Protein:KCNQ2 |
Protein Summary |
Gene summary |
| Gene name: KCNQ2 | ASpdb.0 ID: 3785 | Gene | Gene symbol | KCNQ2 | Gene ID | 3785 |
| Gene name | potassium voltage-gated channel subfamily Q member 2 |
| Synonyms | BFNC|DEE7|EBN|EBN1|ENB1|HNSPC|KCNA11|KV7.2 |
| Cytomap | 20q13.33 |
| Type of gene | protein-coding |
| Description | potassium voltage-gated channel subfamily KQT member 2neuroblastoma-specific potassium channel subunit alpha KvLQT2potassium channel, voltage gated KQT-like subfamily Q, member 2voltage-gated potassium channel subunit Kv7.2 |
| Modification date | 20240416 |
| UniProtAcc | O43526 |
Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez |
| Partner | Gene | GO ID | GO term | PubMed ID |
| Gene | KCNQ2 | GO:0005249 | voltage-gated potassium channel activity | 9836639|27564677 |
| Gene | KCNQ2 | GO:0005516 | calmodulin binding | 27564677 |
| Gene | KCNQ2 | GO:0005886 | plasma membrane | 9836639|10788442 |
| Gene | KCNQ2 | GO:0008076 | voltage-gated potassium channel complex | 9836639|27564677 |
| Gene | KCNQ2 | GO:0071805 | potassium ion transmembrane transport | 9836639|27564677 |
AS Summary |
Information of the canonical protein with experimentally identified structure from PDB (2023). |
| UniProt Acc | File name | PDB ID | Method | Resolution | Chain | Start | End |
| O43526-1 | O43526-1_7cr7_A.pdb | 7CR7 | EM | 3.7 | A | 70 | 600 |
ASpdb's canonical and alternatively spliced isoform information. |
| accession_id | gene_name | canonical_id | alternative_id | canonical_length | alternative_length | canonical_start | canonical_end | type | originalSEQ | variationSEQ | alternative_start | alternative_end |
| O43526 | KCNQ2 | O43526-1 | O43526-2 | 872 | 854 | 417 | 434 | Deletion | none | none | 416 | 416 |
| O43526 | KCNQ2 | O43526-1 | O43526-3 | 872 | 844 | 373 | 382 | Deletion | none | none | 372 | 372 |
| O43526 | KCNQ2 | O43526-1 | O43526-3 | 872 | 844 | 417 | 434 | Deletion | none | none | 406 | 406 |
| O43526 | KCNQ2 | O43526-1 | O43526-4 | 872 | 841 | 417 | 446 | Deletion | none | none | 416 | 416 |
| O43526 | KCNQ2 | O43526-1 | O43526-4 | 872 | 841 | 509 | 509 | Deletion | none | none | 478 | 478 |
| O43526 | KCNQ2 | O43526-1 | O43526-5 | 872 | 843 | 310 | 320 | Deletion | none | none | 309 | 309 |
| O43526 | KCNQ2 | O43526-1 | O43526-5 | 872 | 843 | 417 | 434 | Deletion | none | none | 405 | 405 |
| O43526 | KCNQ2 | O43526-1 | O43526-6 | 872 | 393 | 373 | 393 | Substitution | SSQTQTYGASRLIPPLNQLEL | RYRRRAPATKQLFHFLFSICS | 373 | 393 |
| O43526 | KCNQ2 | O43526-1 | O43526-6 | 872 | 393 | 394 | 872 | Deletion | none | none | 393 | 393 |
Multiple sequence alignment of our canonical and alternatively spliced KCNQ2 |
Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of KCNQ2 |
| UniProt-id | ENSG | ENST | ENSP |
| O43526-1 | ENSG00000075043.21 | ENST00000359125.7 | ENSP00000352035.2 |
| O43526-2 | ENSG00000075043.21 | ENST00000626839.2 | ENSP00000486706.1 |
| O43526-3 | ENSG00000075043.21 | ENST00000360480.7 | ENSP00000353668.3 |
| O43526-4 | ENSG00000075043.21 | ENST00000344462.8 | ENSP00000339611.4 |
| O43526-6 | ENSG00000075043.21 | ENST00000344425.8 | ENSP00000345523.5 |
| UniProt-id | NM ID | NP ID |
| O43526-1 | NM_172107.3 | NP_742105.1 |
| O43526-2 | NM_172106.2 | NP_742104.1 |
| O43526-3 | NM_004518.5 | NP_004509.2 |
| O43526-4 | NM_172108.4 | NP_742106.1 |
| O43526-6 | NM_172109.2 | NP_742107.1 |
Amino acid sequences of our canonical and alternatively spliced KCNQ2 |
| accession_id | Protein sequence |
| O43526-1 | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCRGPLCGCCPGRSSQKVSLKDRVFSSPRGV AAKGKGSPQAQTVRRSPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSI RAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQV LSMEKKLDFLVNIYMQRMGIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQP QSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQS |
| O43526-2 | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPS ADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKES LRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRM GIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGS LVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCA |
| O43526-3 | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW QYYERTVTVPMYRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPS KVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVI EQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAY FGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAH ERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGE |
| O43526-4 | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKV PKSWSFGDRSRARQAFRIKGAASRQNSEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQY SAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGA KEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHERS LSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESDT |
| O43526-5 | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPM YSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSK VPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIE QYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYF GAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHE RSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGES |
| O43526-6 | MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW |
Protein Functional Features |
Main function of this protein. (from UniProt) |
| KCNQ2 (go to UniProt):O43526 |
Retention analysis result of protein across 39 protein features of UniProt such as six molecule processing features, 13 region features, four site features, six amino acid modification features, two natural variation features, five experimental info features, and 3 secondary structure features. Here, because of limited space for viewing, we only show the protein feature retention information belong to the 13 regional features. All retention annotation result can be downloaded at * Minus value of BPloci means that the break pointn is located before the CDS. |
| - Retained protein feature among the 13 regional features. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| O43526 | Transmembrane | 292 | 312 | Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=310;End=320 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=417;End=434 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=373;End=382 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=417;End=434 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=417;End=446 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=509;End=509 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=310;End=320 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=417;End=434 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Substitution;Start=373;End=393 |
| O43526 | Topological domain | 313 | 872 | Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255 | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 222 | 323 | Note=Mediates interaction with SLC5A3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88943 | Type=Deletion;Start=310;End=320 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=373;End=382 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=446 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=509;End=509 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=310;End=320 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Substitution;Start=373;End=393 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 402 | 422 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 402 | 422 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 402 | 422 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=417;End=446 |
| O43526 | Region | 402 | 422 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 402 | 422 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 442 | 488 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=417;End=446 |
| O43526 | Region | 442 | 488 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 598 | 619 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 659 | 680 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 693 | 757 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
| O43526 | Region | 838 | 872 | Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
| O43526 | Compositional bias | 459 | 479 | Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite | Type=Deletion;Start=394;End=872 |
Gene Isoform Structures and Expression Levels for KCNQ2 |
Gene structures of our canonical and alternative spliced genes of KCNQ2* Click on the image to open the UCSC genome browser with custom track showing this image in a new window. |
Expression levels of gene isoforms across GTEx. |
Expression levels of gene isoforms across TCGA. |
Protein Structures |
PDB and CIF files of the predicted protein structures * Here we show the 3D structure of the proteins using Mol*. AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. Model confidence is shown from the pLDDT values per residue. pLDDT corresponds to the model’s prediction of its score on the local Distance Difference Test. It is a measure of local accuracy (from AlphfaFold website). To color code individual residues, we transformed individual PDB files into CIF format. |
| 3D view using mol* of O43526-1 |
| 3D view using mol* of O43526-2 |
| 3D view using mol* of O43526-3 |
| 3D view using mol* of O43526-4 |
| 3D view using mol* of O43526-5 |
| 3D view using mol* of O43526-6 |
pLDDT Score Distribution |
pLDDT score distribution of the predicted protein structures from AlphaFold2* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100. |
Ramachandran Plot of Protein Structures |
Ramachandran plot of the torsional angles - phi (φ)and psi (ψ) - of the residues (amino acids) contained in this protein peptide. |
| Ramachandran plot of O43526-1 |
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| Ramachandran plot of O43526-3 |
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| Ramachandran plot of O43526-5 |
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| Ramachandran plot of O43526-6 |
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Potential Active Site Information |
The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite. |
| UniProt-id | Site score | Size | D score | Volume | Exposure | Enclosure | Contact | Phobic | Philic | Balance | Don/Acc | Residues |
| O43526-1 | 0.961 | 263 | 0.971 | 679.483 | 0.662 | 0.64 | 0.8 | 0.288 | 1.083 | 0.266 | 0.485 | 71,73,74,75,76,77,78,79,80,82,83,84,86,87,88,89,92 ,144,149,150,151,152,153,154,155,156,157,160,163,1 66,167,168,169,172,210,213,214,219,835,836,837,838 ,839,840,841,842,843,844,845,846 |
| O43526-2 | 1.072 | 81 | 1.123 | 201.684 | 0.521 | 0.791 | 1.025 | 1.907 | 0.607 | 3.142 | 0.529 | 123,126,127,130,178,179,182,183,186,194,197,200,20 1,203,204,207 |
| O43526-3 | 1.021 | 112 | 1.07 | 497.693 | 0.719 | 0.672 | 0.81 | 0.652 | 0.839 | 0.777 | 0.901 | 327,331,334,335,337,338,341,342,345,359,362,363,36 6,508,511,512,515,516,519,523,525,526,529,530,532, 534,535,537,538,539,541,542 |
| O43526-4 | 1.017 | 204 | 1.061 | 775.18 | 0.671 | 0.675 | 0.824 | 0.673 | 0.87 | 0.773 | 0.887 | 82,83,86,87,140,144,154,163,166,168,169,172,210,21 3,214,215,216,219,220,222,223,224,226,227,228,229, 230,231,315,318,319,321,322,323,325,326,530,531,53 2,774,775,776,777,800,801,802,803,804,805,806,807 |
| O43526-5 | 1.06 | 82 | 1.14 | 201.341 | 0.575 | 0.716 | 0.853 | 1.767 | 0.431 | 4.099 | 0.888 | 123,126,127,130,179,182,183,186,194,197,198,200,20 1,203,204 |
| O43526-6 | 1.015 | 253 | 0.93 | 688.744 | 0.524 | 0.72 | 0.962 | 0.403 | 1.356 | 0.297 | 0.762 | 30,31,32,33,34,35,36,38,39,40,42,74,75,78,79,82,83 ,86,87,89,95,96,99,140,141,144,145,149,150,151,152 ,153,154,155,156,160,162,163,166,168,169,172,210,2 11,212,213,214 |
Protein Structure and Feature Comparision |
Protein Structure Comparision Using Template Modeling Scores (TM-score). |
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Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Canonical validated structure (PDB)(green) |
| 3D view using mol* of O43526-1_O43526-1_7cr7_A.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical validated structure (PDB)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O43526-1_7cr7_A_O43526-2.pdb |
| 3D view using mol* of O43526-1_7cr7_A_O43526-3.pdb |
| 3D view using mol* of O43526-1_7cr7_A_O43526-4.pdb |
| 3D view using mol* of O43526-1_7cr7_A_O43526-5.pdb |
| 3D view using mol* of O43526-1_7cr7_A_O43526-6.pdb |
Protein Structure Comparision Visualization with mol*. between Canonical predicted structure (AF2)(orange) vs Alternative predicted structure (AF2)(green) |
| 3D view using mol* of O43526-1_O43526-2.pdb |
| 3D view using mol* of O43526-1_O43526-3.pdb |
| 3D view using mol* of O43526-1_O43526-4.pdb |
| 3D view using mol* of O43526-1_O43526-5.pdb |
| 3D view using mol* of O43526-1_O43526-6.pdb |
Protein Feature Comparison of the protein sequendary structures among the protiens. |
Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens. |
Protein-Protein Interaction |
Interactors from UniProt. |
| Accession_id | Subsection | Start | End | Funcitonal feature | Splicing information |
| O43526 | Region | 222 | 323 | Note=Mediates interaction with SLC5A3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88943 | Type=Deletion;Start=310;End=320 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=373;End=382 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=446 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=509;End=509 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=310;End=320 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=417;End=434 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Substitution;Start=373;End=393 |
| O43526 | Region | 317 | 539 | Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677 | Type=Deletion;Start=394;End=872 |
Interactors from STRING. |
| Gene name | Interactors |
Related Drugs to KCNQ2 |
Drugs targeting this gene/protein. (DrugBank) |
| UniProt accession | Gene name | DrugBank ID | Drug name | Drug group | Actions |
| O43526 | KCNQ2 | DB06089 | ICA-105665 | investigational | |
| O43526 | KCNQ2 | DB00321 | Amitriptyline | approved | inhibitor |
| O43526 | KCNQ2 | DB04953 | Ezogabine | approved, investigational | |
| O43526 | KCNQ2 | DB00939 | Meclofenamic acid | approved, vet_approved | other |
Related Diseases to KCNQ2 |
Previous studies relating to the alternative splicing of KCNQ2 and disease information from the MeSH term (PubMed) |
| Gene | PMID | Title | Abstract | MeSH ID | MeSH term |
Clinically important variants in KCNQ2 |
(ClinVar, 04/20/2024) |
| accession_id | uniprot_id | gene_name | Type | Variant | Clinical_significance |
|
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