UniProtKB/SwissProt variant VAR

Variant information

Variant position:

333

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 Phenylalanine (F) at position 333 (C333F, p.Cys333Phe).

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 large size and aromatic (F)

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

BLOSUM score:

-2

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 AHC2; decreased ATPase activity.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs606231430 [ dbSNP | Ensembl ]

Sequence information

Variant position:

333

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

Protein sequence length:

1013

The length of the canonical sequence.

Location on the sequence:

FLIGIIVANVPEGLLATVTV C LTLTAKRMARKNCLVKNLEA

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                         FLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEA

Mouse                         FLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEA

Rat                           FLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEA

Chicken                       FLIGIIVANVPEGLLATVTVCLTLTAKRMARKNCLVKNLEA

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	1 – 1013	Sodium/potassium-transporting ATPase subunit alpha-3
Topological domain	329 – 762	Cytoplasmic

Literature citations

De novo mutations in ATP1A3 cause alternating hemiplegia of childhood.
Heinzen E.L.; Swoboda K.J.; Hitomi Y.; Gurrieri F.; Nicole S.; de Vries B.; Tiziano F.D.; Fontaine B.; Walley N.M.; Heavin S.; Panagiotakaki E.; Neri G.; Koelewijn S.; Kamphorst J.; Geilenkirchen M.; Pelzer N.; Laan L.; Haan J.; Ferrari M.; van den Maagdenberg A.M.; Zucca C.; Bassi M.T.; Franchini F.; Vavassori R.; Giannotta M.; Gobbi G.; Granata T.; Nardocci N.; De Grandis E.; Veneselli E.; Stagnaro M.; Vigevano F.; Oechsler C.; Arzimanoglou A.; Ninan M.; Neville B.; Ebinger F.; Fons C.; Campistol J.; Kemlink D.; Nevsimalova S.; Peeters-Scholte C.; Casaer P.; Casari G.; Sange G.; Spiel G.; Martinelli Boneschi F.; Schyns T.; Crawley F.; Poncelin D.; Fiori S.; Abiusi E.; Di Pietro L.; Sweney M.T.; Newcomb T.M.; Viollet L.; Huff C.; Jorde L.B.; Reyna S.P.; Murphy K.J.; Shianna K.V.; Gumbs C.E.; Little L.; Silver K.; Ptacek L.J.; Ferrari M.D.; Bye A.M.; Herkes G.K.; Whitelaw C.M.; Webb D.; Lynch B.J.; Uldall P.; King M.D.; Scheffer I.E.; Sisodiya S.M.; Mikati M.A.; Goldstein D.B.;
Nat. Genet. 44:1030-1034(2012)
Cited for: VARIANTS AHC2 TYR-137; PHE-137; LEU-140; ASN-220; ASN-274; PHE-333; SER-755; SER-773; ASN-801; ARG-806; SER-810; PRO-811; LYS-815; VAL-919 DEL; ARG-947; ASP-955 AND TYR-992; CHARACTERIZATION OF VARIANTS AHC2 PHE-137; PHE-333; ASN-801; PRO-811 AND LYS-815;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P13637: Variant p.Cys333Phe