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UniProtKB/Swiss-Prot Q9Y653: Variant p.Arg38Trp

Adhesion G-protein coupled receptor G1
Gene: ADGRG1
Variant information

Variant position:  38
The position of the amino-acid change on the UniProtKB canonical protein sequence.

Type of variant:  LP/P [Disclaimer]
The variants are classified into three categories: LP/P, LB/B and US.
  • LP/P: likely pathogenic or pathogenic.
  • LB/B: likely benign or benign.
  • US: uncertain significance

Residue change:  From Arginine (R) to Tryptophan (W) at position 38 (R38W, p.Arg38Trp).
Indicates the amino acid change of the variant. The one-letter and three-letter codes for amino acids used in UniProtKB/Swiss-Prot are those adopted by the commission on Biochemical Nomenclature of the IUPAC-IUB.

Physico-chemical properties:  Change from large size and basic (R) to large size and aromatic (W)
The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:  -3
The score within a Blosum matrix for the corresponding wild-type to variant amino acid change. The log-odds score measures the logarithm for the ratio of the likelihood of two amino acids appearing by chance. The Blosum62 substitution matrix is used. This substitution matrix contains scores for all possible exchanges of one amino acid with another:
  • Lowest score: -4 (low probability of substitution).
  • Highest score: 11 (high probability of substitution).
More information can be found on the following page

Variant description:  In BFPP; abolishes interaction with COL3A1; reduces cell surface localization.
Any additional useful information about the variant.

Other resources:  
Links to websites of interest for the variant.



Sequence information

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:   FLVQGAHGRGHREDFRFCSQ  R NQTHRSSLHYKPTPDLRISI
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                         FLVQGAHGRGHREDFRFCSQRNQTHRSSLHYKPTPDLRISI

Gorilla                       FLVQGAHGRGHREDFRFCSQRNQTHRSSLHYKPTADLRISI

Rhesus macaque                FLVQGAHGRGHREDFRFCSQRNQTHISSLHYKFTPDLRISI

Chimpanzee                    FLVQGAHGRGHREDFRFCSQRNQTHRSSLHYKPTPDLRISI

Mouse                         SLVQGAHSGSPREDFRFCGQRNQTQQSTLHYDQSSEPHIFV

Rat                           FLVQGAHGASPREDFRFCGQRNQTQQSTLHYDQTSEPHIFV

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.

TypePositionsDescription
Chain 26 – 693 Adhesion G-protein coupled receptor G1
Chain 26 – 382 ADGRG1 N-terminal fragment
Topological domain 26 – 402 Extracellular
Glycosylation 39 – 39 N-linked (GlcNAc...) asparagine
Alternative sequence 1 – 175 Missing. In isoform 5.
Alternative sequence 21 – 21 Q -> QASASS. In isoform 3.
Alternative sequence 38 – 207 Missing. In isoform 4.
Mutagenesis 28 – 28 H -> A. Abolishes heparin-binding; when associated with A-29 and A-33.
Mutagenesis 29 – 29 R -> A. Abolishes heparin-binding; when associated with A-28 and A-33.
Mutagenesis 33 – 33 R -> A. Reduces heparin-binding. Abolishes heparin-binding; when associated with A-28 and A-29.


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;

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;

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.