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Table 3 Structural comparisons of disease causing mutant versions of UCHL1 protein

From: Molecular evolutionary and structural analysis of human UCHL1 gene demonstrates the relevant role of intragenic epistasis in Parkinson’s disease and other neurological disorders

Mutations Major changes in residue number Major shifts in region Critical region
Ile93Met 23–24 C12-peptidase Domain 32–39 (Secretion, Signal Motif)
32–38 Secretion signal Motif
45,74–75  
136,148  
222–223 Farnesylation site
Glu7Ala 22–25 C12- peptidase Domain 32–39(Secretion, Signal Motif)
31–38 Secretion signal Motif
45,74–75  
111–112  
190–191,136 CK2 Phosphorylation site
Ser18Tyr 23–25, C12 peptidase Domain 32–39 (Secretion, Signal Motif)
31–38, Secretion signal Motif
45,74–75  
111–112  
150–152  
148,136  
222–223 Farnesylation site
Arg178Gln 23–24 C12-peptidase Domain 32–39(Secretion, Signal Motif
32–39 Secretion signal Motif
136,74  
221–223 Farnesylation site
Ala216Asp 23–24 C12-peptidase Domain  
74–75   ___
136,148   
222–223 Farnesylation site  
  1. This table shows the impact of PD (Parkinson’s disease) and other neurological disorders causing missense mutations on backbone torsion angles of human UCHL1 protein. In the first column, amino acid residue on the left indicates the wild-type residue, whereas the residue on the right is mutated version; number indicates the amino acid position. The second column specifies the positions at which major structural deviations are observed. The third column depicts the deviated region. The fourth column depicts deviated residues shared among all mutant structures of UCHL1 protein