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Q12791

- KCMA1_HUMAN

UniProt

Q12791 - KCMA1_HUMAN

Protein

Calcium-activated potassium channel subunit alpha-1

Gene

KCNMA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 147 (01 Oct 2014)
      Sequence version 2 (13 Apr 2004)
      Previous versions | rss
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    Functioni

    Potassium channel activated by both membrane depolarization or increase in cytosolic Ca2+ that mediates export of K+. It is also activated by the concentration of cytosolic Mg2+. Its activation dampens the excitatory events that elevate the cytosolic Ca2+ concentration and/or depolarize the cell membrane. It therefore contributes to repolarization of the membrane potential. Plays a key role in controlling excitability in a number of systems, such as regulation of the contraction of smooth muscle, the tuning of hair cells in the cochlea, regulation of transmitter release, and innate immunity. In smooth muscles, its activation by high level of Ca2+, caused by ryanodine receptors in the sarcoplasmic reticulum, regulates the membrane potential. In cochlea cells, its number and kinetic properties partly determine the characteristic frequency of each hair cell and thereby helps to establish a tonotopic map. Kinetics of KCNMA1 channels are determined by alternative splicing, phosphorylation status and its combination with modulating beta subunits. Highly sensitive to both iberiotoxin (IbTx) and charybdotoxin (CTX).

    Enzyme regulationi

    Ethanol and carbon monoxide-bound heme increase channel activation. Heme inhibits channel activation.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi439 – 4391MagnesiumBy similarity
    Metal bindingi462 – 4621MagnesiumBy similarity
    Metal bindingi464 – 4641MagnesiumBy similarity
    Metal bindingi1012 – 10121Calcium; via carbonyl oxygen
    Metal bindingi1015 – 10151Calcium; via carbonyl oxygen
    Metal bindingi1018 – 10181Calcium
    Metal bindingi1020 – 10201Calcium

    GO - Molecular functioni

    1. actin binding Source: BHF-UCL
    2. calcium-activated potassium channel activity Source: UniProtKB
    3. large conductance calcium-activated potassium channel activity Source: UniProtKB
    4. metal ion binding Source: UniProtKB-KW
    5. protein binding Source: UniProtKB
    6. voltage-gated potassium channel activity Source: UniProtKB

    GO - Biological processi

    1. adult walking behavior Source: Ensembl
    2. auditory receptor cell differentiation Source: Ensembl
    3. blood coagulation Source: Reactome
    4. cell maturation Source: Ensembl
    5. cellular potassium ion homeostasis Source: UniProtKB
    6. eye blink reflex Source: Ensembl
    7. locomotor rhythm Source: Ensembl
    8. micturition Source: UniProtKB
    9. negative regulation of cell volume Source: UniProtKB
    10. neuromuscular process controlling balance Source: Ensembl
    11. neuronal action potential Source: Ensembl
    12. positive regulation of apoptotic process Source: UniProtKB
    13. potassium ion transmembrane transport Source: RefGenome
    14. potassium ion transport Source: UniProtKB
    15. protein homooligomerization Source: Ensembl
    16. regulation of aldosterone metabolic process Source: Ensembl
    17. regulation of membrane potential Source: UniProtKB
    18. relaxation of vascular smooth muscle Source: Ensembl
    19. response to calcium ion Source: UniProtKB
    20. response to carbon monoxide Source: UniProtKB
    21. response to hypoxia Source: UniProtKB
    22. response to osmotic stress Source: UniProtKB
    23. saliva secretion Source: Ensembl
    24. sensory perception of sound Source: Ensembl
    25. smooth muscle contraction involved in micturition Source: UniProtKB
    26. synaptic transmission Source: Reactome

    Keywords - Molecular functioni

    Ion channel, Potassium channel, Voltage-gated channel

    Keywords - Biological processi

    Ion transport, Potassium transport, Transport

    Keywords - Ligandi

    Calcium, Magnesium, Metal-binding, Potassium

    Enzyme and pathway databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Calcium-activated potassium channel subunit alpha-1
    Alternative name(s):
    BK channel
    BKCA alpha
    Calcium-activated potassium channel, subfamily M subunit alpha-1
    K(VCA)alpha
    KCa1.1
    Maxi K channel
    Short name:
    MaxiK
    Slo-alpha
    Slo1
    Slowpoke homolog
    Short name:
    Slo homolog
    Short name:
    hSlo
    Gene namesi
    Name:KCNMA1
    Synonyms:KCNMA, SLO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 10

    Organism-specific databases

    HGNCiHGNC:6284. KCNMA1.

    Subcellular locationi

    Cell membrane 2 Publications; Multi-pass membrane protein 2 Publications

    GO - Cellular componenti

    1. apical plasma membrane Source: UniProtKB
    2. caveola Source: BHF-UCL
    3. endoplasmic reticulum Source: Ensembl
    4. external side of plasma membrane Source: Ensembl
    5. extracellular vesicular exosome Source: UniProt
    6. integral component of membrane Source: UniProtKB
    7. plasma membrane Source: Reactome
    8. postsynaptic membrane Source: Ensembl
    9. terminal bouton Source: Ensembl
    10. voltage-gated potassium channel complex Source: UniProtKB

    Keywords - Cellular componenti

    Cell membrane, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Generalized epilepsy and paroxysmal dyskinesia (GEPD) [MIM:609446]: Epilepsy is one of the most common and debilitating neurological disorders. Paroxysmal dyskinesias are neurological disorders characterized by sudden, unpredictable, disabling attacks of involuntary movement often requiring life-long treatment. The coexistence of epilepsy and paroxysmal dyskinesia in the same individual or family is an increasingly recognized phenomenon. Patients manifest absence seizures, generalized tonic-clonic seizures, paroxysmal nonkinesigenic dyskinesia, involuntary dystonic or choreiform movements. Onset is usually in childhood and patients may have seizures only, dyskinesia only, or both.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti434 – 4341D → G in GEPD; may have a synergistic effect with ethanol in the triggering of symptoms. 1 Publication
    VAR_023821

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi118 – 1181C → A: Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-119 and A-121. 3 Publications
    Mutagenesisi119 – 1191C → A: Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-118 and A-121. 3 Publications
    Mutagenesisi121 – 1211C → A: Decreased localization to the plasma membrane. Abolishes localization to the plasma membrane; when associated with A-119 and A-121. 3 Publications
    Mutagenesisi269 – 2691L → R or H: No effect in the coupling between calcium and channel opening. 2 Publications
    Mutagenesisi272 – 2721R → E: Induces reduction in the coupling between calcium and channel opening. 2 Publications
    Mutagenesisi275 – 2751R → N: Induces reduction in the coupling between calcium and channel opening. 2 Publications
    Mutagenesisi278 – 2781R → Q: Induces reduction in the coupling between calcium and channel opening. 2 Publications
    Mutagenesisi281 – 2811Q → R: No effect in the coupling between calcium and channel opening. 2 Publications
    Mutagenesisi284 – 2841E → K: No effect in the coupling between calcium and channel opening. 2 Publications
    Mutagenesisi352 – 3521T → S: Activated at more negative voltages. Slower rate of inactivation. Impaired inhibition by HMIMP. No effect on channel inhibition by Iberiotoxin. 2 Publications
    Mutagenesisi354 – 3563GYG → AAA: Loss of function. 1 Publication
    Mutagenesisi380 – 3801F → A: Loss of function. 2 Publications
    Mutagenesisi381 – 3811A → S: Activated at more negative voltages. No effect on inhibition by HMIMP. 2 Publications
    Mutagenesisi384 – 3841V → I: No effect on activation voltage. No effect on inhibition by HMIMP. 2 Publications
    Mutagenesisi680 – 6801C → S: Loss of heme-induced channel inhibition. 2 Publications
    Mutagenesisi681 – 6811H → R: Loss of heme-induced channel inhibition. 2 Publications

    Keywords - Diseasei

    Disease mutation, Epilepsy

    Organism-specific databases

    MIMi609446. phenotype.
    Orphaneti79137. Generalized epilepsy - paroxysmal dyskinesia.
    PharmGKBiPA220.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 12361236Calcium-activated potassium channel subunit alpha-1PRO_0000054132Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Lipidationi118 – 1181S-palmitoyl cysteine2 Publications
    Lipidationi119 – 1191S-palmitoyl cysteine2 Publications
    Lipidationi121 – 1211S-palmitoyl cysteine2 Publications

    Post-translational modificationi

    Phosphorylated Probable. Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity.Curated
    Palmitoylation by ZDHHC22 and ZDHHC23 within the intracellular linker between the S0 and S1 transmembrane domains regulates localization to the plasma membrane. Depalmitoylated by LYPLA1 and LYPLAL1, leading to retard exit from the trans-Golgi network.2 Publications

    Keywords - PTMi

    Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiQ12791.
    PaxDbiQ12791.
    PRIDEiQ12791.

    PTM databases

    PhosphoSiteiQ12791.

    Expressioni

    Tissue specificityi

    Widely expressed. Except in myocytes, it is almost ubiquitously expressed.1 Publication

    Gene expression databases

    ArrayExpressiQ12791.
    BgeeiQ12791.
    GenevestigatoriQ12791.

    Organism-specific databases

    HPAiHPA054648.

    Interactioni

    Subunit structurei

    Homotetramer; which constitutes the calcium-activated potassium channel. Interacts with RAB11B By similarity. Interacts with beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4. Interacts with gamma subunits LRRC26, LRRC38, LRRC52 and LRRC55. Beta and gamma subunits are accessory, and modulate its activity.By similarity6 Publications

    Protein-protein interaction databases

    BioGridi109979. 10 interactions.
    DIPiDIP-29729N.
    IntActiQ12791. 2 interactions.
    MINTiMINT-4825316.

    Structurei

    Secondary structure

    1
    1236
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi261 – 27010
    Helixi277 – 2804
    Beta strandi409 – 4157
    Helixi418 – 43114
    Turni433 – 4375
    Beta strandi439 – 4435
    Helixi450 – 4534
    Helixi456 – 4594
    Beta strandi461 – 4666
    Beta strandi470 – 4723
    Helixi473 – 4786
    Helixi481 – 4833
    Beta strandi485 – 4906
    Helixi498 – 51518
    Beta strandi521 – 5266
    Helixi528 – 5314
    Helixi532 – 5365
    Turni542 – 5454
    Beta strandi547 – 5504
    Helixi551 – 56414
    Helixi568 – 5736
    Turni574 – 5763
    Beta strandi586 – 5883
    Helixi589 – 5979
    Beta strandi600 – 6056
    Helixi608 – 6103
    Helixi615 – 62410
    Beta strandi629 – 6346
    Beta strandi638 – 6403
    Beta strandi645 – 6473
    Beta strandi659 – 6657
    Helixi667 – 6715
    Turni672 – 6743
    Helixi803 – 8053
    Helixi823 – 8253
    Helixi830 – 8356
    Beta strandi842 – 8476
    Beta strandi850 – 8523
    Helixi858 – 8614
    Helixi863 – 8653
    Beta strandi867 – 8693
    Helixi871 – 8733
    Beta strandi877 – 8815
    Helixi883 – 89311
    Beta strandi896 – 9049
    Helixi909 – 9146
    Helixi917 – 9193
    Beta strandi921 – 9277
    Beta strandi936 – 9383
    Helixi941 – 95111
    Helixi996 – 9983
    Beta strandi1001 – 10066
    Helixi1008 – 10114
    Beta strandi1016 – 10183
    Helixi1026 – 10283
    Helixi1030 – 10334
    Beta strandi1037 – 10393
    Helixi1040 – 10445
    Helixi1046 – 10527
    Helixi1054 – 106411
    Helixi1073 – 10797
    Helixi1089 – 10935
    Beta strandi1099 – 11046
    Turni1105 – 11073
    Turni1109 – 11113
    Helixi1112 – 11143
    Helixi1119 – 112911
    Beta strandi1133 – 11419
    Beta strandi1144 – 11463
    Beta strandi1154 – 11596
    Beta strandi1171 – 11766

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2K44NMR-A257-284[»]
    3MT5X-ray3.00A406-1179[»]
    3NAFX-ray3.10A395-681[»]
    A782-1182[»]
    ProteinModelPortaliQ12791.
    SMRiQ12791. Positions 160-681, 800-1179.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12791.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 8686ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini108 – 17871CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini200 – 21415ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini236 – 2394CytoplasmicSequence Analysis
    Topological domaini261 – 2644ExtracellularSequence Analysis
    Topological domaini286 – 30015CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini322 – 33514ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini359 – 3679ExtracellularSequence Analysis
    Topological domaini389 – 1236848CytoplasmicSequence AnalysisAdd
    BLAST

    Intramembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Intramembranei336 – 35823Pore-forming; Name=P regionSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei87 – 10721Helical; Name=Segment S0Sequence AnalysisAdd
    BLAST
    Transmembranei179 – 19921Helical; Name=Segment S1Sequence AnalysisAdd
    BLAST
    Transmembranei215 – 23521Helical; Name=Segment S2Sequence AnalysisAdd
    BLAST
    Transmembranei240 – 26021Helical; Name=Segment S3Sequence AnalysisAdd
    BLAST
    Transmembranei265 – 28521Helical; Name=Segment S4Sequence AnalysisAdd
    BLAST
    Transmembranei301 – 32121Helical; Name=Segment S5Sequence AnalysisAdd
    BLAST
    Transmembranei368 – 38821Helical; Name=Segment S6Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini415 – 558144RCK N-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni556 – 57621Segment S7Add
    BLAST
    Regioni613 – 63321Segment S8Add
    BLAST
    Regioni677 – 6815Heme-binding motif
    Regioni837 – 85721Segment S9Add
    BLAST
    Regioni1032 – 105221Segment S10Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi352 – 3554Selectivity for potassium
    Motifi1003 – 102523Calcium bowlAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi4 – 107Poly-Gly
    Compositional biasi13 – 208Poly-Gly
    Compositional biasi39 – 6022Poly-SerAdd
    BLAST

    Domaini

    The S0 segment is essential for the modulation by the accessory beta subunits KCNMB1, KCNMB2, KCNMB3 and KCNMB4.
    The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.
    The pore-forming domain (also referred as P region) is imbedded into the membrane, and forms the selectivity filter of the pore. It contains the signature sequence of potassium channels that displays selectivity to potassium.
    The RCK N-terminal domain mediates the homotetramerization, thereby promoting the assembly of monomers into functional potassium channel. It includes binding sites for Ca2+ and Mg2+ By similarity.By similarity
    The calcium bowl constitutes one of the Ca2+ sensors and probably acts as a Ca2+-binding site. There are however other Ca2+ sensors regions required for activation of the channel.
    The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation.

    Sequence similaritiesi

    Contains 1 RCK N-terminal domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiCOG1226.
    HOVERGENiHBG052222.
    InParanoidiQ12791.
    KOiK04936.
    PhylomeDBiQ12791.
    TreeFamiTF314283.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    InterProiIPR005821. Ion_trans_dom.
    IPR003091. K_chnl.
    IPR003929. K_chnl_Ca-activ_BK_asu.
    IPR016040. NAD(P)-bd_dom.
    IPR003148. RCK_N.
    [Graphical view]
    PfamiPF03493. BK_channel_a. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02254. TrkA_N. 1 hit.
    [Graphical view]
    PRINTSiPR01449. BKCHANNELA.
    PR00169. KCHANNEL.

    Sequences (7)i

    Sequence statusi: Complete.

    This entry describes 7 isoformsi produced by alternative splicing. Align

    Note: May be partially controlled by hormonal stress. Additional isoforms seem to exist.

    Isoform 1 (identifier: Q12791-1) [UniParc]FASTAAdd to Basket

    Also known as: SAKCA

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MANGGGGGGG SSGGGGGGGG SSLRMSSNIH ANHLSLDASS SSSSSSSSSS     50
    SSSSSSSSSS VHEPKMDALI IPVTMEVPCD SRGQRMWWAF LASSMVTFFG 100
    GLFIILLWRT LKYLWTVCCH CGGKTKEAQK INNGSSQADG TLKPVDEKEE 150
    AVAAEVGWMT SVKDWAGVMI SAQTLTGRVL VVLVFALSIG ALVIYFIDSS 200
    NPIESCQNFY KDFTLQIDMA FNVFFLLYFG LRFIAANDKL WFWLEVNSVV 250
    DFFTVPPVFV SVYLNRSWLG LRFLRALRLI QFSEILQFLN ILKTSNSIKL 300
    VNLLSIFIST WLTAAGFIHL VENSGDPWEN FQNNQALTYW ECVYLLMVTM 350
    STVGYGDVYA KTTLGRLFMV FFILGGLAMF ASYVPEIIEL IGNRKKYGGS 400
    YSAVSGRKHI VVCGHITLES VSNFLKDFLH KDRDDVNVEI VFLHNISPNL 450
    ELEALFKRHF TQVEFYQGSV LNPHDLARVK IESADACLIL ANKYCADPDA 500
    EDASNIMRVI SIKNYHPKIR IITQMLQYHN KAHLLNIPSW NWKEGDDAIC 550
    LAELKLGFIA QSCLAQGLST MLANLFSMRS FIKIEEDTWQ KYYLEGVSNE 600
    MYTEYLSSAF VGLSFPTVCE LCFVKLKLLM IAIEYKSANR ESRILINPGN 650
    HLKIQEGTLG FFIASDAKEV KRAFFYCKAC HDDITDPKRI KKCGCKRPKM 700
    SIYKRMRRAC CFDCGRSERD CSCMSGRVRG NVDTLERAFP LSSVSVNDCS 750
    TSFRAFEDEQ PSTLSPKKKQ RNGGMRNSPN TSPKLMRHDP LLIPGNDQID 800
    NMDSNVKKYD STGMFHWCAP KEIEKVILTR SEAAMTVLSG HVVVCIFGDV 850
    SSALIGLRNL VMPLRASNFH YHELKHIVFV GSIEYLKREW ETLHNFPKVS 900
    ILPGTPLSRA DLRAVNINLC DMCVILSANQ NNIDDTSLQD KECILASLNI 950
    KSMQFDDSIG VLQANSQGFT PPGMDRSSPD NSPVHGMLRQ PSITTGVNIP 1000
    IITELVNDTN VQFLDQDDDD DPDTELYLTQ PFACGTAFAV SVLDSLMSAT 1050
    YFNDNILTLI RTLVTGGATP ELEALIAEEN ALRGGYSTPQ TLANRDRCRV 1100
    AQLALLDGPF ADLGDGGCYG DLFCKALKTY NMLCFGIYRL RDAHLSTPSQ 1150
    CTKRYVITNP PYEFELVPTD LIFCLMQFDH NAGQSRASLS HSSHSSQSSS 1200
    KKSSSVHSIP STANRQNRPK SRESRDKQKY VQEERL 1236
    Length:1,236
    Mass (Da):137,560
    Last modified:April 13, 2004 - v2
    Checksum:iDF9BFEAF374BE553
    GO
    Isoform 2 (identifier: Q12791-2) [UniParc]FASTAAdd to Basket

    Also known as: BKTM

    The sequence of this isoform differs from the canonical sequence as follows:
         698-756: PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAF → L
         828-828: L → LVTGWMPYLGPRVLMTCLDIGVVCMPTDIQSTSPASIKKFKE

    Show »
    Length:1,219
    Mass (Da):135,495
    Checksum:i932986BE30E0D409
    GO
    Isoform 3 (identifier: Q12791-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         643-643: R → RSRKR

    Show »
    Length:1,240
    Mass (Da):138,087
    Checksum:i83DA8EC8C379A3D9
    GO
    Isoform 4 (identifier: Q12791-4) [UniParc]FASTAAdd to Basket

    Also known as: hbr5

    The sequence of this isoform differs from the canonical sequence as follows:
         698-756: PKMSIYKRMR...NDCSTSFRAF → LKVAARSRYSKDPFEFKKETPNSRLVTEPV

    Show »
    Length:1,207
    Mass (Da):134,362
    Checksum:i7B9C03A8BFA5055B
    GO
    Isoform 5 (identifier: Q12791-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         698-756: PKMSIYKRMRRACCFDCGRSERDCSCMSGRVRGNVDTLERAFPLSSVSVNDCSTSFRAF → L

    Show »
    Length:1,178
    Mass (Da):130,999
    Checksum:iAD3C9634F8A21EEC
    GO
    Isoform 6 (identifier: Q12791-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         127-168: EAQKINNGSS...MTSVKDWAGV → ATHFGSPEMP...ALEVARCRRL
         169-1236: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:168
    Mass (Da):17,191
    Checksum:i101980B6E7017A03
    GO
    Isoform 7 (identifier: Q12791-7) [UniParc]FASTAAdd to Basket

    Also known as: gBK

    The sequence of this isoform differs from the canonical sequence as follows:
         698-756: PKMSIYKRMR...NDCSTSFRAF → RWEEHCSLWR...PNSRLVTEPV

    Show »
    Length:1,239
    Mass (Da):138,297
    Checksum:iCE8B6449D8C7B9CC
    GO

    Sequence cautioni

    The sequence AAA50216.1 differs from that shown. Reason: Contaminating sequence. Sequence of unknown origin in the N-terminal part.
    The sequence AAB65837.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAC50353.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAK91504.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence BAD06365.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti25 – 251M → N in AAA50216. (PubMed:7987297)Curated
    Sequence conflicti35 – 351S → G in AAA50216. (PubMed:7987297)Curated
    Sequence conflicti38 – 381A → V in AAA85104. (PubMed:7877450)Curated
    Sequence conflicti449 – 4491N → D in AAD31173. 1 PublicationCurated
    Sequence conflicti805 – 8051N → H in AAC50353. (PubMed:7993625)Curated
    Sequence conflicti1152 – 11521T → A in AAD31173. 1 PublicationCurated
    Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI39730. (PubMed:15164054)Curated
    Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI40870. (PubMed:15164054)Curated
    Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI14074. (PubMed:15164054)Curated
    Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI16162. (PubMed:15164054)Curated
    Isoform 7 (identifier: Q12791-7)
    Sequence conflicti726 – 7272FS → SF no nucleotide entry (PubMed:11880513)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti434 – 4341D → G in GEPD; may have a synergistic effect with ethanol in the triggering of symptoms. 1 Publication
    VAR_023821

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei127 – 16842EAQKI…DWAGV → ATHFGSPEMPPAARSWSGSP PEAAVLRGASSLALEVARCR RL in isoform 6. 1 PublicationVSP_009952Add
    BLAST
    Alternative sequencei169 – 12361068Missing in isoform 6. 1 PublicationVSP_009953Add
    BLAST
    Alternative sequencei643 – 6431R → RSRKR in isoform 3. 1 PublicationVSP_009954
    Alternative sequencei698 – 75659PKMSI…SFRAF → L in isoform 2 and isoform 5. 9 PublicationsVSP_009955Add
    BLAST
    Alternative sequencei698 – 75659PKMSI…SFRAF → LKVAARSRYSKDPFEFKKET PNSRLVTEPV in isoform 4. 2 PublicationsVSP_009956Add
    BLAST
    Alternative sequencei698 – 75659PKMSI…SFRAF → RWEEHCSLWRLESKGNVRRL NYCRGQQTFSVKVKVAARSR YSKDPFEFKKETPNSRLVTE PV in isoform 7. CuratedVSP_009957Add
    BLAST
    Alternative sequencei828 – 8281L → LVTGWMPYLGPRVLMTCLDI GVVCMPTDIQSTSPASIKKF KE in isoform 2. 1 PublicationVSP_009958

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13913 mRNA. Translation: AAA85104.1.
    U23767 mRNA. Translation: AAA92290.1.
    AL157833
    , AL731560, AL731556, AL627447, AC021032, AC011439 Genomic DNA. Translation: CAI39730.1.
    AL157833
    , AC011439, AC021032, AL627447, AL731556, AL731560 Genomic DNA. Translation: CAI39736.1.
    AL627447
    , AL731560, AL731556, AC021032, AC011439, AL157833 Genomic DNA. Translation: CAI16162.1.
    AL627447
    , AC011439, AC021032, AL157833, AL731556, AL731560 Genomic DNA. Translation: CAI16171.1.
    AL731556
    , AC011439, AL157833, AC021032, AL731560, AL627447 Genomic DNA. Translation: CAI14074.1.
    AL731556
    , AC011439, AC021032, AL157833, AL627447, AL731560 Genomic DNA. Translation: CAI14082.1.
    AL731560
    , AL157833, AL731556, AC021032, AC011439, AL627447 Genomic DNA. Translation: CAI40870.1.
    AL731560
    , AC011439, AC021032, AL157833, AL627447, AL731556 Genomic DNA. Translation: CAI40877.1.
    AC067745 Genomic DNA. No translation available.
    AL607069 Genomic DNA. No translation available.
    AL731575 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54599.1.
    BC062659 mRNA. Translation: AAH62659.1.
    BC137115 mRNA. Translation: AAI37116.1.
    BC137137 mRNA. Translation: AAI37138.1.
    U11717 mRNA. Translation: AAC50353.1. Different initiation.
    AY040849 mRNA. Translation: AAK91504.1. Different initiation.
    AB113575 mRNA. Translation: BAD06397.1.
    AB113382 mRNA. Translation: BAD06365.1. Different initiation.
    U02632 mRNA. Translation: AAA50173.1.
    U09384 mRNA. Translation: AAA50216.1. Sequence problems.
    AF025999 mRNA. Translation: AAB88802.1.
    U11058 mRNA. Translation: AAB65837.1. Different initiation.
    AF118141 mRNA. Translation: AAD31173.1.
    CCDSiCCDS53545.1. [Q12791-2]
    CCDS60569.1. [Q12791-1]
    CCDS60571.1. [Q12791-6]
    CCDS7352.1. [Q12791-5]
    PIRiI38596.
    S62904.
    RefSeqiNP_001014797.1. NM_001014797.2.
    NP_001154824.1. NM_001161352.1. [Q12791-1]
    NP_001154825.1. NM_001161353.1. [Q12791-2]
    NP_001258447.1. NM_001271518.1.
    NP_001258451.1. NM_001271522.1. [Q12791-6]
    NP_002238.2. NM_002247.3. [Q12791-5]
    UniGeneiHs.144795.

    Genome annotation databases

    EnsembliENST00000286627; ENSP00000286627; ENSG00000156113. [Q12791-5]
    ENST00000286628; ENSP00000286628; ENSG00000156113. [Q12791-1]
    ENST00000354353; ENSP00000346321; ENSG00000156113. [Q12791-7]
    ENST00000404857; ENSP00000385806; ENSG00000156113. [Q12791-2]
    ENST00000480683; ENSP00000474686; ENSG00000156113. [Q12791-6]
    GeneIDi3778.
    KEGGihsa:3778.
    UCSCiuc001jxj.2. human. [Q12791-5]
    uc001jxn.3. human. [Q12791-1]
    uc001jxo.3. human. [Q12791-2]
    uc001jxs.4. human. [Q12791-6]
    uc009xrt.1. human. [Q12791-4]

    Polymorphism databases

    DMDMi46396283.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13913 mRNA. Translation: AAA85104.1 .
    U23767 mRNA. Translation: AAA92290.1 .
    AL157833
    , AL731560 , AL731556 , AL627447 , AC021032 , AC011439 Genomic DNA. Translation: CAI39730.1 .
    AL157833
    , AC011439 , AC021032 , AL627447 , AL731556 , AL731560 Genomic DNA. Translation: CAI39736.1 .
    AL627447
    , AL731560 , AL731556 , AC021032 , AC011439 , AL157833 Genomic DNA. Translation: CAI16162.1 .
    AL627447
    , AC011439 , AC021032 , AL157833 , AL731556 , AL731560 Genomic DNA. Translation: CAI16171.1 .
    AL731556
    , AC011439 , AL157833 , AC021032 , AL731560 , AL627447 Genomic DNA. Translation: CAI14074.1 .
    AL731556
    , AC011439 , AC021032 , AL157833 , AL627447 , AL731560 Genomic DNA. Translation: CAI14082.1 .
    AL731560
    , AL157833 , AL731556 , AC021032 , AC011439 , AL627447 Genomic DNA. Translation: CAI40870.1 .
    AL731560
    , AC011439 , AC021032 , AL157833 , AL627447 , AL731556 Genomic DNA. Translation: CAI40877.1 .
    AC067745 Genomic DNA. No translation available.
    AL607069 Genomic DNA. No translation available.
    AL731575 Genomic DNA. No translation available.
    CH471083 Genomic DNA. Translation: EAW54599.1 .
    BC062659 mRNA. Translation: AAH62659.1 .
    BC137115 mRNA. Translation: AAI37116.1 .
    BC137137 mRNA. Translation: AAI37138.1 .
    U11717 mRNA. Translation: AAC50353.1 . Different initiation.
    AY040849 mRNA. Translation: AAK91504.1 . Different initiation.
    AB113575 mRNA. Translation: BAD06397.1 .
    AB113382 mRNA. Translation: BAD06365.1 . Different initiation.
    U02632 mRNA. Translation: AAA50173.1 .
    U09384 mRNA. Translation: AAA50216.1 . Sequence problems.
    AF025999 mRNA. Translation: AAB88802.1 .
    U11058 mRNA. Translation: AAB65837.1 . Different initiation.
    AF118141 mRNA. Translation: AAD31173.1 .
    CCDSi CCDS53545.1. [Q12791-2 ]
    CCDS60569.1. [Q12791-1 ]
    CCDS60571.1. [Q12791-6 ]
    CCDS7352.1. [Q12791-5 ]
    PIRi I38596.
    S62904.
    RefSeqi NP_001014797.1. NM_001014797.2.
    NP_001154824.1. NM_001161352.1. [Q12791-1 ]
    NP_001154825.1. NM_001161353.1. [Q12791-2 ]
    NP_001258447.1. NM_001271518.1.
    NP_001258451.1. NM_001271522.1. [Q12791-6 ]
    NP_002238.2. NM_002247.3. [Q12791-5 ]
    UniGenei Hs.144795.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2K44 NMR - A 257-284 [» ]
    3MT5 X-ray 3.00 A 406-1179 [» ]
    3NAF X-ray 3.10 A 395-681 [» ]
    A 782-1182 [» ]
    ProteinModelPortali Q12791.
    SMRi Q12791. Positions 160-681, 800-1179.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109979. 10 interactions.
    DIPi DIP-29729N.
    IntActi Q12791. 2 interactions.
    MINTi MINT-4825316.

    Chemistry

    BindingDBi Q12791.
    ChEMBLi CHEMBL3038495.
    DrugBanki DB00436. Bendroflumethiazide.
    DB00562. Benzthiazide.
    DB00880. Chlorothiazide.
    DB00356. Chlorzoxazone.
    DB01003. Cromoglicate.
    DB00606. Cyclothiazide.
    DB01119. Diazoxide.
    DB00228. Enflurane.
    DB00999. Hydrochlorothiazide.
    DB00774. Hydroflumethiazide.
    DB00232. Methyclothiazide.
    DB01325. Quinethazone.
    DB01021. Trichlormethiazide.
    GuidetoPHARMACOLOGYi 380.

    PTM databases

    PhosphoSitei Q12791.

    Polymorphism databases

    DMDMi 46396283.

    Proteomic databases

    MaxQBi Q12791.
    PaxDbi Q12791.
    PRIDEi Q12791.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000286627 ; ENSP00000286627 ; ENSG00000156113 . [Q12791-5 ]
    ENST00000286628 ; ENSP00000286628 ; ENSG00000156113 . [Q12791-1 ]
    ENST00000354353 ; ENSP00000346321 ; ENSG00000156113 . [Q12791-7 ]
    ENST00000404857 ; ENSP00000385806 ; ENSG00000156113 . [Q12791-2 ]
    ENST00000480683 ; ENSP00000474686 ; ENSG00000156113 . [Q12791-6 ]
    GeneIDi 3778.
    KEGGi hsa:3778.
    UCSCi uc001jxj.2. human. [Q12791-5 ]
    uc001jxn.3. human. [Q12791-1 ]
    uc001jxo.3. human. [Q12791-2 ]
    uc001jxs.4. human. [Q12791-6 ]
    uc009xrt.1. human. [Q12791-4 ]

    Organism-specific databases

    CTDi 3778.
    GeneCardsi GC10M078629.
    HGNCi HGNC:6284. KCNMA1.
    HPAi HPA054648.
    MIMi 600150. gene.
    609446. phenotype.
    neXtProti NX_Q12791.
    Orphaneti 79137. Generalized epilepsy - paroxysmal dyskinesia.
    PharmGKBi PA220.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG1226.
    HOVERGENi HBG052222.
    InParanoidi Q12791.
    KOi K04936.
    PhylomeDBi Q12791.
    TreeFami TF314283.

    Enzyme and pathway databases

    Reactomei REACT_23767. cGMP effects.
    REACT_75896. Ca2+ activated K+ channels.

    Miscellaneous databases

    ChiTaRSi KCNMA1. human.
    EvolutionaryTracei Q12791.
    GenomeRNAii 3778.
    NextBioi 14823.
    PROi Q12791.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12791.
    Bgeei Q12791.
    Genevestigatori Q12791.

    Family and domain databases

    Gene3Di 3.40.50.720. 1 hit.
    InterProi IPR005821. Ion_trans_dom.
    IPR003091. K_chnl.
    IPR003929. K_chnl_Ca-activ_BK_asu.
    IPR016040. NAD(P)-bd_dom.
    IPR003148. RCK_N.
    [Graphical view ]
    Pfami PF03493. BK_channel_a. 1 hit.
    PF00520. Ion_trans. 1 hit.
    PF02254. TrkA_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01449. BKCHANNELA.
    PR00169. KCHANNEL.
    ProtoNeti Search...

    Publicationsi

    1. "Cloning and expression of a human large-conductance calcium-activated potassium channel."
      Dworetzky S.I., Trojnacki J.T., Gribkoff V.K.
      Brain Res. Mol. Brain Res. 27:189-193(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Substantia nigra.
    2. "A human calcium-activated potassium channel gene expressed in vascular smooth muscle."
      McCobb D.P., Fowler N.L., Featherstone T., Lingle C.J., Saito M., Krause J.E., Salkoff L.
      Am. J. Physiol. 269:H767-H777(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5).
      Tissue: Aortic smooth muscle and Umbilical smooth muscle.
    3. "The DNA sequence and comparative analysis of human chromosome 10."
      Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
      , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
      Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORMS 5 AND 6).
      Tissue: Cerebellum, Neuroectoderm and Testis.
    6. "Cloning, expression, and distribution of functionally distinct Ca(2+)-activated K+ channel isoforms from human brain."
      Tseng-Crank J., Foster C.D., Krause J.D., Mertz R., Godinot N., DiChiara T.J., Reinhart P.H.
      Neuron 13:1315-1330(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 17-1236 (ISOFORM 5).
    7. "Calcium-activated potassium channel expression in human myometrium: effect of pregnancy."
      Mazzone J.N., Kaiser R.A., Buxton I.L.O.
      Proc. West. Pharmacol. Soc. 45:184-186(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 5).
      Tissue: Myometrium.
    8. "BK variant from human heart."
      Naruse K.
      Submitted (JUN-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-1236 (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 25-1236 (ISOFORM 2).
      Tissue: Heart.
    9. "Cloning and characterization of human and mouse homologs of the Drosophila calcium-activated potassium channel gene, slowpoke."
      Pallanck L., Ganetzky B.
      Hum. Mol. Genet. 3:1239-1243(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 24-670 (ISOFORM 3), NUCLEOTIDE SEQUENCE [MRNA] OF 323-1236 (ISOFORM 4).
      Tissue: Muscle.
    10. "Identification of potassium channels in human lens epithelium."
      Rae J.L., Shepard A.R.
      (In) Civan M.M. (eds.); Current topics in membranes. The eye's aqueous humor - from secretion to glaucoma, pp.45:69-104, Academic Press, San Diego (1998)
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 25-1236 (ISOFORM 5).
      Tissue: Lens epithelium.
    11. "Characterization of and modulation by a beta-subunit of a human maxi KCa channel cloned from myometrium."
      Wallner M., Meera P., Ottolia M., Kaczorowski G.J., Latorre R., Garcia M.L., Stefani E., Toro L.
      Recept. Channels 3:185-199(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 38-1236 (ISOFORM 5), NUCLEOTIDE SEQUENCE [MRNA] OF 693-764 (ISOFORM 4).
      Tissue: Myometrium.
    12. "Cloning and characterization of BKCA alpha subunit from human pulmonary artery."
      Cairns V.R., Aebly M.R., Rusch N.J.
      Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 66-1236 (ISOFORM 5).
      Tissue: Pulmonary artery.
    13. "Cloning and characterization of glioma BK, a novel BK channel isoform highly expressed in human glioma cells."
      Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y.
      J. Neurosci. 22:1840-1849(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: ALTERNATIVE SPLICING (ISOFORM 7), TISSUE SPECIFICITY.
      Tissue: Glioblastoma.
    14. Erratum
      Liu X., Chang Y., Reinhart P.H., Sontheimer H., Chang Y.
      J. Neurosci. 22:1B-1B(2002)
    15. "Determinant for beta-subunit regulation in high-conductance voltage-activated and Ca(2+)-sensitive K+ channels: an additional transmembrane region at the N-terminus."
      Wallner M., Meera P., Toro L.
      Proc. Natl. Acad. Sci. U.S.A. 93:14922-14927(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN S0.
    16. "Large conductance voltage- and calcium-dependent K+ channel, a distinct member of voltage-dependent ion channels with seven N-terminal transmembrane segments (S0-S6), an extracellular N-terminus, and an intracellular (S9-S10) C-terminus."
      Meera P., Wallner M., Song M., Toro L.
      Proc. Natl. Acad. Sci. U.S.A. 94:14066-14071(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: MEMBRANE TOPOLOGY.
    17. "Role of the S4 segment in a voltage-dependent calcium-sensitive potassium (hSlo) channel."
      Diaz L., Meera P., Amigo J., Stefani E., Alvarez O., Toro L., Latorre R.
      J. Biol. Chem. 273:32430-32436(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN S4, MUTAGENESIS OF LEU-269; ARG-272; ARG-275; ARG-278; GLN-281 AND GLU-284.
    18. "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: INTERACTION WITH KCNMB2.
    19. "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: INTERACTION WITH KCNMB3 AND KCNMB4.
    20. "Identification of a novel tetramerization domain in large conductance K(ca) channels."
      Quirk J.C., Reinhart P.H.
      Neuron 32:13-23(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: HOMOTETRAMERIZATION, MUTAGENESIS OF 354-GLY--GLY-356.
    21. "Consequences of the stoichiometry of Slo1 alpha and auxiliary beta subunits on functional properties of large-conductance Ca2+-activated K+ channels."
      Wang Y.-W., Ding J.-P., Xia X.-M., Lingle C.J.
      J. Neurosci. 22:1550-1561(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNMB1; KCNMB2; KCNMB3 AND KCNMB4.
    22. "Haem can bind to and inhibit mammalian calcium-dependent Slo1 BK channels."
      Tang X.D., Xu R., Reynolds M.F., Garcia M.L., Heinemann S.H., Hoshi T.
      Nature 425:531-535(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: ENZYME REGULATION, MUTAGENESIS OF CYS-680 AND HIS-681.
    23. "Gating mechanism of BK (Slo1) channels: so near, yet so far."
      Magleby K.L.
      J. Gen. Physiol. 121:81-96(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    24. "Palmitoylation of the S0-S1 linker regulates cell surface expression of voltage- and calcium-activated potassium (BK) channels."
      Jeffries O., Geiger N., Rowe I.C., Tian L., McClafferty H., Chen L., Bi D., Knaus H.G., Ruth P., Shipston M.J.
      J. Biol. Chem. 285:33307-33314(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-118; CYS-119 AND CYS-121, MUTAGENESIS OF CYS-118; CYS-119 AND CYS-121.
    25. "Distinct acyl protein transferases and thioesterases control surface expression of calcium-activated potassium channels."
      Tian L., McClafferty H., Knaus H.G., Ruth P., Shipston M.J.
      J. Biol. Chem. 287:14718-14725(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, PALMITOYLATION AT CYS-118; CYS-119 AND CYS-121, DEPALMITOYLATION, MUTAGENESIS OF CYS-118; CYS-119 AND CYS-121.
    26. "LRRC26 auxiliary protein allows BK channel activation at resting voltage without calcium."
      Yan J., Aldrich R.W.
      Nature 466:513-516(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRRC26.
    27. "Characterizing the role of Thr352 in the inhibition of the large conductance Ca2+-activated K+ channels by 1-[1-Hexyl-6-(methyloxy)-1H-indazol-3-yl]-2-methyl-1-propanone."
      Gordon E., Semus S.F., Lozinskaya I.M., Lin Z., Xu X.
      J. Pharmacol. Exp. Ther. 334:402-409(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF THR-352; PHE-380; ALA-381 AND VAL-384.
    28. "BK potassium channel modulation by leucine-rich repeat-containing proteins."
      Yan J., Aldrich R.W.
      Proc. Natl. Acad. Sci. U.S.A. 109:7917-7922(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH GAMMA SUBUNITS LRRC26; LRRC38; LRRC52 AND LRRC55.
    29. "Structure of the human BK channel Ca2+-activation apparatus at 3.0 A resolution."
      Yuan P., Leonetti M.D., Pico A.R., Hsiung Y., MacKinnon R.
      Science 329:182-186(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 406-1179, CALCIUM-BINDING SITES, SUBUNIT.
    30. "Calcium-sensitive potassium channelopathy in human epilepsy and paroxysmal movement disorder."
      Du W., Bautista J.F., Yang H., Diez-Sampedro A., You S.-A., Wang L., Kotagal P., Lueders H.O., Shi J., Cui J., Richerson G.B., Wang Q.K.
      Nat. Genet. 37:733-738(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT GEPD GLY-434.

    Entry informationi

    Entry nameiKCMA1_HUMAN
    AccessioniPrimary (citable) accession number: Q12791
    Secondary accession number(s): F8WA96
    , Q12886, Q12917, Q12921, Q12960, Q13150, Q5JQ23, Q5SQR9, Q96LG8, Q9UBB0, Q9UCX0, Q9UQK6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 13, 2004
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 147 of the entry and version 2 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

    Miscellaneous

    The protein was initially thought to contain two functionally distinct parts: The core channel (from the N-terminus to the S9 segment) that mediates the channel activity, and the cytoplasmic tail (from the S9 segment to the C-terminus) that mediates the calcium sensing. The situation is however more complex, since the core channel also contains binding sites for Ca2+ and Mg2+.

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 10
      Human chromosome 10: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3