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Q9D379

- HYEP_MOUSE

UniProt

Q9D379 - HYEP_MOUSE

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Protein

Epoxide hydrolase 1

Gene
Ephx1
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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
Complete GO annotation...

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

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei2 – 2019Helical; Signal-anchor; Reviewed predictionAdd
BLAST

GO - Cellular componenti

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

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 arginine By 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.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase S33 family.

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti410 – 4101E → K in BAB31132. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 110 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

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