UniProtKB/Swiss-Prot P02768: Variant p.Asp587Asn

• Variant information
• Sequence information
• Literature citations
• All

Variant information

Variant position: 587 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 Aspartate (D) to Asparagine (N) at position 587 (D587N, p.Asp587Asn). 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 acidic (D) to medium size and polar (N) 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: A variant structure of albumin could lead to increased binding of zinc resulting in an asymptomatic augmentation of zinc concentration in the blood. The sequence shown is that of variant albumin A. Additional information on the polymorphism described.
Variant description: In Fukuoka-1/Paris-2. Any additional useful information about the variant.
Other resources: Links to websites of interest for the variant.

• Variant rs76587671 [ dbSNP | Ensembl ]

Sequence information

Variant position: 587 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 609 The length of the canonical sequence.
Location on the sequence: QLKAVMDDFAAFVEKCCKAD D KETCFAEEGKKLVAASQAAL 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.
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	25 – 609	Albumin
Domain	404 – 601	Albumin 3
Site	581 – 581	Not glycated
Site	584 – 584	Not glycated
Site	588 – 588	Not glycated
Site	598 – 598	Not glycated
Modified residue	588 – 588	N6-succinyllysine
Glycosylation	569 – 569	N-linked (Glc) (glycation) lysine; in vitro
Glycosylation	597 – 597	N-linked (Glc) (glycation) lysine; in vitro
Disulfide bond	582 – 591
Beta strand	584 – 587

Literature citations

Point substitutions in albumin genetic variants from Asia.
Arai K.; Madison J.; Shimuzu A.; Putnam F.W.;
Proc. Natl. Acad. Sci. U.S.A. 87:497-501(1990)
Cited for: VARIANT HONOLULU-1 PRO-24; VARIANT HONOLULU-2 GLN-24; VARIANT NAGOYA LYS-143; VARIANT NEW GUINEA ASN-337; VARIANT MANAUS-1/LAMBADI LYS-525; VARIANT FUKUOKA-1 ASN-587; VARIANT OSAKA-1 LYS-589; VARIANT OSAKA-2 LYS-594; Two alloalbumins with identical electrophoretic mobility are produced by differently charged amino acid substitutions.
Minchiotti L.; Galliano M.; Stoppini M.; Ferri G.; Crespeau H.; Rochu D.; Porta F.;
Biochim. Biophys. Acta 1119:232-238(1992)
Cited for: VARIANT SONDRIO LYS-357; VARIANT PARIS-2 ASN-587;