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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P19429: Variant p.Arg162Pro

Troponin I, cardiac muscle
Gene: TNNI3
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Variant information Variant position: help 162 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 Arginine (R) to Proline (P) at position 162 (R162P, p.Arg162Pro). 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 basic (R) to medium size and hydrophobic (P) 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 CMH7. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 162 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 210 The length of the canonical sequence.
Location on the sequence: help PTLRRVRISADAMMQALLGA R AKESLDLRAHLKQVKKEDTE 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                         PTLR-RVRISADAMMQALLGARAKESLDLRAHLKQV---KKEDTE

                              PTLR-RVRISADAMMQALLGTRAKESLDLRAHLKQV---KK

Mouse                         PTLR-RVRISADAMMQALLGTRAKESLDLRAHLKQV---KK

Rat                           PTLR-RVRISADAMMQALLGTRAKESLDLRAHLKQV---KK

Bovine                        PTLR-RVRISADAMMQALLGARAKETLDLRAHLKQV---KK

Rabbit                        PTLRLRVRISADAMMQALLGTRAKETLDLRAHLKQV---KK

Cat                           PTLR-RVRISADAMMQALLGTRAKESLDLRAHLKQV---KK

Horse                         PTLR-RVRISADAMMQALLGTRAKETLDLRAHLKQV---KK

Xenopus laevis                PNLR-RVRLSADAMMMALLGTKHKVSMDLRANLKQVKQTKK

Caenorhabditis elegans        PTLK-KVSKYDNKFKSS---GEVKEKSNFRNNLKVV---KK
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 2 – 210 Troponin I, cardiac muscle
Modified residue 143 – 143 Phosphothreonine; by STK4/MST1
Modified residue 150 – 150 Phosphoserine; by PAK3
Modified residue 166 – 166 Phosphoserine
Modified residue 181 – 181 Phosphothreonine
Helix 160 – 162



Literature citations
Hypertrophic cardiomyopathy: distribution of disease genes, spectrum of mutations, and implications for a molecular diagnosis strategy.
Richard P.; Charron P.; Carrier L.; Ledeuil C.; Cheav T.; Pichereau C.; Benaiche A.; Isnard R.; Dubourg O.; Burban M.; Gueffet J.-P.; Millaire A.; Desnos M.; Schwartz K.; Hainque B.; Komajda M.;
Circulation 107:2227-2232(2003)
Cited for: VARIANTS CMH7 GLN-141; VAL-157; PRO-162; LYS-177 DEL; GLN-186 AND ASN-196; Compound and double mutations in patients with hypertrophic cardiomyopathy: implications for genetic testing and counselling.
Ingles J.; Doolan A.; Chiu C.; Seidman J.; Seidman C.; Semsarian C.;
J. Med. Genet. 42:E59-E59(2005)
Cited for: VARIANTS CMH7 PRO-162; GLN-162 AND HIS-204;
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.