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UniProtKB/Swiss-Prot P06753: Variant p.Thr253Lys

Tropomyosin alpha-3 chain
Gene: TPM3
Variant information

Variant position:  253
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 Threonine (T) to Lysine (K) at position 253 (T253K, p.Thr253Lys).
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 medium size and polar (T) to large size and basic (K)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -1
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:  Probable disease-associated mutation found in patients with undefined congenital myopathy.
Any additional useful information about the variant.

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



Sequence information

Variant position:  253
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  285
The length of the canonical sequence.

Location on the sequence:   LKEAETRAEFAERSVAKLEK  T IDDLEDELYAQKLKYKAISE
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                         LKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISE

Mouse                         LKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISD

Rat                           LKEAETRAEFAERSVAKLEKTIDDLEDKLKCTKEEHLCTQR

Pig                           LKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISE

Bovine                        LKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISE

Caenorhabditis elegans        LKEAETRAEFAERSVQKLQKEVDRLEDELLLEKERVRNLTE

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 2 – 285 Tropomyosin alpha-3 chain
Coiled coil 1 – 285
Modified residue 253 – 253 Phosphothreonine
Modified residue 262 – 262 Phosphotyrosine
Modified residue 272 – 272 Phosphoserine


Literature citations

Mutation update and genotype-phenotype correlations of novel and previously described mutations in TPM2 and TPM3 causing congenital myopathies.
Marttila M.; Lehtokari V.L.; Marston S.; Nyman T.A.; Barnerias C.; Beggs A.H.; Bertini E.; Ceyhan-Birsoy O.; Cintas P.; Gerard M.; Gilbert-Dussardier B.; Hogue J.S.; Longman C.; Eymard B.; Frydman M.; Kang P.B.; Klinge L.; Kolski H.; Lochmueller H.; Magy L.; Manel V.; Mayer M.; Mercuri E.; North K.N.; Peudenier-Robert S.; Pihko H.; Probst F.J.; Reisin R.; Stewart W.; Taratuto A.L.; de Visser M.; Wilichowski E.; Winer J.; Nowak K.; Laing N.G.; Winder T.L.; Monnier N.; Clarke N.F.; Pelin K.; Groenholm M.; Wallgren-Pettersson C.;
Hum. Mutat. 35:779-790(2014)
Cited for: VARIANTS NEM1 PHE-88 AND CYS-168; VARIANTS CAPM1 PHE-88; ALA-151; CYS-168 AND ILE-245; VARIANTS CFTD VAL-100; CYS-168 AND HIS-168; VARIANTS CYS-91 AND LYS-253;

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.