Table 2 CTSA gene point mutations and significance
From: Galactosialidosis: review and analysis of CTSA gene mutations
Mutation | Ex. | Phe. | Mut Pred computational analysis | PPCA three-dimensional reported outputs (Zhou et al. 1996 [[22]]; Rudenko et al. 1998 [[19]]; Takiguchi et al 2000 [[23]]) | Philogenetic conservation | Ref. | ||||
|---|---|---|---|---|---|---|---|---|---|---|
P. | Actionable hypotheses | Confident hypothesis | Very confident hypothesis | SIFT score | Polyphen score | |||||
(g > 0.5, p < 0.05) | (g > 0.75, p < 0.05) | (g > 0.75, p < 0.01) | ||||||||
p.Gln67Arg | 2 | EI | 0.941 | Gain of MoRF binding | Drastically alters folding and stability | T (0,07) | D (0,996) | Shimmoto 1993 [21] | ||
p.Ser69Tyr | 2 | EI | 0.942 | Loss of disorder | Drastically alters folding and stability | D (0,00) | D (1,000) | Zhou 1996 [22] | ||
p.Val83Arg | 2 | EI | 0.957 | Gain of methylation | Gain of disorder | Drastically alters folding and stability | D (0,00) | D (1,000) | Shimmoto 1993 [21] | |
p.Gly103Ser | 3 | EI | 0.974 | D (0,00) | D (1,000) | Groener 2003 [17] | ||||
p.Gly103Val | 3 | EI | 0.962 | D (0,00) | D (1,000) | Kiss 2008 [18] | ||||
p.Ser108Leu | 3 | EI | 0.962 | Loss of disorder | Drastically alters folding and stability | D (0,00) | D (1,000) | Shimmoto 1993 [21] | ||
p.His116Arg | 3 | EI | 0.712 | Gain of methylation | T (0,45) | D (0,999) | This work | |||
p.Val150Met | 5 | EI | 0.947 | Loss of catalytic residue | Drastically alters folding and stability | D (0,00) | D (1,00) | Zhou 1996 [22] | ||
p.Leu254Pro | 8 | EI | 0.921 | Loss of stability; Gain of catalytic residue | Drastically alters folding and stability | D (0,00) | D (1,000) | Zhou 1996 [22] | ||
p.Cys259Arg | 8 | EI | 0.726 | Gain of disorder; Loss of ubiquitination | D (0,00) | D (1,00) | This work | |||
Tyr267Asn | 8 | LI | 0.798 | Gain of disorder; Loss of stability | Milder effect on protein function and residual mature PPCA | D (0,04) | B (0,189) | Shimmoto 1993 [21] | ||
Tyr413Cys | 13 | EI | 0.933 | Drastically alters folding and stability | D (0,00) | D (1,000) | Shimmoto 1993 [21] | |||
p.Met424Tyr | 13 | EI/LI | 0.804 | Generation of a glycosylation site and destabilization of dimerisation | D (0,01) | B (0,214) | Zhou 1996 [22] | |||
p.Arg442Trp | 14 | LI | 0.697 | D (0,01) | D (1,000) | Kiss 2008 [18] | ||||
p.Gly457Ser | 14 | EI | 0.948 | Drastically alters folding and stability | D (0,01) | D (1,000) | Zhou 1996 [22] | |||
p.Phe458Val | 14 | LI | 0.867 | Milder effect on protein function, destabilization or defective dimerisation of the precursor | T (0,15) | D (0,990) | Zhou 1991 [20] | |||
p.Lys471Glu | 14 | J/A | 0.893 | Loss of methylation | Milder effect on protein function, destabilization or defective dimerisation of the precursor | T (0,21) | D (1,000) | Takiguchi 2000 [23] | ||