Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02649: Variant p.Arg163His

Apolipoprotein E
Gene: APOE
Feedback?
Variant information Variant position: help 163 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Arginine (R) to Histidine (H) at position 163 (R163H, p.Arg163His). 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 (R) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 0 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; uncertain significance; ApoE Kochi. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 163 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 MLGQSTEELRVRLASHLRKL R KRLLRDADDLQKRLAVYQAG 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                         MLGQSTEELRVRLASHLRKLRKRLLRDADDLQKRLAVYQAG

Gorilla                       MLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAG

                              MLGQSSEELRARFASHMRKLRKRVLRDAEDLQRRLAVYKAG

Rhesus macaque                MLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLA-----

Chimpanzee                    MLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAG

Mouse                         MLGQSTEEIRARLSTHLRKMRKRLMRDAEDLQKRLAVYKAG

Rat                           MLGQSTEELRSRLSTHLRKMRKRLMRDADDLQKRLAVYKAG

Pig                           MLGQTTEELRSRLASHLRNVRKRLVRDTEDLQKRLAVYQAG

Bovine                        MLGQSTEELRARMASHLRKLPKRLLRDADDLKKRLAVYQAG

Rabbit                        MLGQSTEELARAFSSHLRKLRKRLLRDAEDLQKRMAVYGAG

Sheep                         MLGQSTEELRARMASHLRKLRKRLLRDADDLKKRLAVYQAG

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 143 – 143 Methionine sulfoxide
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
Identification and characterization of a new variant of apolipoprotein E (apo E-Kochi).
Suehiro T.; Yoshida K.; Yamano T.; Ohno F.;
Jpn. J. Med. 29:587-594(1990)
Cited for: VARIANT HLPP3 HIS-163;
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.