UniProtKB/SwissProt variant VAR

Variant information

Variant position:

597

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Glutamine (Q) to Arginine (R) at position 597 (Q597R, p.Gln597Arg).

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 medium size and polar (Q) to large size and basic (R)

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:

In HDLD1.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs2853578 [ dbSNP | Ensembl ]

Sequence information

Variant position:

597

The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:

2261

The length of the canonical sequence.

Location on the sequence:

GPRADPFEDMRYVWGGFAYL Q DVVEQAIIRVLTGTEKKTGV

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                         GPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGTEKKTGV

Mouse                         GPRADPFEDMRYVWGGFAYLQDVVEQAIIRVLTGSEKKTGV

Slime mold                    KIRNEKIPPPTISYGSNAFPRYPPEQGAARVWGG-------

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	1 – 2261	Phospholipid-transporting ATPase ABCA1
Topological domain	43 – 639	Extracellular
Mutagenesis	593 – 593	F -> L. Moderately decreased protein abundance. Highly decreased ATPase activity. Highly decreased phospholipid translocase activity.

Literature citations

Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency.
Brooks-Wilson A.; Marcil M.; Clee S.M.; Zhang L.-H.; Roomp K.; van Dam M.; Yu L.; Brewer C.; Collins J.A.; Molhuizen H.O.F.; Loubser O.; Ouelette B.F.F.; Fichter K.; Ashbourne-Excoffon K.J.D.; Sensen C.W.; Scherer S.; Mott S.; Denis M.; Martindale D.; Frohlich J.; Morgan K.; Koop B.; Pimstone S.; Kastelein J.J.P.; Hayden M.R.;
Nat. Genet. 22:336-345(1999)
Cited for: VARIANTS HDLD1 ARG-597 AND ARG-1477; VARIANT HDLD2 LEU-693 DEL;

Age and residual cholesterol efflux affect HDL cholesterol levels and coronary artery disease in ABCA1 heterozygotes.
Clee S.M.; Kastelein J.J.P.; van Dam M.; Marcil M.; Roomp K.; Zwarts K.Y.; Collins J.A.; Roelants R.; Tamasawa N.; Stulc T.; Suda T.; Ceska R.; Boucher B.; Rondeau C.; DeSouich C.; Brooks-Wilson A.; Molhuizen H.O.F.; Frohlich J.; Genest J. Jr.; Hayden M.R.;
J. Clin. Invest. 106:1263-1270(2000)
Cited for: VARIANTS HDLD1 ARG-597; ILE-929 AND ARG-1477; VARIANTS HDLD2 LEU-693 DEL; THR-1091; 1893-GLU-ASP-1894 DEL AND LEU-2150;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O95477: Variant p.Gln597Arg