Mutations in RYR1

# Exon Nucleotide Aminoacid
1 2 c.103T>C p.Cys35Arg
2 2 c.130C>T p.Arg44Cys
3 6 c.487C>T p.Arg163Cys
4 6 c.488G>T p.Arg163Leu
5 9 c.742G>A p.Gly248Arg
6 9 c.742G>C p.Gly248Arg
7 11 c.982C>T p.Arg328Trp
8 11 c.1021G>C p.Gly341Arg
9 11 c.1021G>A p.Gly341Arg
10 12 c.1201C>T p.Arg401Cys
11 12 c.1209C>G p.Ile403Met
12 14 c.1565A>C p.Tyr522Ser
13 15 c.1597C>T p.Arg533Cys
14 15 c.1598G>A p.Arg533His
15 15 c.1654C>T p.Arg552Trp
16 17 c.1840C>T p.Arg614Cys
17 17 c.1841G>T p.Arg614Leu
18 39 c.6487C>T p.Arg2163Cys
19 39 c.6488G>A p.Arg2163His
20 39 c.6502G>A p.Val2168Met
21 40 c.6617C>G p.Thr2206Arg
22 40 c.6617C>T p.Thr2206Met
23 43 c.7007G>A p.Arg2336His
24 44 c.7042_7045delinsdel p.Gln2348del
25 44 c.7048G>A p.Ala2350Thr
26 44 c.7063C>T p.Arg2355Trp
27 44 c.7124G>C p.Gly2375Ala
28 45 c.7282G>A p.Ala2428Thr
29 45 c.7300G>A p.Gly2434Arg
30 45 c.7304G>A p.Arg2435His
31 46 c.7354C>T p.Arg2452Trp
32 46 c.7360C>T p.Arg2454Cys
33 46 c.7361G>A p.Arg2454His
34 46 c.7372C>T p.Arg2458Cys
35 46 c.7373G>A p.Arg2458His
36 47 c.7522C>T p.Arg2508Cys
37 47 c.7522C>A p.Arg2508Gly
38 47 c.7523G>A p.Arg2508His
39 63 c.9310G>A p.Glu3004Lys
40 87 c.11969G>T p.Gly3990Val
41 100 c.14387A>G p.Tyr4796Cys
42 100 c.14477C>T p.Thr4826Ile
43 100 c.14497C>T p.His4833Tyr
44 101 c.14512C>G p.Leu4838Val
45 101 c.14545G>A p.Val4849Ile
46 101 c.14582G>A p.Arg4861His
47 102 c.14693T>C p.Ile4898Thr

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