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UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P10916: Variant p.Arg58Gln

Myosin regulatory light chain 2, ventricular/cardiac muscle isoform
Gene: MYL2
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Variant information Variant position: help 58 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 Glutamine (Q) at position 58 (R58Q, p.Arg58Gln). 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 polar (Q) 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; impairs calcium binding; bind calcium upon phosphorylation. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 58 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 QNRDGFIDKNDLRDTFAALG R VNVKNEEIDEMIKEAPGPIN 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                         QNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPIN

Mouse                         QNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPIN

Rat                           QNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPIN

Bovine                        QNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMLKEAPGPIN

Rabbit                        QNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPIN
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
Domain 24 – 59 EF-hand 1
Binding site 39 – 39
Binding site 41 – 41
Binding site 48 – 48
Modified residue 52 – 52 Phosphothreonine



Literature citations
Identification of two novel mutations in the ventricular regulatory myosin light chain gene (MYL2) associated with familial and classical forms of hypertrophic cardiomyopathy.
Flavigny J.; Richard P.; Isnard R.; Carrier L.; Charron P.; Bonne G.; Forissier J.F.; Desnos M.; Dubourg O.; Komajda M.; Schwartz K.; Hainque B.;
J. Mol. Med. 76:208-214(1998)
Cited for: VARIANTS CMH10 LEU-18 AND GLN-58; 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; Identification of the genotypes causing hypertrophic cardiomyopathy in northern Sweden.
Moerner S.; Richard P.; Kazzam E.; Hellman U.; Hainque B.; Schwartz K.; Waldenstroem A.;
J. Mol. Cell. Cardiol. 35:841-849(2003)
Cited for: VARIANT CMH10 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.