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Q9CZM9 (KCMB2_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Calcium-activated potassium channel subunit beta-2
Alternative name(s):
BK channel subunit beta-2
Short name=BKbeta2
Calcium-activated potassium channel, subfamily M subunit beta-2
Charybdotoxin receptor subunit beta-2
K(VCA)beta-2
Maxi K channel subunit beta-2
Slo-beta-2
Gene names
Name:Kcnmb2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length235 AA.
Sequence statusComplete.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

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 By similarity.

Subunit structure

Interacts with KCNMA1 tetramer. There are probably 4 molecules of KCMNB2 per KCNMA1 tetramer By similarity.

Subcellular location

Membrane; Multi-pass membrane protein By similarity.

Domain

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 By similarity.

Post-translational modification

N-glycosylated By similarity.

Sequence similarities

Belongs to the KCNMB (TC 8.A.14.1) family. KCNMB2 subfamily. [View classification]

Ontologies

Keywords
   Biological processIon transport
Transport
   Cellular componentMembrane
   DomainTransmembrane
Transmembrane helix
   Molecular functionIon channel
   PTMGlycoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processdetection of calcium ion

Inferred from electronic annotation. Source: Ensembl

neuronal action potential

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentvoltage-gated potassium channel complex

Inferred from electronic annotation. Source: Ensembl

   Molecular_functioncalcium-activated potassium channel activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 235235Calcium-activated potassium channel subunit beta-2
PRO_0000187052

Regions

Topological domain1 – 4646Cytoplasmic Potential
Transmembrane47 – 6721Helical; Name=1; Potential
Topological domain68 – 194127Extracellular Potential
Transmembrane195 – 21521Helical; Name=2; Potential
Topological domain216 – 23520Cytoplasmic Potential
Region1 – 4545Ball and chain

Amino acid modifications

Glycosylation881N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential
Glycosylation1191N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
Q9CZM9 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: F87D3D91C22BBDF2

FASTA23527,120
        10         20         30         40         50         60 
MFIWTSGRTS SSYRQDEKRN IYQKIRDHDL LDKRKTVTAL KAGEDRAILL GLAMMVCSIM 

        70         80         90        100        110        120 
MYFLLGITLL RSYMQSVWTE EAQCALLNVS ITETFNCSFS CGPDCWKLSQ YPCLQVYVNL 

       130        140        150        160        170        180 
TSSGERLLLY HTEETMKINQ KCSYIPKCGN NFEESMSLVS VVMENFRRHQ HFPCYSDPEG 

       190        200        210        220        230 
NQKSVILTKL YSSNVLFHSL FWPTCMMAGG VAIVAMVKLT QYLSLLCERI QRINR 

« Hide

References

« Hide 'large scale' references
[1]"Mouse kcnmb2 subunit of the large conductance calcium-activated K channel (MaxiK, BK)."
Garcia-Valdes J., Eghbali M., Stefani E., Toro L.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Strain: C57BL/6.
Tissue: Kidney.
[2]"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. expand/collapse author list , 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: Embryo.
[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].
Strain: C57BL/6.
Tissue: Brain.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY062429 mRNA. Translation: AAL38982.1.
AK012400 mRNA. Translation: BAB28216.1.
BC046227 mRNA. Translation: AAH46227.1.
BC058957 mRNA. Translation: AAH58957.1.
CCDSCCDS17292.1.
RefSeqNP_082507.1. NM_028231.2.
XP_006535612.1. XM_006535549.1.
XP_006535613.1. XM_006535550.1.
XP_006535614.1. XM_006535551.1.
XP_006535615.1. XM_006535552.1.
UniGeneMm.64790.

3D structure databases

ProteinModelPortalQ9CZM9.
SMRQ9CZM9. Positions 1-45.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ9CZM9.

Proteomic databases

PRIDEQ9CZM9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000119310; ENSMUSP00000112531; ENSMUSG00000037610.
ENSMUST00000119970; ENSMUSP00000113234; ENSMUSG00000037610.
ENSMUST00000178668; ENSMUSP00000136596; ENSMUSG00000037610.
GeneID72413.
KEGGmmu:72413.
UCSCuc008owa.1. mouse.

Organism-specific databases

CTD10242.
MGIMGI:1919663. Kcnmb2.

Phylogenomic databases

eggNOGNOG44064.
GeneTreeENSGT00390000015997.
HOGENOMHOG000290180.
HOVERGENHBG052223.
InParanoidQ9CZM9.
KOK04938.
OMAMKINQKC.
OrthoDBEOG77WWDC.
PhylomeDBQ9CZM9.
TreeFamTF328589.

Gene expression databases

BgeeQ9CZM9.
GenevestigatorQ9CZM9.

Family and domain databases

Gene3D4.10.81.20. 1 hit.
InterProIPR003930. K_chnl_Ca-activ_BK_bsu.
IPR015382. KCNMB2_ball_chain_dom.
[Graphical view]
PANTHERPTHR10258. PTHR10258. 1 hit.
PfamPF03185. CaKB. 1 hit.
PF09303. KcnmB2_inactiv. 1 hit.
[Graphical view]
PRINTSPR01450. BKCHANNELB.
ProtoNetSearch...

Other

NextBio336214.
PROQ9CZM9.
SOURCESearch...

Entry information

Entry nameKCMB2_MOUSE
AccessionPrimary (citable) accession number: Q9CZM9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: July 9, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot