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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02766: Variant p.Arg124His

Transthyretin
Gene: TTR
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Variant information Variant position: help 124 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 Arginine (R) to Histidine (H) at position 124 (R124H, p.Arg124His). 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 large size and basic (R) to medium size and polar (H) 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

Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 124 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 147 The length of the canonical sequence.
Location on the sequence: help ISPFHEHAEVVFTANDSGPR R YTIAALLSPYSYSTTAVVTN 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                         ISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTN

Chimpanzee                    ISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYSTTAVVTI

Mouse                         ISPFHEFADVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN

Rat                           ISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYSTTAVVSN

Pig                           ISPFHEYAEVVFTANDSGRRHYTIAALLSPYSYSTTALVSS

Bovine                        ISPFHEFAEVVFTANDSGPRHYTIAALLSPYSYSTTALVSS

Rabbit                        ISPFHEYAEVVFTANDSGHRSYTIAALLSPFSYSTTAVVSN

Sheep                         ISPFHEYAEVVFTANDSGLRHYTIAALLSPYSYSTTALVSS

Chicken                       LSPFHEYADVVFTANDSGHRHYTIAALLSPFSYSTTAVVSD

Xenopus laevis                LSPFHEYVDVVFTANDAGHRHYTIAVLLTPYSFSSTAIVSE

Xenopus tropicalis            LSPFHEYVDVVFSANDAGHRHYTIAVLLTPYSISSTAVVSE

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 21 – 147 Transthyretin
Binding site 137 – 137
Glycosylation 118 – 118 N-linked (GlcNAc...) asparagine
Mutagenesis 107 – 107 F -> M. Loss of tetramerization; when associated with M-130.
Mutagenesis 130 – 130 L -> M. Loss of tetramerization; when associated with M-107.
Beta strand 124 – 132



Literature citations
X-ray crystallographic studies of two transthyretin variants: further insights into amyloidogenesis.
Neto-Silva R.M.; Macedo-Ribeiro S.; Pereira P.J.B.; Coll M.; Saraiva M.J.; Damas A.M.;
Acta Crystallogr. D 61:333-339(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR PHE-98 AND VARIANT HIS-124; SUBUNIT; A novel compound heterozygote (FAP ATTR Arg104His/ATTR Val30Met) with high serum transthyretin (TTR) and retinol binding protein (RBP) levels.
Terazaki H.; Ando Y.; Misumi S.; Nakamura M.; Ando E.; Matsunaga N.; Shoji S.; Okuyama M.; Ideta H.; Nakagawa K.; Ishizaki T.; Ando M.; Saraiva M.J.;
Biochem. Biophys. Res. Commun. 264:365-370(1999)
Cited for: VARIANT HIS-124; IDENTIFICATION BY MASS SPECTROMETRY;
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.