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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot O14958: Variant p.Leu167His

Calsequestrin-2
Gene: CASQ2
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Variant information Variant position: help 167 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 Leucine (L) to Histidine (H) at position 167 (L167H, p.Leu167His). 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 hydrophobic (L) to medium size and polar (H) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -3 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 CPVT2; alters protein folding; reduces calcium-binding; reduces calcium-dependent oligomerization; decreases sarcoplasmic reticulum Ca(2+) storing capacity; reduces the amplitude of I(Ca)-induced Ca(2+) transients; reduces spontaneous Ca(2+) sparks in permeabilized myocytes. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 167 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 399 The length of the canonical sequence.
Location on the sequence: help EIISSKLEVQAFERIEDYIK L IGFFKSEDSEYYKAFEEAAE 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                         EIISSKLEVQAFERIEDYIKLIGFFKSEDSEYYKAFEEAAE

                              EIINSKLEVQAFERIEDQIKLIGFFKSEESEYYKAFEEAAE

Mouse                         EIVNNKLEVQAFERIEDQTKLLGFFKNEDSEYYKAFQEAAE

Rat                           EIVNNKLEVQAFERIEDQIKLLGFFKNEDSEYYKAFQEAAE

Rabbit                        EIINSKLEVQAFERIEDHIKLIGFFKSADSEYYKAFEEAAE

Chicken                       EVINSKLELQAFDQIDDEIKLIGYFKGEDSEHYKAFEEAAE
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 20 – 399 Calsequestrin-2
Alternative sequence 107 – 178 GFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEY -> D. In isoform 2.
Beta strand 166 – 170



Literature citations
Characterization of human cardiac calsequestrin and its deleterious mutants.
Kim E.; Youn B.; Kemper L.; Campbell C.; Milting H.; Varsanyi M.; Kang C.;
J. Mol. Biol. 373:1047-1057(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (3.8 ANGSTROMS) OF 22-399; SUBUNIT; FUNCTION; CHARACTERIZATION OF VARIANTS CPVT2 GLN-33; HIS-167 AND HIS-307; CHARACTERIZATION OF VARIANTS ALA-66 AND MET-76; Clinical phenotype and functional characterization of CASQ2 mutations associated with catecholaminergic polymorphic ventricular tachycardia.
di Barletta M.R.; Viatchenko-Karpinski S.; Nori A.; Memmi M.; Terentyev D.; Turcato F.; Valle G.; Rizzi N.; Napolitano C.; Gyorke S.; Volpe P.; Priori S.G.;
Circulation 114:1012-1019(2006)
Cited for: VARIANT CPVT2 HIS-167; CHARACTERIZATION OF VARIANT CPVT2 HIS-167; FUNCTION; Catecholaminergic polymorphic ventricular tachycardia-related mutations R33Q and L167H alter calcium sensitivity of human cardiac calsequestrin.
Valle G.; Galla D.; Nori A.; Priori S.G.; Gyorke S.; de Filippis V.; Volpe P.;
Biochem. J. 413:291-303(2008)
Cited for: VARIANTS CPVT2 GLN-33 AND HIS-167; CHARACTERIZATION OF VARIANTS CPVT2 GLN-33 AND HIS-167; FUNCTION;
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.