Expasy logo

UniProtKB/Swiss-Prot variant pages

UniProtKB/Swiss-Prot P15382: Variant p.Thr7Ile

Potassium voltage-gated channel subfamily E member 1
Gene: KCNE1
Feedback?
Variant information Variant position: help 7 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Type of variant: help 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: help From Threonine (T) to Isoleucine (I) at position 7 (T7I, p.Thr7Ile). 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: help Change from medium size and polar (T) to medium size and hydrophobic (I) The physico-chemical property of the reference and variant residues and the change implicated.
BLOSUM score: help -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: help In JLNS2; impairs glycosylation at N-5. Any additional useful information about the variant.
Other resources: help Links to websites of interest for the variant.


Sequence information Variant position: help 7 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: help 129 The length of the canonical sequence.
Location on the sequence: help MILSNT T AVTPFLTKLWQETVQQGGNM 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: help The multiple alignment of the region surrounding the variant against various orthologous sequences. 
Human                         MILSNTTAVTPFLTKLWQETVQQGGNM

Mouse                         MSLPNSTTVLPFLARLWQETAEQGGNV

Rat                           MALSNSTTVLPFLASLWQETDEPGGNM

Pig                           MALSNSTTVLPFLASLWQETDEPGGNM

Rabbit                        MIPPNATAVMPFLTTLGEETAHLQGSS

Cat                           MILPNTTATTPFLNALWQGTAHQGGNT
Sequence annotation in neighborhood: help 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.
TypePositionsDescription
Chain 1 – 129 Potassium voltage-gated channel subfamily E member 1
Site 19 – 19 Interacts with the scolopendra toxin SSD609
Glycosylation 5 – 5 N-linked (GlcNAc...) asparagine
Glycosylation 7 – 7 O-linked (GalNAc...) threonine
Glycosylation 26 – 26 N-linked (GlcNAc...) asparagine
Mutagenesis 5 – 5 N -> Q. No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5; when associated with T-28.
Mutagenesis 6 – 6 T -> F. No measurable effect on assembly with KCNQ1 or cell surface expression of the KCNE1/KCNQ1 channel complex. Loss of glycosylation at T-7.
Mutagenesis 7 – 7 T -> A. 50% reduction of cell surface expression of the KCNE1/KCNQ1 channel complex, and loss of glycosylation at N-5 and T-7; when associated with T-28.
Mutagenesis 15 – 15 K -> D. No change in inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.
Mutagenesis 19 – 19 E -> K. Loss inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.
Helix 4 – 9



Literature citations
Post-translational N-glycosylation of type I transmembrane KCNE1 peptides: implications for membrane protein biogenesis and disease.
Bas T.; Gao G.Y.; Lvov A.; Chandrasekhar K.D.; Gilmore R.; Kobertz W.R.;
J. Biol. Chem. 286:28150-28159(2011)
Cited for: GLYCOSYLATION AT ASN-5 AND ASN-26; CHARACTERIZATION OF VARIANT JLNS2 ILE-7; KCNE1 mutations cause Jervell and Lange-Nielsen syndrome.
Schulze-Bahr E.; Wang Q.; Wedekind H.; Haverkamp W.; Chen Q.; Sun Y.; Rubie C.; Hordt M.; Towbin J.A.; Borggrefe M.; Assmann G.; Qu X.; Somberg J.C.; Breithardt G.; Oberti C.; Funke H.;
Nat. Genet. 17:267-268(1997)
Cited for: VARIANTS JLNS2 ILE-7 AND ASN-76;
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.