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Q9CZM9

- KCMB2_MOUSE

UniProt

Q9CZM9 - KCMB2_MOUSE

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Protein

Calcium-activated potassium channel subunit beta-2

Gene
Kcnmb2
Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript 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 By similarity.

GO - Molecular functioni

  1. calcium-activated potassium channel activity Source: InterPro

GO - Biological processi

  1. detection of calcium ion Source: Ensembl
  2. neuronal action potential Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Ion channel

Keywords - Biological processi

Ion transport, Transport

Enzyme and pathway databases

ReactomeiREACT_199092. Ca2+ activated K+ channels.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:Kcnmb2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 3

Organism-specific databases

MGIiMGI:1919663. Kcnmb2.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 4646Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei47 – 6721Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini68 – 194127Extracellular Reviewed predictionAdd
BLAST
Transmembranei195 – 21521Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini216 – 23520Cytoplasmic Reviewed predictionAdd
BLAST

GO - Cellular componenti

  1. voltage-gated potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 235235Calcium-activated potassium channel subunit beta-2PRO_0000187052Add
BLAST

Amino acid modifications

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

Post-translational modificationi

N-glycosylated By similarity.

Keywords - PTMi

Glycoprotein

Proteomic databases

PRIDEiQ9CZM9.

PTM databases

PhosphoSiteiQ9CZM9.

Expressioni

Gene expression databases

BgeeiQ9CZM9.
GenevestigatoriQ9CZM9.

Interactioni

Subunit structurei

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

Structurei

3D structure databases

ProteinModelPortaliQ9CZM9.
SMRiQ9CZM9. Positions 1-45.

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 By similarity.

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG44064.
GeneTreeiENSGT00390000015997.
HOGENOMiHOG000290180.
HOVERGENiHBG052223.
InParanoidiQ9CZM9.
KOiK04938.
OMAiMKINQKC.
OrthoDBiEOG77WWDC.
PhylomeDBiQ9CZM9.
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.

Q9CZM9-1 [UniParc]FASTAAdd to Basket

« Hide

MFIWTSGRTS SSYRQDEKRN IYQKIRDHDL LDKRKTVTAL KAGEDRAILL    50
GLAMMVCSIM MYFLLGITLL RSYMQSVWTE EAQCALLNVS ITETFNCSFS 100
CGPDCWKLSQ YPCLQVYVNL TSSGERLLLY HTEETMKINQ KCSYIPKCGN 150
NFEESMSLVS VVMENFRRHQ HFPCYSDPEG NQKSVILTKL YSSNVLFHSL 200
FWPTCMMAGG VAIVAMVKLT QYLSLLCERI QRINR 235
Length:235
Mass (Da):27,120
Last modified:June 1, 2001 - v1
Checksum:iF87D3D91C22BBDF2
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY062429 mRNA. Translation: AAL38982.1.
AK012400 mRNA. Translation: BAB28216.1.
BC046227 mRNA. Translation: AAH46227.1.
BC058957 mRNA. Translation: AAH58957.1.
CCDSiCCDS17292.1.
RefSeqiNP_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.
UniGeneiMm.64790.

Genome annotation databases

EnsembliENSMUST00000119310; ENSMUSP00000112531; ENSMUSG00000037610.
ENSMUST00000119970; ENSMUSP00000113234; ENSMUSG00000037610.
ENSMUST00000178668; ENSMUSP00000136596; ENSMUSG00000037610.
GeneIDi72413.
KEGGimmu:72413.
UCSCiuc008owa.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AY062429 mRNA. Translation: AAL38982.1 .
AK012400 mRNA. Translation: BAB28216.1 .
BC046227 mRNA. Translation: AAH46227.1 .
BC058957 mRNA. Translation: AAH58957.1 .
CCDSi CCDS17292.1.
RefSeqi NP_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.
UniGenei Mm.64790.

3D structure databases

ProteinModelPortali Q9CZM9.
SMRi Q9CZM9. Positions 1-45.
ModBasei Search...
MobiDBi Search...

PTM databases

PhosphoSitei Q9CZM9.

Proteomic databases

PRIDEi Q9CZM9.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000119310 ; ENSMUSP00000112531 ; ENSMUSG00000037610 .
ENSMUST00000119970 ; ENSMUSP00000113234 ; ENSMUSG00000037610 .
ENSMUST00000178668 ; ENSMUSP00000136596 ; ENSMUSG00000037610 .
GeneIDi 72413.
KEGGi mmu:72413.
UCSCi uc008owa.1. mouse.

Organism-specific databases

CTDi 10242.
MGIi MGI:1919663. Kcnmb2.

Phylogenomic databases

eggNOGi NOG44064.
GeneTreei ENSGT00390000015997.
HOGENOMi HOG000290180.
HOVERGENi HBG052223.
InParanoidi Q9CZM9.
KOi K04938.
OMAi MKINQKC.
OrthoDBi EOG77WWDC.
PhylomeDBi Q9CZM9.
TreeFami TF328589.

Enzyme and pathway databases

Reactomei REACT_199092. Ca2+ activated K+ channels.

Miscellaneous databases

NextBioi 336214.
PROi Q9CZM9.
SOURCEi Search...

Gene expression databases

Bgeei Q9CZM9.
Genevestigatori Q9CZM9.

Family and domain databases

Gene3Di 4.10.81.20. 1 hit.
InterProi IPR003930. K_chnl_Ca-activ_BK_bsu.
IPR015382. KCNMB2_ball_chain_dom.
[Graphical view ]
PANTHERi PTHR10258. PTHR10258. 1 hit.
Pfami PF03185. CaKB. 1 hit.
PF09303. KcnmB2_inactiv. 1 hit.
[Graphical view ]
PRINTSi PR01450. BKCHANNELB.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiKCMB2_MOUSE
AccessioniPrimary (citable) accession number: Q9CZM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 13, 2004
Last sequence update: June 1, 2001
Last modified: September 3, 2014
This is version 89 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

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