UniProtKB/Swiss-Prot P02647: Variant p.Lys131Met

Apolipoprotein A-I
Gene: APOA1
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Variant information Variant position:

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

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:

From Lysine (K) to Methionine (M) at position 131 (K131M, p.Lys131Met). 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 large size and basic (K) to medium size and hydrophobic (M) 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
Polymorphism:

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.
Other resources:

Links to websites of interest for the variant.

Variant rs4882 [ dbSNP | Ensembl ]

Sequence information Variant position:

131 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

267 The length of the canonical sequence.
Location on the sequence:

SKDLEEVKAKVQPYLDDFQK K WQEEMELYRQKVEPLRAELQ 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                         SKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQ

Gorilla                       SKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQ

                              SKDLEEVKQKVQPYLDDFQKKWQEEVELYRQKVAPLGSELR

Rhesus macaque                SKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELH

Chimpanzee                    SKDLEEVKAKVQPYLDDFQKKWQEEMELYRQKVEPLRAELQ

Mouse                         NKDLEEVKQKVQPYLDEFQKKWKEDVELYRQKVAPLGAELQ

Rat                           NKDLENVKQKMQPHLDEFQEKWNEEVEAYRQKLEPLGTELH

Pig                           SKDLEEVKKKVQPYLDDFQNKWQEEMETYRQKMAPLGAEFR

Bovine                        HKDLEEVKQKVQPYLDEFQKKWHEEVEIYRQKVAPLGEEFR

Rabbit                        NKDLQEVRQKVQPYLDEFQKKWQEEVERYRQKVEPLGAELR

Chicken                       TKDLEEVKEKIRPFLDQFSAKWTEELEQYRQRLTPVAQELK

Zebrafish                     MTDVEDLRSKLEPHRAELYTALQKHIDEYREKLEPVFQEYS

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 – 267	Proapolipoprotein A-I
Chain	25 – 267	Apolipoprotein A-I
Chain	25 – 266	Truncated apolipoprotein A-I
Repeat	123 – 144	4
Region	68 – 267	10 X approximate tandem repeats
Modified residue	136 – 136	Methionine sulfoxide
Mutagenesis	124 – 124	Y -> F. Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-139, F-190, F-216 and F-260.
Mutagenesis	139 – 139	Y -> F. Abolished chlorination and nitration without preventing inhibition in presence of myeloproxidase; when associated with F-42, F-53, F-124, F-190, F-216 and F-260.

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.