<p>An evidence describes the source of an annotation, e.g. an experiment that has been published in the scientific literature, an orthologous protein, a record from another database, etc.</p>
<p><a href="/manual/evidences">More…</a></p>
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli
<p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>
Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Blocks human and/or rat Kv11.1/KCNH2/ERG1, Kv11.2/KCNH6/ERG2 and Kv11.3/KCNH7/ERG3 by binding to channel outer vestibule (S5P domain) with a 1:1 stoichiometry. Inhibition data are the following: hERG1 (reversible, Kd=7.7 nM (PubMed:16497878), IC50=3.3 nM (PubMed:11136720), IC50=11.9 nM (PubMed:21205913)), rERG1 (reversible, Kd=19 nM) (PubMed:16497878), hERG2 (reversible, Kd=77 nM) (PubMed:16497878), rERG2 (irreversible, Kd=4.2 nM) (PubMed:16497878), hERG3 (reversible, Kd=11.5 nM) (PubMed:16497878) and rERG3 (reversible, Kd=747 nM) (PubMed:16497878) potassium channels. Has also a minimal effect on rat ELK1/KCNH4 potassium channels (9% inhibition at 100 nM (PubMed:15137031)). Both this toxin and CnErgTx1 (AC Q86QT3) share mechanism of action and have overlapping binding sites on ERG1 (PubMed:12719233). The potency of these two toxins is not affected by elevating potassium ion concentration from 2 to 98 mM (PubMed:12719233). In addition, at high toxin concentrations, block of ERG1 macroscopic currents by these two toxins is incomplete (88%) (PubMed:12719233). The blockade by this toxin is preferentially closed channel state-dependent, with a component of open, but not inactive state-dependent blockade (PubMed:12860380). This toxin produces a concentration-dependent prolongation of QTc in the isolated rabbit heart (16.3% at 100 nM) (PubMed:21205913).6 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
The inhibition potency of the toxin for ERG1 decreases as temperature increases (IC50=7.6 nM and IC50=15.3 nM at room temperature and 37 degrees Celsius, respectively), likely due to changes in the structure of the channel binding site.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
The toxin (at 100 nM) does not inhibit hEAG1/KCNH1, hBK/KCa1.1/KCNMA1, hSK1/KCa2.1/KCNN1, rSK2/KCa2.2/KCNN2, hIK/KCa3.1/KCNN4, KCNQ1+KCNE1, KCNQ2+KCNQ3 and KCNQ4 channels (PubMed:11136720). The toxin (at 50 nM) does not inhibit Kv1.2/KCNA2, Kv1.4/KCNA4, Kv2.1/KCNB1, Kv4.3/KCND3, Kir1.1/KCNJ1 (PubMed:15137031).2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei
Crucial for Kv11/ERG channel binding, plugs its side chain into the channel selectivity filter2 Publications
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p>
<p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections (‘Function’, ‘PTM / Processing’, ‘Pathology and Biotech’) according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei
Crucial for Kv11/ERG channel binding2 Publications
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p>
<p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
<p>This subsection of the ‘Names and Taxonomy’ section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p>
<p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
<p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p>
<p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini
<p>This subsection of the ‘Names and taxonomy’ section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi
<p>This subsection of the ‘Names and taxonomy’ section shows the unique identifier assigned by the <span class="caps">NCBI</span> to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri
<p>This subsection of the ‘Names and taxonomy’ section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei
<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
Feature key
Position(s)
DescriptionActions
Graphical view
Length
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
R → A: 6.7-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
P → A: 1.7-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
D → A: 3.4-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
K → A: 2.7-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
E → A: 0.8-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
Y → A: 14.7-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
Q → A: 2.3-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
F → A: 8.2-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
K → A: 86.4-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
R → A: 70.6-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
F → A: 52.2-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
K → A: 14.6-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
R → A: 7.4-fold decrease in affinity to Kv11/ERG potassium channels.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
R → K: 60% loss of toxicity. No loss of activity; when associated with K-53.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
V → A: 1.2-fold decrease in affinity to ERG-potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
F → A: 1.4-fold decrease in affinity to ERG-potassium channels.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
F → K: No loss of activity. No loss of activity but gain in inhibition of native calcium- activated potassium channels with Kd of about 72 nM; when associated with K-48.2 Publications
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
D → A: 1.1-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
1
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">‘Pathology and Biotech’</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi
F → A: 3.2-fold decrease in affinity to Kv11/ERG potassium channels.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
<p>This subsection of the ‘PTM / Processing’ section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000035313
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
<p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
<p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
<p>This subsection of the <span class="caps">PTM</span> / Processing”:/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - PTMi
<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni
<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression"><span class="caps">P92958</span></a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression"><span class="caps">Q8TDN4</span></a>, <a href="http://www.uniprot.org/uniprot/O14734#expression"><span class="caps">O14734</span></a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi
Expressed by the venom gland.Curated
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This subsection of the ‘Structure’ section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi
<p>Manually validated information inferred from a combination of experimental and computational evidence.</p>
<p><a href="/manual/evidences#ECO:0000244">More…</a></p> Manual assertion inferred from combination of experimental and computational evidencei
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini
Has the CSalpha/beta fold, which comprises one or two short alpha helices connected to anti-parallel beta-sheets stabilized by three or four disulfide bonds.1 Publication
<p>Manually curated information for which there is published experimental evidence.</p>
<p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini
Cited for: STRUCTURE BY NMR OF 22-57, DISULFIDE BONDS, MUTAGENESIS OF ARG-22; PRO-23; ASP-25; LYS-27; GLU-30; TYR-32; GLN-33; PHE-35; LYS-39; ARG-41; PHE-42; LYS-44; ARG-48; VAL-50; PHE-53; ASP-55 AND PHE-57.
<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Domaini
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the ‘Sequence’ section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i8B85BF8660816666
<p>This section provides links to the UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
<p>This subsection of the <a href="http://www.uniprot.org/manual/cross_references_section">Cross-references</a> section provides links to various web resources that are relevant for a specific protein.<p><a href='/help/web_resource' target='_top'>More...</a></p>Web resourcesi
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei
KGX21_MESEU
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi
Integrated into UniProtKB/Swiss-Prot:
October 31, 2003
Last sequence update:
June 1, 2001
Last modified:
November 2, 2016
This is version 73 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi
<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Caution
Has been classified as a gamma-KTx toxin due to its molecular target (Kv11/ERG), but may be classified as an alpha-KTx since it shares a high level of homology in both primary and 3D structures with other alpha-KTx scorpion toxins. However, it is noteworthy that surface by which BeKm-1 interacts with ERG1 is formed by residues located in the alpha-helix and the following loop, while the traditional functional site of other alpha-KTxs is formed by residues on the beta-sheet.1 Publication
<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p>
<p><a href="/manual/evidences#ECO:0000305">More…</a></p> Manual assertion inferred by curator fromi
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Technical termi
