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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02649: Variant p.Lys164Gln

Apolipoprotein E
Gene: APOE
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Variant information Variant position: help 164 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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: help From Lysine (K) to Glutamine (Q) at position 164 (K164Q, p.Lys164Gln). 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: help Change from large size and basic (K) to medium size and polar (Q) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In HLPP3; ApoE2**. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 164 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 317 The length of the canonical sequence.
Location on the sequence: help LGQSTEELRVRLASHLRKLR K RLLRDADDLQKRLAVYQAGA 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         LGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAGA

Gorilla                       LGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGA

                              LGQSSEELRARFASHMRKLRKRVLRDAEDLQRRLAVYKAGV

Rhesus macaque                LGQSTEELRARLASHLRKLRKRLLRDADDLQKRLA------

Chimpanzee                    LGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGA

Mouse                         LGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAGA

Rat                           LGQSTEELRSRLSTHLRKMRKRLMRDADDLQKRLAVYKAGA

Pig                           LGQTTEELRSRLASHLRNVRKRLVRDTEDLQKRLAVYQAGL

Bovine                        LGQSTEELRARMASHLRKLPKRLLRDADDLKKRLAVYQAGA

Rabbit                        LGQSTEELARAFSSHLRKLRKRLLRDAEDLQKRMAVYGAGA

Sheep                         LGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAGA
Sequence annotation in neighborhood: help 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 19 – 317 Apolipoprotein E
Repeat 146 – 167 4
Region 80 – 255 8 X 22 AA approximate tandem repeats
Region 158 – 168 LDL and other lipoprotein receptors binding
Binding site 162 – 165
Modified residue 147 – 147 Phosphoserine; by FAM20C
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.
Mutagenesis 167 – 167 L -> A. Increased binding to LDL receptor; when associated with R-157.
Mutagenesis 168 – 168 R -> A. Decreased binding to LDL receptor.
Mutagenesis 172 – 172 D -> A. Restores the LDL receptor binding activity of ApoE2.
Helix 149 – 180



Literature citations
No reference for the current variant in UniProtKB/Swiss-Prot.
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.