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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02766: Variant p.Ala117Gly

Transthyretin
Gene: TTR
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Variant information Variant position: help 117 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help LP/P [Disclaimer] 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 Glycine (G) at position 117 (A117G, p.Ala117Gly). 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 glycine (G) 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
Variant description: help In AMYL-TTR; amyloid polyneuropathy. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 117 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 SYWKALGISPFHEHAEVVFT A NDSGPRRYTIAALLSPYSYS 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                         SYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYS

Chimpanzee                    SYWKALGISPFHEHAEVVFTANDSGPRRYTIAALLSPYSYS

Mouse                         SYWKTLGISPFHEFADVVFTANDSGHRHYTIAALLSPYSYS

Rat                           SYWKALGISPFHEYAEVVFTANDSGHRHYTIAALLSPYSYS

Pig                           SYWKALGISPFHEYAEVVFTANDSGRRHYTIAALLSPYSYS

Bovine                        SYWKSLGISPFHEFAEVVFTANDSGPRHYTIAALLSPYSYS

Rabbit                        SYWKALGISPFHEYAEVVFTANDSGHRSYTIAALLSPFSYS

Sheep                         SYWKSLGISPFHEYAEVVFTANDSGLRHYTIAALLSPYSYS

Chicken                       SYWKGLGLSPFHEYADVVFTANDSGHRHYTIAALLSPFSYS

Xenopus laevis                AFWGKLGLSPFHEYVDVVFTANDAGHRHYTIAVLLTPYSFS

Xenopus tropicalis            TFWRKLGLSPFHEYVDVVFSANDAGHRHYTIAVLLTPYSIS
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 107 – 118



Literature citations
Familial amyloidotic polyneuropathy with late-onset and well-preserved autonomic function: a Japanese kindred with novel mutant transthyretin (Ala97 to Gly).
Yasuda T.; Sobue G.; Doyu M.; Nakazato M.; Shiomi K.; Yanagi T.; Mitsuma T.;
J. Neurol. Sci. 121:97-102(1994)
Cited for: VARIANT AMYL-TTR GLY-117; Usefulness of MALDI/TOF mass spectrometry of immunoprecipitated serum variant transthyretin in the diagnosis of familial amyloid polyneuropathy.
Tachibana N.; Tokuda T.; Yoshida K.; Taketomi T.; Nakazato M.; Li Y.F.; Masuda Y.; Ikeda S.;
Amyloid 6:282-288(1999)
Cited for: VARIANTS AMYL-TTR LEU-50; VAL-53; ALA-58; ARG-70; GLY-117 AND SER-117; IDENTIFICATION BY MASS SPECTROMETRY; Genetic microheterogeneity of human transthyretin detected by IEF.
Altland K.; Benson M.D.; Costello C.E.; Ferlini A.; Hazenberg B.P.C.; Hund E.; Kristen A.V.; Linke R.P.; Merlini G.; Salvi F.; Saraiva M.J.; Singer R.; Skinner M.; Winter P.;
Electrophoresis 28:2053-2064(2007)
Cited for: VARIANTS AMYL-TTR PRO-32; ILE-40; SER-44; ALA-50; MET-50; LEU-53; VAL-53; PRO-56; THR-65; ALA-67; ALA-69; ILE-69; ALA-80; LEU-84; LEU-88; ALA-91; TYR-97; PHE-98; SER-104; ASN-104; THR-104; ALA-114; GLY-117; ASN-126; MET-127; VAL-127; MET-131 AND ILE-142; VARIANTS ILE-33; SER-121 AND THR-129; VARIANT CHICAGO MET-139;
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.