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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02647: Variant p.Glu222Lys

Apolipoprotein A-I
Gene: APOA1
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Variant information Variant position: help 222 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Glutamate (E) to Lysine (K) at position 222 (E222K, p.Glu222Lys). 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 medium size and acidic (E) to large size and basic (K) 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

Polymorphism: help Genetic variations in APOA1 can result in APOA1 deficiency and are associated with low levels of HDL cholesterol [MIM:107680]. Additional information on the polymorphism described.
Variant description: help In Munster-4. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 222 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 267 The length of the canonical sequence.
Location on the sequence: help LEALKENGGARLAEYHAKAT E HLSTLSEKAKPALEDLRQGL 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                         LEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGL

Gorilla                       LEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGL

                              LEALKEGGGASLAEYHARASEQLSALGEKARPALEDLRQGL

Rhesus macaque                LEALKENGGARLAEYHAKASEHLSTLSEKAKPALEDLRQGL

Chimpanzee                    LEALKENGGARLAEYHAKATEHLSTLSEKAKPALEDLRQGL

Mouse                         LAELKSN--PTLNEYHTRAKTHLKTLGEKARPALEDLRHSL

Rat                           LTEIKNH--PTLIEYHTKASDHLKTLGEKAKPALDDLGQGL

Pig                           FEALKEGGGS-LAEYQAKAQEQLKALGEKAKPALEDLRQGL

Bovine                        LEALKEGGGS-LAEYHAKASEQLKALGEKAKPVLEDLRQGL

Rabbit                        LESIKEGGGASLAEYQAKAREHLSVLSEKARPALEDLRQGL

Chicken                       LEEIREKGIPQASEYQAKVMEQLSNLREKMTPLVQEFRERL

Zebrafish                     LEDLRTMAAPYAEEYKEQLVKAVEEAREKIAPHTQDLQTRM

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 – 267 Proapolipoprotein A-I
Chain 25 – 267 Apolipoprotein A-I
Chain 25 – 266 Truncated apolipoprotein A-I
Repeat 211 – 232 8
Region 68 – 267 10 X approximate tandem repeats



Literature citations
Structural analysis of human apolipoprotein A-I variants. Amino acid substitutions are nonrandomly distributed throughout the apolipoprotein A-I primary structure.
von Eckardstein A.; Funke H.; Walter M.; Altland K.; Benninghoven A.; Assmann G.;
J. Biol. Chem. 265:8610-8617(1990)
Cited for: VARIANTS GLU-113; MET-131; GLY-163; VAL-171 AND LYS-222;
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.