Sequence information
Variant position: 580 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:
RFQKTLYVEEVVPNVIEPSF
G LGRIMYTVFEHTFHVREGDE
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 RFQKTLYVEEVVPNVIEPSFG LGRIMYTVFEHTFHVREGDE
Mouse RFQKTLHVEEVVPSVIEPSFG LGRIMYTILEHTFHVREGDE
Caenorhabditis elegans KYTKKIHVQEITPSVIEPSYG IGRIMYALLEHSFRQREGDE
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.
Literature citations
Functional analyses of glycyl-tRNA synthetase mutations suggest a key role for tRNA-charging enzymes in peripheral axons.
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.;
J. Neurosci. 26:10397-10406(2006)
Cited for: SUBCELLULAR LOCATION; VARIANTS CMT2D GLY-125 AND ARG-294; CHARACTERIZATION OF VARIANTS CMT2D GLY-125 AND ARG-294; VARIANTS HMN5A PRO-183; ARG-472 AND ARG-580; CHARACTERIZATION OF VARIANTS HMN5A PRO-183; ARG-472 AND ARG-580;
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;
Long-range structural effects of a Charcot-Marie-Tooth disease-causing mutation in human glycyl-tRNA synthetase.
Xie W.; Nangle L.A.; Zhang W.; Schimmel P.; Yang X.-L.;
Proc. Natl. Acad. Sci. U.S.A. 104:9976-9981(2007)
Cited for: X-RAY CRYSTALLOGRAPHY (2.85 ANGSTROMS) OF 55-739; VARIANT ARG-580; SUBUNIT;
Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.
Antonellis A.; Ellsworth R.E.; Sambuughin N.; Puls I.; Abel A.; Lee-Lin S.Q.; Jordanova A.; Kremensky I.; Christodoulou K.; Middleton L.T.; Sivakumar K.; Ionasescu V.; Funalot B.; Vance J.M.; Goldfarb L.G.; Fischbeck K.H.; Green E.D.;
Am. J. Hum. Genet. 72:1293-1299(2003)
Cited for: VARIANTS CMT2D GLY-125 AND ARG-294; VARIANTS HMN5A PRO-183 AND ARG-580; TISSUE SPECIFICITY;
Disclaimer:
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.