Table 2.
Position | Mutant | Rate | Aggregation Conditions | Ref. |
---|---|---|---|---|
N-terminus | Ac-αSa | 0 | PBS, 137 mM NaCl, pH 7.4, 140 μM αS, 600 rpm | [168] |
Lys6 | K6Ub | −1 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Lys10 | K10Ub | −1 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Lys12 | K12Ub | −1 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Lys21 | K21Ub | −1 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Lys23 | K23Ub | −1 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Lys32 | K32Ub | −2 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Lys34 | K34Ub | −2 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Tyr39 | nY39 | −1 | 50 mM Tris, 150 mM NaCl, pH 7.5, 10 μM αS, 1000 rpm | [99] |
pY39 | −2 | 20 mM Tris, 100 mM NaCl, pH 7.4, 100 μM αS, 1300 rpm | [102] | |
Lys46 | K46Ub | −2 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] |
Thr72 | gT72 | −2 | 10 mM phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [189] |
Thr75 | gT75 | −2 | 10 mM phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [189] |
Thr81 | gT81 | −2 | 10 mM phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [189] |
Ser87 | gS87 | −2 | 10 mM phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [187] |
pS87, S129Ab | −2 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [164] | |
Lys96 | K96 SUMO1 | −2 | 10 mM sodium phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [178] |
K96 SUMO3 | −1 | 10 mM sodium phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [178] | |
K96Ub | −2 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [103] | |
Lys102 | K102 SUMO1 | −2 | 10 mM sodium phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [178] |
K102 SUMO3 | −2 | 10 mM sodium phosphate, 0.05% NaN3, pH 7.4, 50 μM αS, 1000 rpm | [178] | |
Tyr125 | nY125 | −2 | 50 mM Tris, 150 mM NaCl, pH 7.5, 10 μM αS, 1000 rpm | [99] |
pY125 | −2 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [162] | |
Ser129 | pS129 | −1 | 10 mM PBS, 0.05% NaN3, pH 7.4, 100 μM αS, shaking | [162] |
There is significant disagreement in the literature on the effect of N-terminal acetylation on aggregation.
While all other mutations and PTMs are presented as single site modifications, pS87 is included with the accompanying S129A mutation since those were the only data available. It is scored as −1 using the S129A aggregation rate as a pseudo-WT control to isolate the effect of Ser87 phosphorylation.