UniProtKB/Swiss-Prot P02649: Variant p.Gly145Asp

Apolipoprotein E
Gene: APOE
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Variant information Variant position:

145 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant:

US 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 Glycine (G) to Aspartate (D) at position 145 (G145D, p.Gly145Asp). 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 glycine (G) to medium size and acidic (D) 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:

Found in a patient with hypercholesterolemia; uncertain significance; ApoE1 Weisgraber. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs267606664 [ dbSNP | Ensembl ]

Sequence information 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:

DMEDVCGRLVQYRGEVQAML G QSTEELRVRLASHLRKLRKR 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                         DMEDVCGRLVQYRGEVQAMLGQSTEELRVRLASHLRKLRKR

Gorilla                       DMEDVRGRLAQYRGEVQAMLGQSTEELRARLASHLRKLRKR

                              DMEDVRNRLTQYRGELQAMLGQSSEELRARFASHMRKLRKR

Rhesus macaque                DMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKR

Chimpanzee                    DMEDVRGRLVQYRGEVQAMLGQSTEELRARLASHLRKLRKR

Mouse                         DMEDLRNRLGQYRNEVHTMLGQSTEEIRARLSTHLRKMRKR

Rat                           DMEDLRNRLGQYRNEVNTMLGQSTEELRSRLSTHLRKMRKR

Pig                           DMEDVRNRLVLYRSEVHNMLGQTTEELRSRLASHLRNVRKR

Bovine                        DMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLPKR

Rabbit                        DMEDVCNRLAQYRGEAQAMLGQSTEELARAFSSHLRKLRKR

Sheep                         DMEDLRNRLAQYRSEVQAMLGQSTEELRARMASHLRKLRKR

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
Chain	19 – 317	Apolipoprotein E
Repeat	124 – 145	3
Region	80 – 255	8 X 22 AA approximate tandem repeats
Modified residue	143 – 143	Methionine sulfoxide
Modified residue	147 – 147	Phosphoserine; by FAM20C
Mutagenesis	127 – 127	E -> A. No effect on plasma lipoprotein distribution.
Mutagenesis	157 – 157	S -> R. Increased binding to LDL receptor; when associated with A-167.
Mutagenesis	158 – 158	H -> A. Decreased binding to LDL receptor.
Mutagenesis	161 – 161	K -> A. Decreased binding to LDL receptor.
Mutagenesis	162 – 162	L -> P. Decreased binding to LDL receptor.
Turn	143 – 145

Literature citations
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;

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.