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Literature summary for 6.1.1.14 extracted from

  • Antonellis, A.; Lee-Lin, S.Q.; Wasterlain, A.; Leo, P.; Quezado, M.; Goldfarb, L.G.; Myung, K.; Burgess, S.; Fischbeck, K.H.; Green, E.D.
    Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons (2006), J. Neurosci., 26, 10397-10406.
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
gene GARS, allele-specific expression analysis, expression of wild-type enzyme in Escherichia coli strain BL21(DE3), expression of EGFP-tagged enzyme in COS-7 cells, wild-type GARS-EGFP associates with granules in both the cell body and neurite projections of 42% of EGFP-positive transfected MN-1 cells Homo sapiens

Protein Variants

Protein Variants Comment Organism
E71G modeled in yeast the mutation causes growth defects and impaired viability Homo sapiens
G240R the GARS mutation does not impair transcription or translation, modeled in yeast the mutation causes growth defects and impaired viability Homo sapiens
G526R modeled in yeast the mutation causes growth defects and impaired viability Homo sapiens
H418R modeled in yeast the mutation causes growth defects and impaired viability Homo sapiens
L129P modeled in yeast the mutation causes growth defects and impaired viability Homo sapiens
additional information mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells, and four of the five mutations show loss-of-function, GARS-associated granules occur in the neurite projections of cultured neurons and in the peripheral nerve axons of normal human tissue Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
axon of peripheral nerves Homo sapiens 30424
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
 Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glycine + tRNAGly Homo sapiens mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells AMP + diphosphate + glycyl-tRNAGly
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P41250
-
-

Source Tissue

Source Tissue Comment Organism Textmining
nerve peripheral Homo sapiens
-
SH-SY5Y cell
-
 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycine + tRNAGly
-
 Homo sapiens AMP + diphosphate + glycyl-tRNAGly
-
 ?
ATP + glycine + tRNAGly mutations in the enzyme cause Charcot-Marie-Tooth disease type 2D, CMT2D, and distal spinal muscular atrophy type V, dSMA-V, axonal neuropathies characterized by a phenotype that is more severe in the upper extremities, in most cases, mutant GARS protein mislocalizes in neuronal cells Homo sapiens AMP + diphosphate + glycyl-tRNAGly
-
 ?

Synonyms

Synonyms Comment Organism
Glycyl-tRNA synthetase
-
 Homo sapiens
GlyRS
-
 Homo sapiens

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens