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Protein

Calcium-activated potassium channel subunit beta-2

Gene

KCNMB2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Regulatory subunit of the calcium activated potassium KCNMA1 (maxiK) channel. Modulates the calcium sensitivity and gating kinetics of KCNMA1, thereby contributing to KCNMA1 channel diversity. Acts as a negative regulator that confers rapid and complete inactivation of KCNMA1 channel complex. May participate in KCNMA1 inactivation in chromaffin cells of the adrenal gland or in hippocampal CA1 neurons.2 Publications

GO - Molecular functioni

  • calcium-activated potassium channel activity Source: UniProtKB
  • ion channel inhibitor activity Source: ProtInc
  • potassium channel regulator activity Source: ProtInc

GO - Biological processi

  • action potential Source: UniProtKB
  • blood coagulation Source: Reactome
  • detection of calcium ion Source: UniProtKB
  • neuronal action potential Source: UniProtKB
  • potassium ion transmembrane transport Source: GOC
  • potassium ion transport Source: UniProtKB
  • regulation of vasoconstriction Source: UniProtKB
  • synaptic transmission Source: GO_Central
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_23767. cGMP effects.
REACT_75896. Ca2+ activated K+ channels.

Protein family/group databases

TCDBi8.A.14.1.3. the ca(2+)-activated k(+) channel auxiliary subunit slowpoke- (slo) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Calcium-activated potassium channel subunit beta-2
Alternative name(s):
BK channel subunit beta-2
Short name:
BKbeta2
Short name:
Hbeta2
Calcium-activated potassium channel, subfamily M subunit beta-2
Charybdotoxin receptor subunit beta-2
Hbeta3
K(VCA)beta-2
Maxi K channel subunit beta-2
Slo-beta-2
Gene namesi
Name:KCNMB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6286. KCNMB2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei47 – 6721Helical; Name=1Sequence AnalysisAdd
BLAST
Topological domaini68 – 194127ExtracellularSequence AnalysisAdd
BLAST
Transmembranei195 – 21521Helical; Name=2Sequence AnalysisAdd
BLAST
Topological domaini216 – 23520CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi2 – 43FIW → GGG: Abolishes inactivation of KCNMA1 channel. 1 Publication

Organism-specific databases

PharmGKBiPA30066.

Chemistry

DrugBankiDB01110. Miconazole.
DB00721. Procaine.

Polymorphism and mutation databases

DMDMi46396054.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Calcium-activated potassium channel subunit beta-2PRO_0000187051Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi88 – 881N-linked (GlcNAc...)Sequence Analysis
Glycosylationi96 – 961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis

Post-translational modificationi

N-glycosylated.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

PaxDbiQ9Y691.
PRIDEiQ9Y691.

PTM databases

PhosphoSiteiQ9Y691.

Expressioni

Tissue specificityi

Expressed in kidney, heart and brain. Highly expressed in ovary. Expressed at low level in other tissues.3 Publications

Gene expression databases

BgeeiQ9Y691.
CleanExiHS_KCNMB2.
ExpressionAtlasiQ9Y691. baseline and differential.
GenevisibleiQ9Y691. HS.

Organism-specific databases

HPAiCAB022649.

Interactioni

Subunit structurei

Interacts with KCNMA1 tetramer. There are probably 4 molecules of KCMNB2 per KCNMA1 tetramer.1 Publication

Protein-protein interaction databases

BioGridi115536. 1 interaction.
IntActiQ9Y691. 1 interaction.
MINTiMINT-8381989.
STRINGi9606.ENSP00000351068.

Structurei

Secondary structure

1
235
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi12 – 154Combined sources
Helixi22 – 298Combined sources
Turni30 – 323Combined sources
Beta strandi33 – 353Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JO6NMR-A1-45[»]
ProteinModelPortaliQ9Y691.
SMRiQ9Y691. Positions 1-45.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y691.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 4545Ball and chainAdd
BLAST

Domaini

The ball and chain domain mediates the inactivation of KCNMA1. It occludes the conduction pathway of KCNMA1 channels, and comprises the pore-blocking ball domain (residues 1-17) and the chain domain (residues 20-45) linking it to the transmembrane segment. The ball domain is made up of a flexible N-terminus anchored at a well ordered loop-helix motif. The chain domain consists of a 4-turn helix with an unfolded linker at its C-terminus.2 Publications

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44064.
GeneTreeiENSGT00390000015997.
HOVERGENiHBG052223.
InParanoidiQ9Y691.
KOiK04938.
OMAiKMFIWTS.
PhylomeDBiQ9Y691.
TreeFamiTF328589.

Family and domain databases

Gene3Di4.10.81.20. 1 hit.
InterProiIPR003930. K_chnl_Ca-activ_BK_bsu.
IPR015382. KCNMB2_ball_chain_dom.
[Graphical view]
PANTHERiPTHR10258. PTHR10258. 1 hit.
PfamiPF03185. CaKB. 1 hit.
PF09303. KcnmB2_inactiv. 1 hit.
[Graphical view]
PRINTSiPR01450. BKCHANNELB.

Sequencei

Sequence statusi: Complete.

Q9Y691-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFIWTSGRTS SSYRHDEKRN IYQKIRDHDL LDKRKTVTAL KAGEDRAILL
60 70 80 90 100
GLAMMVCSIM MYFLLGITLL RSYMQSVWTE ESQCTLLNAS ITETFNCSFS
110 120 130 140 150
CGPDCWKLSQ YPCLQVYVNL TSSGEKLLLY HTEETIKINQ KCSYIPKCGK
160 170 180 190 200
NFEESMSLVN VVMENFRKYQ HFSCYSDPEG NQKSVILTKL YSSNVLFHSL
210 220 230
FWPTCMMAGG VAIVAMVKLT QYLSLLCERI QRINR
Length:235
Mass (Da):27,130
Last modified:November 1, 1999 - v1
Checksum:i5752021DF27D8CF5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099137 mRNA. Translation: AAD23380.1.
AF209747 mRNA. Translation: AAF36562.1.
BC017825 mRNA. Translation: AAH17825.1.
CCDSiCCDS3223.1.
RefSeqiNP_001265840.1. NM_001278911.1.
NP_005823.1. NM_005832.4.
NP_852006.1. NM_181361.2.
XP_011510627.1. XM_011512325.1.
UniGeneiHs.478368.

Genome annotation databases

EnsembliENST00000358316; ENSP00000351068; ENSG00000197584.
ENST00000420517; ENSP00000408252; ENSG00000197584.
ENST00000432997; ENSP00000407592; ENSG00000197584.
ENST00000452583; ENSP00000397483; ENSG00000197584.
GeneIDi10242.
KEGGihsa:10242.
UCSCiuc003fjd.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF099137 mRNA. Translation: AAD23380.1.
AF209747 mRNA. Translation: AAF36562.1.
BC017825 mRNA. Translation: AAH17825.1.
CCDSiCCDS3223.1.
RefSeqiNP_001265840.1. NM_001278911.1.
NP_005823.1. NM_005832.4.
NP_852006.1. NM_181361.2.
XP_011510627.1. XM_011512325.1.
UniGeneiHs.478368.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1JO6NMR-A1-45[»]
ProteinModelPortaliQ9Y691.
SMRiQ9Y691. Positions 1-45.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115536. 1 interaction.
IntActiQ9Y691. 1 interaction.
MINTiMINT-8381989.
STRINGi9606.ENSP00000351068.

Chemistry

DrugBankiDB01110. Miconazole.
DB00721. Procaine.

Protein family/group databases

TCDBi8.A.14.1.3. the ca(2+)-activated k(+) channel auxiliary subunit slowpoke- (slo) family.

PTM databases

PhosphoSiteiQ9Y691.

Polymorphism and mutation databases

DMDMi46396054.

Proteomic databases

PaxDbiQ9Y691.
PRIDEiQ9Y691.

Protocols and materials databases

DNASUi10242.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000358316; ENSP00000351068; ENSG00000197584.
ENST00000420517; ENSP00000408252; ENSG00000197584.
ENST00000432997; ENSP00000407592; ENSG00000197584.
ENST00000452583; ENSP00000397483; ENSG00000197584.
GeneIDi10242.
KEGGihsa:10242.
UCSCiuc003fjd.3. human.

Organism-specific databases

CTDi10242.
GeneCardsiGC03P177990.
HGNCiHGNC:6286. KCNMB2.
HPAiCAB022649.
MIMi605214. gene.
neXtProtiNX_Q9Y691.
PharmGKBiPA30066.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG44064.
GeneTreeiENSGT00390000015997.
HOVERGENiHBG052223.
InParanoidiQ9Y691.
KOiK04938.
OMAiKMFIWTS.
PhylomeDBiQ9Y691.
TreeFamiTF328589.

Enzyme and pathway databases

ReactomeiREACT_23767. cGMP effects.
REACT_75896. Ca2+ activated K+ channels.

Miscellaneous databases

EvolutionaryTraceiQ9Y691.
GeneWikiiKCNMB2.
GenomeRNAii10242.
NextBioi38800.
PROiQ9Y691.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Y691.
CleanExiHS_KCNMB2.
ExpressionAtlasiQ9Y691. baseline and differential.
GenevisibleiQ9Y691. HS.

Family and domain databases

Gene3Di4.10.81.20. 1 hit.
InterProiIPR003930. K_chnl_Ca-activ_BK_bsu.
IPR015382. KCNMB2_ball_chain_dom.
[Graphical view]
PANTHERiPTHR10258. PTHR10258. 1 hit.
PfamiPF03185. CaKB. 1 hit.
PF09303. KcnmB2_inactiv. 1 hit.
[Graphical view]
PRINTSiPR01450. BKCHANNELB.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular basis of fast inactivation in voltage and Ca2+-activated K+ channels: a transmembrane beta-subunit homolog."
    Wallner M., Meera P., Toro L.
    Proc. Natl. Acad. Sci. U.S.A. 96:4137-4142(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DOMAIN, TISSUE SPECIFICITY, INTERACTION WITH KCNMA1.
    Tissue: Neuroepithelium.
  2. "Cloning and functional characterization of novel large conductance calcium-activated potassium channel beta subunits, hKCNMB3 and hKCNMB4."
    Brenner R., Jegla T.J., Wickenden A., Liu Y., Aldrich R.W.
    J. Biol. Chem. 275:6453-6461(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Tissue: Ovary.
  3. "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: Embryonic testis.
  4. "Molecular basis for the inactivation of Ca2+- and voltage-dependent BK channels in adrenal chromaffin cells and rat insulinoma tumor cells."
    Xia X.-M., Ding J.-P., Lingle C.J.
    J. Neurosci. 19:5255-5264(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN, TISSUE SPECIFICITY.
  5. "A neuronal beta subunit (KCNMB4) makes the large conductance, voltage- and Ca2+-activated K+ channel resistant to charybdotoxin and iberiotoxin."
    Meera P., Wallner M., Toro L.
    Proc. Natl. Acad. Sci. U.S.A. 97:5562-5567(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  6. "Inactivation of BK channels by the NH2 terminus of the beta2 auxiliary subunit: an essential role of a terminal peptide segment of three hydrophobic residues."
    Xia X.-M., Ding J.-P., Lingle C.J.
    J. Gen. Physiol. 121:125-148(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF 2-PHE--TRP-4.
  7. "New disguises for an old channel: MaxiK channel beta-subunits."
    Orio P., Rojas P., Ferreira G., Latorre R.
    News Physiol. Sci. 17:156-161(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  8. "NMR structure of the 'ball-and-chain' domain of KCNMB2, the beta 2-subunit of large conductance Ca2+- and voltage-activated potassium channels."
    Bentrop D., Beyermann M., Wissmann R., Fakler B.
    J. Biol. Chem. 276:42116-42121(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 1-45.

Entry informationi

Entry nameiKCMB2_HUMAN
AccessioniPrimary (citable) accession number: Q9Y691
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: November 1, 1999
Last modified: July 22, 2015
This is version 117 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.