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Protein

Voltage-gated potassium channel subunit beta-2

Gene

Kcnab2

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:8576199). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (PubMed:11825900, PubMed:21209188). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:8576199). Modulates the functional properties of KCNA4 (By similarity). Modulates the functional properties of KCNA5 (PubMed:8576199). Enhances KCNB2 channel activity (PubMed:8824288). Modulates the functional properties of KCNA5 (PubMed:8576199). Binds NADPH and has NADPH-dependent aldoketoreductase activity (By similarity). Has broad substrate specificity and can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro) (By similarity).By similarity4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631NADPBy similarity
Binding sitei85 – 851NADPBy similarity
Active sitei90 – 901Proton donor/acceptorBy similarity
Binding sitei90 – 901NADPBy similarity
Binding sitei214 – 2141NADPBy similarity
Binding sitei254 – 2541NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 572NADPBy similarity
Nucleotide bindingi188 – 1892NADPBy similarity
Nucleotide bindingi243 – 2486NADPBy similarity
Nucleotide bindingi323 – 3297NADPBy similarity

GO - Molecular functioni

  1. aldo-keto reductase (NADP) activity Source: UniProtKB
  2. potassium channel regulator activity Source: UniProtKB
  3. voltage-gated potassium channel activity Source: InterPro

GO - Biological processi

  1. hematopoietic progenitor cell differentiation Source: MGI
  2. NADPH oxidation Source: UniProtKB
  3. neuromuscular process Source: UniProtKB
  4. oxidation-reduction process Source: UniProtKB
  5. protein heterooligomerization Source: Ensembl
  6. regulation of potassium ion transmembrane transport Source: UniProtKB
  7. regulation of protein localization to cell surface Source: UniProtKB
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

ReactomeiREACT_199077. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-2 (EC:1.1.1.-By similarity)
Alternative name(s):
K(+) channel subunit beta-2
Kv-beta-2
Neuroimmune protein F5
Gene namesi
Name:Kcnab2
Synonyms:Ckbeta2, I2rf5, Kcnb3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 4

Organism-specific databases

MGIiMGI:109239. Kcnab2.

Subcellular locationi

Cytoplasm By similarity. Membrane 2 Publications; Peripheral membrane protein Curated; Cytoplasmic side Curated. Cell membrane By similarity; Peripheral membrane protein Curated; Cytoplasmic side Curated. Cell projectionaxon 1 Publication. Cell junctionsynapsesynaptosome 1 Publication. Cytoplasmcytoskeleton By similarity
Note: Recruited to the cytoplasmic side of the cell membrane via its interaction with pore-forming potassium channel alpha subunits. Associates with microtubules when unphosphorylated.By similarity

GO - Cellular componenti

  1. axon terminus Source: UniProtKB
  2. cytosol Source: UniProtKB
  3. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  4. juxtaparanode region of axon Source: UniProtKB
  5. membrane Source: UniProtKB
  6. pinceau fiber Source: UniProtKB
  7. potassium channel complex Source: UniProtKB
  8. voltage-gated potassium channel complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Disruption phenotypei

Mutant mice are born at the expected Mendelian rate and are fertile, but exhibit occasional seizures and have a median lifespan of 255 days, which is much shorter than the 400 days typically observed for heterozygotes (PubMed:11825900). The reduction in lifespan depends strongly on the genetic background; median survival is 138 days for B6 mice, 255 days for B6/129 mice and over 400 days for 129/SvEv mice (PubMed:15720404). Mice exhibit whole body tremors after swimming in cold water, which is not observed in wild-type (PubMed:11825900). The whole body tremors observed after swimming in cold water differ between mouse strains; the observed differences are largely due to differences in the decrease of the core body temperature (PubMed:15720404). Mice lacking both KCNAB1 and KCNAB2 have a median survival of 114 days instead of the 255 days observed for mice lacking only KCNAB2, but show no aggravation of the whole body tremors observed after swimming in cold water (PubMed:15720404). Mice lacking KCNAB2 show subtle deficits in associative learning and aberrant excitability of neurons from the lateral amygdala (PubMed:21209188).3 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901Y → F: No detectable phenotype. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Voltage-gated potassium channel subunit beta-2PRO_0000148747Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91PhosphoserineBy similarity
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei112 – 1121Phosphoserine1 Publication
Modified residuei124 – 1241N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by PRKCZ; may be regulated by incorporation in a complex composed of PRKCZ and SQSTM1.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP62482.
PaxDbiP62482.
PRIDEiP62482.

PTM databases

PhosphoSiteiP62482.

Expressioni

Tissue specificityi

Detected in brain (PubMed:21357749). Detected at basket cell terminals in cerebellum and in the juxtaparanodal region of nodes of Ranvier (at protein level) (PubMed:11825900). Strongest expression in brain and eye. Highest levels in brain detected in brainstem and diencephalon. Strong expression also detected in lung and heart. Moderate expression in kidney, T-lymphocytes and skeletal muscle.4 Publications

Developmental stagei

Not detected prior to birth, low levels of expression detected from postnatal days 1 to 7. Expression reaches adult levels by postnatal day 21.1 Publication

Gene expression databases

BgeeiP62482.
ExpressionAtlasiP62482. baseline and differential.
GenevestigatoriP62482.

Interactioni

Subunit structurei

Homotetramer (By similarity). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (By similarity). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Interacts with KCNA1 (By similarity). Interacts with KCNA2 (By similarity). Interacts with KCNA4 and KCND3 (By similarity). Interacts (in unphosphorylated form) with MAPRE1 (By similarity). Interacts with KCNA5 (PubMed:8576199, PubMed:8824288). Interacts with KCNB2 (PubMed:8824288). Forms a ternary complex with SQSTM1 and PRKCZ (By similarity).By similarity2 Publications

Protein-protein interaction databases

BioGridi200884. 3 interactions.
IntActiP62482. 6 interactions.
MINTiMINT-138568.

Structurei

3D structure databases

ProteinModelPortaliP62482.
SMRiP62482. Positions 36-361.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

In contrast to KCNAB1, the shorter N-terminal domain of KCNAB2 cannot mediate closure of delayed rectifier potassium channels by physically obstructing the pore.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP62482.
KOiK04883.
OrthoDBiEOG71G9TR.
PhylomeDBiP62482.
TreeFamiTF324563.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005401. K_chnl_volt-dep_bsu_KCNAB2.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P62482-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS
60 70 80 90 100
CLGLGTWVTF GGQITDEMAE HLMTLAYDNG INLFDTAEVY AAGKAEVVLG
110 120 130 140 150
NIIKKKGWRR SSLVITTKIF WGGKAETERG LSRKHIIEGL KASLERLQLE
160 170 180 190 200
YVDVVFANRP DPNTPMEETV RAMTHVINQG MAMYWGTSRW SSMEIMEAYS
210 220 230 240 250
VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA MTWSPLACGI
260 270 280 290 300
VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
310 320 330 340 350
CTLPQLAIAW CLRNEGVSSV LLGASNAEQL MENIGAIQVL PKLSSSIVHE
360
IDSILGNKPY SKKDYRS
Length:367
Mass (Da):41,021
Last modified:July 5, 2004 - v1
Checksum:i5303FD1411B324FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti64 – 641I → L in AAB37263 (PubMed:8824288).Curated
Sequence conflicti99 – 1002LG → FR in AAA75174 (PubMed:1573677).Curated
Sequence conflicti202 – 2021A → G in AAB37263 (PubMed:8824288).Curated
Sequence conflicti266 – 2661S → L in AAA75174 (PubMed:1573677).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48983 mRNA. Translation: AAB00829.1.
U65592 mRNA. Translation: AAB37263.1.
U31908 mRNA. Translation: AAA75174.1.
BC039178 mRNA. Translation: AAH39178.1.
CCDSiCCDS19000.1.
RefSeqiNP_001239585.1. NM_001252656.1.
NP_034728.2. NM_010598.3.
UniGeneiMm.388924.

Genome annotation databases

EnsembliENSMUST00000105648; ENSMUSP00000101273; ENSMUSG00000028931.
ENSMUST00000160884; ENSMUSP00000125058; ENSMUSG00000028931.
GeneIDi16498.
KEGGimmu:16498.
UCSCiuc008wal.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L48983 mRNA. Translation: AAB00829.1.
U65592 mRNA. Translation: AAB37263.1.
U31908 mRNA. Translation: AAA75174.1.
BC039178 mRNA. Translation: AAH39178.1.
CCDSiCCDS19000.1.
RefSeqiNP_001239585.1. NM_001252656.1.
NP_034728.2. NM_010598.3.
UniGeneiMm.388924.

3D structure databases

ProteinModelPortaliP62482.
SMRiP62482. Positions 36-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200884. 3 interactions.
IntActiP62482. 6 interactions.
MINTiMINT-138568.

PTM databases

PhosphoSiteiP62482.

Proteomic databases

MaxQBiP62482.
PaxDbiP62482.
PRIDEiP62482.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000105648; ENSMUSP00000101273; ENSMUSG00000028931.
ENSMUST00000160884; ENSMUSP00000125058; ENSMUSG00000028931.
GeneIDi16498.
KEGGimmu:16498.
UCSCiuc008wal.2. mouse.

Organism-specific databases

CTDi8514.
MGIiMGI:109239. Kcnab2.

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP62482.
KOiK04883.
OrthoDBiEOG71G9TR.
PhylomeDBiP62482.
TreeFamiTF324563.

Enzyme and pathway databases

ReactomeiREACT_199077. Voltage gated Potassium channels.

Miscellaneous databases

NextBioi289815.
PROiP62482.
SOURCEiSearch...

Gene expression databases

BgeeiP62482.
ExpressionAtlasiP62482. baseline and differential.
GenevestigatoriP62482.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005401. K_chnl_volt-dep_bsu_KCNAB2.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Functional differences in Kv1.5 currents expressed in mammalian cell lines are due to the presence of endogenous Kv beta 2.1 subunits."
    Uebele V.N., England S.K., Chaudhary A., Tamkun M.M., Snyders D.J.
    J. Biol. Chem. 271:2406-2412(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH KCNA5, SUBCELLULAR LOCATION.
    Tissue: Fibroblast.
  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], TISSUE SPECIFICITY, INTERACTION WITH KCNA5 AND KCNB2, FUNCTION.
    Tissue: Brain cortex.
  3. "Characterization of a novel mRNA expressed by neurons in mature brain."
    Cohen J.A., Arai M., Prak E.L., Brooks S.A., Young L.H., Prystowsky M.B.
    J. Neurosci. Res. 31:273-284(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
    Strain: C57BL/6N.
    Tissue: Brain and T-cell.
  4. "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.
  5. "Genetic analysis of the mammalian K+ channel beta subunit Kvbeta 2 (Kcnab2)."
    McCormack K., Connor J.X., Zhou L., Ho L.L., Ganetzky B., Chiu S.Y., Messing A.
    J. Biol. Chem. 277:13219-13228(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF TYR-90.
  6. Cited for: DISRUPTION PHENOTYPE.
  7. "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates Kv1 channel axonal targeting."
    Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B., Trimmer J.S.
    J. Cell Biol. 192:813-824(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-20 AND SER-112, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Deletion of the mouse homolog of KCNAB2, a gene linked to monosomy 1p36, results in associative memory impairments and amygdala hyperexcitability."
    Perkowski J.J., Murphy G.G.
    J. Neurosci. 31:46-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: DISRUPTION PHENOTYPE, FUNCTION.

Entry informationi

Entry nameiKCAB2_MOUSE
AccessioniPrimary (citable) accession number: P62482
Secondary accession number(s): P97381, Q60942, Q64284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: March 4, 2015
This is version 103 of the entry and version 1 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

External Data

Dasty 3

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 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.