Mutations in RYR1

# Exon Nucleotide Aminoacid
1 2 c.103T>C p.35Cys>Arg
2 6 c.487C>T p.163Arg>Cys
3 6 c.488G>T p.163Arg>Leu
4 9 c.742G>A p.248Gly>Arg
5 9 c.742G>C p.248Gly>Arg
6 11 c.1021G>A p.341Gly>Arg
7 12 c.1201C>T p.401Arg>Cys
8 12 c.1209C>G p.403Ile>Met
9 14 c.1565A>C p.522Tyr>Ser
10 15 c.1589G>A p.530Arg>His
11 15 c.1654C>T p.552Arg>Trp
12 17 c.1840C>T p.614Arg>Cys
13 17 c.1841G>T p.614Arg>Leu
14 39 c.6487C>T p.2163Arg>Cys
15 39 c.6488G>A p.2163Arg>His
16 39 c.6502G>A p.2168Val>Met
17 40 c.6617C>G p.2206Thr>Arg
18 40 c.6617C>T p.2206Thr>Met
19 43 c.7007G>A p.2336Arg>His
20 44 c.7042GAG>del p.2348Gln>del
21 44 c.7048G>A p.2350Ala>Thr
22 44 c.7063C>T p.2355Arg>Trp
23 44 c.7124G>C p.2375Gly>Ala
24 45 c.7282G>A p.2428Ala>Thr
25 45 c.7300G>A p.2434Gly>Arg
26 45 c.7304G>A p.2435Arg>His
27 46 c.7354C>T p.2452Arg>Trp
28 46 c.7360C>T p.2454Arg>Cys
29 46 c.7361G>A p.2454Arg>His
30 46 c.7372C>T p.2458Arg>Cys
31 46 c.7373G>A p.2458Arg>His
32 47 c.7522C>T p.2508Arg>Cys
33 47 c.7523G>A p.2508Arg>His
34 63 c.9310G>A p.3104Glu>Lys
35 87 c.11969G>T p.3990Gly>Val
36 100 c.14387A>G p.4796Tyr>Cys
37 100 c.14477C>T p.4826Thr>Ile
38 100 c.14497C>T p.4833His>Tyr
39 101 c.14512C>G p.4838Leu>Val
40 101 c.14545G>A p.4849Val>Ile
41 101 c.14582G>A p.4861Arg>His
42 102 c.14693T>C p.4898Ile>Thr

Mutations in CACNA1S

There are currently two mutations in the dihydropyridine recepter (Gen: CACNA1S) which are accepted as diagnostic mutations by the EMHG.

  • p.Arg1086His  c.3257G>A
  • p.Arg174Trp   c.520C>T 

References:

Weiss RG, O’Connell KM, Flucher BE, Allen PD, Grabner M, Dirksen RT.  Functional analysis of the R1086H malignant hyperthermia mutation in the DHPR reveals an unexpected influence of the III-IV loop on skeletal muscle EC coupling. Am J Physiol Cell Physiol 2004; 287: C1094-102

Eltit JM, Bannister RA, Moua O, Altamirano F, Hopkins PM, Pessah IN, Molinski TF, Lopez JR, Beam KG, Allen PD: Malignant hyperthermia susceptibility arising from altered resting coupling between the skeletal muscle L-type Ca2+ channel and the type 1 ryanodine receptor. Proc Natl Acad Sci U S A 2012; 109: 7923-8