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Protein

Voltage-gated potassium channel subunit beta-1

Gene

KCNAB1

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

Functioni

Cytoplasmic potassium channel subunit that modulates the characteristics of the channel-forming alpha-subunits (PubMed:7499366, PubMed:7603988, PubMed:17156368,PubMed:17540341, PubMed:19713757). Modulates action potentials via its effect on the pore-forming alpha subunits (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (By similarity). Mediates closure of delayed rectifier potassium channels by physically obstructing the pore via its N-terminal domain and increases the speed of channel closure for other family members (PubMed:9763623). Promotes the closure of KCNA1, KCNA2 and KCNA5 channels (PubMed:7499366, PubMed:7890032, PubMed:7603988, PubMed:7649300, PubMed:8938711, PubMed:12077175, PubMed:12130714, PubMed:15361858, PubMed:17540341, PubMed:19713757). Accelerates KCNA4 channel closure (PubMed:7890032, PubMed:7649300, PubMed:7890764, PubMed:9763623). Accelerates the closure of heteromeric channels formed by KCNA1 and KCNA4 (PubMed:17156368). Accelerates the closure of heteromeric channels formed by KCNA2, KCNA5 and KCNA6 (By similarity). Isoform KvB1.2 has no effect on KCNA1, KCNA2 or KCNB1 (PubMed:7890032, PubMed:7890764). Enhances KCNB1 and KCNB2 channel activity (By similarity). Binds NADPH; this is required for efficient down-regulation of potassium channel activity (PubMed:17540341). Has NADPH-dependent aldoketoreductase activity (By similarity). Oxidation of the bound NADPH strongly decreases N-type inactivation of potassium channel activity (By similarity).By similarityCurated13 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei115 – 1151NADPBy similarity
Binding sitei137 – 1371NADPBy similarity
Active sitei142 – 1421Proton donor/acceptorBy similarity
Binding sitei142 – 1421NADPBy similarity
Binding sitei266 – 2661NADPBy similarity
Binding sitei306 – 3061NADPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi108 – 1092NADPBy similarity
Nucleotide bindingi240 – 2412NADPBy similarity
Nucleotide bindingi295 – 3006NADPBy similarity
Nucleotide bindingi375 – 3817NADPBy similarity

GO - Molecular functioni

  • aldo-keto reductase (NADP) activity Source: UniProtKB
  • NADPH binding Source: UniProtKB
  • potassium channel regulator activity Source: UniProtKB
  • voltage-gated potassium channel activity Source: InterPro

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Oxidoreductase, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

NADP, Potassium

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Protein family/group databases

TCDBi8.A.5.1.1. the voltage-gated k(+) channel -subunit (kv) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-1 (EC:1.1.1.-By similarity)
Alternative name(s):
K(+) channel subunit beta-1
Kv-beta-1
Gene namesi
Name:KCNAB1
Synonyms:KCNA1B
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:6228. KCNAB1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • plasma membrane Source: Reactome
  • potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cytoplasm, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi307 – 3071Y → F: Reduces affinity for NADPH. 1 Publication
Mutagenesisi316 – 3161R → E: Nearly abolishes NADPH binding. 1 Publication

Organism-specific databases

PharmGKBiPA370.

Polymorphism and mutation databases

BioMutaiKCNAB1.
DMDMi18202500.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 419419Voltage-gated potassium channel subunit beta-1PRO_0000148739Add
BLAST

Proteomic databases

MaxQBiQ14722.
PaxDbiQ14722.
PRIDEiQ14722.

PTM databases

PhosphoSiteiQ14722.

Expressioni

Tissue specificityi

In brain, expression is most prominent in caudate nucleus, hippocampus and thalamus. Significant expression also detected in amygdala and subthalamic nucleus. Also expressed in both healthy and cardiomyopathic heart. Up to four times more abundant in left ventricle than left atrium.2 Publications

Gene expression databases

BgeeiQ14722.
CleanExiHS_KCNAB1.
ExpressionAtlasiQ14722. baseline and differential.
GenevisibleiQ14722. HS.

Organism-specific databases

HPAiHPA044550.

Interactioni

Subunit structurei

Homotetramer (By similarity). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (Probable). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Interacts with KCNA1 (By similarity). Interacts with the dimer formed by GNB1 and GNG2; this enhances KCNA1 binding (By similarity). Interacts with KCNA4 (PubMed:9763623). Interacts with KCNA5 (PubMed:12130714). Interacts with KCNB2 (By similarity). Interacts with SQSTM1 (By similarity). Part of a complex containing KCNA1, KCNA4 and LGI1; interaction with LGI1 inhibits down-regulation of KCNA1 channel activity (By similarity).By similarityCurated2 Publications

Protein-protein interaction databases

BioGridi113626. 12 interactions.
IntActiQ14722. 2 interactions.

Structurei

3D structure databases

DisProtiDP00090.
ProteinModelPortaliQ14722.
SMRiQ14722. Positions 91-413.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domaini

The N-terminal domain of the beta subunit mediates closure of delayed rectifier potassium channels by physically obstructing the pore.2 Publications

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOVERGENiHBG052216.
InParanoidiQ14722.
KOiK04882.
OMAiAYGNWIT.
PhylomeDBiQ14722.
TreeFamiTF324563.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005400. K_chnl_volt-dep_bsu_KCNAB1.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01578. KCNAB1CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform KvB1.3 (identifier: Q14722-1) [UniParc]FASTAAdd to basket

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

        10         20         30         40         50
MLAARTGAAG SQISEENTKL RRQSGFSVAG KDKSPKKASE NAKDSSLSPS
60 70 80 90 100
GESQLRARQL ALLREVEMNW YLKLCDLSSE HTTVCTTGMP HRNLGKSGLR
110 120 130 140 150
VSCLGLGTWV TFGGQISDEV AERLMTIAYE SGVNLFDTAE VYAAGKAEVI
160 170 180 190 200
LGSIIKKKGW RRSSLVITTK LYWGGKAETE RGLSRKHIIE GLKGSLQRLQ
210 220 230 240 250
LEYVDVVFAN RPDSNTPMEE IVRAMTHVIN QGMAMYWGTS RWSAMEIMEA
260 270 280 290 300
YSVARQFNMI PPVCEQAEYH LFQREKVEVQ LPELYHKIGV GAMTWSPLAC
310 320 330 340 350
GIISGKYGNG VPESSRASLK CYQWLKERIV SEEGRKQQNK LKDLSPIAER
360 370 380 390 400
LGCTLPQLAV AWCLRNEGVS SVLLGSSTPE QLIENLGAIQ VLPKMTSHVV
410
NEIDNILRNK PYSKKDYRS
Length:419
Mass (Da):46,563
Last modified:November 1, 1996 - v1
Checksum:iEFFDA78568007A7A
GO
Isoform KvB1.1 (identifier: Q14722-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: MLAARTGAAG...TTVCTTGMPH → MQVSIACTEH...STAKQTGMKY

Show »
Length:401
Mass (Da):44,710
Checksum:iF9F17404DF35FDA1
GO
Isoform KvB1.2 (identifier: Q14722-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-91: MLAARTGAAG...TTVCTTGMPH → MHLYKPACAD...TTRAETGMAY

Show »
Length:408
Mass (Da):45,492
Checksum:i0C7CD8C23411F8E0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti290 – 2901V → L in CAA58208 (PubMed:8938711).Curated
Isoform KvB1.2 (identifier: Q14722-3)
Sequence conflicti16 – 161L → S in AAC50113 (PubMed:7890764).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 9191MLAAR…TGMPH → MQVSIACTEHNLKSRNGEDR LLSKQSSTAPNVVNAARAKF RTVAIIARSLGTFTPQHHIS LKESTAKQTGMKY in isoform KvB1.1. 4 PublicationsVSP_001051Add
BLAST
Alternative sequencei1 – 9191MLAAR…TGMPH → MHLYKPACADIPSPKLGLPK SSESALKCRWHLAVTKTQPQ AACKPVRPSGAAEQKYVEKF LRVHGISLQETTRAETGMAY in isoform KvB1.2. 4 PublicationsVSP_001050Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47665 mRNA. Translation: AAC41926.1.
U16953 mRNA. Translation: AAC50122.1.
L39833 mRNA. Translation: AAC37573.1.
U33428 mRNA. Translation: AAC50953.1.
X83127 mRNA. Translation: CAA58208.1.
AK057059 mRNA. Translation: BAG51856.1.
AK127240 mRNA. Translation: BAG54461.1.
AK292693 mRNA. Translation: BAF85382.1.
AK292999 mRNA. Translation: BAF85688.1.
CH471052 Genomic DNA. Translation: EAW78732.1.
CH471052 Genomic DNA. Translation: EAW78733.1.
CH471052 Genomic DNA. Translation: EAW78734.1.
BC043166 mRNA. Translation: AAH43166.1.
U17968 mRNA. Translation: AAC50113.1.
CCDSiCCDS3174.1. [Q14722-1]
CCDS3175.1. [Q14722-3]
CCDS33882.1. [Q14722-2]
PIRiI55463.
I59393.
RefSeqiNP_003462.2. NM_003471.3. [Q14722-3]
NP_751891.1. NM_172159.3. [Q14722-2]
NP_751892.1. NM_172160.2. [Q14722-1]
UniGeneiHs.654519.
Hs.703187.

Genome annotation databases

EnsembliENST00000302490; ENSP00000305858; ENSG00000169282. [Q14722-2]
ENST00000471742; ENSP00000418956; ENSG00000169282. [Q14722-3]
ENST00000490337; ENSP00000419952; ENSG00000169282. [Q14722-1]
GeneIDi7881.
KEGGihsa:7881.
UCSCiuc003far.2. human. [Q14722-1]
uc003fas.2. human. [Q14722-3]
uc003fat.2. human. [Q14722-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L47665 mRNA. Translation: AAC41926.1.
U16953 mRNA. Translation: AAC50122.1.
L39833 mRNA. Translation: AAC37573.1.
U33428 mRNA. Translation: AAC50953.1.
X83127 mRNA. Translation: CAA58208.1.
AK057059 mRNA. Translation: BAG51856.1.
AK127240 mRNA. Translation: BAG54461.1.
AK292693 mRNA. Translation: BAF85382.1.
AK292999 mRNA. Translation: BAF85688.1.
CH471052 Genomic DNA. Translation: EAW78732.1.
CH471052 Genomic DNA. Translation: EAW78733.1.
CH471052 Genomic DNA. Translation: EAW78734.1.
BC043166 mRNA. Translation: AAH43166.1.
U17968 mRNA. Translation: AAC50113.1.
CCDSiCCDS3174.1. [Q14722-1]
CCDS3175.1. [Q14722-3]
CCDS33882.1. [Q14722-2]
PIRiI55463.
I59393.
RefSeqiNP_003462.2. NM_003471.3. [Q14722-3]
NP_751891.1. NM_172159.3. [Q14722-2]
NP_751892.1. NM_172160.2. [Q14722-1]
UniGeneiHs.654519.
Hs.703187.

3D structure databases

DisProtiDP00090.
ProteinModelPortaliQ14722.
SMRiQ14722. Positions 91-413.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113626. 12 interactions.
IntActiQ14722. 2 interactions.

Chemistry

ChEMBLiCHEMBL5884.

Protein family/group databases

TCDBi8.A.5.1.1. the voltage-gated k(+) channel -subunit (kv) family.

PTM databases

PhosphoSiteiQ14722.

Polymorphism and mutation databases

BioMutaiKCNAB1.
DMDMi18202500.

Proteomic databases

MaxQBiQ14722.
PaxDbiQ14722.
PRIDEiQ14722.

Protocols and materials databases

DNASUi7881.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000302490; ENSP00000305858; ENSG00000169282. [Q14722-2]
ENST00000471742; ENSP00000418956; ENSG00000169282. [Q14722-3]
ENST00000490337; ENSP00000419952; ENSG00000169282. [Q14722-1]
GeneIDi7881.
KEGGihsa:7881.
UCSCiuc003far.2. human. [Q14722-1]
uc003fas.2. human. [Q14722-3]
uc003fat.2. human. [Q14722-2]

Organism-specific databases

CTDi7881.
GeneCardsiGC03P155755.
HGNCiHGNC:6228. KCNAB1.
HPAiHPA044550.
MIMi601141. gene.
neXtProtiNX_Q14722.
PharmGKBiPA370.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOVERGENiHBG052216.
InParanoidiQ14722.
KOiK04882.
OMAiAYGNWIT.
PhylomeDBiQ14722.
TreeFamiTF324563.

Enzyme and pathway databases

ReactomeiREACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiKCNAB1. human.
GeneWikiiKCNAB1.
GenomeRNAii7881.
NextBioi30342.
PROiQ14722.
SOURCEiSearch...

Gene expression databases

BgeeiQ14722.
CleanExiHS_KCNAB1.
ExpressionAtlasiQ14722. baseline and differential.
GenevisibleiQ14722. HS.

Family and domain databases

Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red.
IPR005983. K_chnl_volt-dep_bsu_KCNAB.
IPR005399. K_chnl_volt-dep_bsu_KCNAB-rel.
IPR005400. K_chnl_volt-dep_bsu_KCNAB1.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01578. KCNAB1CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel K+ channel beta-subunit (hKv beta 1.3) is produced via alternative mRNA splicing."
    England S.K., Uebele V.N., Kodali J., Bennett P.B., Tamkun M.M.
    J. Biol. Chem. 270:28531-28534(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.3), FUNCTION.
    Tissue: Heart left ventricle.
  2. "Molecular cloning and functional expression of a novel potassium channel beta-subunit from human atrium."
    Majumder K., De Biasi M., Wang Z., Wible B.A.
    FEBS Lett. 361:13-16(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.2), FUNCTION, SUBUNIT.
    Tissue: Heart atrium.
  3. "Characterization of a voltage-gated K+ channel beta subunit expressed in human heart."
    England S.K., Uebele V.N., Shear H., Kodali J., Bennett P.B., Tamkun M.M.
    Proc. Natl. Acad. Sci. U.S.A. 92:6309-6313(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.2), FUNCTION, TISSUE SPECIFICITY.
    Tissue: Heart left ventricle.
  4. "Alternative splicing of the human Shaker K+ channel beta 1 gene and functional expression of the beta 2 gene product."
    Mccormack K., McCormack T., Tanouye M.A., Rudy B., Stuehmer W.
    FEBS Lett. 370:32-36(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.1), FUNCTION.
    Tissue: Hippocampus.
  5. "Structural and functional characterization of human potassium channel subunit beta 1 (KCNA1B)."
    Leicher T., Roeper J., Weber K., Wang X., Pongs O.
    Neuropharmacology 35:787-795(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM KVB1.1), ALTERNATIVE SPLICING, FUNCTION, TISSUE SPECIFICITY.
    Tissue: Brain cortex.
  6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS KVB1.1; KVB1.2 AND KVB1.3).
    Tissue: Hippocampus, Thymus and Trachea.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM KVB1.1).
    Tissue: Brain.
  9. "A novel beta subunit increases rate of inactivation of specific voltage-gated potassium channel alpha subunits."
    Morales M.J., Castellino R.C., Crews A.L., Rasmusson R.L., Strauss H.C.
    J. Biol. Chem. 270:6272-6277(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-147 (ISOFORM KVB1.2), FUNCTION.
    Tissue: Heart.
  10. "Separable effects of human Kvbeta1.2 N- and C-termini on inactivation and expression of human Kv1.4."
    Accili E.A., Kuryshev Y.A., Wible B.A., Brown A.M.
    J. Physiol. (Lond.) 512:325-336(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.
  11. "Episodic ataxia type 1 mutations in the human Kv1.1 potassium channel alter hKvbeta 1-induced N-type inactivation."
    Maylie B., Bissonnette E., Virk M., Adelman J.P., Maylie J.G.
    J. Neurosci. 22:4786-4793(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Modulation of the human Kv1.5 channel by protein kinase C activation: role of the Kvbeta1.2 subunit."
    Williams C.P., Hu N., Shen W., Mashburn A.B., Murray K.T.
    J. Pharmacol. Exp. Ther. 302:545-550(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNA5.
  13. "Control of human potassium channel inactivation by editing of a small mRNA hairpin."
    Bhalla T., Rosenthal J.J., Holmgren M., Reenan R.
    Nat. Struct. Mol. Biol. 11:950-956(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "Episodic ataxia type 1 mutations in the KCNA1 gene impair the fast inactivation properties of the human potassium channels Kv1.4-1.1/Kvbeta1.1 and Kv1.4-1.1/Kvbeta1.2."
    Imbrici P., D'Adamo M.C., Kullmann D.M., Pessia M.
    Eur. J. Neurosci. 24:3073-3083(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "NADPH binding to beta-subunit regulates inactivation of voltage-gated K(+) channels."
    Tipparaju S.M., Liu S.Q., Barski O.A., Bhatnagar A.
    Biochem. Biophys. Res. Commun. 359:269-276(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, DOMAIN, MUTAGENESIS OF TYR-307 AND ARG-316.
  16. "The molecular basis for the actions of Kvbeta1.2 on the opening and closing of the Kv1.2 delayed rectifier channel."
    Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.
    Channels 3:314-322(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DOMAIN.

Entry informationi

Entry nameiKCAB1_HUMAN
AccessioniPrimary (citable) accession number: Q14722
Secondary accession number(s): A8K9H8
, A8KAD4, B3KPZ4, Q13031, Q13302, Q16547, Q6PI60, Q99869
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: November 1, 1996
Last modified: June 24, 2015
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.