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P07099

- HYEP_HUMAN

UniProt

P07099 - HYEP_HUMAN

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Protein

Epoxide hydrolase 1

Gene

EPHX1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 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
  2. epoxide hydrolase activity Source: ProtInc

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-KW
  2. 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-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 Source: UniProtKB-KW
  2. integral component of membrane Source: UniProtKB-KW
Complete GO annotation...

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

PaxDbiP07099.
PeptideAtlasiP07099.
PRIDEiP07099.

PTM databases

PhosphoSiteiP07099.

Expressioni

Tissue specificityi

Found in liver.1 Publication

Gene expression databases

BgeeiP07099.
ExpressionAtlasiP07099. baseline and differential.
GenevestigatoriP07099.

Organism-specific databases

HPAiHPA020593.

Interactioni

Protein-protein interaction databases

BioGridi108366. 18 interactions.
IntActiP07099. 2 interactions.

Structurei

3D structure databases

ProteinModelPortaliP07099.
SMRiP07099. Positions 46-454.
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

        10         20         30         40         50
MWLEILLTSV LGFAIYWFIS RDKEETLPLE DGWWGPGTRS AAREDDSIRP
60 70 80 90 100
FKVETSDEEI HDLHQRIDKF RFTPPLEDSC FHYGFNSNYL KKVISYWRNE
110 120 130 140 150
FDWKKQVEIL NRYPHFKTKI EGLDIHFIHV KPPQLPAGHT PKPLLMVHGW
160 170 180 190 200
PGSFYEFYKI IPLLTDPKNH GLSDEHVFEV ICPSIPGYGF SEASSKKGFN
210 220 230 240 250
SVATARIFYK LMLRLGFQEF YIQGGDWGSL ICTNMAQLVP SHVKGLHLNM
260 270 280 290 300
ALVLSNFSTL TLLLGQRFGR FLGLTERDVE LLYPVKEKVF YSLMRESGYM
310 320 330 340 350
HIQCTKPDTV GSALNDSPVG LAAYILEKFS TWTNTEFRYL EDGGLERKFS
360 370 380 390 400
LDDLLTNVML YWTTGTIISS QRFYKENLGQ GWMTQKHERM KVYVPTGFSA
410 420 430 440 450
FPFELLHTPE KWVRFKYPKL ISYSYMVRGG HFAAFEEPEL LAQDIRKFLS

VLERQ
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.
ENST00000614058; ENSP00000480004; 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 46-454.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 108366. 18 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

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 .
ENST00000614058 ; ENSP00000480004 ; 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

Bgeei P07099.
ExpressionAtlasi P07099. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 155 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