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UniProtKB/Swiss-Prot P02766: Variant p.Tyr134Cys

Transthyretin
Gene: TTR
Variant information

Variant position:  134
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  Disease [Disclaimer]
The variants are classified into three categories: Disease, Polymorphism and Unclassified.
  • Disease: Variants implicated in disease according to literature reports.
  • Polymorphism: Variants not reported to be implicated in disease.
  • Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:  From Tyrosine (Y) to Cysteine (C) at position 134 (Y134C, p.Tyr134Cys).
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 large size and aromatic (Y) to medium size and polar (C)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -2
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:  In AMYL-TTR; amyloid polyneuropathy.
Any additional useful information about the variant.

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



Sequence information

Variant position:  134
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  147
The length of the canonical sequence.

Location on the sequence:   VFTANDSGPRRYTIAALLSP  Y SYSTTAVVTNPKE
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: 
The multiple alignment of the region surrounding the variant against various orthologous sequences.

Human                         VFTANDSGPRRYTIAALLSPYSYSTTAVVTNPKE---

Chimpanzee                    VFTANDSGPRRYTIAALLSPYSYSTTAVVTIPKE

Mouse                         VFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN

Rat                           VFTANDSGHRHYTIAALLSPYSYSTTAVVSNPQN

Pig                           VFTANDSGRRHYTIAALLSPYSYSTTALVSSPKE

Bovine                        VFTANDSGPRHYTIAALLSPYSYSTTALVSSPKA

Rabbit                        VFTANDSGHRSYTIAALLSPFSYSTTAVVSNPQE

Sheep                         VFTANDSGLRHYTIAALLSPYSYSTTALVSSPKE

Chicken                       VFTANDSGHRHYTIAALLSPFSYSTTAVVSDPQE

Xenopus laevis                VFTANDAGHRHYTIAVLLTPYSFSSTAIVSEPHD

Xenopus tropicalis            VFSANDAGHRHYTIAVLLTPYSISSTAVVSEPHD

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.

TypePositionsDescription
Chain 21 – 147 Transthyretin
Glycosylation 118 – 118 N-linked (GlcNAc...) asparagine
Mutagenesis 130 – 130 L -> M. Loss of tetramerization; when associated with M-107.


Literature citations

Disulfide-bond formation in the transthyretin mutant Y114C prevents amyloid fibril formation in vivo and in vitro.
Eneqvist T.; Olofsson A.; Ando Y.; Miyakawa T.; Katsuragi S.; Jass J.; Lundgren E.; Sauer-Eriksson A.E.;
Biochemistry 41:13143-13151(2002)
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR CYS-134;

Cys114-linked dimers of transthyretin are compatible with amyloid formation.
Karlsson A.; Olofsson A.; Eneqvist T.; Sauer-Eriksson A.E.;
Biochemistry 44:13063-13070(2005)
Cited for: X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 21-147 OF VARIANT AMYL-TTR CYS-134;

A novel variant of transthyretin (Tyr114 to Cys) deduced from the nucleotide sequences of gene fragments from familial amyloidotic polyneuropathy in Japanese sibling cases.
Ueno S.; Uemichi T.; Yorifuji S.; Tarui S.;
Biochem. Biophys. Res. Commun. 169:143-147(1990)
Cited for: VARIANT AMYL-TTR CYS-134;

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.