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Protein

Voltage-gated potassium channel subunit beta-1

Gene

Kcnab1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:10454353). Modulates action potentials via its effect on the pore-forming alpha subunits (PubMed:10454353). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (PubMed:8824288). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members (By similarity). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels (By similarity). Accelerates KCNA4 channel closure (By similarity). Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4 (By similarity). Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity). Enhances KCNB1 and KCNB2 channel activity (PubMed:8824288). Binds NADPH; this is required for efficient down-regulation of potassium channel activity (By similarity). Has NADPH-dependent aldoketoreductase activity (By similarity). Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei97 – 971NADPBy similarity
Binding sitei119 – 1191NADPBy similarity
Active sitei124 – 1241Proton donor/acceptorBy similarity
Binding sitei124 – 1241NADPBy similarity
Binding sitei248 – 2481NADPBy similarity
Binding sitei288 – 2881NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi90 – 912NADPBy similarity
Nucleotide bindingi222 – 2232NADPBy similarity
Nucleotide bindingi277 – 2826NADPBy similarity
Nucleotide bindingi357 – 3637NADPBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Oxidoreductase, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

NADP, Potassium

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-1 (EC:1.1.1.-By similarity)
Alternative name(s):
K(+) channel subunit beta-1
Kv-beta-1
Gene namesi
Name:Kcnab1
Synonyms:Kvb1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:109155. Kcnab1.

Subcellular locationi

  • Cytoplasm By similarity
  • Membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity; Cytoplasmic side By similarity

  • Note: Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits.By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant mice show subtle defects in learning (PubMed:10454353). Such learning impairments are not detectable in older mice and are not observed when mice are kept in a stimulating environment (PubMed:14511342, PubMed:15530391).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 401401Voltage-gated potassium channel subunit beta-1PRO_0000148740Add
BLAST

Proteomic databases

EPDiP63143.
MaxQBiP63143.
PaxDbiP63143.
PeptideAtlasiP63143.
PRIDEiP63143.

PTM databases

iPTMnetiP63143.
PhosphoSiteiP63143.

Expressioni

Tissue specificityi

Detected in brain, in hippocampus and striatum (at protein level) (PubMed:10454353). Predominantly expressed in brain. No expression found in heart, skeletal muscle or kidney. In the late embryonic and early neonatal brain, highly expressed in hippocampus, cerebral cortex, caudate putamen, colliculus and cerebellum.2 Publications

Developmental stagei

Expressed from embryonic day 16. Expressed throughout embryonic development, in neonate and in adult.1 Publication

Gene expression databases

BgeeiP63143.
GenevisibleiP63143. MM.

Interactioni

Subunit structurei

Homotetramer (By similarity). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (Probable). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Interacts with KCNA1 (By similarity). Interacts with the dimer formed by GNB1 and GNG2; this enhances KCNA1 binding (By similarity). Interacts with KCNA4 (By similarity). Interacts with KCNB2 and KCNA5 (PubMed:8824288). Interacts with SQSTM1 (By similarity). Part of a complex containing KCNA1, KCNA4 and LGI1; interaction with LGI1 inhibits down-regulation of KCNA1 channel activity (By similarity).By similarityCurated1 Publication

Protein-protein interaction databases

BioGridi200883. 1 interaction.
IntActiP63143. 2 interactions.
STRINGi10090.ENSMUSP00000047480.

Structurei

3D structure databases

ProteinModelPortaliP63143.
SMRiP63143. Positions 73-395.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain of the beta subunit mediates closure of delayed rectifier potassium channels by physically obstructing the pore.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG1575. Eukaryota.
COG0667. LUCA.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP63143.
KOiK04882.
OMAiMGLVVWS.
OrthoDBiEOG71G9TR.
TreeFamiTF324563.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005400. K_chnl_volt-dep_bsu_KCNAB1.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01578. KCNAB1CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P63143-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQVSIACTEH NLKSRNGEDR LLSKQSSNAP NVVNAARAKF RTVAIIARSL
60 70 80 90 100
GTFTPQHHIS LKESTAKQTG MKYRNLGKSG LRVSCLGLGT WVTFGGQISD
110 120 130 140 150
EVAERLMTIA YESGVNLFDT AEVYAAGKAE VILGSIIKKK GWRRSSLVIT
160 170 180 190 200
TKLYWGGKAE TERGLSRKHI IEGLKGSLQR LQLEYVDVVF ANRPDSNTPM
210 220 230 240 250
EEIVRAMTHV INQGMAMYWG TSRWSAMEIM EAYSVARQFN MIPPVCEQAE
260 270 280 290 300
YHLFQREKVE VQLPELYHKI GVGAMTWSPL ACGIISGKYG NGVPESSRAS
310 320 330 340 350
LKCYQWLKER IVSEEGRKQQ NKLKDLSPIA ERLGCTLPQL AVAWCLRNEG
360 370 380 390 400
VSSVLLGSST PEQLIENLGA IQVLPKMTSH VVNEIDNILR NKPYSKKDYR

S
Length:401
Mass (Da):44,723
Last modified:July 27, 2011 - v2
Checksum:i09F7860DCD3728B6
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti28 – 281N → T in AAB87085 (PubMed:9468385).Curated
Sequence conflicti28 – 281N → T in CAA65936 (Ref. 3) Curated
Sequence conflicti57 – 571H → D in AAB37262 (PubMed:8824288).Curated
Sequence conflicti175 – 1751K → N in CAA65936 (Ref. 3) Curated
Sequence conflicti191 – 1911A → S in AAB37262 (PubMed:8824288).Curated
Sequence conflicti282 – 2821C → Y in AAB37262 (PubMed:8824288).Curated
Sequence conflicti329 – 3291I → F in AAB37262 (PubMed:8824288).Curated
Sequence conflicti349 – 3491E → D in AAB37262 (PubMed:8824288).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033003 mRNA. Translation: AAB87085.1.
U65591 mRNA. Translation: AAB37262.1.
X97281 mRNA. Translation: CAA65936.1.
AK138467 mRNA. Translation: BAE23670.1.
CH466547 Genomic DNA. Translation: EDL15543.1.
BC014701 mRNA. Translation: AAH14701.1.
CCDSiCCDS38447.1.
RefSeqiNP_034727.3. NM_010597.4.
UniGeneiMm.316402.

Genome annotation databases

EnsembliENSMUST00000049230; ENSMUSP00000047480; ENSMUSG00000027827.
GeneIDi16497.
KEGGimmu:16497.
UCSCiuc008pkj.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033003 mRNA. Translation: AAB87085.1.
U65591 mRNA. Translation: AAB37262.1.
X97281 mRNA. Translation: CAA65936.1.
AK138467 mRNA. Translation: BAE23670.1.
CH466547 Genomic DNA. Translation: EDL15543.1.
BC014701 mRNA. Translation: AAH14701.1.
CCDSiCCDS38447.1.
RefSeqiNP_034727.3. NM_010597.4.
UniGeneiMm.316402.

3D structure databases

ProteinModelPortaliP63143.
SMRiP63143. Positions 73-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200883. 1 interaction.
IntActiP63143. 2 interactions.
STRINGi10090.ENSMUSP00000047480.

PTM databases

iPTMnetiP63143.
PhosphoSiteiP63143.

Proteomic databases

EPDiP63143.
MaxQBiP63143.
PaxDbiP63143.
PeptideAtlasiP63143.
PRIDEiP63143.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000049230; ENSMUSP00000047480; ENSMUSG00000027827.
GeneIDi16497.
KEGGimmu:16497.
UCSCiuc008pkj.2. mouse.

Organism-specific databases

CTDi7881.
MGIiMGI:109155. Kcnab1.

Phylogenomic databases

eggNOGiKOG1575. Eukaryota.
COG0667. LUCA.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP63143.
KOiK04882.
OMAiMGLVVWS.
OrthoDBiEOG71G9TR.
TreeFamiTF324563.

Enzyme and pathway databases

ReactomeiR-MMU-1296072. Voltage gated Potassium channels.

Miscellaneous databases

PROiP63143.
SOURCEiSearch...

Gene expression databases

BgeeiP63143.
GenevisibleiP63143. MM.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005400. K_chnl_volt-dep_bsu_KCNAB1.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01578. KCNAB1CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Mouse brain potassium channel beta1 subunit mRNA: cloning and distribution during development."
    Butler D.M., Ono J.K., Chang T., McCaman R.E., Barish M.E.
    J. Neurobiol. 34:135-150(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
    Strain: Swiss Webster.
    Tissue: Hippocampus.
  2. "A new K+ channel beta subunit to specifically enhance Kv2.2 (CDRK) expression."
    Fink M., Duprat F., Lesage F., Heurteaux C., Romey G., Barhanin J., Lazdunski M.
    J. Biol. Chem. 271:26341-26348(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, FUNCTION.
    Tissue: Brain.
  3. "Expression of a potassium channel beta-subunit in mouse fibroblasts."
    Metzler M., Repp R., Kreuder J., Borkhardt A., Koschinski A., Lampert F., Dreyer F., Repp H.
    Submitted (AUG-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: BALB/cJ.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Spinal cord.
  5. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Eye.
  7. "Reduced K+ channel inactivation, spike broadening, and after-hyperpolarization in Kvbeta1.1-deficient mice with impaired learning."
    Giese K.P., Storm J.F., Reuter D., Fedorov N.B., Shao L.R., Leicher T., Pongs O., Silva A.J.
    Learn. Memory 5:257-273(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY.
  8. "Learning and memory impairments in Kv beta 1.1-null mutants are rescued by environmental enrichment or ageing."
    Need A.C., Irvine E.E., Giese K.P.
    Eur. J. Neurosci. 18:1640-1644(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  9. "Increased neuronal excitability, synaptic plasticity, and learning in aged Kvbeta1.1 knockout mice."
    Murphy G.G., Fedorov N.B., Giese K.P., Ohno M., Friedman E., Chen R., Silva A.J.
    Curr. Biol. 14:1907-1915(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKCAB1_MOUSE
AccessioniPrimary (citable) accession number: P63143
Secondary accession number(s): P97380
, Q61763, Q63277, Q91WM5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%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).
50%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.