UniProtKB/SwissProt variant VAR

Variant information

Variant position:

1214

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

Type of variant:

Disease [Disclaimer]

The variants are classified into three categories: Disease, Polymorphism and Unclassified.

Disease: Variants implicated in disease according to literature reports.
Polymorphism: Variants not reported to be implicated in disease.
Unclassified: Variants with uncertain implication in disease according to literature reports. Evidence against or in favor of a pathogenic role is limited and/or conflicting.

Residue change:

From Arginine (R) to Glutamine (Q) at position 1214 (R1214Q, p.Arg1214Gln).

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 medium size and polar (Q)

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 HHF1; severe.

Any additional useful information about the variant.

Other resources:

Links to websites of interest for the variant.

Variant rs367850779 [ dbSNP | Ensembl ]

Sequence information

Variant position:

1214

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

Protein sequence length:

1581

The length of the canonical sequence.

Location on the sequence:

TTQLPLLSHFAETVEGLTTI R AFRYEARFQQKLLEYTDSNN

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                         TTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNN

Rat                           TTQLPLLSHFAETVEGLTTIRAFRYEARFQQKLLEYTDSNN

Slime mold                    VSRSPIYAHFSETLAGVTTIRAFKDVARFVTENERLLDENQ

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 – 1581	ATP-binding cassette sub-family C member 8
Topological domain	1181 – 1251	Cytoplasmic
Domain	1012 – 1306	ABC transmembrane type-1 2
Alternative sequence	51 – 1581	Missing. In isoform 3.

Literature citations

Functional analyses of novel mutations in the sulfonylurea receptor 1 associated with persistent hyperinsulinemic hypoglycemia of infancy.
Shyng S.-L.; Ferrigni T.; Shepard J.B.; Nestorowicz A.; Glaser B.; Permutt M.A.; Nichols C.G.;
Diabetes 47:1145-1151(1998)
Cited for: CHARACTERIZATION OF VARIANTS HHF1 GLN-125; SER-188; LEU-591; MET-1138; GLN-1214; SER-1381; PHE-1387 DEL AND HIS-1393;

Genetic heterogeneity in familial hyperinsulinism.
Nestorowicz A.; Glaser B.; Wilson B.A.; Shyng S.-L.; Nichols C.G.; Stanley C.A.; Thornton P.S.; Permutt M.A.;
Hum. Mol. Genet. 7:1119-1128(1998)
Cited for: VARIANTS HHF1 GLN-74; GLN-125; SER-188; ASP-406; LEU-591; MET-1138; GLN-1214; ARG-1378; SER-1381; PHE-1387 DEL AND HIS-1393;

Genotype-phenotype correlations in children with congenital hyperinsulinism due to recessive mutations of the adenosine triphosphate-sensitive potassium channel genes.
Henwood M.J.; Kelly A.; MacMullen C.; Bhatia P.; Ganguly A.; Thornton P.S.; Stanley C.A.;
J. Clin. Endocrinol. Metab. 90:789-794(2005)
Cited for: VARIANTS HHF1 SER-27; TRP-74; SER-188; GLN-495; LYS-501; SER-686; TRP-1214; GLN-1214; ASN-1336; PHE-1387 DEL; HIS-1471 AND ASN-1471;

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot Q09428: Variant p.Arg1214Gln