KCAB1_HUMAN
ID KCAB1_HUMAN Reviewed; 419 AA.
AC Q14722; A8K9H8; A8KAD4; B3KPZ4; Q13031; Q13302; Q16547; Q6PI60; Q99869;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=Voltage-gated potassium channel subunit beta-1;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P63144};
DE AltName: Full=K(+) channel subunit beta-1;
DE AltName: Full=Kv-beta-1;
GN Name=KCNAB1; Synonyms=KCNA1B;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.3), AND FUNCTION.
RC TISSUE=Heart left ventricle;
RX PubMed=7499366; DOI=10.1074/jbc.270.48.28531;
RA England S.K., Uebele V.N., Kodali J., Bennett P.B., Tamkun M.M.;
RT "A novel K+ channel beta-subunit (hKv beta 1.3) is produced via alternative
RT mRNA splicing.";
RL J. Biol. Chem. 270:28531-28534(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.2), FUNCTION, AND SUBUNIT.
RC TISSUE=Heart atrium;
RX PubMed=7890032; DOI=10.1016/0014-5793(95)00120-x;
RA Majumder K., De Biasi M., Wang Z., Wible B.A.;
RT "Molecular cloning and functional expression of a novel potassium channel
RT beta-subunit from human atrium.";
RL FEBS Lett. 361:13-16(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.2), FUNCTION, AND TISSUE
RP SPECIFICITY.
RC TISSUE=Heart left ventricle;
RX PubMed=7603988; DOI=10.1073/pnas.92.14.6309;
RA England S.K., Uebele V.N., Shear H., Kodali J., Bennett P.B., Tamkun M.M.;
RT "Characterization of a voltage-gated K+ channel beta subunit expressed in
RT human heart.";
RL Proc. Natl. Acad. Sci. U.S.A. 92:6309-6313(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.1), AND FUNCTION.
RC TISSUE=Hippocampus;
RX PubMed=7649300; DOI=10.1016/0014-5793(95)00785-8;
RA Mccormack K., McCormack T., Tanouye M.A., Rudy B., Stuehmer W.;
RT "Alternative splicing of the human Shaker K+ channel beta 1 gene and
RT functional expression of the beta 2 gene product.";
RL FEBS Lett. 370:32-36(1995).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.1), ALTERNATIVE SPLICING,
RP FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain cortex;
RX PubMed=8938711; DOI=10.1016/0028-3908(96)00133-5;
RA Leicher T., Roeper J., Weber K., Wang X., Pongs O.;
RT "Structural and functional characterization of human potassium channel
RT subunit beta 1 (KCNA1B).";
RL Neuropharmacology 35:787-795(1996).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS KVB1.1; KVB1.2 AND
RP KVB1.3).
RC TISSUE=Hippocampus, Thymus, and Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM KVB1.1).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-147 (ISOFORM KVB1.2), AND FUNCTION.
RC TISSUE=Heart;
RX PubMed=7890764; DOI=10.1074/jbc.270.11.6272;
RA Morales M.J., Castellino R.C., Crews A.L., Rasmusson R.L., Strauss H.C.;
RT "A novel beta subunit increases rate of inactivation of specific voltage-
RT gated potassium channel alpha subunits.";
RL J. Biol. Chem. 270:6272-6277(1995).
RN [10]
RP FUNCTION, AND DOMAIN.
RX PubMed=9763623; DOI=10.1111/j.1469-7793.1998.325be.x;
RA Accili E.A., Kuryshev Y.A., Wible B.A., Brown A.M.;
RT "Separable effects of human Kvbeta1.2 N- and C-termini on inactivation and
RT expression of human Kv1.4.";
RL J. Physiol. (Lond.) 512:325-336(1998).
RN [11]
RP FUNCTION.
RX PubMed=12077175; DOI=10.1523/jneurosci.22-12-04786.2002;
RA Maylie B., Bissonnette E., Virk M., Adelman J.P., Maylie J.G.;
RT "Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel
RT alter hKvbeta 1-induced N-type inactivation.";
RL J. Neurosci. 22:4786-4793(2002).
RN [12]
RP FUNCTION, AND INTERACTION WITH KCNA5.
RX PubMed=12130714; DOI=10.1124/jpet.102.033357;
RA Williams C.P., Hu N., Shen W., Mashburn A.B., Murray K.T.;
RT "Modulation of the human Kv1.5 channel by protein kinase C activation: role
RT of the Kvbeta1.2 subunit.";
RL J. Pharmacol. Exp. Ther. 302:545-550(2002).
RN [13]
RP FUNCTION.
RX PubMed=15361858; DOI=10.1038/nsmb825;
RA Bhalla T., Rosenthal J.J., Holmgren M., Reenan R.;
RT "Control of human potassium channel inactivation by editing of a small mRNA
RT hairpin.";
RL Nat. Struct. Mol. Biol. 11:950-956(2004).
RN [14]
RP FUNCTION.
RX PubMed=17156368; DOI=10.1111/j.1460-9568.2006.05186.x;
RA Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.;
RT "Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast
RT inactivation properties of the human potassium channels Kv1.4-1.1/Kvbeta1.1
RT and Kv1.4-1.1/Kvbeta1.2.";
RL Eur. J. Neurosci. 24:3073-3083(2006).
RN [15]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND MUTAGENESIS OF TYR-307 AND
RP ARG-316.
RX PubMed=17540341; DOI=10.1016/j.bbrc.2007.05.102;
RA Tipparaju S.M., Liu S.Q., Barski O.A., Bhatnagar A.;
RT "NADPH binding to beta-subunit regulates inactivation of voltage-gated K(+)
RT channels.";
RL Biochem. Biophys. Res. Commun. 359:269-276(2007).
RN [16]
RP FUNCTION, AND DOMAIN.
RX PubMed=19713757; DOI=10.4161/chan.3.5.9558;
RA Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.;
RT "The molecular basis for the actions of Kvbeta1.2 on the opening and
RT closing of the Kv1.2 delayed rectifier channel.";
RL Channels 3:314-322(2009).
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits (PubMed:7499366,
CC PubMed:7603988, PubMed:17156368,PubMed:17540341, PubMed:19713757).
CC Modulates action potentials via its effect on the pore-forming alpha
CC subunits (By similarity). Promotes expression of the pore-forming alpha
CC subunits at the cell membrane, and thereby increases channel activity
CC (By similarity). Mediates closure of delayed rectifier potassium
CC channels by physically obstructing the pore via its N-terminal domain
CC and increases the speed of channel closure for other family members
CC (PubMed:9763623). Promotes the closure of KCNA1, KCNA2 and KCNA5
CC channels (PubMed:7499366, PubMed:7890032, PubMed:7603988,
CC PubMed:7649300, PubMed:8938711, PubMed:12077175, PubMed:12130714,
CC PubMed:15361858, PubMed:17540341, PubMed:19713757). Accelerates KCNA4
CC channel closure (PubMed:7890032, PubMed:7649300, PubMed:7890764,
CC PubMed:9763623). Accelerates the closure of heteromeric channels formed
CC by KCNA1 and KCNA4 (PubMed:17156368). Accelerates the closure of
CC heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity).
CC Isoform KvB1.2 has no effect on KCNA1, KCNA2 or KCNB1 (PubMed:7890032,
CC PubMed:7890764). Enhances KCNB1 and KCNB2 channel activity (By
CC similarity). Binds NADPH; this is required for efficient down-
CC regulation of potassium channel activity (PubMed:17540341). Has NADPH-
CC dependent aldoketoreductase activity (By similarity). Oxidation of the
CC bound NADPH strongly decreases N-type inactivation of potassium channel
CC activity (By similarity). {ECO:0000250|UniProtKB:P63143,
CC ECO:0000250|UniProtKB:P63144, ECO:0000269|PubMed:12077175,
CC ECO:0000269|PubMed:12130714, ECO:0000269|PubMed:15361858,
CC ECO:0000269|PubMed:17156368, ECO:0000269|PubMed:17540341,
CC ECO:0000269|PubMed:19713757, ECO:0000269|PubMed:7499366,
CC ECO:0000269|PubMed:7603988, ECO:0000269|PubMed:7649300,
CC ECO:0000269|PubMed:7890032, ECO:0000269|PubMed:7890764,
CC ECO:0000269|PubMed:8938711, ECO:0000269|PubMed:9763623, ECO:0000305}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
CC potassium channel alpha subunits gives rise to a heterooctamer
CC (Probable). Identified in potassium channel complexes containing KCNA1,
CC KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity).
CC Interacts with KCNA1 (By similarity). Interacts with the dimer formed
CC by GNB1 and GNG2; this enhances KCNA1 binding (By similarity).
CC Interacts with KCNA4 (PubMed:9763623). Interacts with KCNA5
CC (PubMed:12130714). Interacts with KCNB2 (By similarity). Interacts with
CC SQSTM1 (By similarity). Part of a complex containing KCNA1, KCNA4 and
CC LGI1; interaction with LGI1 inhibits down-regulation of KCNA1 channel
CC activity (By similarity). {ECO:0000250|UniProtKB:P63143,
CC ECO:0000250|UniProtKB:P63144, ECO:0000269|PubMed:12130714,
CC ECO:0000269|PubMed:9763623, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17540341}. Membrane
CC {ECO:0000250|UniProtKB:P63144}; Peripheral membrane protein
CC {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell membrane
CC {ECO:0000269|PubMed:17540341}; Peripheral membrane protein
CC {ECO:0000269|PubMed:17540341}; Cytoplasmic side
CC {ECO:0000269|PubMed:17540341}. Note=Recruited to the cytoplasmic side
CC of the cell membrane via its interaction with pore-forming potassium
CC channel alpha subunits. {ECO:0000269|PubMed:17540341}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=KvB1.3;
CC IsoId=Q14722-1; Sequence=Displayed;
CC Name=KvB1.1;
CC IsoId=Q14722-2; Sequence=VSP_001051;
CC Name=KvB1.2;
CC IsoId=Q14722-3; Sequence=VSP_001050;
CC -!- TISSUE SPECIFICITY: In brain, expression is most prominent in caudate
CC nucleus, hippocampus and thalamus. Significant expression also detected
CC in amygdala and subthalamic nucleus. Also expressed in both healthy and
CC cardiomyopathic heart. Up to four times more abundant in left ventricle
CC than left atrium. {ECO:0000269|PubMed:7603988,
CC ECO:0000269|PubMed:8938711}.
CC -!- DOMAIN: The N-terminal domain of the beta subunit mediates closure of
CC delayed rectifier potassium channels by physically obstructing the
CC pore. {ECO:0000269|PubMed:19713757, ECO:0000269|PubMed:9763623}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; L47665; AAC41926.1; -; mRNA.
DR EMBL; U16953; AAC50122.1; -; mRNA.
DR EMBL; L39833; AAC37573.1; -; mRNA.
DR EMBL; U33428; AAC50953.1; -; mRNA.
DR EMBL; X83127; CAA58208.1; -; mRNA.
DR EMBL; AK057059; BAG51856.1; -; mRNA.
DR EMBL; AK127240; BAG54461.1; -; mRNA.
DR EMBL; AK292693; BAF85382.1; -; mRNA.
DR EMBL; AK292999; BAF85688.1; -; mRNA.
DR EMBL; CH471052; EAW78732.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78733.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78734.1; -; Genomic_DNA.
DR EMBL; BC043166; AAH43166.1; -; mRNA.
DR EMBL; U17968; AAC50113.1; -; mRNA.
DR CCDS; CCDS3174.1; -. [Q14722-1]
DR CCDS; CCDS3175.1; -. [Q14722-3]
DR CCDS; CCDS33882.1; -. [Q14722-2]
DR PIR; I55463; I55463.
DR PIR; I59393; I59393.
DR RefSeq; NP_001295146.1; NM_001308217.1.
DR RefSeq; NP_001295151.1; NM_001308222.1.
DR RefSeq; NP_003462.2; NM_003471.3. [Q14722-3]
DR RefSeq; NP_751891.1; NM_172159.3. [Q14722-2]
DR RefSeq; NP_751892.1; NM_172160.2. [Q14722-1]
DR AlphaFoldDB; Q14722; -.
DR SMR; Q14722; -.
DR BioGRID; 113626; 14.
DR IntAct; Q14722; 5.
DR STRING; 9606.ENSP00000419952; -.
DR ChEMBL; CHEMBL5884; -.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR TCDB; 8.A.5.1.1; the voltage-gated k(+) channel Beta-subunit (kvBeta) family.
DR iPTMnet; Q14722; -.
DR PhosphoSitePlus; Q14722; -.
DR BioMuta; KCNAB1; -.
DR DMDM; 18202500; -.
DR jPOST; Q14722; -.
DR MassIVE; Q14722; -.
DR MaxQB; Q14722; -.
DR PaxDb; Q14722; -.
DR PeptideAtlas; Q14722; -.
DR PRIDE; Q14722; -.
DR ProteomicsDB; 60145; -. [Q14722-1]
DR ProteomicsDB; 60146; -. [Q14722-2]
DR ProteomicsDB; 60147; -. [Q14722-3]
DR ABCD; Q14722; 4 sequenced antibodies.
DR Antibodypedia; 18386; 419 antibodies from 33 providers.
DR DNASU; 7881; -.
DR Ensembl; ENST00000302490.12; ENSP00000305858.8; ENSG00000169282.18. [Q14722-2]
DR Ensembl; ENST00000471742.5; ENSP00000418956.1; ENSG00000169282.18. [Q14722-3]
DR Ensembl; ENST00000490337.6; ENSP00000419952.1; ENSG00000169282.18. [Q14722-1]
DR GeneID; 7881; -.
DR KEGG; hsa:7881; -.
DR MANE-Select; ENST00000490337.6; ENSP00000419952.1; NM_172160.3; NP_751892.1.
DR UCSC; uc003far.3; human. [Q14722-1]
DR CTD; 7881; -.
DR DisGeNET; 7881; -.
DR GeneCards; KCNAB1; -.
DR HGNC; HGNC:6228; KCNAB1.
DR HPA; ENSG00000169282; Tissue enhanced (brain).
DR MIM; 601141; gene.
DR neXtProt; NX_Q14722; -.
DR OpenTargets; ENSG00000169282; -.
DR PharmGKB; PA370; -.
DR VEuPathDB; HostDB:ENSG00000169282; -.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000156760; -.
DR HOGENOM; CLU_023205_2_0_1; -.
DR InParanoid; Q14722; -.
DR OMA; VDLWQVH; -.
DR OrthoDB; 1106773at2759; -.
DR PhylomeDB; Q14722; -.
DR TreeFam; TF324563; -.
DR PathwayCommons; Q14722; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR SignaLink; Q14722; -.
DR BioGRID-ORCS; 7881; 7 hits in 1066 CRISPR screens.
DR ChiTaRS; KCNAB1; human.
DR GeneWiki; KCNAB1; -.
DR GenomeRNAi; 7881; -.
DR Pharos; Q14722; Tbio.
DR PRO; PR:Q14722; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q14722; protein.
DR Bgee; ENSG00000169282; Expressed in blood vessel layer and 187 other tissues.
DR ExpressionAtlas; Q14722; baseline and differential.
DR Genevisible; Q14722; HS.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IDA:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0034705; C:potassium channel complex; IDA:UniProtKB.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IMP:CAFA.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0070402; F:NADPH binding; IDA:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0019904; F:protein domain specific binding; IPI:CAFA.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:1902260; P:negative regulation of delayed rectifier potassium channel activity; IBA:GO_Central.
DR GO; GO:1903817; P:negative regulation of voltage-gated potassium channel activity; IMP:CAFA.
DR GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
DR GO; GO:1902259; P:regulation of delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
DR DisProt; DP00090; -.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR InterPro; IPR005400; K_chnl_volt-dep_bsu_KCNAB1.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43150; PTHR43150; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR01578; KCNAB1CHANEL.
DR PRINTS; PR01577; KCNABCHANNEL.
DR SUPFAM; SSF51430; SSF51430; 1.
DR TIGRFAMs; TIGR01293; Kv_beta; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Ion channel; Ion transport;
KW Membrane; NADP; Oxidoreductase; Potassium; Potassium transport;
KW Reference proteome; Transport; Voltage-gated channel.
FT CHAIN 1..419
FT /note="Voltage-gated potassium channel subunit beta-1"
FT /id="PRO_0000148739"
FT REGION 1..52
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..24
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 142
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 108..109
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 115
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 137
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 142
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 240..241
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 266
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 295..300
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 306
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 375..381
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT VAR_SEQ 1..91
FT /note="MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASENAKDSSLSPSGE
FT SQLRARQLALLREVEMNWYLKLCDLSSEHTTVCTTGMPH -> MQVSIACTEHNLKSRN
FT GEDRLLSKQSSTAPNVVNAARAKFRTVAIIARSLGTFTPQHHISLKESTAKQTGMKY
FT (in isoform KvB1.1)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:7649300,
FT ECO:0000303|PubMed:8938711"
FT /id="VSP_001051"
FT VAR_SEQ 1..91
FT /note="MLAARTGAAGSQISEENTKLRRQSGFSVAGKDKSPKKASENAKDSSLSPSGE
FT SQLRARQLALLREVEMNWYLKLCDLSSEHTTVCTTGMPH -> MHLYKPACADIPSPKL
FT GLPKSSESALKCRWHLAVTKTQPQAACKPVRPSGAAEQKYVEKFLRVHGISLQETTRAE
FT TGMAY (in isoform KvB1.2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:7603988, ECO:0000303|PubMed:7890032,
FT ECO:0000303|PubMed:7890764"
FT /id="VSP_001050"
FT MUTAGEN 307
FT /note="Y->F: Reduces affinity for NADPH."
FT /evidence="ECO:0000269|PubMed:17540341"
FT MUTAGEN 316
FT /note="R->E: Nearly abolishes NADPH binding."
FT /evidence="ECO:0000269|PubMed:17540341"
FT CONFLICT 290
FT /note="V -> L (in Ref. 5; CAA58208)"
FT /evidence="ECO:0000305"
FT CONFLICT Q14722-3:16
FT /note="L -> S (in Ref. 9; AAC50113)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 419 AA; 46563 MW; EFFDA78568007A7A CRC64;
MLAARTGAAG SQISEENTKL RRQSGFSVAG KDKSPKKASE NAKDSSLSPS GESQLRARQL
ALLREVEMNW YLKLCDLSSE HTTVCTTGMP HRNLGKSGLR VSCLGLGTWV TFGGQISDEV
AERLMTIAYE SGVNLFDTAE VYAAGKAEVI LGSIIKKKGW RRSSLVITTK LYWGGKAETE
RGLSRKHIIE GLKGSLQRLQ LEYVDVVFAN RPDSNTPMEE IVRAMTHVIN QGMAMYWGTS
RWSAMEIMEA YSVARQFNMI PPVCEQAEYH LFQREKVEVQ LPELYHKIGV GAMTWSPLAC
GIISGKYGNG VPESSRASLK CYQWLKERIV SEEGRKQQNK LKDLSPIAER LGCTLPQLAV
AWCLRNEGVS SVLLGSSTPE QLIENLGAIQ VLPKMTSHVV NEIDNILRNK PYSKKDYRS
