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Q9D379

- HYEP_MOUSE

UniProt

Q9D379 - HYEP_MOUSE

Protein

Epoxide hydrolase 1

Gene

Ephx1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 111 (01 Oct 2014)
      Sequence version 2 (27 Jul 2011)
      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

    GO - Biological processi

    1. aromatic compound catabolic process Source: UniProtKB-KW
    2. cellular aromatic compound metabolic process Source: MGI
    3. response to organic cyclic compound Source: MGI
    4. response to toxic substance Source: UniProtKB-KW

    Keywords - Molecular functioni

    Hydrolase

    Keywords - Biological processi

    Aromatic hydrocarbons catabolism, Detoxification

    Enzyme and pathway databases

    SABIO-RKQ9D379.

    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
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 1

    Organism-specific databases

    MGIiMGI:95405. 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

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 455455Epoxide hydrolase 1PRO_0000080856Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei295 – 2951Omega-N-methylated arginineBy similarity
    Modified residuei439 – 4391N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Methylation

    Proteomic databases

    MaxQBiQ9D379.
    PaxDbiQ9D379.
    PRIDEiQ9D379.

    PTM databases

    PhosphoSiteiQ9D379.

    Expressioni

    Gene expression databases

    ArrayExpressiQ9D379.
    BgeeiQ9D379.
    CleanExiMM_EPHX1.
    GenevestigatoriQ9D379.

    Interactioni

    Protein-protein interaction databases

    IntActiQ9D379. 6 interactions.
    MINTiMINT-1862106.
    STRINGi10090.ENSMUSP00000047551.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9D379.
    SMRiQ9D379. Positions 113-248.
    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.
    GeneTreeiENSGT00390000002210.
    HOGENOMiHOG000132894.
    HOVERGENiHBG002366.
    InParanoidiP97869.
    KOiK01253.
    OMAiAERTYAN.
    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.

    Q9D379-1 [UniParc]FASTAAdd to Basket

    « Hide

    MWLELILASV LGFVIYWFVS RDKEETLPLE DGWWGPGSKP SAKEDESIRP    50
    FKVETSDEEI KDLHQRIDRF RASPPLEGSR FHYGFNSSYL KKVVSFWRNE 100
    FDWRKQVEIL NQYPHFKTKI EGLDIHFIHV KPPQLPSGRT PKPLLMVHGW 150
    PGSFYEFYKI IPLLTDPKTH GLSDEHVFEV ICPSIPGYGF SEASSKKGLN 200
    SVATARIFYK LMSRLGFQKF YIQGGDWGSL ICTNIAQMVP NHVKGLHLNM 250
    SFISRNIYSL TPLLGQRFGR FLGYTEKDLE LLYPFKEKVF YNIMRESGYL 300
    HIQATKPDTV GCALNDSPVG LAAYILEKFS TWTKSEYREL EDGGLERKFS 350
    LEDLLTNIMI YWTTGTIVSS QRFYKENLGQ GVMVHRHEGM KVFVPTGYSA 400
    FPSEILHAPE KWVKVKYPKL ISYSYMERGG HFAAFEEPKL LAQDIRKFVS 450
    LAELQ 455
    Length:455
    Mass (Da):52,577
    Last modified:July 27, 2011 - v2
    Checksum:i1567F619D9114C58
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti410 – 4101E → K in BAB31132. (PubMed:16141072)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89491 mRNA. Translation: AAB49762.1.
    AK018249 mRNA. Translation: BAB31132.1.
    CH466555 Genomic DNA. Translation: EDL13136.1.
    BC045194 mRNA. Translation: AAH45194.1.
    BC061493 mRNA. Translation: AAH61493.1.
    CCDSiCCDS15579.1.
    RefSeqiNP_034275.1. NM_010145.2.
    UniGeneiMm.9075.

    Genome annotation databases

    EnsembliENSMUST00000036928; ENSMUSP00000047551; ENSMUSG00000038776.
    GeneIDi13849.
    KEGGimmu:13849.
    UCSCiuc007dwz.1. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U89491 mRNA. Translation: AAB49762.1 .
    AK018249 mRNA. Translation: BAB31132.1 .
    CH466555 Genomic DNA. Translation: EDL13136.1 .
    BC045194 mRNA. Translation: AAH45194.1 .
    BC061493 mRNA. Translation: AAH61493.1 .
    CCDSi CCDS15579.1.
    RefSeqi NP_034275.1. NM_010145.2.
    UniGenei Mm.9075.

    3D structure databases

    ProteinModelPortali Q9D379.
    SMRi Q9D379. Positions 113-248.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9D379. 6 interactions.
    MINTi MINT-1862106.
    STRINGi 10090.ENSMUSP00000047551.

    Chemistry

    ChEMBLi CHEMBL1075293.

    Protein family/group databases

    MEROPSi S33.971.

    PTM databases

    PhosphoSitei Q9D379.

    Proteomic databases

    MaxQBi Q9D379.
    PaxDbi Q9D379.
    PRIDEi Q9D379.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000036928 ; ENSMUSP00000047551 ; ENSMUSG00000038776 .
    GeneIDi 13849.
    KEGGi mmu:13849.
    UCSCi uc007dwz.1. mouse.

    Organism-specific databases

    CTDi 2052.
    MGIi MGI:95405. Ephx1.

    Phylogenomic databases

    eggNOGi COG0596.
    GeneTreei ENSGT00390000002210.
    HOGENOMi HOG000132894.
    HOVERGENi HBG002366.
    InParanoidi P97869.
    KOi K01253.
    OMAi AERTYAN.
    TreeFami TF313813.

    Enzyme and pathway databases

    SABIO-RK Q9D379.

    Miscellaneous databases

    ChiTaRSi EPHX1. mouse.
    NextBioi 284700.
    PROi Q9D379.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9D379.
    Bgeei Q9D379.
    CleanExi MM_EPHX1.
    Genevestigatori Q9D379.

    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. "The Ephx1(d) allele encoding an Arg338Cys substitution is associated with heat lability."
      Hartsfield J.K. Jr., Everett E.T.
      Mamm. Genome 11:915-918(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: C57BL/6J.
      Tissue: Liver.
    2. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: C57BL/6J.
      Tissue: Medulla oblongata.
    3. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
      Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
      Strain: FVB/N.
      Tissue: Colon and Mammary tumor.
    5. Lubec G., Kang S.U.
      Submitted (APR-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 339-347, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: C57BL/6.
      Tissue: Brain.
    6. "Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
      Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
      Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-439, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.

    Entry informationi

    Entry nameiHYEP_MOUSE
    AccessioniPrimary (citable) accession number: Q9D379
    Secondary accession number(s): P97869
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 15, 2002
    Last sequence update: July 27, 2011
    Last modified: October 1, 2014
    This is version 111 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. Peptidase families
      Classification of peptidase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3