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UniProtKB/Swiss-Prot P34913: Variant p.Arg287Gln

Bifunctional epoxide hydrolase 2
Gene: EPHX2
Variant information

Variant position:  287
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LB/B
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Arginine (R) to Glutamine (Q) at position 287 (R287Q, p.Arg287Gln).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from large size and basic (R) to medium size and polar (Q)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  1
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  No effect on phosphatase activity; decreased epoxyde hydrolase activity.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

Variant position:  287
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  555
The length of the canonical sequence.

Location on the sequence:   FPESWYSWRYQIPALAQAGY  R VLAMDMKGYGESSAPPEIEE
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.

Residue conservation: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         FPESWYSWRYQIPALAQAGYRVLAMDMKGYGESSAPPEIEE

Mouse                         FPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEE

Rat                           FPESWFSWRYQIPALAQAGFRVLAIDMKGYGDSSSPPEIEE

Pig                           FPESWFSWRYQIPALAQAGFRVLAVDMKGYGESSAPPEIEE

Sequence annotation in neighborhood:  
The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
  • Type: the type of sequence feature.
  • Positions: endpoints of the sequence feature.
  • Description: contains additional information about the feature.

TypePositionsDescription
Chain 1 – 555 Bifunctional epoxide hydrolase 2
Domain 259 – 531 AB hydrolase-1
Region 235 – 555 Epoxide hydrolase
Beta strand 287 – 291


Literature citations

cDNA cloning and expression of a soluble epoxide hydrolase from human liver.
Beetham J.K.; Tian T.; Hammock B.D.;
Arch. Biochem. Biophys. 305:197-201(1993)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1); PARTIAL PROTEIN SEQUENCE; VARIANT GLN-287;

Identification and functional characterization of human soluble epoxide hydrolase genetic polymorphisms.
Sandberg M.; Hassett C.; Adman E.T.; Meijer J.; Omiecinski C.J.;
J. Biol. Chem. 275:28873-28881(2000)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1); VARIANTS GLN-287 AND ARG-403 INS;

Submission
NIEHS SNPs program;
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]; VARIANTS ALA-21; GLN-52; ARG-55; CYS-103; TYR-154; LEU-225; GLN-287; VAL-369 AND GLY-470;

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)
Cited for: FUNCTION; CATALYTIC ACTIVITY; CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470;

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)
Cited for: CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES; CHARACTERIZATION OF VARIANTS ARG-55; CYS-103; TYR-154; GLN-287 AND GLY-470;

Disclaimer: Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.