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Table 2 Annotations for cytoplasmic aaRSs - mutations that were observed to be naturally present in corresponding mammalian aaRSs are highlighted (bold)

From: Evolutionary and structural annotation of disease-associated mutations in human aminoacyl-tRNA synthetases

aaRS Mutation Sequence spread in homologs (%) Structure RSA Intermolecular interaction Domain References
GRS (II) Ala111Val ‘A’: 77, ‘S’: 21, ‘E’: 1, ‘-’: 1 NA NA - - [3339]
Glu125Gly ‘E’: 84, ‘-’: 10, ‘D’: 6 H 22.7 - -
Pro152Leu ‘P’: 99, ‘-’: 1 H 75.0 Dimerization -
Leu183Pro ‘L’: 90, ‘-’: 8, ‘M’: 1, ‘V’: 1 E 54.3 Dimerization Catalytic
Cys211Arg ‘C’: 100 E 34.8 Dimerization Catalytic
Pro288Lys ‘P’: 98, ‘-’: 2 S 94.1 Dimerization Catalytic
Gly294Arg ‘G’: 81, ‘-’: 16, ‘P’: 1, ‘K’: 1, ‘T’: 1 E 0.0 - Catalytic
Pro298Leu ‘P’: 97, ‘-’: 3 S 0.7 - Catalytic
Ile334Phe ‘I’: 81, ‘-’: 8, ‘L’: 8, ‘V’: 2, ‘C’: 1 S 11.2 Dimerization Catalytic
His472Arg ‘H’: 80, ‘-’: 20 H 3.3 - -
Asp554Asn ‘D’: 81, ‘-’: 8, ‘K’: 7, ‘G’: 2, ‘N’: 1, ‘S’: 1 - - - -
Gly580Arg ‘G’: 92, ‘-’: 8 E 14.3 - -
Ser635Leu ‘S’: 83, ‘-’: 8, ‘T’: 7, ‘A’: 2 H 24.6 - C-terminal
Gly652Ala ‘G’: 85, ‘H’: 8, ‘-’: 7 S 46.4 - C-terminal
LRS (I) Lys82Arg ‘K’: 81, ‘-’: 18, ‘N’: 1 - 22.4 - Catalytic [40]
Tyr373Cys ‘Y’: 100 E 21.3 - Catalytic
YRS (I) Gly41Arg ‘G’: 74, ‘-’: 26 E 40.4 ATP/amino-acid binding Catalytic [41]
Glu196Lys ‘E’: 74, ‘-’: 25, ‘P’: 1 H 16.9 - Catalytic
ARS (I) Asn71Tyr ‘N’: 97, ‘-’: 3 E 0.0 - Catalytic [4244]
Arg329His ‘R’: 98, ‘-’: 2 H 4.3 - Catalytic
Glu778Ala ‘E’: 79, ‘T’: 10, ‘A’: 6, ‘G’: 2, ‘S’: 2, ‘V’: 1 - - - -
Asp893Asn ‘D’: 75, ‘P’: 21, ‘N’: 2, ‘X’: 1, ‘-’: 1 - - - -
KRS (II) Leu133His ‘L’: 100 H 2.4   Anti-codon binding [45, 46]
Ile302Met ‘I’: 100 S 29.5   Catalytic
Thr623Ser ‘T’: 77, ‘P’: 16, ‘-’: 4, ‘A’: 1, ‘M’: 1, ‘V’: 1 - -   -
  1. RSA values (%) in bold indicate buried positions that were ordered in the crystal structures. Also see Figure 2.