Variant position: 38 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:
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 FLVQGAHGRGHREDFRFCSQ RNQTHRSSLHYKPTPDLRISI
Gorilla FLVQGAHGRGHREDFRFCSQ RNQTHRSSLHYKPTADLRISI
Rhesus macaque FLVQGAHGRGHREDFRFCSQ RNQTHISSLHYKFTPDLRISI
Chimpanzee FLVQGAHGRGHREDFRFCSQ RNQTHRSSLHYKPTPDLRISI
Mouse SLVQGAHSGSPREDFRFCGQ RNQTQQSTLHYDQSSEPHIFV
Rat FLVQGAHGASPREDFRFCGQ RNQTQQSTLHYDQTSEPHIFV
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
26 – 693 Adhesion G-protein coupled receptor G1
26 – 382 ADGRG1 N-terminal fragment
26 – 402 Extracellular
39 – 39 N-linked (GlcNAc...) asparagine
1 – 175 Missing. In isoform 5.
21 – 21 Q -> QASASS. In isoform 3.
38 – 207 Missing. In isoform 4.
28 – 28 H -> A. Abolishes heparin-binding; when associated with A-29 and A-33.
29 – 29 R -> A. Abolishes heparin-binding; when associated with A-28 and A-33.
33 – 33 R -> A. Reduces heparin-binding. Abolishes heparin-binding; when associated with A-28 and A-29.
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.;
Cited for: VARIANTS BFPP TRP-38; CYS-88; SER-91; SER-346 AND TRP-565;
Genotype-phenotype analysis of human frontoparietal polymicrogyria syndromes.
Piao X.; Chang B.S.; Bodell A.; Woods K.; Benzeev B.; Topcu M.; Guerrini R.; Goldberg-Stern H.; Sztriha L.; Dobyns W.B.; Barkovich A.J.; Walsh C.A.;
Ann. Neurol. 58:680-687(2005)
Cited for: VARIANTS BFPP GLN-38; TRP-38; SER-349; TRP-565 AND ARG-640;
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.