Variant position: 7 The position of the amino-acid change on the UniProtKB canonical protein sequence.
Protein sequence length: 129 The length of the canonical sequence.
Location on the sequence:
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 MILSNT TAVTPFLTKLWQETVQQGGNM
Mouse MSLPNS TTVLPFLARLWQETAEQGGNV
Rat MALSNS TTVLPFLASLWQETDEPGGNM
Pig MALSNS TTVLPFLASLWQETDEPGGNM
Rabbit MIPPNA TAVMPFLTTLGEETAHLQGSS
Cat MILPNT TATTPFLNALWQGTAHQGGNT
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
1 – 129 Potassium voltage-gated channel subfamily E member 1
19 – 19 Interacts with the scolopendra toxin SSD609
5 – 5 N-linked (GlcNAc...) asparagine
7 – 7 O-linked (GalNAc...) threonine
26 – 26 N-linked (GlcNAc...) asparagine
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.
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.
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.
15 – 15 K -> D. No change in inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.
19 – 19 E -> K. Loss inhibition of the complex KCNQ1-KCNE1 by the scolopendra toxin SSD609.
4 – 9
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;
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.