UniProtKB/SwissProt variant VAR

Variant information

Variant position:

279

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 Isoleucine (I) to Asparagine (N) at position 279 (I279N, p.Ile279Asn).

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 hydrophobic (I) to medium size and polar (N)

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 DEE17; the mutant protein has some abnormal cytoplasmic localization.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs587777054 [ dbSNP | Ensembl ]

Sequence information

Variant position:

279

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

Protein sequence length:

354

The length of the canonical sequence.

Location on the sequence:

FFIDTSIILFLNKKDLFGEK I KKSPLTICFPEYTGPNTYED

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                         FFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYTGPNTYED

Mouse                         FFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYED

Rat                           FFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYPGSNTYED

Bovine                        FFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYTGSNTYED

Xenopus laevis                WFTDTSIILFLNKKDIFQEKIKSSPLTICFPEYTGPNSFTE

Caenorhabditis elegans        WFTDTSIILFLNKKDLFEEKIKKSPLTICFPEYSGRQDYHE

Drosophila                    WFTDTSIILFLNKKDLFEEKIRKSPLTICFPEYTGGQEYGE

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	2 – 354	Guanine nucleotide-binding protein G(o) subunit alpha
Domain	32 – 354	G-alpha
Alternative sequence	249 – 354	MLFDSICNNKFFIDTSIILFLNKKDLFGEKIKKSPLTICFPEYTGPNTYEDAAAYIQAQFESKNRSPNKEIYCHMTCATDTNNIQVVFDAVTDIIIANNLRGCGLY -> KLFDSICNNKWFTDTSIILFLNKKDIFEEKIKKSPLTICFPEYTGPSAFTEAVAYIQAQYESKNKSAHKEIYTHVTCATDTNNIQFVFDAVTDVIIAKNLRGCGLY. In isoform Alpha-2.
Helix	272 – 281

Literature citations

De Novo mutations in GNAO1, encoding a Galphao subunit of heterotrimeric G proteins, cause epileptic encephalopathy.
Nakamura K.; Kodera H.; Akita T.; Shiina M.; Kato M.; Hoshino H.; Terashima H.; Osaka H.; Nakamura S.; Tohyama J.; Kumada T.; Furukawa T.; Iwata S.; Shiihara T.; Kubota M.; Miyatake S.; Koshimizu E.; Nishiyama K.; Nakashima M.; Tsurusaki Y.; Miyake N.; Hayasaka K.; Ogata K.; Fukuda A.; Matsumoto N.; Saitsu H.;
Am. J. Hum. Genet. 93:496-505(2013)
Cited for: VARIANTS DEE17 GLY-174; 191-THR--PHE-197 DEL; ARG-203 AND ASN-279; CHARACTERIZATION OF VARIANTS DEE17 GLY-174; 191-THR--PHE-197 DEL; ARG-203 AND ASN-279; INVOLVEMENT IN DEE17;

De novo mutations in SLC1A2 and CACNA1A are important causes of epileptic encephalopathies.
Epi4K Consortium;
Am. J. Hum. Genet. 99:287-298(2016)
Cited for: VARIANT DEE17 ASN-279;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P09471: Variant p.Ile279Asn