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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10916: Variant p.Glu22Lys

Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Gene: MYL2
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Variant information Variant position: help 22 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 Glutamate (E) to Lysine (K) at position 22 (E22K, p.Glu22Lys). 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 acidic (E) to large size and basic (K) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help 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: help In CMH10; some patients present with mid-left ventricular chamber thickening; significantly decrease calcium binding affinity; loss of phosphorylation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 22 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 166 The length of the canonical sequence.
Location on the sequence: help APKKAKKRAGGANSNVFSMF E QTQIQEFKEAFTIMDQNRDG 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                         APKKAKKRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDG

Mouse                         APKKAKKRIEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDG

Rat                           SPKKAKKRLEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDG

Bovine                        SPKKAKKRAEGANYNVFSMFEQTQIQEFKEAFTIMDQNRDG

Rabbit                        SPKKAKKRAEGANSNVFSMFEQTQIQEFKEAFTIMDQNRDG
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 – 166 Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Binding site 37 – 37
Binding site 39 – 39
Binding site 41 – 41
Modified residue 2 – 2 N,N,N-trimethylalanine
Modified residue 14 – 14 Deamidated asparagine
Modified residue 15 – 15 Phosphoserine; by ZIPK/DAPK3
Modified residue 19 – 19 Phosphoserine



Literature citations
Mutations in either the essential or regulatory light chains of myosin are associated with a rare myopathy in human heart and skeletal muscle.
Poetter K.; Jiang H.; Hassanzadeh S.; Master S.R.; Chang A.; Dalakas M.C.; Rayment I.; Sellers J.R.; Fananapazir L.; Epstein N.D.;
Nat. Genet. 13:63-69(1996)
Cited for: VARIANTS CMH10 THR-13; LYS-22 AND ALA-95; Familial hypertrophic cardiomyopathy mutations in the regulatory light chains of myosin affect their structure, Ca2+ binding, and phosphorylation.
Szczesna D.; Ghosh D.; Li Q.; Gomes A.V.; Guzman G.; Arana C.; Zhi G.; Stull J.T.; Potter J.D.;
J. Biol. Chem. 276:7086-7092(2001)
Cited for: VARIANTS CMH10 THR-13; LEU-18; LYS-22; GLN-58 AND ALA-95; CHARACTERIZATION OF VARIANTS CMH10 THR-13; LEU-18; LYS-22; GLN-58 AND ALA-95; Systematic analysis of the regulatory and essential myosin light chain genes: genetic variants and mutations in hypertrophic cardiomyopathy.
Kabaeva Z.T.; Perrot A.; Wolter B.; Dietz R.; Cardim N.; Correia J.M.; Schulte H.D.; Aldashev A.A.; Mirrakhimov M.M.; Osterziel K.J.;
Eur. J. Hum. Genet. 10:741-748(2002)
Cited for: VARIANTS CMH10 LYS-22 AND GLN-58;
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.