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Q12791

- KCMA1_HUMAN

UniProt

Q12791 - KCMA1_HUMAN

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Protein

Calcium-activated potassium channel subunit alpha-1

Gene
KCNMA1, KCNMA, SLO
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 – 4391Magnesium By similarity
Metal bindingi462 – 4621Magnesium By similarity
Metal bindingi464 – 4641Magnesium By 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
Complete GO annotation...

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; Multi-pass membrane protein 2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 8686Extracellular Reviewed predictionAdd
BLAST
Transmembranei87 – 10721Helical; Name=Segment S0; Reviewed predictionAdd
BLAST
Topological domaini108 – 17871Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei179 – 19921Helical; Name=Segment S1; Reviewed predictionAdd
BLAST
Topological domaini200 – 21415Extracellular Reviewed predictionAdd
BLAST
Transmembranei215 – 23521Helical; Name=Segment S2; Reviewed predictionAdd
BLAST
Topological domaini236 – 2394Cytoplasmic Reviewed prediction
Transmembranei240 – 26021Helical; Name=Segment S3; Reviewed predictionAdd
BLAST
Topological domaini261 – 2644Extracellular Reviewed prediction
Transmembranei265 – 28521Helical; Name=Segment S4; Reviewed predictionAdd
BLAST
Topological domaini286 – 30015Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei301 – 32121Helical; Name=Segment S5; Reviewed predictionAdd
BLAST
Topological domaini322 – 33514Extracellular Reviewed predictionAdd
BLAST
Intramembranei336 – 35823Pore-forming; Name=P region; Reviewed predictionAdd
BLAST
Topological domaini359 – 3679Extracellular Reviewed prediction
Transmembranei368 – 38821Helical; Name=Segment S6; Reviewed predictionAdd
BLAST
Topological domaini389 – 1236848Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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

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 Inferred. Phosphorylation by kinases such as PKA and/or PKG. In smooth muscles, phosphorylation affects its activity.
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.7 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.

Miscellaneous databases

EvolutionaryTraceiQ12791.

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 KCNMB4.2 Publications
The S4 segment, which is characterized by a series of positively charged amino acids at every third position, is part of the voltage-sensor.2 Publications
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.2 Publications
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.2 Publications
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.2 Publications
The heme-binding motif mediates inhibition of channel activation by heme. Carbon monoxide-bound heme leads to increased channel activation.2 Publications

Sequence similaritiesi

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

Note: Ref.13 (no nucleotide entry) sequence is in conflict in positions: 726-727:SF->FS.

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.

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. VSP_009952Add
BLAST
Alternative sequencei169 – 12361068Missing in isoform 6. VSP_009953Add
BLAST
Alternative sequencei643 – 6431R → RSRKR in isoform 3. VSP_009954
Alternative sequencei698 – 75659PKMSI…SFRAF → L in isoform 2 and isoform 5. VSP_009955Add
BLAST
Alternative sequencei698 – 75659PKMSI…SFRAF → LKVAARSRYSKDPFEFKKET PNSRLVTEPV in isoform 4. VSP_009956Add
BLAST
Alternative sequencei698 – 75659PKMSI…SFRAF → RWEEHCSLWRLESKGNVRRL NYCRGQQTFSVKVKVAARSR YSKDPFEFKKETPNSRLVTE PV in isoform 7. VSP_009957Add
BLAST
Alternative sequencei828 – 8281L → LVTGWMPYLGPRVLMTCLDI GVVCMPTDIQSTSPASIKKF KE in isoform 2. VSP_009958

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti25 – 251M → N in AAA50216. 1 Publication
Sequence conflicti35 – 351S → G in AAA50216. 1 Publication
Sequence conflicti38 – 381A → V in AAA85104. 1 Publication
Sequence conflicti449 – 4491N → D in AAD31173. 1 Publication
Sequence conflicti805 – 8051N → H in AAC50353. 1 Publication
Sequence conflicti1152 – 11521T → A in AAD31173. 1 Publication
Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI39730. 1 Publication
Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI40870. 1 Publication
Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI14074. 1 Publication
Sequence conflicti1230 – 12367YVQEERL → KEMVYR in CAI16162. 1 Publication

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.
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 .
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 146 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

Similar proteinsi