-hydroxy-(11S,12S)-epoxy- (5Z,8Z,14Z)-eicosatrienoate as substrate | ||||
150.4 nmol/min/mg | with palmitoyl-lysophosphatidic acid as substrate | ||||
193.5 nmol/min/mg | with stearoyl-lysophosphatidic acid as substrate | ||||
191.6 nmol/min/mg | with oleoyl-lysophosphatidic acid as substrate | ||||
157.9 nmol/min/mg | with arachidonoyl-lysophosphatidic acid as substrate | ||||
26.8 nmol/min/mg | with arachidoyl-lysophosphatidic acid as substrate | ||||
171.1 nmol/min/mg | with 1-alkyl lysophosphatidic acid (C18:0) as substrate | ||||
60.6 nmol/min/mg | with sphingosine-1-phosphate as substrate | ||||
101.3 nmol/min/mg | with geranylgeranyl pyrophosphate as substrate |
kcat are 14 sec-1, 354 sec-1, 167 sec-1, 125 sec-1, 177 sec-1, 250 sec-1, 18 sec-1 and 136 sec-1 for farnesyl pyro-phosphate, 1-myristoyl-2-hydroxy-3-glycerophosphate, 1-palmityl-2-hydroxy-3-glycerophosphate, 1-stearyl-2-hydroxy-3-glycerophosphate, 1-oleoyl-2-hydroxy-3-glycerophosphate, 1-arachidonoyl-2-hydroxy-3-glycerophosphate, sphingosine-1-phosphate and N-acetyl-ceramide-phosphate, respectively.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 9 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 11 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 123-124 | phosphate (UniProtKB | ChEBI) | ||||
Sequence: TN | ||||||
Binding site | 185 | Mg2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Active site | 335 | Nucleophile | ||||
Sequence: D | ||||||
Binding site | 383 | substrate | ||||
Sequence: Y | ||||||
Active site | 466 | Proton donor | ||||
Sequence: Y | ||||||
Active site | 524 | Proton acceptor | ||||
Sequence: H |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Cellular Component | extracellular exosome | |
Cellular Component | peroxisomal matrix | |
Cellular Component | peroxisome | |
Molecular Function | 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity | |
Molecular Function | epoxide hydrolase activity | |
Molecular Function | lipid phosphatase activity | |
Molecular Function | lysophosphatidic acid phosphatase activity | |
Molecular Function | magnesium ion binding | |
Molecular Function | phosphatase activity | |
Molecular Function | protein homodimerization activity | |
Molecular Function | toxic substance binding | |
Biological Process | cholesterol homeostasis | |
Biological Process | dephosphorylation | |
Biological Process | epoxide metabolic process | |
Biological Process | phospholipid dephosphorylation | |
Biological Process | positive regulation of gene expression | |
Biological Process | regulation of cholesterol metabolic process | |
Biological Process | response to toxic substance | |
Biological Process | stilbene catabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Protein family/group databases
Chemistry
Names & Taxonomy
Protein names
- Recommended nameBifunctional epoxide hydrolase 2
Including 2 domains:
- Recommended nameCytosolic epoxide hydrolase 2
- EC number
- Short namesCEH
- Alternative names
- Recommended nameLipid-phosphate phosphatase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionP34913
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
Disease & Variants
Features
Showing features for mutagenesis, natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 9 | Loss of phosphatase activity. | ||||
Sequence: D → A | ||||||
Natural variant | VAR_055392 | 21 | in dbSNP:rs72473930 | |||
Sequence: G → A | ||||||
Natural variant | VAR_055393 | 52 | in dbSNP:rs72475803 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_051059 | 55 | decreased phosphatase activity; no effect on epoxyde hydrolase activity; dbSNP:rs41507953 | |||
Sequence: K → R | ||||||
Natural variant | VAR_033991 | 103 | decreased phosphatase activity; no effect on epoxyde hydrolase activity; dbSNP:rs17057255 | |||
Sequence: R → C | ||||||
Natural variant | VAR_055394 | 154 | decreased phosphatase activity; no effect on epoxyde hydrolase activity; dbSNP:rs57699806 | |||
Sequence: C → Y | ||||||
Natural variant | VAR_055395 | 225 | in dbSNP:rs72475821 | |||
Sequence: P → L | ||||||
Natural variant | VAR_014852 | 287 | no effect on phosphatase activity; decreased epoxyde hydrolase activity; dbSNP:rs751141 | |||
Sequence: R → Q | ||||||
Natural variant | VAR_055396 | 369 | in dbSNP:rs72475894 | |||
Sequence: M → V | ||||||
Natural variant | VAR_022613 | 403 | ||||
Sequence: R → RR | ||||||
Natural variant | VAR_055397 | 470 | no effect on phosphatase activity and epoxyde hydrolase activity; dbSNP:rs68053459 | |||
Sequence: E → G | ||||||
Mutagenesis | 522 | Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. | ||||
Sequence: C → S |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 667 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, lipidation.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000084111 | 1-555 | Bifunctional epoxide hydrolase 2 | |||
Sequence: MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM | ||||||
Modified residue | 43 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 55 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 191 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 215 | N6-acetyllysine | ||||
Sequence: K | ||||||
Modified residue | 370 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 421 | N6-succinyllysine | ||||
Sequence: K | ||||||
Modified residue | 455 | N6-succinyllysine | ||||
Sequence: K | ||||||
Lipidation | 522 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine | ||||
Sequence: C | ||||||
Modified residue | 554 | N6-succinyllysine | ||||
Sequence: K |
Post-translational modification
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).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Induction
By compounds that cause peroxisome proliferation such as clofibrate, tiadenol and fenofibrate.
Gene expression databases
Organism-specific databases
Structure
Family & Domains
Features
Showing features for region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-224 | Phosphatase | ||||
Sequence: MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITLSQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTAILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEVVFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNT | ||||||
Region | 235-555 | Epoxide hydrolase | ||||
Sequence: SDMSHGYVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIKWLDSDARNPPVVSKM | ||||||
Domain | 259-531 | AB hydrolase-1 | ||||
Sequence: PAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNTPFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMHKVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSLGRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKP | ||||||
Motif | 553-555 | Microbody targeting signal | ||||
Sequence: SKM |
Domain
The N-terminal domain has phosphatase activity. The C-terminal domain has epoxide hydrolase activity.
Sequence similarities
Belongs to the AB hydrolase superfamily. Epoxide hydrolase family.
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
P34913-1
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.
- Name1
- Length555
- Mass (Da)62,616
- Last updated2005-06-07 v2
- Checksum1B5ACE7F80F9A26C
P34913-2
- Name2
- Differences from canonical
- 1-53: Missing
P34913-3
- Name3
- Differences from canonical
- 1-66: Missing
Computationally mapped potential isoform sequences
There are 4 potential isoforms mapped to this entry
Features
Showing features for alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_045598 | 1-53 | in isoform 2 | |||
Sequence: Missing | ||||||
Alternative sequence | VSP_045597 | 1-66 | in isoform 3 | |||
Sequence: Missing | ||||||
Sequence conflict | 5 | in Ref. 1; AAA02756 | ||||
Sequence: A → G | ||||||
Sequence conflict | 257-258 | in Ref. 1; AAA02756 | ||||
Sequence: SG → W | ||||||
Sequence conflict | 409 | in Ref. 5; BAG53362 | ||||
Sequence: F → L | ||||||
Sequence conflict | 473 | in Ref. 5; BAG53362 | ||||
Sequence: W → R | ||||||
Sequence conflict | 494 | in Ref. 5; BAG53362 | ||||
Sequence: E → G |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
L05779 EMBL· GenBank· DDBJ | AAA02756.1 EMBL· GenBank· DDBJ | mRNA | ||
X97024 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97025 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97026 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97027 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97028 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97029 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97030 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97031 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97032 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97033 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97034 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97035 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97036 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97037 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
X97038 EMBL· GenBank· DDBJ | CAA65751.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF233334 EMBL· GenBank· DDBJ | AAG14966.1 EMBL· GenBank· DDBJ | mRNA | ||
AF233335 EMBL· GenBank· DDBJ | AAG14967.1 EMBL· GenBank· DDBJ | mRNA | ||
AF233336 EMBL· GenBank· DDBJ | AAG14968.1 EMBL· GenBank· DDBJ | mRNA | ||
BT006885 EMBL· GenBank· DDBJ | AAP35531.1 EMBL· GenBank· DDBJ | mRNA | ||
AK096089 EMBL· GenBank· DDBJ | BAG53210.1 EMBL· GenBank· DDBJ | mRNA | ||
AK096770 EMBL· GenBank· DDBJ | BAG53362.1 EMBL· GenBank· DDBJ | mRNA | ||
EU584434 EMBL· GenBank· DDBJ | ACD11487.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
AF311103 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471080 EMBL· GenBank· DDBJ | EAW63548.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471080 EMBL· GenBank· DDBJ | EAW63549.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471080 EMBL· GenBank· DDBJ | EAW63551.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC007708 EMBL· GenBank· DDBJ | AAH07708.1 EMBL· GenBank· DDBJ | mRNA | ||
BC011628 EMBL· GenBank· DDBJ | AAH11628.1 EMBL· GenBank· DDBJ | mRNA | ||
BC013874 EMBL· GenBank· DDBJ | AAH13874.1 EMBL· GenBank· DDBJ | mRNA |