UniProtKB/Swiss-Prot P02766: Variant p.Gly67Arg

Transthyretin
Gene: TTR
Chromosomal location: 18q12.1
Variant information

Variant position:  67
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 have been found in patients and disease-association is reported in literature. However, this classification is not a definitive assessment of variant pathogenicity.
  • Polymorphism: No disease-association has been reported.
  • Unclassified: Variants have been found in patients but disease-association remains unclear.

Residue change:  From Glycine (G) to Arginine (R) at position 67 (G67R, p.Gly67Arg).
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 glycine (G) to large size and basic (R)
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.



Sequence information

Variant position:  67
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:   NVAVHVFRKAADDTWEPFAS  G KTSESGELHGLTTEEEFVEG
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                         NVAVHVFRKAADDTWEPFASGKTSESGELHGLTTEEEFVEG

Chimpanzee                    NVAVHVFKKAADETWEPFASGKTSESGELHGLTTEEEFVEG

Mouse                         DVAVKVFKKTSEGSWEPFASGKTAESGELHGLTTDEKFVEG

Rat                           DVAVKVFKKTADGSWEPFASGKTAESGELHGLTTDEKFTEG

Pig                           NVGVKVFKKAADGTWEPFALGKTSEFGELHGLTTDEKFVEG

Bovine                        NVGVKVFKKAADETWEPFASGKTSESGELHGLTTEDKFVEG

Rabbit                        DVSVHVFKKAADETWEPFASGKTSKTGELHGLTTSEKFVEG

Sheep                         NVGVKVFKKAADETWEPFASGKTSDSGELHGLTTEDKFVEG

Chicken                       NVAVKVFKKAADGTWQDFATGKTTEFGEIHELTTEEQFVEG

Xenopus laevis                NLLVNVFRQTESGKWEQITSGKTTELGEIHNLTTDEQFTEG

Xenopus tropicalis            NLLVQVFRNT-EGNWELISSGKTTELGEIHNIITDEQFTEG

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
Binding site 74 – 74 Thyroid hormones
Modified residue 62 – 62 4-carboxyglutamate; in a patient with Moyamoya disease
Beta strand 61 – 68


Literature citations

A novel transthyretin mutation associated with familial amyloidotic polyneuropathy.
Murakami T.; Maeda S.; Yi S.; Ikegawa S.; Kawashima E.; Onodera S.; Shimada K.; Araki S.;
Biochem. Biophys. Res. Commun. 182:520-526(1992)
Cited for: VARIANT AMYL-TTR ARG-67;

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.