UniProtKB/SwissProt variant VAR

Variant information

Variant position:

346

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 Cysteine (C) to Serine (S) at position 346 (C346S, p.Cys346Ser).

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 medium size and polar (C) to small size and polar (S)

The physico-chemical property of the reference and variant residues and the change implicated.

BLOSUM score:

-1

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 autoproteolytic cleavage; reduces cell surface localization.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs121908463 [ dbSNP | Ensembl ]

Sequence information

Variant position:

346

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:

TEPVVLTFQHQLQPKNVTLQ C VFWVEDPTLSSPGHWSSAGC

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                         TEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGC

Gorilla                       TEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGC

Rhesus macaque                TEPVVLTFQHQPQPKNVTLQCVFWVEDPTLSNPGRWSSAGC

Chimpanzee                    TEPVVLTFQHQLQPKNVTLQCVFWVEDPTLSSPGHWSSAGC

Mouse                         SDPVVLTFQHQPQPKNVTLQCVFWVEDPASSSTGSWSSAGC

Rat                           SDPVVLTFQHQPQPKNVTLQCVFWVEDPASSSTGSWSSEGC

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
Domain	343 – 394	GPS
Glycosylation	341 – 341	N-linked (GlcNAc...) asparagine

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;

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;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q9Y653: Variant p.Cys346Ser