All variants in the MYL2 gene

Information The variants shown are described using the NM_000432.3 transcript reference sequence.

33 entries on 1 page. Showing entries 1 - 33.
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Effect     
Exon     
AscendingDNA change (cDNA)     
RNA change     
Protein     
Type     
DNA change (genomic) (hg19)     
Reference     
DB-ID     
Frequency     
Variant remarks     
ClassClinical     
Owner     
./. 02 c.37G>A - p.Ala13Thr human cosmid - GenBank MYL2_00003 - The amino acid that is mutated, as well as the flanking sequence, shows strong evolutionary conservation. The individual with the Ala13Thr mutation was strikingly similar to that seen in patients with ELC mutations in that is showed the pronounced mid cavity obstruction. - Qi Ming
./. 02 c.37G>A - p.Ala13Thr BL21 expression host cells; Sf9 cells - GenBank MYL2_00003 - A13T mutation, located near the phosphorylation site (Ser-15) of the human cardiac regulatory light chain, had 3-fold lower KCa than wild-type light chain, whereas phosphorylation of this mutant increased the Ca2+ affinity 6-fold. Phosphorylated A13T demonstrated a 15-fold greater affinity for Ca2+ than phosphorylated HCRLC-WT, whereas nonphosphorylated A13T bound Ca2+ with a 3-fold lower affinity than nonphosphorylated-WT. The binding of Ca2+ to the A13T mutant, which had the highesalpha-helical content among all FHC mutants in the apo-state, caused a decrease (not increase) in it's alpha-helical content from 29% to 25%. - Qi Ming
./. 02 c.37G>A - p.Ala13Thr Blood - GenBank MYL2_00003 - No other mutations were identified in this family in the additional seven FHC genes screened. There was no family history of sudden death. - Qi Ming
./. 02 c.37G>A - p.Ala13Thr Blood - GenBank MYL2_00003 - The present results suggest that either the MYL2 mutation or the MYH7 mutation alone may cause HCM respectively, but the presence of both MYL2 and the MYH7 mutation may result in a more severe disease than either mutation alone as seen in the case of the proband. - Qi Ming
./. 02 c.52T>C - p.Phe18Leu Blood - GenBank MYL2_00001 - The Phe18Leu mutation was found in all clinically affected patients, in four unaffected, and in none of the three individuals with - Qi Ming
./. 02 c.52T>C - p.Phe18Leu Human cosmid - GenBank MYL2_00001 - Detected from the mutations in the regulatory light chain. The amino acids that are mutated, as well as he flanking sequence, show strong evolutionary conservation. The cardiac morphology in three patients from two unrelated families with the Glu22Lys mutation was strikingly similar to that seen in patients with ELC mutation. - Qi Ming
./. 02 c.54C>A - p.Phe18Leu BL21 expression host cells; Sf9 cells - GenBank MYL2_00005 - (The article doesn't mention if it's c.54C>A or c.54C>G.) Associated with a typical form of hypertrophic cardiomyopathy, which causes increased left ventricular wall thickness and abnormal electrocardiograph find- ings with no mid-cavity obliteration; decreased the Ca2+ binding affinity ~3-fold compared with HCRLC-WT. No effect of phosphorylation on Ca2+ binding to F18L was observed. - Qi Ming
./. 02 c.54C>A - p.Phe18Leu Blood - GenBank MYL2_00005 - MYL2 mutations are predicted to alter the phosphorylation site and the Ca2+ binding properties. Distribution of the disease genes of the full 197 case series was as follows: MYBPC3, 26%; MYH7, 25%; TNNT2, 4%; TNNI3, 4%; MYL2, 2.5%; and MYL<0.5%. - Qi Ming
./. 02 c.59T>C - p.Met20Thr unknown - GenBank MYL2_00023 NA - - Qi Ming
./. 02 c.64G>A - p.Glu22Lys BL21 expression host cells; Sf9 cells - GenBank MYL2_00006 - The KCa value for E22K was decreased be ~17-fold compared with the wild-type light chain. Was Associated with a particular subtype of cardiac hypertrophy defined by mid-left ventricular obstruction. The phosphorylation of the FHC mutants affected their Ca2+ binding properties and prevented the E22K mutant from becoming phosphorylated. The nonphosphorylated E22K migrates slower than the nonphosphorylated wild-type HCRLC. E22K mutation results in an increase in the alpha-helical content of HCRLC from 18% to 24%. - Qi Ming
./. 02 c.64G>A - p.Glu22Lys Blood - GenBank MYL2_00006 - This base change caused a loss of one of two normal Taq I restriction sites in the exon 2 amplimer allowing its independent confirmation by restriction enzyme digestion. - Qi Ming
./. 02 c.64G>A - p.Glu22Lys BL21 expression host cells - GenBank MYL2_00006 - Affect the Ca2+ ability, the Ca2+sensitivity of ATPase activity and recovered force. - Qi Ming
./. 03 c.132T>C - p.Ile44Ile Blood - GenBank MYL2_00012 - Five more frequent SNPs were located in the exon flanking regions of introns 4 and 5 of MYL2 (three nucleotide substitutions, one insertion and one deletion). - Qi Ming
./. 03 c.141C>A - p.Asn47Lys Blood - GenBank MYL2_00011 - No other mutations were identified in this patient in the additional seven FHC genes screened. There was no family history of sudden death. - Qi Ming
./. 03 c.141C>A - p.Asn47Lys BL21 expression host cells - GenBank MYL2_00011 - Affect the Ca2+ ability, the Ca2+sensitivity of ATPase activity and recovered force. - Qi Ming
./. 03 c.169G>C - p.Gly57Arg unknown - GenBank MYL2_00022 NA - - Qi Ming
./. 04 c.172_173insAG - p.Arg58GlnfsX3 unknown - GenBank MYL2_00021 NA - - Qi Ming
./. 04 c.173G>A - p.Arg58Gln Blood - GenBank MYL2_00002 - The mutation Arg58Gln was found in all affected subjects, in three with - Qi Ming
./. 04 c.173G>A - p.Arg58Gln BL21 expression host cells; Sf9 cells - GenBank MYL2_00002 - Associated with a typical form of hypertrophic cardiomyopathy, which causes increased left ventricular wall thickness and abnormal electrocardiograph findings with no mid-cavity obliteration. Ca2+ binding to the R58Q mutant was restored upon phosphorylation. The R58Q mutation completely impaired Ca2+ binding (did not bind Ca2+ in the nonphosphorylated state but did bind Ca2+ when phosphorylated) The R58Q mutant did not bind Ca2+ in its nonphosphorylated form, and Ca2+ did not significantly affect its alpha-helical content. However, the phosphorylation restored its Ca2+ binding and the amount of alpha-helical content greatly increased on binding of Ca2+ to phosphorylated R58Q. - Qi Ming
./. 04 c.173G>A - p.Arg58Gln Blood - GenBank MYL2_00002 - The Arg58Gln mutation was not observed in 210 control alleles subjected to SSCP analysis or in proband - Qi Ming
./. 04 c.173G>A - p.Arg58Gln Blood - GenBank MYL2_00002 - MYL2 mutations are predicted to alter the phosphorylation site and the Ca2+ binding properties. Distribution of the disease genes of the full 197 case series was as follows: MYBPC3, 26%; MYH7, 25%; TNNT2, 4%; TNNI3, 4%; MYL2, 2.5%; and MYL<0.5%. - Qi Ming
./. 04 c.173G>A - p.Arg58Gln BL21 expression host cells - GenBank MYL2_00002 - Affect the Ca2+ ability, the Ca2+sensitivity of ATPase activity and recovered force. - Qi Ming
./. 04 c.256T>C - p.Phe86Leu unknown - GenBank MYL2_00020 NA - - Qi Ming
./. 05 c.275-2A>G - - Blood - GenBank MYL2_00013 - MYL2 mutations are predicted to alter the phosphorylation site and the Ca2+ binding properties. Distribution of the disease genes of the full 197 case series was as follows: MYBPC3, 26%; MYH7, 25%; TNNT2, 4%; TNNI3, 4%; MYL2, 2.5%; and MYL<0.5%. - Qi Ming
./. 05 c.283C>G - p.Pro95Ala BL21 expression host cells; Sf9 cells - GenBank MYL2_00007 - Associated with a particular subtype of cardiac hypertrophy defined by mid-left ventricular obstruction; decreased the Ca2+ binding affinity 3-fold compared with HCRLC-WT. P95A mutant also had an increase in alpha-helical content upon Ca2+ binding. - Qi Ming
./. 05 c.283C>G - p.Pro95Ala BL21 expression host cells - GenBank MYL2_00007 - Affect the Ca2+ ability, the Ca2+sensitivity of ATPase activity and recovered force. - Qi Ming
./. 05 c.284C>G - p.Pro95Arg Human cosmid - GenBank MYL2_00004 - Shows strong evolutionary conservation. The Pro94Arg mutations inhuman RLC map to the interface between the COOH- and NH2 terminal domains of the RLC. - Qi Ming
./. 06 c.354-1G>C - - Blood - GenBank MYL2_00014 - - - Qi Ming
./. 06 c.359G>A - p.Arg120Gln unknown - GenBank MYL2_00019 NA - - Qi Ming
./. 06 c.380C>T - p.Ala127Val unknown - GenBank MYL2_00018 NA - - Qi Ming
./. 06 c.401A>C - p.Glu134Ala unknown - GenBank MYL2_00017 NA - - Qi Ming
./. 07 c.418G>A - p.Ala140Thr unknown - GenBank MYL2_00016 NA - - Qi Ming
./. 07 c.459G>C - p.Lys153Asn unknown - GenBank MYL2_00015 NA - - Qi Ming
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