##gff-version 3 Q14721 UniProtKB Chain 1 858 . . . ID=PRO_0000054042;Note=Potassium voltage-gated channel subfamily B member 1 Q14721 UniProtKB Topological domain 1 186 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Transmembrane 187 208 . . . Note=Helical%3B Name%3DSegment S1;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 209 228 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Transmembrane 229 250 . . . Note=Helical%3B Name%3DSegment S2;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 251 259 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Transmembrane 260 280 . . . Note=Helical%3B Name%3DSegment S3;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 281 294 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Transmembrane 295 316 . . . Note=Helical%3B Voltage-sensor%3B Name%3DSegment S4;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 317 330 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Transmembrane 331 351 . . . Note=Helical%3B Name%3DSegment S5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 352 364 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Intramembrane 365 376 . . . Note=Helical%3B Name%3DPore helix;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Intramembrane 377 384 . . . Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 385 391 . . . Note=Extracellular;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Transmembrane 392 420 . . . Note=Helical%3B Name%3DSegment S6;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Topological domain 421 858 . . . Note=Cytoplasmic;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Region 1 21 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Region 59 75 . . . Note=Self-association;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Region 448 481 . . . Note=Self-association;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Region 471 524 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Region 538 574 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Region 770 807 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Region 836 858 . . . Note=Disordered;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Motif 377 382 . . . Note=Selectivity filter;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P63142 Q14721 UniProtKB Motif 590 596 . . . Note=FFAT;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:33124732;Dbxref=PMID:33124732 Q14721 UniProtKB Compositional bias 471 487 . . . Note=Basic and acidic residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Compositional bias 488 506 . . . Note=Polar residues;Ontology_term=ECO:0000256;evidence=ECO:0000256|SAM:MobiDB-lite Q14721 UniProtKB Modified residue 15 15 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 128 128 . . . Note=Phosphotyrosine%3B by Src;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 444 444 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03717 Q14721 UniProtKB Modified residue 457 457 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:Q03717 Q14721 UniProtKB Modified residue 484 484 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 496 496 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 503 503 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 519 519 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 520 520 . . . Note=Phosphoserine%3B by CDK5%3B in vitro;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 541 541 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 567 567 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 590 590 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 593 593 . . . Note=Phosphoserine;Ontology_term=ECO:0000305;evidence=ECO:0000305|PubMed:33124732;Dbxref=PMID:33124732 Q14721 UniProtKB Modified residue 607 607 . . . Note=Phosphoserine%3B by CDK5;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 656 656 . . . Note=Phosphoserine%3B by CDK5%3B in vitro;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 720 720 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 772 772 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 800 800 . . . Note=Phosphoserine;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Modified residue 805 805 . . . Note=Phosphoserine%3B by CDK5%2C MAPK14%3B in vitro;Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Cross-link 474 474 . . . Note=Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO);Ontology_term=ECO:0000250;evidence=ECO:0000250|UniProtKB:P15387 Q14721 UniProtKB Natural variant 306 306 . . . ID=VAR_075573;Note=In DEE26%3B reduces sensitivity and cooperativity of the voltage sensor for channel opening and greatly suppresses repetitive firing in cultured cortical neurons. R->C;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26477325;Dbxref=dbSNP:rs1555889130,PMID:26477325 Q14721 UniProtKB Natural variant 347 347 . . . ID=VAR_071991;Note=In DEE26%3B inhibits ion selectivity and gain of a depolarizing inward cation conductance%3B trafficks normally to the cell surface. S->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25164438;Dbxref=dbSNP:rs587777848,PMID:25164438 Q14721 UniProtKB Natural variant 374 374 . . . ID=VAR_071992;Note=In DEE26%3B inhibits ion selectivity and gain of a depolarizing inward cation conductance%3B trafficks normally to the cell surface. T->I;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25164438;Dbxref=dbSNP:rs587777849,PMID:25164438 Q14721 UniProtKB Natural variant 378 378 . . . ID=VAR_075574;Note=In DEE26%3B change in the ion selectivity from potassium-selective to nonselective cation channels and significant decrease in cell membrane localization. V->A;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26503721;Dbxref=PMID:26503721 Q14721 UniProtKB Natural variant 379 379 . . . ID=VAR_071993;Note=In DEE26%3B inhibits ion selectivity and gain of a depolarizing inward cation conductance%3B trafficks normally to the cell surface. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:25164438;Dbxref=dbSNP:rs587777850,PMID:25164438 Q14721 UniProtKB Natural variant 401 401 . . . ID=VAR_075575;Note=In DEE26%3B dominant-negative mutation resulting in loss of endogenous channel currents and greatly suppresses repetitive firing in cultured cortical neurons. G->R;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:26477325;Dbxref=PMID:26477325 Q14721 UniProtKB Natural variant 616 616 . . . ID=VAR_062182;Note=T->N;Dbxref=dbSNP:rs2229006 Q14721 UniProtKB Natural variant 616 616 . . . ID=VAR_062183;Note=T->S;Dbxref=dbSNP:rs2229006 Q14721 UniProtKB Natural variant 825 825 . . . ID=VAR_034049;Note=P->S;Dbxref=dbSNP:rs34467662 Q14721 UniProtKB Natural variant 857 857 . . . ID=VAR_062184;Note=S->N;Dbxref=dbSNP:rs34280195 Q14721 UniProtKB Mutagenesis 71 71 . . . Note=No effect on channel activity. E->Q;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12560340;Dbxref=PMID:12560340 Q14721 UniProtKB Mutagenesis 74 74 . . . Note=Reduces interaction with KCNG1 and self-interaction and impairs plasma membrane subcellular localization%2C homotetramerization and hetetrotetramerization with KCNG4%3B when associated with R-75. D->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19717558,ECO:0000269|PubMed:24901643;Dbxref=PMID:19717558,PMID:24901643 Q14721 UniProtKB Mutagenesis 75 75 . . . Note=Reduces interaction with KCNG1 and self-interaction and impairs plasma membrane subcellular localization%2C homotetramerization and hetetrotetramerization with KCNG4%3B when associated with R-74. D->R;Ontology_term=ECO:0000269,ECO:0000269;evidence=ECO:0000269|PubMed:19717558,ECO:0000269|PubMed:24901643;Dbxref=PMID:19717558,PMID:24901643 Q14721 UniProtKB Mutagenesis 79 79 . . . Note=Increases channel activity. D->E;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:12560340;Dbxref=PMID:12560340 Q14721 UniProtKB Mutagenesis 105 105 . . . Note=Reduces channel activity. Inhibits interaction with KCNG4. Impairs hetetrotetramerization with KCNG1%2C KCNG3 or KCNG4. Does not impair homotetramerization. H->V%2CR;Ontology_term=ECO:0000269;evidence=ECO:0000269|PubMed:19074135;Dbxref=PMID:19074135 Q14721 UniProtKB Beta strand 31 37 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Beta strand 40 45 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Helix 46 50 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Helix 56 60 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Helix 66 72 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Beta strand 73 77 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Turn 78 81 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Beta strand 82 85 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Helix 89 91 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7SPD Q14721 UniProtKB Helix 92 101 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Helix 112 122 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5 Q14721 UniProtKB Helix 126 128 . . . Ontology_term=ECO:0007829;evidence=ECO:0007829|PDB:7RE5