Variant position: 635 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 739 The length of the canonical sequence.
Location on the sequence:
The residue change on the sequence. Unless the variant is located at the beginning or at the end of the protein sequence, both residues upstream (20) and downstream (20) of the variant will be shown.
Residue conservation: The multiple alignment of the region surrounding the variant against various orthologous sequences.
Human KCSVLPLSQNQEFMPFVKEL SEALTRHGVSHKVDDSSGSIG
Mouse KCSVLPLSQNQEFMPFVKEL SEALTRNGVSHKVDDSSGSIG
Rat KCSVLPLSQNQEFMPFVKEL SEALTRNGVSHKVDDSSGSIG
Caenorhabditis elegans KCSVLPISANDTLIPVMDAV KEELSRFEMSYKVDDSSGTIG
Sequence annotation in neighborhood: The regions or sites of interest surrounding the variant. In general the features listed are posttranslational modifications, binding sites, enzyme active sites, local secondary structure or other characteristics reported in the cited references. The "Sequence annotation in neighborhood" lines have a fixed format:
Type: the type of sequence feature. Positions: endpoints of the sequence feature. Description: contains additional information about the feature.
Impaired function is a common feature of neuropathy-associated glycyl-tRNA synthetase mutations.
Griffin L.B.; Sakaguchi R.; McGuigan D.; Gonzalez M.A.; Searby C.; Zuchner S.; Hou Y.M.; Antonellis A.;
Hum. Mutat. 35:1363-1371(2014)
Cited for: SUBCELLULAR LOCATION; VARIANTS CMT2D VAL-111; ASN-200; PHE-265; ARG-294; LEU-298; PHE-334; ARG-472; ASN-554; ARG-580 AND ALA-652; VARIANT LEU-635; CHARACTERIZATION OF VARIANTS CMT2D VAL-111; GLY-125; PRO-183; ASN-200; PHE-265; ARG-294; LEU-298; PHE-334; ARG-472; ASN-554; ARG-580 AND ALA-652; CHARACTERIZATION OF VARIANT LEU-635;
Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy.
Cader M.Z.; Ren J.; James P.A.; Bird L.E.; Talbot K.; Stammers D.K.;
FEBS Lett. 581:2959-2964(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS) OF 55-739; FUNCTION; SUBUNIT; CHARACTERIZATION OF VARIANT LEU-635; CATALYTIC ACTIVITY; BIOPHYSICOCHEMICAL PROPERTIES;
Severe childhood SMA and axonal CMT due to anticodon binding domain mutations in the GARS gene.
James P.A.; Cader M.Z.; Muntoni F.; Childs A.M.; Crow Y.J.; Talbot K.;
Cited for: VARIANT LEU-635; VARIANTS CMT2D PHE-334 AND ALA-652;
Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. They are not in any way intended to be used as a substitute for professional medical advice, diagnostic, treatment or care.