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Literature summary for 6.1.1.14 extracted from

  • Nangle, L.A.; Zhang, W.; Xie, W.; Yang, X.L.; Schimmel, P.
    Charcot-Marie-Tooth disease-associated mutant tRNA synthetases linked to altered dimer interface and neurite distribution defect (2007), Proc. Natl. Acad. Sci. USA, 104, 11239-11244.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.1.1.14

Cloned(Commentary)

Cloned (Comment) Organism
expression of CMT-causing mutant variants and wild-type enzymes in neuroblastoma cells that sprout primitive neurites Homo sapiens

Protein Variants

Protein Variants Comment Organism
D500N naturally occuring mutation in the catalytic domain, the mutation lies in the disordered insertion III and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
E71G naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
G240R naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
G526R naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
G598A naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
H418R naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
I280F naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
L129P naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
additional information GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, most catalytic-domain mutations are at the dimer interface, overview, mapping mutations onto human GlyRS crystal structure show them within a band encompassing both sides of the dimer interface, with two CMT-causing mutations being at sites that are complementary partners of a kissing contact across the dimer interface, the CMT phenotype does not correlate with aminoacylation activity, overview Homo sapiens
P234KY naturally occuring mutation in the catalytic domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens
S581L naturally occuring mutation in the anticodon binding domain, the mutation lies in a conserved region and causes Charcot-Marie-Tooth peripheral neuropathies Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
 Homo sapiens 5829
-

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 GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview AMP + diphosphate + glycyl-tRNAGly
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
 gene GARS
-

Source Tissue

Source Tissue Comment Organism Textmining
brain
-
 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 GlyRS mutations cause Charcot-Marie-Tooth peripheral neuropathies, at least 10 different mutant alleles, overview Homo sapiens AMP + diphosphate + glycyl-tRNAGly
-
 ?

Subunits

Subunits Comment Organism
dimer homodimer, crystal structure Homo sapiens

Synonyms

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Homo sapiens