Variant position: 167 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 399 The length of the canonical sequence.
Location on the sequence:
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 EIISSKLEVQAFERIEDYIK LIGFFKSEDSEYYKAFEEAAE
Mouse EIVNNKLEVQAFERIEDQTK LLGFFKNEDSEYYKAFQEAAE
Rat EIVNNKLEVQAFERIEDQIK LLGFFKNEDSEYYKAFQEAAE
Rabbit EIINSKLEVQAFERIEDHIK LIGFFKSADSEYYKAFEEAAE
Chicken EVINSKLELQAFDQIDDEIK LIGYFKGEDSEHYKAFEEAAE
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.
Type Positions Description
20 – 399 Calsequestrin-2
107 – 178 GFDEEGSLYILKGDRTIEFDGEFAADVLVEFLLDLIEDPVEIISSKLEVQAFERIEDYIKLIGFFKSEDSEY -> D. In isoform 2.
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.;
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;
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