BAIT

EPHX2

CEH, SEH
epoxide hydrolase 2, cytoplasmic
Homo sapiens
PREY

EPHX2

CEH, SEH
epoxide hydrolase 2, cytoplasmic
Homo sapiens

Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Publication

Polymorphisms in human soluble epoxide hydrolase: effects on enzyme activity, enzyme stability, and quaternary structure.

Srivastava PK, Sharma VK, Kalonia DS, Grant DF

Human soluble epoxide hydrolase (hsEH) has been shown to play a role in regulating blood pressure and inflammation. HsEH consists of an N-terminal phosphatase and a C-terminal epoxide hydrolase domain. In the present study, we examined the effects of polymorphisms in the hsEH gene on phosphatase activity, enzyme stability, and protein quaternary structure. The results showed that mutants Lys55Arg, Arg103Cys, ... [more]

Arch. Biochem. Biophys. Jul. 15, 2004; 427(2);164-9 [Pubmed: 15196990]

Throughput

  • Low Throughput

Additional Notes

  • EPHX2-R287Q and EPHX2-R103C double mutant disrupts dimer formation
  • Variants (Uniprot IDs): P34913:VAR_014852 and P34913:VAR_033991 double mutant disrupts dimer formation
  • in dbSNP: rs751141 and rs17057255 double mutant disrupts dimer formation
  • most frequent allele exists as dimer

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
EPHX2 EPHX2
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
854918
EPHX2 EPHX2
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
908540
EPHX2 EPHX2
Cross-Linking-MS (XL-MS)
Cross-Linking-MS (XL-MS)

An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).

High-BioGRID
-

Curated By

  • BioGRID