Variant position: 145 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 317 The length of the canonical sequence.
Location on the sequence:
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 DMEDVCGRLVQYRGEVQAML GQSTEELRVRLASHLRKLRKR
Gorilla DMEDVRGRLAQYRGEVQAML GQSTEELRARLASHLRKLRKR
Rhesus macaque DMEDVRSRLVQYRSEVQAML GQSTEELRARLASHLRKLRKR
Chimpanzee DMEDVRGRLVQYRGEVQAML GQSTEELRARLASHLRKLRKR
Mouse DMEDLRNRLGQYRNEVHTML GQSTEEIRARLSTHLRKMRKR
Rat DMEDLRNRLGQYRNEVNTML GQSTEELRSRLSTHLRKMRKR
Pig DMEDVRNRLVLYRSEVHNML GQTTEELRSRLASHLRNVRKR
Bovine DMEDLRNRLAQYRSEVQAML GQSTEELRARMASHLRKLPKR
Rabbit DMEDVCNRLAQYRGEAQAML GQSTEELARAFSSHLRKLRKR
Sheep DMEDLRNRLAQYRSEVQAML GQSTEELRARMASHLRKLRKR
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.
Type Positions Description
19 – 317 Apolipoprotein E
124 – 145 3
80 – 255 8 X 22 AA approximate tandem repeats
143 – 143 Methionine sulfoxide
147 – 147 Phosphoserine; by FAM20C
127 – 127 E -> A. No effect on plasma lipoprotein distribution.
157 – 157 S -> R. Increased binding to LDL receptor; when associated with A-167.
158 – 158 H -> A. Decreased binding to LDL receptor.
161 – 161 K -> A. Decreased binding to LDL receptor.
162 – 162 L -> P. Decreased binding to LDL receptor.
143 – 145
Common and rare genotypes of human apolipoprotein E determined by specific restriction profiles of polymerase chain reaction-amplified DNA.
Richard P.; Thomas G.; de Zulueta M.P.; de Gennes J.-L.; Thomas M.; Cassaigne A.; Bereziat G.; Iron A.;
Clin. Chem. 40:24-29(1994)
Cited for: VARIANTS HLPP3 ARG-130; SER-154; CYS-160 AND CYS-176; VARIANT ASP-145;
Global molecular analysis and APOE mutations in a cohort of autosomal dominant hypercholesterolemia patients in France.
Wintjens R.; Bozon D.; Belabbas K.; Mbou F.; Girardet J.P.; Tounian P.; Jolly M.; Boccara F.; Cohen A.; Karsenty A.; Dubern B.; Carel J.C.; Azar-Kolakez A.; Feillet F.; Labarthe F.; Gorsky A.M.; Horovitz A.; Tamarindi C.; Kieffer P.; Lienhardt A.; Lascols O.; Di Filippo M.; Dufernez F.;
J. Lipid Res. 57:482-491(2016)
Cited for: VARIANTS PRO-46 AND ASP-145; VARIANT HLPP3 CYS-163; VARIANT SBHD LEU-167 DEL;
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.