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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P0DJI8: Variant p.Ala70Val

Serum amyloid A-1 protein
Gene: SAA1
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Variant information Variant position: help 70 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 Alanine (A) to Valine (V) at position 70 (A70V, p.Ala70Val). 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 small size and hydrophobic (A) to medium size and hydrophobic (V) 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

Polymorphism: help At least 5 different SAA1 alleles have been described: SAA1.1 (SAA1alpha), SAA1.2 (SAA1beta), SAA1.3 (SAA1gamma), SAA1.4 (SAA1delta), SAA1.5 (also named SAA1beta but which differs from SAA1.2). We use here the revised nomenclature described in PubMed:10211414. The sequence shown is that of SAA1.2. Additional information on the polymorphism described.
Variant description: help In allele SAA1.1. Any additional useful information about the variant.


Sequence information Variant position: help 70 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 122 The length of the canonical sequence.
Location on the sequence: help SDKYFHARGNYDAAKRGPGG A WAAEVITDARENIQRFFGHG 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                         SDKYFHARGNYDAAKRGPGGAWAAEVITDARENIQRFFGHG

Mouse                         SDKYFHARGNYDAAQRGPGGVWAAEKISDGREAFQEFFGRG

Rabbit                        ADKYFHARGNYDAAQRGPGGVWAAKVISDAREDLQRLMGHG

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 – 122 Serum amyloid A-1 protein
Chain 19 – 94 Amyloid protein A
Chain 20 – 122 Serum amyloid protein A(2-104)
Chain 20 – 121 Serum amyloid protein A(2-103)
Chain 20 – 120 Serum amyloid protein A(2-102)
Chain 21 – 122 Serum amyloid protein A(3-104)
Chain 22 – 119 Serum amyloid protein A(4-101)
Mutagenesis 65 – 65 R -> A. Reduces affinity for heparin; when associated with A-33 and A-37.
Mutagenesis 80 – 80 R -> A. Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-89.
Mutagenesis 89 – 89 H -> A. Reduces affinity for heparin and nearly abolishes association with HDL; when associated with A-18 and A-80.
Helix 67 – 86



Literature citations
Human serum amyloid A (SAA): biosynthesis and postsynthetic processing of preSAA and structural variants defined by complementary DNA.
Sipe J.D.; Colten H.R.; Goldberger G.; Edge M.D.; Tack B.F.; Cohen A.S.; Whitehead A.S.;
Biochemistry 24:2931-2936(1985)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1); VARIANTS VAL-70; ALA-75 AND SER-77; Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person.
Kluve-Beckerman B.; Dwulet F.E.; Benson M.D.;
J. Clin. Invest. 82:1670-1675(1988)
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE SAA1.1); VARIANTS VAL-70; ALA-75 AND SER-77; The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
The MGC Project Team;
Genome Res. 14:2121-2127(2004)
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ALLELE SAA1.1); VARIANTS VAL-70; ALA-75 AND SER-77;
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.