UniProtKB/Swiss-Prot P51787: Variant p.Ala341Val

Potassium voltage-gated channel subfamily KQT member 1
Gene: KCNQ1
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Variant information Variant position:

341 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 Alanine (A) to Valine (V) at position 341 (A341V, p.Ala341Val). 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 small size and hydrophobic (A) to medium size and hydrophobic (V) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score:

0 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 LQT1. Any additional useful information about the variant.
Other resources:

Links to websites of interest for the variant.

Variant rs12720459 [ dbSNP | Ensembl ]

Sequence information Variant position:

341 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length:

676 The length of the canonical sequence.
Location on the sequence:

QTWVGKTIASCFSVFAISFF A LPAGILGSGFALKVQQKQRQ 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                         QTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQ

Mouse                         QTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQ

Rat                           QTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQ

Pig                           QTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQ

Rabbit                        QTWVGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQ

Xenopus laevis                QTWIGKTIASCFSVFAISFFALPAGILGSGFALKVQQKQRQ

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 – 676	Potassium voltage-gated channel subfamily KQT member 1
Transmembrane	328 – 348	Helical; Name=Segment S6
Mutagenesis	324 – 324	V -> L. Has a voltage-gated potassium channel activity. Inhibition of voltage-gated potassium channel activity by KCNE4.
Mutagenesis	326 – 326	K -> R. Has a voltage-gated potassium channel activity. Disrupts KCNE4-mediated voltage-gated potassium channel activity inhibition.
Mutagenesis	327 – 327	T -> V. Has a voltage-gated potassium channel activity. Disrupts KCNE4-mediated voltage-gated potassium channel activity inhibition.
Mutagenesis	328 – 328	I -> L. Has a voltage-gated potassium channel activity. Inhibition of voltage-gated potassium channel activity by KCNE4.
Mutagenesis	338 – 338	S -> C. Inhibits voltage-gated potassium channel activity.
Mutagenesis	340 – 340	F -> C. Inhibits voltage-gated potassium channel activity.

Literature citations
KVLQT1 mutations in three families with familial or sporadic long QT syndrome.
Russell M.W.; Dick M. II; Collins F.S.; Brody L.C.;
Hum. Mol. Genet. 5:1319-1324(1996)
Cited for: VARIANTS LQT1 SER-314 AND VAL-341; Evidence of a long QT founder gene with varying phenotypic expression in South African families.
de Jager T.; Corbett C.H.; Badenhorst J.C.; Brink P.A.; Corfield V.A.;
J. Med. Genet. 33:567-573(1996)
Cited for: VARIANT LQT1 VAL-341; KVLQT1 C-terminal missense mutation causes a forme fruste long-QT syndrome.
Donger C.; Denjoy I.; Berthet M.; Neyroud N.; Cruaud C.; Bennaceur M.; Chivoret G.; Schwartz K.; Coumel P.; Guicheney P.;
Circulation 96:2778-2781(1997)
Cited for: VARIANTS LQT1 ARG-168; CYS-174; GLN-190; MET-254; LYS-261; ASP-269; ARG-309; SER-314; SER-315; ALA-320; ARG-325; VAL-341; PHE-342; VAL-344; THR-371 AND CYS-555; New mutations in the KVLQT1 potassium channel that cause long-QT syndrome.
Li H.; Chen Q.; Moss A.J.; Robinson J.L.; Goytia V.; Perry J.C.; Vincent G.M.; Priori S.G.; Lehmann M.H.; Denfield S.W.; Duff D.; Kaine S.; Shimizu W.; Schwartz P.J.; Wang Q.; Towbin J.A.;
Circulation 97:1264-1269(1998)
Cited for: VARIANT LQT1 VAL-341; Spectrum of mutations in long-QT syndrome genes. KVLQT1, HERG, SCN5A, KCNE1, and KCNE2.
Splawski I.; Shen J.; Timothy K.W.; Lehmann M.H.; Priori S.G.; Robinson J.L.; Moss A.J.; Schwartz P.J.; Towbin J.A.; Vincent G.M.; Keating M.T.;
Circulation 102:1178-1185(2000)
Cited for: VARIANTS LQT1 CYS-111; LYS-160; ARG-168; HIS-174; SER-179; SER-184; PRO-194; LEU-225; CYS-243; ARG-248; MET-254; PRO-266; ASP-269; PHE-273; ILE-310; ILE-312; ARG-325; GLU-341; VAL-341; TRP-349; GLN-366; ILE-391; ARG-448; PHE-566; CYS-583 AND GLN-594; Compendium of cardiac channel mutations in 541 consecutive unrelated patients referred for long QT syndrome genetic testing.
Tester D.J.; Will M.L.; Haglund C.M.; Ackerman M.J.;
Heart Rhythm 2:507-517(2005)
Cited for: VARIANTS LQT1 71-ALA--PRO-73 DEL; THR-73; GLY-115; TYR-122; ILE-133; PHE-136; LYS-160; ARG-168; CYS-174; GLN-190; PHE-204; LEU-225; ASN-235; ASN-242; CYS-243; MET-254; 254-VAL--PHE-256 DEL; CYS-259; LEU-259; ASP-261; PRO-266; SER-269; ASP-269; PHE-273; ARG-273; SER-276 DEL; LEU-277; HIS-278; LYS-290; ASP-292; CYS-293; VAL-302; ARG-304; SER-305; ILE-312; SER-314; ARG-314; ASP-314; CYS-315; ARG-316; ALA-322; PHE-339 DEL; VAL-341; SER-343; GLU-344; VAL-344; GLU-345; TRP-349; PRO-353; ARG-362; TRP-366; HIS-374; SER-380; TYR-389; TRP-452; GLY-524; GLU-526; TRP-539; LEU-546; CYS-555; HIS-555; TYR-566; SER-567; ARG-568; MET-587; THR-590; HIS-591; GLN-594; MET-619 AND SER-626; Spectrum of pathogenic mutations and associated polymorphisms in a cohort of 44 unrelated patients with long QT syndrome.
Millat G.; Chevalier P.; Restier-Miron L.; Da Costa A.; Bouvagnet P.; Kugener B.; Fayol L.; Gonzalez Armengod C.; Oddou B.; Chanavat V.; Froidefond E.; Perraudin R.; Rousson R.; Rodriguez-Lafrasse C.;
Clin. Genet. 70:214-227(2006)
Cited for: VARIANTS LQT1 CYS-231; PRO-243; CYS-259; HIS-259; PHE-273; SER-314; GLU-316; VAL-341; VAL-344 AND SER-626; Spectrum and prevalence of mutations from the first 2,500 consecutive unrelated patients referred for the FAMILION long QT syndrome genetic test.
Kapplinger J.D.; Tester D.J.; Salisbury B.A.; Carr J.L.; Harris-Kerr C.; Pollevick G.D.; Wilde A.A.; Ackerman M.J.;
Heart Rhythm 6:1297-1303(2009)
Cited for: VARIANTS LQT1 VAL-2; SER-7; THR-46; 64-PRO--PRO-70 DEL; PHE-66; THR-73; CYS-111; LEU-117; LEU-127; ILE-133; PRO-134; ALA-144; MET-153; MET-162; ARG-168; MET-172; CYS-174; HIS-174; THR-178; SER-179; HIS-184; ARG-186; GLN-190; LEU-190; TRP-195; VAL-198; ALA-199; MET-204; MET-215; MET-224; LEU-225; CYS-231; HIS-231; ASN-235; GLY-241; ASN-242; CYS-243; PRO-250; MET-254; CYS-259; LEU-259; VAL-262; PRO-266; SER-268; ASP-269; SER-269; ASP-272; PHE-273; VAL-274; LEU-277; PRO-277; GLU-280; CYS-281; PRO-282; GLY-283; ASP-292; CYS-293; GLU-302; VAL-302; PRO-303; ARG-305; SER-305; ARG-306; ILE-312; CYS-314; SER-314; CYS-315; VAL-316; SER-320; ALA-322; MET-322; ARG-325; TYR-339; GLU-341; GLY-341; VAL-341; PHE-342; LEU-343; ARG-350; SER-351; ARG-354; MET-360; ARG-362; HIS-365; GLN-366; TRP-366; HIS-374; GLY-379; LYS-385; PRO-389; THR-391 INS; TRP-397; ARG-398; GLU-446; LEU-448; TRP-451; SER-460; LEU-477; TRP-511; GLN-518; ARG-520; SER-522; GLY-524; THR-525; VAL-525; TRP-533; GLN-539; TRP-539; ILE-541; LYS-543; LEU-546; ARG-547; CYS-555; HIS-555; SER-555; GLU-557; PHE-566; PRO-566; TYR-566; THR-567; ARG-568; GLU-569; LEU-571; MET-587; ASP-589; CYS-591; HIS-591; GLN-594; PRO-594; GLU-596 DEL; LYS-596; MET-600; ASN-611; HIS-614 DEL; SER-626 AND ARG-635;

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.