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UniProtKB/Swiss-Prot P0DP24: Variant p.Asn98Ser

Calmodulin-2
Gene: CALM2
Variant information

Variant position:  98
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  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:  From Asparagine (N) to Serine (S) at position 98 (N98S, p.Asn98Ser).
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 (N) to small size and polar (S)
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:  In LQT15; the mutant has significantly reduced calcium affinity compared to wild-type; calmodulin-RYR2 interaction is defective at low intracellular Ca(2+) concentrations and restored at moderate to high Ca(2+) concentrations; increased RYR2 calcium-release channel activity; decreased calcium-dependent inactivation of L-type calcium channel; not changed protein abundance; not changed structure; significantly reduced ryanodine-sensitive calcium-release channel activity; decreased of KCNN2 calcium-activated potassium channel activity; not changed KCNN2 expression; not changed KCNN2 location at membrane.
Any additional useful information about the variant.

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



Sequence information

Variant position:  98
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Protein sequence length:  149
The length of the canonical sequence.

Location on the sequence:   KDTDSEEEIREAFRVFDKDG  N GYISAAELRHVMTNLGEKLT
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                         KDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLT

Mouse                         KDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLT

Rat                           KDTDSEEEIREAFRVFDKDGNGYISAAELRHVMTNLGEKLT

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 – 149 Calmodulin-2
Domain 81 – 116 EF-hand 3
Calcium binding 94 – 105 3
Region 77 – 149 Necessary and sufficient for interaction with PCP4
Modified residue 82 – 82 Phosphoserine
Modified residue 95 – 95 N6-acetyllysine
Modified residue 100 – 100 Phosphotyrosine
Modified residue 102 – 102 Phosphoserine
Modified residue 111 – 111 Phosphothreonine
Modified residue 116 – 116 N6,N6,N6-trimethyllysine; alternate
Modified residue 116 – 116 N6-methyllysine; alternate
Beta strand 98 – 101


Literature citations

Novel calmodulin mutations associated with congenital arrhythmia susceptibility.
Makita N.; Yagihara N.; Crotti L.; Johnson C.N.; Beckmann B.M.; Roh M.S.; Shigemizu D.; Lichtner P.; Ishikawa T.; Aiba T.; Homfray T.; Behr E.R.; Klug D.; Denjoy I.; Mastantuono E.; Theisen D.; Tsunoda T.; Satake W.; Toda T.; Nakagawa H.; Tsuji Y.; Tsuchiya T.; Yamamoto H.; Miyamoto Y.; Endo N.; Kimura A.; Ozaki K.; Motomura H.; Suda K.; Tanaka T.; Schwartz P.J.; Meitinger T.; Kaeaeb S.; Guicheney P.; Shimizu W.; Bhuiyan Z.A.; Watanabe H.; Chazin W.J.; George A.L. Jr.;
Circ. Cardiovasc. Genet. 7:466-474(2014)
Cited for: INVOLVEMENT IN LQT15; VARIANTS LQT15 ILE-98; SER-98; GLU-132; HIS-134 AND PRO-136; CHARACTERIZATION OF VARIANTS LQT15 ILE-98; GLU-132; HIS-134 AND PRO-136;

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.