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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P02766: Variant p.Phe53Leu

Transthyretin
Gene: TTR
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Variant information Variant position: help 53 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 Phenylalanine (F) to Leucine (L) at position 53 (F53L, p.Phe53Leu). 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 aromatic (F) to medium size and hydrophobic (L) 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 AMYLD1; 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 53 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 MVKVLDAVRGSPAINVAVHV F RKAADDTWEPFASGKTSESG 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                         MVKVLDAVRGSPAINVAVHVFRKAADDTWEPFASGKTSESG

Chimpanzee                    MVKVLDAVRGSPAINVAVHVFKKAADETWEPFASGKTSESG

Mouse                         MVKVLDAVRGSPAVDVAVKVFKKTSEGSWEPFASGKTAESG

Rat                           MVKVLDAVRGSPAVDVAVKVFKKTADGSWEPFASGKTAESG

Pig                           MVKVLDAVRGSPAVNVGVKVFKKAADGTWEPFALGKTSEFG

Bovine                        MVKVLDAVRGSPAANVGVKVFKKAADETWEPFASGKTSESG

Rabbit                        MVKVLDAVRGSPAVDVSVHVFKKAADETWEPFASGKTSKTG

Sheep                         MVKVLDAVRGSPAANVGVKVFKKAADETWEPFASGKTSDSG

Chicken                       MVKVLDAVRGSPAANVAVKVFKKAADGTWQDFATGKTTEFG

Xenopus laevis                MVKVLDAVRGIPAANLLVNVFRQTESGKWEQITSGKTTELG

Xenopus tropicalis            MVKVLDAVRGIPAANLLVQVFRNT-EGNWELISSGKTTELG
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 35 – 35
Modified residue 62 – 62 4-carboxyglutamate; in a patient with Moyamoya disease
Modified residue 72 – 72 Phosphoserine
Beta strand 49 – 55



Literature citations
A second transthyretin mutation at position 33 (Leu/Phe) associated with familial amyloidotic polyneuropathy.
Harding J.; Skare J.; Skinner M.;
Biochim. Biophys. Acta 1097:183-186(1991)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-67; VARIANT AMYLD1 LEU-53; Two-tiered DNA-based diagnosis of transthyretin amyloidosis reveals two novel point mutations.
Li S.; Minnerath S.; Li K.; Dyck P.J.; Sommer S.S.;
Neurology 41:893-898(1991)
Cited for: VARIANTS AMYLD1 LEU-53 AND LEU-84; Misdiagnosis of hereditary amyloidosis as AL (primary) amyloidosis.
Lachmann H.J.; Booth D.R.; Booth S.E.; Bybee A.; Gilbertson J.A.; Gillmore J.D.; Pepys M.B.; Hawkins P.N.;
N. Engl. J. Med. 346:1786-1791(2002)
Cited for: VARIANTS AMYLD1 MET-50; LEU-53; VAL-53; VAL-58; GLU-67; ALA-80; SER-140 AND ILE-142; 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 AMYLD1 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.