Variant position: 278 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 457 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 PSLLIVILSWISFWINMDAA PARVGLGITTVLTMTTQSSGS
Mouse PSLLIVILSWISFWINMDAA PARVGLGITTVLTMTTQSSGS
Rat PSLLIVILSWISFWINMDAA PARVGLGITTVLTMTTQSSGS
Bovine PSLLIVILSWISFWINMDAA PARVGLGITTVLTMTTQSSGS
Zebrafish PSLLIVILSWVSFWINMDAA PARVGLGITTVLTMTTQSSGS
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.
Type Positions Description
29 – 457 Glycine receptor subunit alpha-1
278 – 298 Helical; Name=2
289 – 289 Important for obstruction of the ion pore in the closed conformation
282 – 282 G -> A. Increased single-channel conductance. No effect on glycine sensitivity, but decreased rate of activation.
278 – 280
Allosteric and hyperekplexic mutant phenotypes investigated on an alpha1 glycine receptor transmembrane structure.
Moraga-Cid G.; Sauguet L.; Huon C.; Malherbe L.; Girard-Blanc C.; Petres S.; Murail S.; Taly A.; Baaden M.; Delarue M.; Corringer P.J.;
Proc. Natl. Acad. Sci. U.S.A. 112:2865-2870(2015)
Cited for: X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) OF 246-338 AND 418-446; FUNCTION; ENZYME REGULATION; SUBUNIT; SUBCELLULAR LOCATION; TOPOLOGY; CHARACTERIZATION OF VARIANTS HKPX1 GLU-254; THR-278; GLN-299 AND MET-308; MUTAGENESIS OF GLY-282 AND LYS-304;
Novel GLRA1 missense mutation (P250T) in dominant hyperekplexia defines an intracellular determinant of glycine receptor channel gating.
Saul B.; Kuner T.; Sobetzko D.; Brune W.; Hanefeld F.; Meinck H.-M.; Becker C.-M.;
J. Neurosci. 19:869-877(1999)
Cited for: VARIANT HKPX1 THR-278;
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