Sequence information
Variant position: 91 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 693 The length of the canonical sequence.
Location on the sequence:
FPAAHPASRSFPDPRGLYHF
C LYWNRHAGRLHLLYGKRDFL
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 FPAAHPASRSFPDPRGLYHFC LYWNRHAGRLHLLYGKRDFL
Gorilla FPAARPASQSFPDPRGLYHFC LYWNRHAGRLHLLYGKHDFL
Rhesus macaque FPEAHPASRSFPHPRGLYHFC LYWDRHAGRLHLLYGKHDFL
Chimpanzee FPAAHPASQSFPDPRGLYHFC LYWNRHAGRLHLLYGKRDFL
Mouse FLAAPDIPRFFPEPRGLYHFC LYWSRHTGRLHLRYGKHDYL
Rat FPAAPDIPYFFPEPRGLYHFC LYWSRHTGRLHLRYGKNDYL
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
Chain
26 – 693
Adhesion G-protein coupled receptor G1
Chain
26 – 382
ADGRG1 N-terminal fragment
Topological domain
26 – 402
Extracellular
Alternative sequence
1 – 175
Missing. In isoform 5.
Alternative sequence
38 – 207
Missing. In isoform 4.
Literature citations
Disease-associated GPR56 mutations cause bilateral frontoparietal polymicrogyria via multiple mechanisms.
Chiang N.Y.; Hsiao C.C.; Huang Y.S.; Chen H.Y.; Hsieh I.J.; Chang G.W.; Lin H.H.;
J. Biol. Chem. 286:14215-14225(2011)
Cited for: SUBUNIT; SUBCELLULAR LOCATION (ADGRG1 N-TERMINAL FRAGMENT); GLYCOSYLATION; CHARACTERIZATION OF VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346; SER-349; TRP-565 AND ARG-640; MUTAGENESIS OF THR-383;
Disease-associated mutations prevent GPR56-collagen III interaction.
Luo R.; Jin Z.; Deng Y.; Strokes N.; Piao X.;
PLoS ONE 7:E29818-E29818(2012)
Cited for: LIGAND-BINDING; CHARACTERIZATION OF VARIANTS BFPP GLN-38; TRP-38; CYS-88 AND SER-91;
G protein-coupled receptor-dependent development of human frontal cortex.
Piao X.; Hill R.S.; Bodell A.; Chang B.S.; Basel-Vanagaite L.; Straussberg R.; Dobyns W.B.; Qasrawi B.; Winter R.M.; Innes A.M.; Voit T.; Ross M.E.; Michaud J.L.; Descarie J.-C.; Barkovich A.J.; Walsh C.A.;
Science 303:2033-2036(2004)
Cited for: VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346 AND TRP-565;
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.