UniProtKB - P34913 (HYES_HUMAN)
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- BLAST>sp|P34913|HYES_HUMAN Bifunctional epoxide hydrolase 2 OS=Homo sapiens OX=9606 GN=EPHX2 PE=1 SV=2 MTLRAAVFDLDGVLALPAVFGVLGRTEEALALPRGLLNDAFQKGGPEGATTRLMKGEITL SQWIPLMEENCRKCSETAKVCLPKNFSIKEIFDKAISARKINRPMLQAALMLRKKGFTTA ILTNTWLDDRAERDGLAQLMCELKMHFDFLIESCQVGMVKPEPQIYKFLLDTLKASPSEV VFLDDIGANLKPARDLGMVTILVQDTDTALKELEKVTGIQLLNTPAPLPTSCNPSDMSHG YVTVKPRVRLHFVELGSGPAVCLCHGFPESWYSWRYQIPALAQAGYRVLAMDMKGYGESS APPEIEEYCMEVLCKEMVTFLDKLGLSQAVFIGHDWGGMLVWYMALFYPERVRAVASLNT PFIPANPNMSPLESIKANPVFDYQLYFQEPGVAEAELEQNLSRTFKSLFRASDESVLSMH KVCEAGGLFVNSPEEPSLSRMVTEEEIQFYVQQFKKSGFRGPLNWYRNMERNWKWACKSL GRKILIPALMVTAEKDFVLVPQMSQHMEDWIPHLKRGHIEDCGHWTQMDKPTEVNQILIK WLDSDARNPPVVSKM
- Align
Bifunctional epoxide hydrolase 2
EPHX2
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
<p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi
4 Publications<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Polymorphisms in human soluble epoxide hydrolase."
Przybyla-Zawislak B.D., Srivastava P.K., Vazquez-Matias J., Mohrenweiser H.W., Maxwell J.E., Hammock B.D., Bradbury J.A., Enayetallah A.E., Zeldin D.C., Grant D.F.
Mol. Pharmacol. 64:482-490(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470. - Ref.11"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. the chemical reaction it catalyzes. This information usually correlates with the presence of an EC (Enzyme Commission) number in the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.10"Polymorphisms in human soluble epoxide hydrolase."
Przybyla-Zawislak B.D., Srivastava P.K., Vazquez-Matias J., Mohrenweiser H.W., Maxwell J.E., Hammock B.D., Bradbury J.A., Enayetallah A.E., Zeldin D.C., Grant D.F.
Mol. Pharmacol. 64:482-490(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure."
Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.
Arch. Biochem. Biophys. 427:164-169(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.19"Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis."
Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.
Biochemistry 43:4716-4723(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE; MAGNESIUM AND EPOXIDE HYDROLASE INHIBITOR, ACTIVE SITE. - Ref.20"Human soluble epoxide hydrolase: structural basis of inhibition by 4-(3-cyclohexylureido)-carboxylic acids."
Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.
Protein Sci. 15:58-64(2006) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) IN COMPLEXES WITH DIALKYLUREA INHIBITORS AND MAGNESIUM, ACTIVE SITE.
<p>This subsection of the ‘Function’ section describes an enzyme regulatory mechanism and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/enzyme_regulation' target='_top'>More...</a></p>Enzyme regulationi
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi
- KM=21 µM for threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure."
Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.
Arch. Biochem. Biophys. 427:164-169(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
- KM=1.7 µM for 8,9-EET1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=3.4 µM for 11,12-EET1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=15 µM for 14,15-EET1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=1.5 µM for leukotoxin1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- KM=1.1 mM for p-nitrophenyl phosphate3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure."
Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.
Arch. Biochem. Biophys. 427:164-169(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
- Vmax=338 nmol/min/mg enzyme with threo-9,10-phosphonooxy-hydroxy-octadecanoic acid3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure."
Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.
Arch. Biochem. Biophys. 427:164-169(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
- Vmax=0.9 µmol/min/mg enzyme with 8,9-EET as substrate1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=4.5 µmol/min/mg enzyme with 11,12-EET as substrate1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=7 µmol/min/mg enzyme with 14,15-EET as substrate1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=0.55 µmol/min/mg enzyme with leukotoxin as substrate1 Publication
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.17"EH3 (ABHD9): the first member of a new epoxide hydrolase family with high activity for fatty acid epoxides."
Decker M., Adamska M., Cronin A., Di Giallonardo F., Burgener J., Marowsky A., Falck J.R., Morisseau C., Hammock B.D., Gruzdev A., Zeldin D.C., Arand M.
J. Lipid Res. 53:2038-2045(2012) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
- Vmax=5.8 nmol/min/mg enzyme with p-nitrophenyl phosphate3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.11"The N-terminal domain of mammalian soluble epoxide hydrolase is a phosphatase."
Cronin A., Mowbray S., Durk H., Homburg S., Fleming I., Fisslthaler B., Oesch F., Arand M.
Proc. Natl. Acad. Sci. U.S.A. 100:1552-1557(2003) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, FUNCTION AS PHOSPHATASE, MUTAGENESIS OF ASP-9. - Ref.12"The soluble epoxide hydrolase encoded by EPXH2 is a bifunctional enzyme with novel lipid phosphate phosphatase activity."
Newman J.W., Morisseau C., Harris T.R., Hammock B.D.
Proc. Natl. Acad. Sci. U.S.A. 100:1558-1563(2003) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, CATALYTIC ACTIVITY, FUNCTION AS LIPID PHOSPHATASE, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES. - Ref.13"Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure."
Srivastava P.K., Sharma V.K., Kalonia D.S., Grant D.F.
Arch. Biochem. Biophys. 427:164-169(2004) [PubMed] [Europe PMC] [Abstract]Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 9 | Magnesium1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 11 | Magnesium1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 185 | Magnesium1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 335 | Nucleophile5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei | 383 | Substrate5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 466 | Proton donor5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Function’ section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 524 | Proton acceptor5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 10-hydroxy-9-(phosphonooxy)octadecanoate phosphatase activity Source: UniProtKB-EC
- epoxide hydrolase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- lipid phosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- magnesium ion binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- phosphatase activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- signaling receptor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
- toxic substance binding Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Biological processi
- cellular calcium ion homeostasis Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- cholesterol homeostasis Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- dephosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- drug metabolic process Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- epoxide metabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- epoxygenase P450 pathway Source: Reactome
- inflammatory response Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- long-chain fatty acid biosynthetic process Source: Reactome
- phospholipid dephosphorylation Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- positive regulation of blood vessel diameter Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- positive regulation of gene expression Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- protein targeting to peroxisome Source: Reactome
- reactive oxygen species metabolic process Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- regulation of blood pressure Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- regulation of cholesterol metabolic process Source: UniProtKB <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypei
- response to toxic substance Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
- stilbene catabolic process Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- xenobiotic metabolic process Source: UniProtKB <p>Non-traceable Author Statement</p> <p>Used for statements in the abstract, introduction or discussion of a paper that cannot be traced back to another publication.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#nas">GO evidence code guide</a></p> Non-traceable author statementi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Hydrolase, Multifunctional enzyme |
| Biological process | Aromatic hydrocarbons catabolism, Detoxification, Lipid metabolism |
| Ligand | Magnesium, Metal-binding |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.3.2.10 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) R-HSA-9018682 Biosynthesis of maresins R-HSA-9033241 Peroxisomal protein import |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P34913 |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-EPHX2 Epoxide_hydrolase |
MEROPS protease database More...MEROPSi | S33.973 |
Chemistry databases
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001105 |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: Bifunctional epoxide hydrolase 2Including the following 2 domains: Cytosolic epoxide hydrolase 2 (EC:3.3.2.104 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
Short name: CEH Alternative name(s): Epoxide hydratase Soluble epoxide hydrolase Short name: SEH Lipid-phosphate phosphatase (EC:3.1.3.762 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:EPHX2 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Homo sapiens (Human) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 9606 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
Organism-specific databases
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000120915.13 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3402 EPHX2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 132811 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P34913 |
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
Peroxisome
Other locations
Cytosol
- cytosol Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
Extracellular region or secreted
- extracellular exosome Source: UniProtKBInferred from high throughput direct assayi
Peroxisome
- peroxisomal matrix Source: Reactome
- peroxisome Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
Cytoplasm, Peroxisome<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 9 | D → A: Loss of phosphatase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 522 | C → S: Loss of S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine-induced inhibition of epoxide hydrolase activity. 1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Organism-specific databases
DisGeNET More...DisGeNETi | 2053 |
MalaCards human disease database More...MalaCardsi | EPHX2 |
Open Targets More...OpenTargetsi | ENSG00000120915 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27830 |
Chemistry databases
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2409 |
Drug and drug target database More...DrugBanki | DB08257 4-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}BUTANOIC ACID DB08258 6-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEXANOIC ACID DB08259 7-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEPTANOIC ACID DB08256 N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE DB02029 N-Cyclohexyl-N'-(4-Iodophenyl)Urea DB04213 N-Cyclohexyl-N'-(Propyl)Phenyl Urea DB03677 N-Cyclohexyl-N'-Decylurea |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2970 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EPHX2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 67476665 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000084111 | 1 – 555 | Bifunctional epoxide hydrolase 2Add BLAST | 555 |
Amino acid modifications
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 43 | N6-acetyllysineCombined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 55 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 191 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 215 | N6-acetyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 370 | PhosphoserineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 421 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 455 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position(s) and the type of covalently attached lipid group(s).<p><a href='/help/lipid' target='_top'>More...</a></p>Lipidationi | 522 | S-(15-deoxy-Delta12,14-prostaglandin J2-9-yl)cysteine1 Publication <p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| <p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei | 554 | N6-succinyllysineBy similarity <p>Manually curated information which has been propagated from a related experimentally characterized protein.</p> <p><a href="/manual/evidences#ECO:0000250">More...</a></p> Manual assertion inferred from sequence similarity toi | 1 |
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
Acetylation, Lipoprotein, PhosphoproteinProteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P34913 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P34913 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P34913 |
PeptideAtlas More...PeptideAtlasi | P34913 |
PRoteomics IDEntifications database More...PRIDEi | P34913 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54953 |
PTM databases
DEPOD human dephosphorylation database More...DEPODi | P34913 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P34913 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P34913 |
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000120915 |
CleanEx database of gene expression profiles More...CleanExi | HS_EPHX2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P34913 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P34913 HS |
Organism-specific databases
Human Protein Atlas More...HPAi | HPA023094 HPA023660 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.19"Structure of human epoxide hydrolase reveals mechanistic inferences on bifunctional catalysis in epoxide and phosphate ester hydrolysis."
Gomez G.A., Morisseau C., Hammock B.D., Christianson D.W.
Biochemistry 43:4716-4723(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE; MAGNESIUM AND EPOXIDE HYDROLASE INHIBITOR, ACTIVE SITE. - Ref.22"Optimization of piperidyl-ureas as inhibitors of soluble epoxide hydrolase."
Eldrup A.B., Soleymanzadeh F., Farrow N.A., Kukulka A., De Lombaert S.
Bioorg. Med. Chem. Lett. 20:571-575(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, ACTIVE SITE. - Ref.23"Substituted pyrazoles as novel sEH antagonist: investigation of key binding interactions within the catalytic domain."
Lo H.Y., Man C.C., Fleck R.W., Farrow N.A., Ingraham R.H., Kukulka A., Proudfoot J.R., Betageri R., Kirrane T., Patel U., Sharma R., Hoermann M.A., Kabcenell A., Lombaert S.D.
Bioorg. Med. Chem. Lett. 20:6379-6383(2010) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH SYNTHETIC INHIBITOR, ACTIVE SITE.
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- protein homodimerization activity Source: UniProtKB <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayi
- signaling receptor binding Source: UniProtKB <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactioni
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108367, 5 interactors |
Protein interaction database and analysis system More...IntActi | P34913, 5 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000430269 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P34913 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 5 – 8 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 12 – 14 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 15 – 17 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 19 – 29 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 36 – 42 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 45 – 47 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 49 – 54 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 57 – 59 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 60 – 72 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 13 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 77 – 79 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 88 – 97 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 103 – 114 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 118 – 123 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 131 – 133 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 140 – 145 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 147 – 152 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 153 – 156 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 160 – 162 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 163 – 173 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 177 – 179 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 180 – 185 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 187 – 195 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 199 – 202 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 206 – 217 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 234 – 236 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 237 – 245 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 248 – 255 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 257 – 264 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 271 – 274 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 275 – 277 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 278 – 283 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 287 – 291 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 305 – 308 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 310 – 324 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 329 – 334 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 336 – 347 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 349 – 351 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 352 – 359 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 367 – 369 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 371 – 376 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 379 – 382 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 383 – 386 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 392 – 398 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 401 – 408 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 412 – 414 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 419 – 421 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 424 – 426 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 428 – 431 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 440 – 442 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 444 – 455 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 12 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 456 – 459 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 460 – 464 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 465 – 468 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 469 – 477 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code ‘T’.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 478 – 481 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 488 – 493 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 497 – 499 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 501 – 504 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 507 – 509 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 515 – 519 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 526 – 529 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| <p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 531 – 545 | Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0000244">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei | 15 |
3D structure databases
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P34913 |
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P34913 |
Database of comparative protein structure models More...ModBasei | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P34913 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
Domains and Repeats
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini | 259 – 531 | AB hydrolase-1Sequence analysisAdd BLAST | 273 |
Region
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 1 – 224 | PhosphataseAdd BLAST | 224 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 123 – 124 | Phosphate binding1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 2 | |
| <p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni | 235 – 555 | Epoxide hydrolaseAdd BLAST | 321 |
Motif
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Family and Domains’ section describes a short (usually not more than 20 amino acids) conserved sequence motif of biological significance.<p><a href='/help/motif' target='_top'>More...</a></p>Motifi | 553 – 555 | Microbody targeting signalSequence analysis | 3 |
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3085 Eukaryota KOG4178 Eukaryota COG1011 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063213 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000028073 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006095 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P34913 |
KEGG Orthology (KO) More...KOi | K08726 |
Identification of Orthologs from Complete Genome Data More...OMAi | GHWTQMD |
Database of Orthologous Groups More...OrthoDBi | EOG091G078G |
Database for complete collections of gene phylogenies More...PhylomeDBi | P34913 |
TreeFam database of animal gene trees More...TreeFami | TF315395 |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.150.240, 1 hit 3.40.50.1000, 2 hits 3.40.50.1820, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058 AB_hydrolase IPR000073 AB_hydrolase_1 IPR000639 Epox_hydrolase-like IPR036412 HAD-like_sf IPR006439 HAD-SF_hydro_IA IPR011945 HAD-SF_ppase_IA/epoxid_hydro_N IPR023214 HAD_sf IPR023198 PGP-like_dom2 |
Pfam protein domain database More...Pfami | View protein in Pfam PF00561 Abhydrolase_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00111 ABHYDROLASE PR00412 EPOXHYDRLASE |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53474 SSF53474, 1 hit SSF56784 SSF56784, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02247 HAD-1A3-hyp, 1 hit TIGR01509 HAD-SF-IA-v3, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3)i
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basketAdded to basket
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.
10 20 30 40 50
MTLRAAVFDL DGVLALPAVF GVLGRTEEAL ALPRGLLNDA FQKGGPEGAT
60 70 80 90 100
TRLMKGEITL SQWIPLMEEN CRKCSETAKV CLPKNFSIKE IFDKAISARK
110 120 130 140 150
INRPMLQAAL MLRKKGFTTA ILTNTWLDDR AERDGLAQLM CELKMHFDFL
160 170 180 190 200
IESCQVGMVK PEPQIYKFLL DTLKASPSEV VFLDDIGANL KPARDLGMVT
210 220 230 240 250
ILVQDTDTAL KELEKVTGIQ LLNTPAPLPT SCNPSDMSHG YVTVKPRVRL
260 270 280 290 300
HFVELGSGPA VCLCHGFPES WYSWRYQIPA LAQAGYRVLA MDMKGYGESS
310 320 330 340 350
APPEIEEYCM EVLCKEMVTF LDKLGLSQAV FIGHDWGGML VWYMALFYPE
360 370 380 390 400
RVRAVASLNT PFIPANPNMS PLESIKANPV FDYQLYFQEP GVAEAELEQN
410 420 430 440 450
LSRTFKSLFR ASDESVLSMH KVCEAGGLFV NSPEEPSLSR MVTEEEIQFY
460 470 480 490 500
VQQFKKSGFR GPLNWYRNME RNWKWACKSL GRKILIPALM VTAEKDFVLV
510 520 530 540 550
PQMSQHMEDW IPHLKRGHIE DCGHWTQMDK PTEVNQILIK WLDSDARNPP
VVSKM
The sequence of this isoform differs from the canonical sequence as follows:
1-53: Missing.
10 20 30 40 50
MKGEITLSQW IPLMEENCRK CSETAKVCLP KNFSIKEIFD KAISARKINR
60 70 80 90 100
PMLQAALMLR KKGFTTAILT NTWLDDRAER DGLAQLMCEL KMHFDFLIES
110 120 130 140 150
CQVGMVKPEP QIYKFLLDTL KASPSEVVFL DDIGANLKPA RDLGMVTILV
160 170 180 190 200
QDTDTALKEL EKVTGIQLLN TPAPLPTSCN PSDMSHGYVT VKPRVRLHFV
210 220 230 240 250
ELGSGPAVCL CHGFPESWYS WRYQIPALAQ AGYRVLAMDM KGYGESSAPP
260 270 280 290 300
EIEEYCMEVL CKEMVTFLDK LGLSQAVFIG HDWGGMLVWY MALFYPERVR
310 320 330 340 350
AVASLNTPFI PANPNMSPLE SIKANPVFDY QLYFQEPGVA EAELEQNLSR
360 370 380 390 400
TFKSLFRASD ESVLSMHKVC EAGGLFVNSP EEPSLSRMVT EEEIQFYVQQ
410 420 430 440 450
FKKSGFRGPL NWYRNMERNW KWACKSLGRK ILIPALMVTA EKDFVLVPQM
460 470 480 490 500
SQHMEDWIPH LKRGHIEDCG HWTQMDKPTE VNQILIKWLD SDARNPPVVS
KM
The sequence of this isoform differs from the canonical sequence as follows:
1-66: Missing.
10 20 30 40 50
MEENCRKCSE TAKVCLPKNF SIKEIFDKAI SARKINRPML QAALMLRKKG
60 70 80 90 100
FTTAILTNTW LDDRAERDGL AQLMCELKMH FDFLIESCQV GMVKPEPQIY
110 120 130 140 150
KFLLDTLKAS PSEVVFLDDI GANLKPARDL GMVTILVQDT DTALKELEKV
160 170 180 190 200
TGIQLLNTPA PLPTSCNPSD MSHGYVTVKP RVRLHFVELG SGPAVCLCHG
210 220 230 240 250
FPESWYSWRY QIPALAQAGY RVLAMDMKGY GESSAPPEIE EYCMEVLCKE
260 270 280 290 300
MVTFLDKLGL SQAVFIGHDW GGMLVWYMAL FYPERVRAVA SLNTPFIPAN
310 320 330 340 350
PNMSPLESIK ANPVFDYQLY FQEPGVAEAE LEQNLSRTFK SLFRASDESV
360 370 380 390 400
LSMHKVCEAG GLFVNSPEEP SLSRMVTEEE IQFYVQQFKK SGFRGPLNWY
410 420 430 440 450
RNMERNWKWA CKSLGRKILI PALMVTAEKD FVLVPQMSQH MEDWIPHLKR
460 470 480
GHIEDCGHWT QMDKPTEVNQ ILIKWLDSDA RNPPVVSKM
Experimental Info
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 5 | A → G in AAA02756 (PubMed:8342951).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 257 – 258 | SG → W in AAA02756 (PubMed:8342951).Curated | 2 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 409 | F → L in BAG53362 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 473 | W → R in BAG53362 (PubMed:14702039).Curated | 1 | |
| <p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti | 494 | E → G in BAG53362 (PubMed:14702039).Curated | 1 |
Natural variant
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_055392 | 21 | G → A1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_055393 | 52 | R → Q1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_051059 | 55 | K → R Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_033991 | 103 | R → C Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_055394 | 154 | C → Y Decreased phosphatase activity; no effect on epoxyde hydrolase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_055395 | 225 | P → L1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_014852 | 287 | R → Q No effect on phosphatase activity; decreased epoxyde hydrolase activity. 5 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_055396 | 369 | M → V1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_022613 | 403 | R → RR2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 | |
| <p>This subsection of the ‘Sequence’ section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_055397 | 470 | E → G No effect on phosphatase activity and epoxyde hydrolase activity. 3 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
| 1 |
Alternative sequence
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L05779 mRNA Translation: AAA02756.1 X97024 , X97025, X97026, X97027, X97028, X97029, X97030, X97031, X97032, X97033, X97034, X97035, X97036, X97037, X97038 Genomic DNA Translation: CAA65751.1 AF233334 mRNA Translation: AAG14966.1 AF233335 mRNA Translation: AAG14967.1 AF233336 mRNA Translation: AAG14968.1 BT006885 mRNA Translation: AAP35531.1 AK096089 mRNA Translation: BAG53210.1 AK096770 mRNA Translation: BAG53362.1 EU584434 Genomic DNA Translation: ACD11487.1 AF311103 Genomic DNA No translation available. CH471080 Genomic DNA Translation: EAW63548.1 CH471080 Genomic DNA Translation: EAW63549.1 CH471080 Genomic DNA Translation: EAW63551.1 BC007708 mRNA Translation: AAH07708.1 BC011628 mRNA Translation: AAH11628.1 BC013874 mRNA Translation: AAH13874.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS59097.1 [P34913-2] CCDS59098.1 [P34913-3] CCDS6060.1 [P34913-1] |
Protein sequence database of the Protein Information Resource More...PIRi | JC4711 |
NCBI Reference Sequences More...RefSeqi | NP_001243411.1, NM_001256482.1 [P34913-2] NP_001243412.1, NM_001256483.1 [P34913-3] NP_001243413.1, NM_001256484.1 [P34913-2] NP_001970.2, NM_001979.5 [P34913-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.212088 |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2] ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1] ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2053 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2053 |
UCSC genome browser More...UCSCi | uc003xfu.5 human [P34913-1] |
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityi
Alternative splicing, Polymorphism<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P34913 | UPI0004437F02 | 561 | |||
| P34913-2 | 502 | ||||
| UPI0005092ACE | 326 | ||||
| P34913-3 | 489 | ||||
| Bifunctional epoxide hydrolase 2 (Fragment) | 158 |
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P34913 | UPI0004437F02 | 561 | |||
| UPI0007329660 | 569 | ||||
| UPI0005F53EAB | 556 | ||||
| EPHX2 isoform 1 | 555 | ||||
| EPHX2 isoform 1 | 555 | ||||
| +40 | |||||
| Protein | Similar proteins | Species | Score | Length | |
|---|---|---|---|---|---|
| P34913 | UPI0004437F02 | 561 | |||
| UPI0007329660 | 569 | ||||
| UPI0005F53EAB | 556 | ||||
| Epoxide hydrolase 2 | 555 | ||||
| Epoxide hydrolase 2 | 555 | ||||
| +128 | |||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
| NIEHS-SNPs |
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | L05779 mRNA Translation: AAA02756.1 X97024 , X97025, X97026, X97027, X97028, X97029, X97030, X97031, X97032, X97033, X97034, X97035, X97036, X97037, X97038 Genomic DNA Translation: CAA65751.1 AF233334 mRNA Translation: AAG14966.1 AF233335 mRNA Translation: AAG14967.1 AF233336 mRNA Translation: AAG14968.1 BT006885 mRNA Translation: AAP35531.1 AK096089 mRNA Translation: BAG53210.1 AK096770 mRNA Translation: BAG53362.1 EU584434 Genomic DNA Translation: ACD11487.1 AF311103 Genomic DNA No translation available. CH471080 Genomic DNA Translation: EAW63548.1 CH471080 Genomic DNA Translation: EAW63549.1 CH471080 Genomic DNA Translation: EAW63551.1 BC007708 mRNA Translation: AAH07708.1 BC011628 mRNA Translation: AAH11628.1 BC013874 mRNA Translation: AAH13874.1 |
The Consensus CDS (CCDS) project More...CCDSi | CCDS59097.1 [P34913-2] CCDS59098.1 [P34913-3] CCDS6060.1 [P34913-1] |
Protein sequence database of the Protein Information Resource More...PIRi | JC4711 |
NCBI Reference Sequences More...RefSeqi | NP_001243411.1, NM_001256482.1 [P34913-2] NP_001243412.1, NM_001256483.1 [P34913-3] NP_001243413.1, NM_001256484.1 [P34913-2] NP_001970.2, NM_001979.5 [P34913-1] |
UniGene gene-oriented nucleotide sequence clusters More...UniGenei | Hs.212088 |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1S8O | X-ray | 2.60 | A | 1-555 | [»] | |
| 1VJ5 | X-ray | 2.35 | A | 1-555 | [»] | |
| 1ZD2 | X-ray | 3.00 | P | 1-555 | [»] | |
| 1ZD3 | X-ray | 2.30 | A | 1-555 | [»] | |
| 1ZD4 | X-ray | 2.70 | A | 1-555 | [»] | |
| 1ZD5 | X-ray | 2.60 | A | 1-555 | [»] | |
| 3ANS | X-ray | 1.98 | A/B | 230-555 | [»] | |
| 3ANT | X-ray | 2.40 | A/B | 230-555 | [»] | |
| 3I1Y | X-ray | 2.47 | A | 1-555 | [»] | |
| 3I28 | X-ray | 1.95 | A | 1-555 | [»] | |
| 3KOO | X-ray | 2.79 | A | 1-555 | [»] | |
| 3OTQ | X-ray | 3.00 | A | 1-555 | [»] | |
| 3PDC | X-ray | 2.60 | A/B | 226-548 | [»] | |
| 3WK4 | X-ray | 2.11 | A | 1-555 | [»] | |
| 3WK5 | X-ray | 2.77 | A | 1-555 | [»] | |
| 3WK6 | X-ray | 2.10 | A | 1-555 | [»] | |
| 3WK7 | X-ray | 2.20 | A | 1-555 | [»] | |
| 3WK8 | X-ray | 2.20 | A | 1-555 | [»] | |
| 3WK9 | X-ray | 2.20 | A | 1-555 | [»] | |
| 3WKA | X-ray | 2.01 | A | 1-555 | [»] | |
| 3WKB | X-ray | 2.20 | A | 1-555 | [»] | |
| 3WKC | X-ray | 2.20 | A | 1-555 | [»] | |
| 3WKD | X-ray | 2.48 | A | 1-555 | [»] | |
| 3WKE | X-ray | 2.75 | A | 1-555 | [»] | |
| 4C4X | X-ray | 2.17 | A/B | 230-555 | [»] | |
| 4C4Y | X-ray | 2.41 | A | 230-555 | [»] | |
| 4C4Z | X-ray | 2.06 | A/B | 230-555 | [»] | |
| 4HAI | X-ray | 2.55 | A | 1-555 | [»] | |
| 4J03 | X-ray | 2.92 | A | 1-555 | [»] | |
| 4JNC | X-ray | 1.96 | A | 238-549 | [»] | |
| 4OCZ | X-ray | 2.94 | A | 1-555 | [»] | |
| 4OD0 | X-ray | 2.92 | A | 1-555 | [»] | |
| 4X6X | X-ray | 1.80 | A/B | 230-555 | [»] | |
| 4X6Y | X-ray | 2.10 | A/B | 230-555 | [»] | |
| 4Y2J | X-ray | 2.15 | A | 1-555 | [»] | |
| 4Y2P | X-ray | 2.05 | A | 1-555 | [»] | |
| 4Y2Q | X-ray | 2.40 | A | 1-555 | [»] | |
| 4Y2R | X-ray | 2.45 | A | 1-555 | [»] | |
| 4Y2S | X-ray | 2.30 | A | 1-555 | [»] | |
| 4Y2T | X-ray | 2.40 | A | 1-555 | [»] | |
| 4Y2U | X-ray | 2.75 | A | 1-555 | [»] | |
| 4Y2V | X-ray | 2.40 | A | 1-555 | [»] | |
| 4Y2X | X-ray | 2.50 | A | 1-555 | [»] | |
| 4Y2Y | X-ray | 2.30 | A | 1-555 | [»] | |
| 5AHX | X-ray | 2.00 | A | 1-548 | [»] | |
| 5AI0 | X-ray | 1.75 | A | 1-548 | [»] | |
| 5AI4 | X-ray | 1.93 | A | 1-548 | [»] | |
| 5AI5 | X-ray | 2.28 | A | 1-548 | [»] | |
| 5AI6 | X-ray | 2.30 | A | 1-548 | [»] | |
| 5AI8 | X-ray | 1.85 | A | 1-548 | [»] | |
| 5AI9 | X-ray | 1.80 | A | 1-548 | [»] | |
| 5AIA | X-ray | 2.26 | A | 1-548 | [»] | |
| 5AIB | X-ray | 1.95 | A | 1-548 | [»] | |
| 5AIC | X-ray | 1.89 | A | 1-548 | [»] | |
| 5AK3 | X-ray | 2.28 | A | 1-548 | [»] | |
| 5AK4 | X-ray | 1.79 | A | 1-548 | [»] | |
| 5AK5 | X-ray | 2.22 | A | 1-548 | [»] | |
| 5AK6 | X-ray | 2.15 | A | 1-548 | [»] | |
| 5AKE | X-ray | 2.26 | A | 1-548 | [»] | |
| 5AKG | X-ray | 2.51 | A | 1-548 | [»] | |
| 5AKH | X-ray | 2.10 | A | 1-548 | [»] | |
| 5AKI | X-ray | 1.81 | A | 1-548 | [»] | |
| 5AKJ | X-ray | 2.03 | A | 1-548 | [»] | |
| 5AKK | X-ray | 1.90 | A | 1-548 | [»] | |
| 5AKL | X-ray | 2.00 | A | 1-548 | [»] | |
| 5AKX | X-ray | 2.09 | A | 1-548 | [»] | |
| 5AKY | X-ray | 2.18 | A | 1-548 | [»] | |
| 5AKZ | X-ray | 2.18 | A | 1-548 | [»] | |
| 5ALD | X-ray | 2.26 | A | 1-548 | [»] | |
| 5ALE | X-ray | 1.95 | A | 1-548 | [»] | |
| 5ALF | X-ray | 2.32 | A | 1-548 | [»] | |
| 5ALG | X-ray | 2.40 | A | 1-548 | [»] | |
| 5ALH | X-ray | 1.90 | A | 1-548 | [»] | |
| 5ALI | X-ray | 1.85 | A | 1-548 | [»] | |
| 5ALJ | X-ray | 2.10 | A | 1-548 | [»] | |
| 5ALK | X-ray | 2.33 | A | 1-548 | [»] | |
| 5ALL | X-ray | 2.20 | A | 1-548 | [»] | |
| 5ALM | X-ray | 2.00 | A | 1-548 | [»] | |
| 5ALN | X-ray | 2.00 | A | 1-548 | [»] | |
| 5ALO | X-ray | 2.00 | A | 1-548 | [»] | |
| 5ALP | X-ray | 2.06 | A | 1-548 | [»] | |
| 5ALQ | X-ray | 2.78 | A | 1-548 | [»] | |
| 5ALR | X-ray | 2.60 | A | 1-548 | [»] | |
| 5ALS | X-ray | 2.57 | A | 1-548 | [»] | |
| 5ALT | X-ray | 2.15 | A | 1-548 | [»] | |
| 5ALU | X-ray | 1.87 | A | 1-548 | [»] | |
| 5ALV | X-ray | 1.80 | A | 1-548 | [»] | |
| 5ALW | X-ray | 2.20 | A | 1-548 | [»] | |
| 5ALX | X-ray | 2.23 | A | 1-548 | [»] | |
| 5ALY | X-ray | 1.90 | A | 1-548 | [»] | |
| 5ALZ | X-ray | 2.30 | A | 1-548 | [»] | |
| 5AM0 | X-ray | 1.88 | A | 1-548 | [»] | |
| 5AM1 | X-ray | 2.15 | A | 1-548 | [»] | |
| 5AM2 | X-ray | 1.70 | A | 1-548 | [»] | |
| 5AM3 | X-ray | 2.20 | A | 1-548 | [»] | |
| 5AM4 | X-ray | 1.87 | A | 1-548 | [»] | |
| 5AM5 | X-ray | 2.26 | A | 1-548 | [»] | |
| 5FP0 | X-ray | 2.35 | A | 1-548 | [»] | |
| 5MWA | X-ray | 1.55 | A | 2-224 | [»] | |
| 6AUM | X-ray | 2.95 | A | 1-555 | [»] | |
Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase More...ProteinModelPortali | P34913 | |||||
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | P34913 | |||||
Database of comparative protein structure models More...ModBasei | Search... | |||||
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... | |||||
Protein-protein interaction databases
The Biological General Repository for Interaction Datasets (BioGrid) More...BioGridi | 108367, 5 interactors |
Protein interaction database and analysis system More...IntActi | P34913, 5 interactors |
STRING: functional protein association networks More...STRINGi | 9606.ENSP00000430269 |
Chemistry databases
BindingDB database of measured binding affinities More...BindingDBi | P34913 |
ChEMBL database of bioactive drug-like small molecules More...ChEMBLi | CHEMBL2409 |
Drug and drug target database More...DrugBanki | DB08257 4-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}BUTANOIC ACID DB08258 6-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEXANOIC ACID DB08259 7-{[(CYCLOHEXYLAMINO)CARBONYL]AMINO}HEPTANOIC ACID DB08256 N-[(CYCLOHEXYLAMINO)CARBONYL]GLYCINE DB02029 N-Cyclohexyl-N'-(4-Iodophenyl)Urea DB04213 N-Cyclohexyl-N'-(Propyl)Phenyl Urea DB03677 N-Cyclohexyl-N'-Decylurea |
IUPHAR/BPS Guide to PHARMACOLOGY More...GuidetoPHARMACOLOGYi | 2970 |
SwissLipids knowledge resource for lipid biology More...SwissLipidsi | SLP:000001105 |
Protein family/group databases
ESTHER database of the Alpha/Beta-hydrolase fold superfamily of proteins More...ESTHERi | human-EPHX2 Epoxide_hydrolase |
MEROPS protease database More...MEROPSi | S33.973 |
PTM databases
DEPOD human dephosphorylation database More...DEPODi | P34913 |
iPTMnet integrated resource for PTMs in systems biology context More...iPTMneti | P34913 |
Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat. More...PhosphoSitePlusi | P34913 |
Polymorphism and mutation databases
BioMuta curated single-nucleotide variation and disease association database More...BioMutai | EPHX2 |
Domain mapping of disease mutations (DMDM) More...DMDMi | 67476665 |
Proteomic databases
Encyclopedia of Proteome Dynamics More...EPDi | P34913 |
MaxQB - The MaxQuant DataBase More...MaxQBi | P34913 |
PaxDb, a database of protein abundance averages across all three domains of life More...PaxDbi | P34913 |
PeptideAtlas More...PeptideAtlasi | P34913 |
PRoteomics IDEntifications database More...PRIDEi | P34913 |
ProteomicsDB human proteome resource More...ProteomicsDBi | 54953 |
Protocols and materials databases
The DNASU plasmid repository More...DNASUi | 2053 |
| Structural Biology Knowledgebase | Search... |
Genome annotation databases
Ensembl eukaryotic genome annotation project More...Ensembli | ENST00000380476; ENSP00000369843; ENSG00000120915 [P34913-2] ENST00000521400; ENSP00000430269; ENSG00000120915 [P34913-1] ENST00000521780; ENSP00000430302; ENSG00000120915 [P34913-3] |
Database of genes from NCBI RefSeq genomes More...GeneIDi | 2053 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | hsa:2053 |
UCSC genome browser More...UCSCi | uc003xfu.5 human [P34913-1] |
Organism-specific databases
Comparative Toxicogenomics Database More...CTDi | 2053 |
DisGeNET More...DisGeNETi | 2053 |
Eukaryotic Pathogen Database Resources More...EuPathDBi | HostDB:ENSG00000120915.13 |
GeneCards: human genes, protein and diseases More...GeneCardsi | EPHX2 |
Human Gene Nomenclature Database More...HGNCi | HGNC:3402 EPHX2 |
Human Protein Atlas More...HPAi | HPA023094 HPA023660 |
MalaCards human disease database More...MalaCardsi | EPHX2 |
Online Mendelian Inheritance in Man (OMIM) More...MIMi | 132811 gene |
neXtProt; the human protein knowledge platform More...neXtProti | NX_P34913 |
Open Targets More...OpenTargetsi | ENSG00000120915 |
The Pharmacogenetics and Pharmacogenomics Knowledge Base More...PharmGKBi | PA27830 |
GenAtlas: human gene database More...GenAtlasi | Search... |
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | KOG3085 Eukaryota KOG4178 Eukaryota COG1011 LUCA |
Ensembl GeneTree More...GeneTreei | ENSGT00530000063213 |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | HOG000028073 |
The HOVERGEN Database of Homologous Vertebrate Genes More...HOVERGENi | HBG006095 |
InParanoid: Eukaryotic Ortholog Groups More...InParanoidi | P34913 |
KEGG Orthology (KO) More...KOi | K08726 |
Identification of Orthologs from Complete Genome Data More...OMAi | GHWTQMD |
Database of Orthologous Groups More...OrthoDBi | EOG091G078G |
Database for complete collections of gene phylogenies More...PhylomeDBi | P34913 |
TreeFam database of animal gene trees More...TreeFami | TF315395 |
Enzyme and pathway databases
BRENDA Comprehensive Enzyme Information System More...BRENDAi | 3.3.2.10 2681 |
Reactome - a knowledgebase of biological pathways and processes More...Reactomei | R-HSA-2142670 Synthesis of epoxy (EET) and dihydroxyeicosatrienoic acids (DHET) R-HSA-9018682 Biosynthesis of maresins R-HSA-9033241 Peroxisomal protein import |
SABIO-RK: Biochemical Reaction Kinetics Database More...SABIO-RKi | P34913 |
Miscellaneous databases
ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data More...ChiTaRSi | EPHX2 human |
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | P34913 |
The Gene Wiki collection of pages on human genes and proteins More...GeneWikii | Epoxide_hydrolase_2 |
Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens More...GenomeRNAii | 2053 |
Protein Ontology More...PROi | PR:P34913 |
The Stanford Online Universal Resource for Clones and ESTs More...SOURCEi | Search... |
Gene expression databases
Bgee dataBase for Gene Expression Evolution More...Bgeei | ENSG00000120915 |
CleanEx database of gene expression profiles More...CleanExi | HS_EPHX2 |
ExpressionAtlas, Differential and Baseline Expression More...ExpressionAtlasi | P34913 baseline and differential |
Genevisible search portal to normalized and curated expression data from Genevestigator More...Genevisiblei | P34913 HS |
Family and domain databases
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 1.10.150.240, 1 hit 3.40.50.1000, 2 hits 3.40.50.1820, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR029058 AB_hydrolase IPR000073 AB_hydrolase_1 IPR000639 Epox_hydrolase-like IPR036412 HAD-like_sf IPR006439 HAD-SF_hydro_IA IPR011945 HAD-SF_ppase_IA/epoxid_hydro_N IPR023214 HAD_sf IPR023198 PGP-like_dom2 |
Pfam protein domain database More...Pfami | View protein in Pfam PF00561 Abhydrolase_1, 1 hit |
Protein Motif fingerprint database; a protein domain database More...PRINTSi | PR00111 ABHYDROLASE PR00412 EPOXHYDRLASE |
Superfamily database of structural and functional annotation More...SUPFAMi | SSF53474 SSF53474, 1 hit SSF56784 SSF56784, 1 hit |
TIGRFAMs; a protein family database More...TIGRFAMsi | TIGR02247 HAD-1A3-hyp, 1 hit TIGR01509 HAD-SF-IA-v3, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | HYES_HUMAN | |
| <p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | P34913Primary (citable) accession number: P34913 Secondary accession number(s): B2Z3B1 , B3KTU8, B3KUA0, G3V134, J3KPH7, Q16764, Q9HBJ1, Q9HBJ2 | |
| <p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 1, 1994 |
| Last sequence update: | June 7, 2005 | |
| Last modified: | June 20, 2018 | |
| This is version 183 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Chordata Protein Annotation Program | |
| Disclaimer | Any 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. | |
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
3D-structure, Complete proteome, Direct protein sequencing, Reference proteomeDocuments
- Human chromosome 8
Human chromosome 8: entries, gene names and cross-references to MIM - Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations - Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations - MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
