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Center for Computational Systems Medicine
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Protein Summary

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AS Summary

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Protein Functional Features

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Gene Isoform Structures and Expression Levels

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Protein Structures

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pLDDT Score Distribution

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Ramachandran Plot of Protein Structures

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Potential Active Site Information

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Protein Structure and Feature Comparision

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Protein-Protein Interaction

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Related Drugs

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Related Diseases

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Clinically Important Variants

Protein:KCNQ2

Protein Summary

check button Gene summary
Gene name: KCNQ2
ASpdb.0 ID: 3785
Gene
Gene symbol

KCNQ2

Gene ID

3785

Gene namepotassium voltage-gated channel subfamily Q member 2
SynonymsBFNC|DEE7|EBN|EBN1|ENB1|HNSPC|KCNA11|KV7.2
Cytomap

20q13.33

Type of geneprotein-coding
Descriptionpotassium 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 date20240416
UniProtAcc

O43526


check button Gene ontology of this gene with evidence of Inferred from Direct Assay (IDA) from Entrez
PartnerGeneGO IDGO termPubMed ID
GeneKCNQ2

GO:0005249

voltage-gated potassium channel activity

9836639|27564677

GeneKCNQ2

GO:0005516

calmodulin binding

27564677

GeneKCNQ2

GO:0005886

plasma membrane

9836639|10788442

GeneKCNQ2

GO:0008076

voltage-gated potassium channel complex

9836639|27564677

GeneKCNQ2

GO:0071805

potassium ion transmembrane transport

9836639|27564677



AS Summary

check button Information of the canonical protein with experimentally identified structure from PDB (2023).
UniProt AccFile namePDB IDMethodResolutionChainStartEnd
O43526-1O43526-1_7cr7_A.pdb7CR7EM3.7A70600

check button ASpdb's canonical and alternatively spliced isoform information.
accession_idgene_namecanonical_idalternative_idcanonical_lengthalternative_lengthcanonical_startcanonical_endtypeoriginalSEQvariationSEQalternative_startalternative_end
O43526KCNQ2O43526-1O43526-2872854417434Deletionnonenone416416
O43526KCNQ2O43526-1O43526-3872844373382Deletionnonenone372372
O43526KCNQ2O43526-1O43526-3872844417434Deletionnonenone406406
O43526KCNQ2O43526-1O43526-4872841417446Deletionnonenone416416
O43526KCNQ2O43526-1O43526-4872841509509Deletionnonenone478478
O43526KCNQ2O43526-1O43526-5872843310320Deletionnonenone309309
O43526KCNQ2O43526-1O43526-5872843417434Deletionnonenone405405
O43526KCNQ2O43526-1O43526-6872393373393SubstitutionSSQTQTYGASRLIPPLNQLELRYRRRAPATKQLFHFLFSICS373393
O43526KCNQ2O43526-1O43526-6872393394872Deletionnonenone393393

check buttonMultiple sequence alignment of our canonical and alternatively spliced KCNQ2

check button Matched gene isoform IDs with Ensembl and RefSeq of our canonical and alternative spliced genes of KCNQ2
UniProt-idENSGENSTENSP
O43526-1ENSG00000075043.21ENST00000359125.7ENSP00000352035.2
O43526-2ENSG00000075043.21ENST00000626839.2ENSP00000486706.1
O43526-3ENSG00000075043.21ENST00000360480.7ENSP00000353668.3
O43526-4ENSG00000075043.21ENST00000344462.8ENSP00000339611.4
O43526-6ENSG00000075043.21ENST00000344425.8ENSP00000345523.5

UniProt-idNM IDNP ID
O43526-1NM_172107.3NP_742105.1
O43526-2NM_172106.2NP_742104.1
O43526-3NM_004518.5NP_004509.2
O43526-4NM_172108.4NP_742106.1
O43526-6NM_172109.2NP_742107.1

check buttonAmino acid sequences of our canonical and alternatively spliced KCNQ2
accession_idProtein sequence
O43526-1MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG
WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI
AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW
GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW
QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSKGSPCRGPLCGCCPGRSSQKVSLKDRVFSSPRGV
AAKGKGSPQAQTVRRSPSADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSI
RAVCVMRFLVSKRKFKESLRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQV
LSMEKKLDFLVNIYMQRMGIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQP
QSHPRQGHGTSPVGDHGSLVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQS
O43526-2MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG
WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI
AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW
GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW
QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPS
ADQSLEDSPSKVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKES
LRPYDVMDVIEQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRM
GIPPTETEAYFGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGS
LVRIPPPPAHERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCA
O43526-3MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG
WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI
AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW
GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW
QYYERTVTVPMYRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPS
KVPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVI
EQYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAY
FGAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAH
ERSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGE
O43526-4MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG
WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI
AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW
GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW
QYYERTVTVPMYSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSKV
PKSWSFGDRSRARQAFRIKGAASRQNSEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIEQY
SAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYFGA
KEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHERS
LSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGESDT
O43526-5MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG
WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI
AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW
GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTWQYYERTVTVPM
YSSQTQTYGASRLIPPLNQLELLRNLKSKSGLAFRKDPPPEPSPSQKVSLKDRVFSSPRGVAAKGKGSPQAQTVRRSPSADQSLEDSPSK
VPKSWSFGDRSRARQAFRIKGAASRQNSEEASLPGEDIVDDKSCPCEFVTEDLTPGLKVSIRAVCVMRFLVSKRKFKESLRPYDVMDVIE
QYSAGHLDMLSRIKSLQSRVDQIVGRGPAITDKDRTKGPAEAELPEDPSMMGRLGKVEKQVLSMEKKLDFLVNIYMQRMGIPPTETEAYF
GAKEPEPAPPYHSPEDSREHVDRHGCIVKIVRSSSSTGQKNFSAPPAAPPVQCPPSTSWQPQSHPRQGHGTSPVGDHGSLVRIPPPPAHE
RSLSAYGGGNRASMEFLRQEDTPGCRPPEGNLRDSDTSISIPSVDHEELERSFSGFSISQSKENLDALNSCYAAVAPCAKVRPYIAEGES
O43526-6MVQKSRNGGVYPGPSGEKKLKVGFVGLDPGAPDSTRDGALLIAGSEAPKRGSILSKPRAGGAGAGKPPKRNAFYRKLQNFLYNVLERPRG
WAFIYHAYVFLLVFSCLVLSVFSTIKEYEKSSEGALYILEIVTIVVFGVEYFVRIWAAGCCCRYRGWRGRLKFARKPFCVIDIMVLIASI
AVLAAGSQGNVFATSALRSLRFLQILRMIRMDRRGGTWKLLGSVVYAHSKELVTAWYIGFLCLILASFLVYLAEKGENDHFDTYADALWW
GLITLTTIGYGDKYPQTWNGRLLAATFTLIGVSFFALPAGILGSGFALKVQEQHRQKHFEKRRNPAAGLIQSAWRFYATNLSRTDLHSTW

Protein Functional Features

check buttonMain function of this protein. (from UniProt)
KCNQ2 (go to UniProt):O43526

check buttonRetention 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

download page

* Minus value of BPloci means that the break pointn is located before the CDS.
- Retained protein feature among the 13 regional features.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
O43526Transmembrane292312Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=310;End=320
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=417;End=434
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=373;End=382
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=417;End=434
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=417;End=446
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=509;End=509
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=310;End=320
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=417;End=434
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Substitution;Start=373;End=393
O43526Topological domain313872Note=Cytoplasmic;Ontology_term=ECO:0000255;evidence=ECO:0000255Type=Deletion;Start=394;End=872
O43526Region222323Note=Mediates interaction with SLC5A3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88943Type=Deletion;Start=310;End=320
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=434
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=373;End=382
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=434
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=446
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=509;End=509
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=310;End=320
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=434
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Substitution;Start=373;End=393
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=394;End=872
O43526Region402422Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=417;End=434
O43526Region402422Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=417;End=434
O43526Region402422Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=417;End=446
O43526Region402422Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=417;End=434
O43526Region402422Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872
O43526Region442488Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=417;End=446
O43526Region442488Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872
O43526Region598619Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872
O43526Region659680Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872
O43526Region693757Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872
O43526Region838872Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872
O43526Compositional bias459479Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-liteType=Deletion;Start=394;End=872


Gene Isoform Structures and Expression Levels for KCNQ2

check buttonGene 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.
gene isoform structure of KCNQ2

check button Expression levels of gene isoforms across GTEx.
gtex expression

check button Expression levels of gene isoforms across TCGA.
tcga expression


Protein Structures

check button 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

check button pLDDT score distribution of the predicted protein structures from AlphaFold2
* AlphaFold produces a per-residue confidence score (pLDDT) between 0 and 100.
pLDDT distribution across the protein length of O43526-1
all structure
pLDDT distribution across the protein length of O43526-2
all structure
pLDDT distribution across the protein length of O43526-3
all structure
pLDDT distribution across the protein length of O43526-4
all structure
pLDDT distribution across the protein length of O43526-5
all structure
pLDDT distribution across the protein length of O43526-6
all structure


Ramachandran Plot of Protein Structures


check button 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
all structure
Ramachandran plot of O43526-3
all structure
Ramachandran plot of O43526-5
all structure
Ramachandran plot of O43526-6
all structure

Potential Active Site Information


check button The potential binding sites of these proteins were identified using SiteMap, a module of the Schrodinger suite.
UniProt-idSite scoreSizeD scoreVolumeExposureEnclosureContactPhobicPhilicBalanceDon/AccResidues
O43526-10.9612630.971679.4830.6620.640.80.2881.0830.2660.48571,73,74,75,76,77,78,79,80,82,83,84,86,87,88,89,92
,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
O43526-21.072811.123201.6840.5210.7911.0251.9070.6073.1420.529123,126,127,130,178,179,182,183,186,194,197,200,20
1,203,204,207
O43526-31.0211121.07497.6930.7190.6720.810.6520.8390.7770.901327,331,334,335,337,338,341,342,345,359,362,363,36
6,508,511,512,515,516,519,523,525,526,529,530,532,
534,535,537,538,539,541,542
O43526-41.0172041.061775.180.6710.6750.8240.6730.870.7730.88782,83,86,87,140,144,154,163,166,168,169,172,210,21
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

O43526-51.06821.14201.3410.5750.7160.8531.7670.4314.0990.888123,126,127,130,179,182,183,186,194,197,198,200,20
1,203,204
O43526-61.0152530.93688.7440.5240.720.9620.4031.3560.2970.76230,31,32,33,34,35,36,38,39,40,42,74,75,78,79,82,83
,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


check button Protein Structure Comparision Using Template Modeling Scores (TM-score).
all structure

check button 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

check button 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

check button 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

check button Protein Feature Comparison of the protein sequendary structures among the protiens.
./stats/secondary_structure/figure/O43526-1_vs_O43526-2.png
all structure<
./stats/secondary_structure/figure/O43526-1_vs_O43526-3.png
all structure<
./stats/secondary_structure/figure/O43526-1_vs_O43526-4.png
all structure<
./stats/secondary_structure/figure/O43526-1_vs_O43526-5.png
all structure<
./stats/secondary_structure/figure/O43526-1_vs_O43526-6.png
all structure<

check button Protein Feature Comparison of the relative accessible surface area (ASA) among the protiens.
./stats/relative_asa/O43526-1_vs_O43526-2.png
all structure<
./stats/relative_asa/O43526-1_vs_O43526-3.png
all structure<
./stats/relative_asa/O43526-1_vs_O43526-4.png
all structure<
./stats/relative_asa/O43526-1_vs_O43526-5.png
all structure<
./stats/relative_asa/O43526-1_vs_O43526-6.png
all structure<


Protein-Protein Interaction


check button Interactors from UniProt.
Accession_idSubsectionStartEndFuncitonal featureSplicing information
O43526Region222323Note=Mediates interaction with SLC5A3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:O88943Type=Deletion;Start=310;End=320
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=434
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=373;End=382
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=434
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=446
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=509;End=509
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=310;End=320
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=417;End=434
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Substitution;Start=373;End=393
O43526Region317539Note=Mediates interaction with calmodulin;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:27564677;Dbxref=PMID:27564677Type=Deletion;Start=394;End=872


check button Interactors from STRING.
Gene nameInteractors


Related Drugs to KCNQ2


check button Drugs targeting this gene/protein.
(DrugBank)
UniProt accessionGene nameDrugBank IDDrug nameDrug groupActions
O43526KCNQ2DB06089ICA-105665investigational
O43526KCNQ2DB00321Amitriptylineapprovedinhibitor
O43526KCNQ2DB04953Ezogabineapproved, investigational
O43526KCNQ2DB00939Meclofenamic acidapproved, vet_approvedother

Related Diseases to KCNQ2


check button Previous studies relating to the alternative splicing of KCNQ2 and disease information from the MeSH term (PubMed)
GenePMIDTitleAbstractMeSH IDMeSH term


Clinically important variants in KCNQ2


check button (ClinVar, 04/20/2024)
accession_iduniprot_idgene_nameTypeVariantClinical_significance