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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P63316: Variant p.Cys84Tyr

Troponin C, slow skeletal and cardiac muscles
Gene: TNNC1
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Variant information Variant position: help 84 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 Cysteine (C) to Tyrosine (Y) at position 84 (C84Y, p.Cys84Tyr). 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 medium size and polar (C) to large size and aromatic (Y) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In CMH13; increases calcium sensitivity of the myofilaments. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 84 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 161 The length of the canonical sequence.
Location on the sequence: help VDEDGSGTVDFDEFLVMMVR C MKDDSKGKSEEELSDLFRMF 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                         VDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMF

Mouse                         VDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMF

Pig                           VDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMF

Bovine                        VDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMF

Rabbit                        VDEDGSGTVDFDEFLVMMVRCMKDDSKGKSEEELSDLFRMF

Chicken                       VDEDGSGTVDFDEFLVMMVRCMKDDSKGKTEEELSDLFRMF

Drosophila                    VDEDGSGQIEFEEFTTLAARFLVEEDAEAMMAELKEAFRLY
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 1 – 161 Troponin C, slow skeletal and cardiac muscles
Domain 52 – 87 EF-hand 2
Binding site 65 – 65
Binding site 67 – 67
Binding site 69 – 69
Binding site 71 – 71
Binding site 76 – 76
Modified residue 98 – 98 Phosphoserine
Helix 74 – 85



Literature citations
Molecular and functional characterization of novel hypertrophic cardiomyopathy susceptibility mutations in TNNC1-encoded troponin C.
Landstrom A.P.; Parvatiyar M.S.; Pinto J.R.; Marquardt M.L.; Bos J.M.; Tester D.J.; Ommen S.R.; Potter J.D.; Ackerman M.J.;
J. Mol. Cell. Cardiol. 45:281-288(2008)
Cited for: VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145; CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145; A functional and structural study of troponin C mutations related to hypertrophic cardiomyopathy.
Pinto J.R.; Parvatiyar M.S.; Jones M.A.; Liang J.; Ackerman M.J.; Potter J.D.;
J. Biol. Chem. 284:19090-19100(2009)
Cited for: CHARACTERIZATION OF VARIANTS CMH13 VAL-8; TYR-84; ASP-134 AND GLU-145;
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.