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P07099

- HYEP_HUMAN

UniProt

P07099 - HYEP_HUMAN

Protein

Epoxide hydrolase 1

Gene

EPHX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 154 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water.

    Catalytic activityi

    Cis-stilbene oxide + H2O = (+)-(1R,2R)-1,2-diphenylethane-1,2-diol.

    GO - Molecular functioni

    1. cis-stilbene-oxide hydrolase activity Source: UniProtKB-EC
    2. epoxide hydrolase activity Source: ProtInc

    GO - Biological processi

    1. aromatic compound catabolic process Source: UniProtKB-KW
    2. response to organic cyclic compound Source: Ensembl
    3. response to toxic substance Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism, Detoxification

    Enzyme and pathway databases

    SABIO-RKP07099.

    Protein family/group databases

    MEROPSiS33.971.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Epoxide hydrolase 1 (EC:3.3.2.9)
    Alternative name(s):
    Epoxide hydratase
    Microsomal epoxide hydrolase
    Gene namesi
    Name:EPHX1
    Synonyms:EPHX, EPOX
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:3401. EPHX1.

    Subcellular locationi

    GO - Cellular componenti

    1. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    2. integral component of membrane Source: UniProtKB-KW

    Keywords - Cellular componenti

    Endoplasmic reticulum, Membrane, Microsome

    Pathology & Biotechi

    Involvement in diseasei

    In some populations, the high activity haplotype tyr113/his139 is overrepresented among women suffering from pregnancy-induced hypertension (pre-eclampsia) when compared with healthy controls.1 Publication
    Familial hypercholanemia (FHCA) [MIM:607748]: A disorder characterized by elevated serum bile acid concentrations, itching, and fat malabsorption.
    Note: The disease is caused by mutations affecting the gene represented in this entry.

    Organism-specific databases

    MIMi132810. gene+phenotype.
    607748. phenotype.
    Orphaneti238475. Familial hypercholanemia.
    1912. Fetal hydantoin syndrome.
    PharmGKBiPA27829.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 455455Epoxide hydrolase 1PRO_0000080855Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei295 – 2951Omega-N-methylated arginineBy similarity

    Keywords - PTMi

    Methylation

    Proteomic databases

    MaxQBiP07099.
    PaxDbiP07099.
    PeptideAtlasiP07099.
    PRIDEiP07099.

    PTM databases

    PhosphoSiteiP07099.

    Expressioni

    Tissue specificityi

    Found in liver.1 Publication

    Gene expression databases

    ArrayExpressiP07099.
    BgeeiP07099.
    GenevestigatoriP07099.

    Organism-specific databases

    HPAiHPA020593.

    Interactioni

    Protein-protein interaction databases

    BioGridi108366. 8 interactions.
    IntActiP07099. 2 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP07099.
    SMRiP07099. Positions 47-454.
    ModBaseiSearch...
    MobiDBiSearch...

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei2 – 2019Helical; Signal-anchorSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase S33 family.Curated

    Keywords - Domaini

    Signal-anchor, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG0596.
    HOVERGENiHBG002366.
    InParanoidiP07099.
    KOiK01253.
    OMAiHLNMALV.
    PhylomeDBiP07099.
    TreeFamiTF313813.

    Family and domain databases

    Gene3Di3.40.50.1820. 1 hit.
    InterProiIPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR010497. Epoxide_hydro_N.
    IPR016292. Epoxide_hydrolase.
    [Graphical view]
    PfamiPF00561. Abhydrolase_1. 1 hit.
    PF06441. EHN. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001112. Epoxide_hydrolase. 1 hit.
    PRINTSiPR00412. EPOXHYDRLASE.
    SUPFAMiSSF53474. SSF53474. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P07099-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWLEILLTSV LGFAIYWFIS RDKEETLPLE DGWWGPGTRS AAREDDSIRP    50
    FKVETSDEEI HDLHQRIDKF RFTPPLEDSC FHYGFNSNYL KKVISYWRNE 100
    FDWKKQVEIL NRYPHFKTKI EGLDIHFIHV KPPQLPAGHT PKPLLMVHGW 150
    PGSFYEFYKI IPLLTDPKNH GLSDEHVFEV ICPSIPGYGF SEASSKKGFN 200
    SVATARIFYK LMLRLGFQEF YIQGGDWGSL ICTNMAQLVP SHVKGLHLNM 250
    ALVLSNFSTL TLLLGQRFGR FLGLTERDVE LLYPVKEKVF YSLMRESGYM 300
    HIQCTKPDTV GSALNDSPVG LAAYILEKFS TWTNTEFRYL EDGGLERKFS 350
    LDDLLTNVML YWTTGTIISS QRFYKENLGQ GWMTQKHERM KVYVPTGFSA 400
    FPFELLHTPE KWVRFKYPKL ISYSYMVRGG HFAAFEEPEL LAQDIRKFLS 450
    VLERQ 455
    Length:455
    Mass (Da):52,949
    Last modified:November 1, 1988 - v1
    Checksum:i88E333838C841390
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti15 – 151I → V in BAG36227. (PubMed:14702039)Curated
    Sequence conflicti112 – 1121R → K1 PublicationCurated
    Sequence conflicti148 – 1481H → N(PubMed:3502697)Curated
    Sequence conflicti148 – 1481H → N1 PublicationCurated
    Sequence conflicti243 – 2431V → L1 PublicationCurated
    Sequence conflicti348 – 3481K → S in CAA68486. (PubMed:3502697)Curated
    Sequence conflicti406 – 4061L → F in CAA68486. (PubMed:3502697)Curated
    Sequence conflicti420 – 4201L → V in CAA68486. (PubMed:3502697)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431R → T.1 Publication
    Corresponds to variant rs3738046 [ dbSNP | Ensembl ].
    VAR_023303
    Natural varianti44 – 441E → Q.1 Publication
    VAR_018347
    Natural varianti49 – 491R → C in allele EPHX1*2. 1 Publication
    Corresponds to variant rs2234697 [ dbSNP | Ensembl ].
    VAR_013298
    Natural varianti113 – 1131Y → H in allele EPHX1*3; 55% of wild type enzyme activity. 4 Publications
    Corresponds to variant rs1051740 [ dbSNP | Ensembl ].
    VAR_005295
    Natural varianti139 – 1391H → R in allele EPHX1*4; 62% of wild type enzyme activity. 4 Publications
    Corresponds to variant rs2234922 [ dbSNP | Ensembl ].
    VAR_005296
    Natural varianti260 – 2601L → P in allele EPHX1*1G. 1 Publication
    VAR_013299
    Natural varianti275 – 2751T → A.
    Corresponds to variant rs35073925 [ dbSNP | Ensembl ].
    VAR_051828
    Natural varianti285 – 2851V → L.1 Publication
    Corresponds to variant rs45449793 [ dbSNP | Ensembl ].
    VAR_023304
    Natural varianti396 – 3961T → I Either a rare polymorphism or a sequencing error. 1 Publication
    VAR_005297
    Natural varianti408 – 4081T → M.1 Publication
    Corresponds to variant rs45495897 [ dbSNP | Ensembl ].
    VAR_023305
    Natural varianti452 – 4521L → Q.1 Publication
    Corresponds to variant rs45563137 [ dbSNP | Ensembl ].
    VAR_023306
    Natural varianti454 – 4541R → Q in allele EPHX1*5. 1 Publication
    Corresponds to variant rs2234701 [ dbSNP | Ensembl ].
    VAR_013300

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03518 mRNA. Translation: AAA61305.1.
    X07936 mRNA. Translation: CAA30759.1.
    Y00424 mRNA. Translation: CAA68486.1.
    L25878 mRNA. Translation: AAA52389.1.
    L25879 mRNA. Translation: AAA52390.1.
    U06661
    , U06656, U06657, U06658, U06659, U06660 Genomic DNA. Translation: AAB60649.1.
    AK313436 mRNA. Translation: BAG36227.1.
    AY948961 Genomic DNA. Translation: AAX81410.1.
    AL591895 Genomic DNA. Translation: CAH71994.1.
    BC003567 mRNA. Translation: AAH03567.1.
    BC008291 mRNA. Translation: AAH08291.1.
    BC095430 mRNA. Translation: AAH95430.1.
    M36374 mRNA. Translation: AAA59580.1.
    AF253417 Genomic DNA. Translation: AAC41694.1.
    AF276626 Genomic DNA. Translation: AAF87726.1.
    AF276627 Genomic DNA. Translation: AAF87727.1.
    AF276628 Genomic DNA. Translation: AAF87728.1.
    AF276629 Genomic DNA. Translation: AAF87729.1.
    AF276630 Genomic DNA. Translation: AAF87730.1.
    AF276631 Genomic DNA. Translation: AAF87731.1.
    AF276632 Genomic DNA. Translation: AAF87732.1.
    AF276633 Genomic DNA. Translation: AAF87733.1.
    AF276634 Genomic DNA. Translation: AAF87734.1.
    AF276635 Genomic DNA. Translation: AAF87735.1.
    AF276636 Genomic DNA. Translation: AAF87736.1.
    AF276637 Genomic DNA. Translation: AAF87737.1.
    AF276638 Genomic DNA. Translation: AAF87738.1.
    CCDSiCCDS1547.1.
    PIRiA29939.
    RefSeqiNP_000111.1. NM_000120.3.
    NP_001129490.1. NM_001136018.3.
    NP_001278092.1. NM_001291163.1.
    UniGeneiHs.89649.

    Genome annotation databases

    EnsembliENST00000272167; ENSP00000272167; ENSG00000143819.
    ENST00000366837; ENSP00000355802; ENSG00000143819.
    GeneIDi2052.
    KEGGihsa:2052.
    UCSCiuc001hpk.3. human.

    Polymorphism databases

    DMDMi123926.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    NIEHS-SNPs

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    J03518 mRNA. Translation: AAA61305.1 .
    X07936 mRNA. Translation: CAA30759.1 .
    Y00424 mRNA. Translation: CAA68486.1 .
    L25878 mRNA. Translation: AAA52389.1 .
    L25879 mRNA. Translation: AAA52390.1 .
    U06661
    , U06656 , U06657 , U06658 , U06659 , U06660 Genomic DNA. Translation: AAB60649.1 .
    AK313436 mRNA. Translation: BAG36227.1 .
    AY948961 Genomic DNA. Translation: AAX81410.1 .
    AL591895 Genomic DNA. Translation: CAH71994.1 .
    BC003567 mRNA. Translation: AAH03567.1 .
    BC008291 mRNA. Translation: AAH08291.1 .
    BC095430 mRNA. Translation: AAH95430.1 .
    M36374 mRNA. Translation: AAA59580.1 .
    AF253417 Genomic DNA. Translation: AAC41694.1 .
    AF276626 Genomic DNA. Translation: AAF87726.1 .
    AF276627 Genomic DNA. Translation: AAF87727.1 .
    AF276628 Genomic DNA. Translation: AAF87728.1 .
    AF276629 Genomic DNA. Translation: AAF87729.1 .
    AF276630 Genomic DNA. Translation: AAF87730.1 .
    AF276631 Genomic DNA. Translation: AAF87731.1 .
    AF276632 Genomic DNA. Translation: AAF87732.1 .
    AF276633 Genomic DNA. Translation: AAF87733.1 .
    AF276634 Genomic DNA. Translation: AAF87734.1 .
    AF276635 Genomic DNA. Translation: AAF87735.1 .
    AF276636 Genomic DNA. Translation: AAF87736.1 .
    AF276637 Genomic DNA. Translation: AAF87737.1 .
    AF276638 Genomic DNA. Translation: AAF87738.1 .
    CCDSi CCDS1547.1.
    PIRi A29939.
    RefSeqi NP_000111.1. NM_000120.3.
    NP_001129490.1. NM_001136018.3.
    NP_001278092.1. NM_001291163.1.
    UniGenei Hs.89649.

    3D structure databases

    ProteinModelPortali P07099.
    SMRi P07099. Positions 47-454.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108366. 8 interactions.
    IntActi P07099. 2 interactions.

    Chemistry

    BindingDBi P07099.
    ChEMBLi CHEMBL1968.

    Protein family/group databases

    MEROPSi S33.971.

    PTM databases

    PhosphoSitei P07099.

    Polymorphism databases

    DMDMi 123926.

    Proteomic databases

    MaxQBi P07099.
    PaxDbi P07099.
    PeptideAtlasi P07099.
    PRIDEi P07099.

    Protocols and materials databases

    DNASUi 2052.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000272167 ; ENSP00000272167 ; ENSG00000143819 .
    ENST00000366837 ; ENSP00000355802 ; ENSG00000143819 .
    GeneIDi 2052.
    KEGGi hsa:2052.
    UCSCi uc001hpk.3. human.

    Organism-specific databases

    CTDi 2052.
    GeneCardsi GC01P225997.
    HGNCi HGNC:3401. EPHX1.
    HPAi HPA020593.
    MIMi 132810. gene+phenotype.
    607748. phenotype.
    neXtProti NX_P07099.
    Orphaneti 238475. Familial hypercholanemia.
    1912. Fetal hydantoin syndrome.
    PharmGKBi PA27829.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0596.
    HOVERGENi HBG002366.
    InParanoidi P07099.
    KOi K01253.
    OMAi HLNMALV.
    PhylomeDBi P07099.
    TreeFami TF313813.

    Enzyme and pathway databases

    SABIO-RK P07099.

    Miscellaneous databases

    ChiTaRSi EPHX1. human.
    GeneWikii EPHX1.
    GenomeRNAii 2052.
    NextBioi 8343.
    PROi P07099.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P07099.
    Bgeei P07099.
    Genevestigatori P07099.

    Family and domain databases

    Gene3Di 3.40.50.1820. 1 hit.
    InterProi IPR029058. AB_hydrolase.
    IPR000073. AB_hydrolase_1.
    IPR000639. Epox_hydrolase-like.
    IPR010497. Epoxide_hydro_N.
    IPR016292. Epoxide_hydrolase.
    [Graphical view ]
    Pfami PF00561. Abhydrolase_1. 1 hit.
    PF06441. EHN. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001112. Epoxide_hydrolase. 1 hit.
    PRINTSi PR00412. EPOXHYDRLASE.
    SUPFAMi SSF53474. SSF53474. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Human microsomal xenobiotic epoxide hydrolase. Complementary DNA sequence, complementary DNA-directed expression in COS-1 cells, and chromosomal localization."
      Skoda R.C., Demierre A., McBride O.W., Gonzalez F.J., Meyer U.A.
      J. Biol. Chem. 263:1549-1554(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-19.
    2. "Nucleotide sequence of a human microsomal epoxide hydrolase cDNA clone."
      Wilson N.M., Omiecinski C.J.
      Submitted (JUL-1988) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Fetal liver.
    3. "Nucleotide and deduced amino acid sequence of human liver microsomal epoxide hydrolase."
      Jackson M.R., Craft J.A., Burchell B.
      Nucleic Acids Res. 15:7188-7188(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Liver.
    4. "Human microsomal epoxide hydrolase: genetic polymorphism and functional expression in vitro of amino acid variants."
      Hassett C., Aicher L., Sidhu J.S., Omiecinski C.J.
      Hum. Mol. Genet. 3:421-428(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], VARIANTS HIS-113; ARG-139 AND ILE-396.
      Tissue: Liver.
    5. Erratum
      Hassett C., Aicher L., Sidhu J.S., Omiecinski C.J.
      Hum. Mol. Genet. 3:1214-1214(1994)
    6. "The human microsomal epoxide hydrolase gene (EPHX1): complete nucleotide sequence and structural characterization."
      Hassett C., Robinson K.B., Beck N.B., Omiecinski C.J.
      Genomics 23:433-442(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    7. "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].
      Tissue: Brain cortex.
    8. NIEHS SNPs program
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-43; HIS-113; ARG-139; LEU-285; MET-408 AND GLN-452.
    9. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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].
      Tissue: Skin, Testis and Uterus.
    11. "Partial nucleotide sequence of a cloned cDNA for human liver microsomal epoxide hydrolase."
      Craft J.A., Jackson M.R., Burchell B.
      Biochem. Soc. Trans. 15:708-709(1987)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 9-327.
      Tissue: Liver.
    12. "Identification of 6 new polymorphisms, g.11177G>A, g.14622C>T (R49C), g.17540T>C, g.17639T>C, g.30929T>C, g.31074G>A (R454Q), in the human microsomal epoxide hydrolase gene (EPHX1) in a French population."
      Belmahdi F., Chevalier D., Lo-Guidice J.-M., Allorge D., Cauffiez C., Lafitte J.-J., Broly F.
      Hum. Mutat. 16:450-450(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-197; 242-310 AND 348-455, VARIANTS CYS-49; HIS-113; ARG-139; PRO-260 AND GLN-454.
    13. "Inhibition of human m-epoxide hydrolase gene expression in a case of hypercholanemia."
      Zhu Q.S., Xing W., Qian B., von Dippe P., Shneider B.L., Fox V.L., Levy D.
      Biochim. Biophys. Acta 1638:208-216(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: INVOLVEMENT IN HYPERCHOLANEMIA, TISSUE SPECIFICITY.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Two exonic single nucleotide polymorphisms in the microsomal epoxide hydrolase gene are jointly associated with preeclampsia."
      Laasanen J., Romppanen E.-L., Hiltunen M., Helisalmi S., Mannermaa A., Punnonen K., Heinonen S.
      Eur. J. Hum. Genet. 10:569-573(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS HIS-113 AND ARG-139, DISEASE.
    16. Cited for: VARIANT GLN-44.
    17. "Functional analysis of human microsomal epoxide hydrolase genetic variants."
      Hosagrahara V.P., Rettie A.E., Hassett C., Omiecinski C.J.
      Chem. Biol. Interact. 150:149-159(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION OF VARIANTS HIS-113 AND ARG-139.

    Entry informationi

    Entry nameiHYEP_HUMAN
    AccessioniPrimary (citable) accession number: P07099
    Secondary accession number(s): B2R8N0
    , Q5VTJ6, Q9NP75, Q9NPE7, Q9NQU6, Q9NQU7, Q9NQU8, Q9NQU9, Q9NQV0, Q9NQV1, Q9NQV2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 154 of the entry and version 1 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. Peptidase families
      Classification of peptidase families and list of entries
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3