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Protein

Voltage-gated potassium channel subunit beta-2

Gene

Kcnab2

Organism
Rattus norvegicus (Rat)
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:9763623, PubMed:21357749). Contributes to the regulation of nerve signaling, and prevents neuronal hyperexcitability (By similarity). Promotes expression of the pore-forming alpha subunits at the cell membrane, and thereby increases channel activity (PubMed:10896669, PubMed:16770729, PubMed:18003609, PubMed:21357749). Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:21357749). Modulates the functional properties of KCNA4 (PubMed:9763623). Modulates the functional properties of KCNA5 (By similarity). Enhances KCNB2 channel activity (By similarity). Binds NADPH and has NADPH-dependent aldoketoreductase activity (PubMed:18672894, PubMed:21209188). Has broad substrate specificity and can catalyze the reduction of methylglyoxal, 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro) (PubMed:18672894).By similarity6 Publications

pH dependencei

Optimum pH is 7.2-7.4.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631NADPCombined sources1 Publication
Binding sitei85 – 851NADPCombined sources1 Publication
Active sitei90 – 901Proton donor/acceptor1 Publication
Binding sitei90 – 901NADP1 Publication
Binding sitei214 – 2141NADPCombined sources1 Publication
Binding sitei254 – 2541NADPCombined sources1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 572NADPCombined sources1 Publication
Nucleotide bindingi188 – 1892NADPCombined sources1 Publication
Nucleotide bindingi243 – 2486NADPCombined sources1 Publication
Nucleotide bindingi262 – 2643NADPCombined sources
Nucleotide bindingi323 – 33311NADPCombined sources1 PublicationAdd
BLAST

GO - Molecular functioni

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

GO - Biological processi

  • hematopoietic progenitor cell differentiation Source: Ensembl
  • myoblast differentiation Source: RGD
  • NADPH oxidation Source: UniProtKB
  • oxidation-reduction process Source: UniProtKB
  • protein heterooligomerization Source: RGD
  • regulation of potassium ion transmembrane transport Source: UniProtKB
  • regulation of protein localization to cell surface Source: UniProtKB
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_352543. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-2 (EC:1.1.1.-2 Publications)
Alternative name(s):
K(+) channel subunit beta-2
Kv-beta-2
Gene namesi
Name:Kcnab2
Synonyms:Ckbeta2, Kcnb3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Chromosome 5

Organism-specific databases

RGDi61828. Kcnab2.

Subcellular locationi

GO - Cellular componenti

  • axon Source: UniProtKB
  • cell junction Source: UniProtKB-KW
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  • juxtaparanode region of axon Source: UniProtKB
  • neuron projection Source: UniProtKB
  • pinceau fiber Source: UniProtKB
  • potassium channel complex Source: UniProtKB
  • synapse Source: UniProtKB-KW
  • voltage-gated potassium channel complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane, Synapse, Synaptosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi9 – 91S → A: Impairs interaction with MAPRE1 and association with microtubules. 1 Publication
Mutagenesisi20 – 201S → A: No effect on interaction with MAPRE1 and association with microtubules. 1 Publication
Mutagenesisi31 – 311S → A: Impairs interaction with MAPRE1 and association with microtubules. 1 Publication
Mutagenesisi90 – 901Y → F: Abolishes enzyme activity, but has no effect on NADPH binding. 2 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Voltage-gated potassium channel subunit beta-2PRO_0000148748Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei20 – 201Phosphoserine1 Publication
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei112 – 1121Phosphoserine1 Publication
Modified residuei124 – 1241N6-acetyllysineBy similarity

Post-translational modificationi

Phosphorylated by PRKCZ; may be regulated by incorporation in a complex composed of PRKCZ and SQSTM1.1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP62483.
PRIDEiP62483.

PTM databases

PhosphoSiteiP62483.

Expressioni

Tissue specificityi

Detected in brain (PubMed:9334400, PubMed:21357749). Detected in the middle third of the molecular layer of the dentate gyrus in hippocampus (PubMed:9334400). Detected in neurons in the deep cerebellar nucleus (PubMed:23318870). Detected in globus pallidus and pars reticulata of the substantia nigra (PubMed:9334400). Detected in cerebellum (PubMed:23318870). Detected at axon terminal plexuses of cerebellar granule cells (PubMed:9334400). Detected in the juxtaparanodal region of nodes of Ranvier in cerebellum (at protein level) (PubMed:9334400). Detected in mesenteric arteries (PubMed:15618540).4 Publications

Gene expression databases

GenevisibleiP62483. RN.

Interactioni

Subunit structurei

Homotetramer (PubMed:10884227, PubMed:16002581, PubMed:18004376, PubMed:18806782, PubMed:20534430, PubMed:20360102, PubMed:23705070). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (PubMed:10884227, PubMed:16002581, PubMed:18004376, PubMed:18806782, PubMed:20534430, PubMed:20360102, PubMed:23705070). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (PubMed:9334400). Interacts with KCNA1 (PubMed:23318870, PubMed:10884227). Interacts with KCNA2 (PubMed:18003609, PubMed:21357749, PubMed:23318870, PubMed:16002581, PubMed:18004376, PubMed:18806782, PubMed:20534430, PubMed:20360102, PubMed:23705070). Interacts with KCNA4 and KCND3 (PubMed:12860406). Interacts with KCNA5 (By similarity). Interacts with KCNB2 (By similarity). Interacts (in unphosphorylated form) with MAPRE1 (PubMed:21357749). Forms a ternary complex with SQSTM1 and PRKCZ (PubMed:10477520).By similarity14 Publications

Protein-protein interaction databases

BioGridi248350. 7 interactions.
IntActiP62483. 1 interaction.
STRINGi10116.ENSRNOP00000015840.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi38 – 425Combined sources
Beta strandi48 – 558Combined sources
Helixi59 – 635Combined sources
Helixi66 – 7813Combined sources
Beta strandi83 – 875Combined sources
Helixi90 – 934Combined sources
Helixi94 – 10613Combined sources
Helixi110 – 1123Combined sources
Beta strandi114 – 1218Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1324Combined sources
Helixi133 – 14715Combined sources
Beta strandi152 – 1598Combined sources
Helixi166 – 17813Combined sources
Beta strandi181 – 1899Combined sources
Helixi192 – 20413Combined sources
Beta strandi212 – 2165Combined sources
Helixi223 – 23614Combined sources
Beta strandi239 – 2435Combined sources
Helixi247 – 2526Combined sources
Turni253 – 2575Combined sources
Helixi264 – 2663Combined sources
Helixi271 – 2788Combined sources
Helixi280 – 29920Combined sources
Helixi303 – 31210Combined sources
Beta strandi319 – 3224Combined sources
Helixi327 – 3348Combined sources
Helixi335 – 3428Combined sources
Helixi345 – 35511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EXBX-ray2.10A36-367[»]
1QRQX-ray2.80A/B/C/D36-360[»]
2A79X-ray2.90A36-367[»]
2R9RX-ray2.40A/G36-367[»]
3EAUX-ray1.82A36-361[»]
3EB3X-ray2.00A36-361[»]
3EB4X-ray2.00A36-361[»]
3LNMX-ray2.90A/C36-367[»]
3LUTX-ray2.90A1-367[»]
4JTAX-ray2.50A/P36-367[»]
4JTCX-ray2.56A/G36-367[»]
4JTDX-ray2.54A/G36-367[»]
ProteinModelPortaliP62483.
SMRiP62483. Positions 36-361.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP62483.

Family & Domainsi

Domaini

In contrast to KCNAB1, the shorter N-terminal domain of KCNAB2 cannot mediate closure of delayed rectifier potassium channels by physically obstructing the pore.By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP62483.
KOiK04883.
OMAiAGYTMWE.
OrthoDBiEOG71G9TR.
PhylomeDBiP62483.
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.
IPR005401. K_chnl_volt-dep_bsu_KCNAB2.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.

Sequencei

Sequence statusi: Complete.

P62483-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS
60 70 80 90 100
CLGLGTWVTF GGQITDEMAE HLMTLAYDNG INLFDTAEVY AAGKAEVVLG
110 120 130 140 150
NIIKKKGWRR SSLVITTKIF WGGKAETERG LSRKHIIEGL KASLERLQLE
160 170 180 190 200
YVDVVFANRP DPNTPMEETV RAMTHVINQG MAMYWGTSRW SSMEIMEAYS
210 220 230 240 250
VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA MTWSPLACGI
260 270 280 290 300
VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
310 320 330 340 350
CTLPQLAIAW CLRNEGVSSV LLGASNAEQL MENIGAIQVL PKLSSSIVHE
360
IDSILGNKPY SKKDYRS
Length:367
Mass (Da):41,021
Last modified:July 5, 2004 - v1
Checksum:i5303FD1411B324FC
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76724 mRNA. Translation: CAA54142.1.
PIRiS45312.
RefSeqiNP_059000.1. NM_017304.2.
XP_008762564.1. XM_008764342.1.
XP_008762565.1. XM_008764343.1.
UniGeneiRn.10757.

Genome annotation databases

EnsembliENSRNOT00000015840; ENSRNOP00000015840; ENSRNOG00000011550.
GeneIDi29738.
KEGGirno:29738.
UCSCiRGD:61828. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X76724 mRNA. Translation: CAA54142.1.
PIRiS45312.
RefSeqiNP_059000.1. NM_017304.2.
XP_008762564.1. XM_008764342.1.
XP_008762565.1. XM_008764343.1.
UniGeneiRn.10757.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1EXBX-ray2.10A36-367[»]
1QRQX-ray2.80A/B/C/D36-360[»]
2A79X-ray2.90A36-367[»]
2R9RX-ray2.40A/G36-367[»]
3EAUX-ray1.82A36-361[»]
3EB3X-ray2.00A36-361[»]
3EB4X-ray2.00A36-361[»]
3LNMX-ray2.90A/C36-367[»]
3LUTX-ray2.90A1-367[»]
4JTAX-ray2.50A/P36-367[»]
4JTCX-ray2.56A/G36-367[»]
4JTDX-ray2.54A/G36-367[»]
ProteinModelPortaliP62483.
SMRiP62483. Positions 36-361.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248350. 7 interactions.
IntActiP62483. 1 interaction.
STRINGi10116.ENSRNOP00000015840.

PTM databases

PhosphoSiteiP62483.

Proteomic databases

PaxDbiP62483.
PRIDEiP62483.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000015840; ENSRNOP00000015840; ENSRNOG00000011550.
GeneIDi29738.
KEGGirno:29738.
UCSCiRGD:61828. rat.

Organism-specific databases

CTDi8514.
RGDi61828. Kcnab2.

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP62483.
KOiK04883.
OMAiAGYTMWE.
OrthoDBiEOG71G9TR.
PhylomeDBiP62483.
TreeFamiTF324563.

Enzyme and pathway databases

ReactomeiREACT_352543. Voltage gated Potassium channels.

Miscellaneous databases

EvolutionaryTraceiP62483.
NextBioi289815.
PROiP62483.

Gene expression databases

GenevisibleiP62483. RN.

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.
IPR005401. K_chnl_volt-dep_bsu_KCNAB2.
IPR023210. NADP_OxRdtase_dom.
[Graphical view]
PANTHERiPTHR11732. PTHR11732. 1 hit.
PfamiPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSiPR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMiSSF51430. SSF51430. 1 hit.
TIGRFAMsiTIGR01293. Kv_beta. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Inactivation properties of voltage-gated K+ channels altered by presence of beta-subunit."
    Rettig J., Heinemann S.H., Wunder F., Lorra C., Parcej D.N., Dolly J.O., Pongs O.
    Nature 369:289-294(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Brain cortex.
  2. "Association and colocalization of the Kvbeta1 and Kvbeta2 beta-subunits with Kv1 alpha-subunits in mammalian brain K+ channel complexes."
    Rhodes K.J., Strassle B.W., Monaghan M.M., Bekele-Arcuri Z., Matos M.F., Trimmer J.S.
    J. Neurosci. 17:8246-8258(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA1; KCNA2; KCNA4; KCNA6 AND KCNAB1, SUBUNIT, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  3. "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.
  4. "Differential stimulation of PKC phosphorylation of potassium channels by ZIP1 and ZIP2."
    Gong J., Xu J., Bezanilla M., van Huizen R., Derin R., Li M.
    Science 285:1565-1569(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1 AND PRKCZ, PHOSPHORYLATION BY PRKCZ.
  5. "Subunit composition determines Kv1 potassium channel surface expression."
    Manganas L.N., Trimmer J.S.
    J. Biol. Chem. 275:29685-29693(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Subunit composition and novel localization of K+ channels in spinal cord."
    Rasband M.N., Trimmer J.S.
    J. Comp. Neurol. 429:166-176(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA1 AND KCNA2, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  7. "Differential association of the auxiliary subunit Kvbeta2 with Kv1.4 and Kv4.3 K+ channels."
    Wang L., Takimoto K., Levitan E.S.
    FEBS Lett. 547:162-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA4 AND KCND3.
  8. "Heteromultimeric Kv1 channels contribute to myogenic control of arterial diameter."
    Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K., Chen T., Cole W.
    Circ. Res. 96:216-224(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, TISSUE SPECIFICITY.
  9. "The p62 scaffold regulates nerve growth factor-induced NF-kappaB activation by influencing TRAF6 polyubiquitination."
    Wooten M.W., Geetha T., Seibenhener M.L., Babu J.R., Diaz-Meco M.T., Moscat J.
    J. Biol. Chem. 280:35625-35629(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SQSTM1; IKBKB AND TRAF6.
  10. "Glycosylation and cell surface expression of Kv1.2 potassium channel are regulated by determinants in the pore region."
    Fujita T., Utsunomiya I., Ren J., Matsushita Y., Kawai M., Sasaki S., Hoshi K., Miyatake T., Taguchi K.
    Neurochem. Res. 31:589-596(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  11. "Catalytic mechanism and substrate specificity of the beta-subunit of the voltage-gated potassium channel."
    Tipparaju S.M., Barski O.A., Srivastava S., Bhatnagar A.
    Biochemistry 47:8840-8854(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF TYR-90, ACTIVE SITE.
  12. "Homeostatic regulation of Kv1.2 potassium channel trafficking by cyclic AMP."
    Connors E.C., Ballif B.A., Morielli A.D.
    J. Biol. Chem. 283:3445-3453(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH KCNA2, SUBUNIT.
  13. "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates Kv1 channel axonal targeting."
    Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B., Trimmer J.S.
    J. Cell Biol. 192:813-824(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH KCNA2 AND MAPRE1, TISSUE SPECIFICITY, IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-9; SER-20 AND SER-112, MUTAGENESIS OF SER-9; SER-20 AND SER-31.
  14. "Deletion of the mouse homolog of KCNAB2, a gene linked to monosomy 1p36, results in associative memory impairments and amygdala hyperexcitability."
    Perkowski J.J., Murphy G.G.
    J. Neurosci. 31:46-54(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF TYR-90.
  15. "A defined heteromeric KV1 channel stabilizes the intrinsic pacemaking and regulates the output of deep cerebellar nuclear neurons to thalamic targets."
    Ovsepian S.V., Steuber V., Le Berre M., O'Hara L., O'Leary V.B., Dolly J.O.
    J. Physiol. (Lond.) 591:1771-1791(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNA1 AND KCNA2, TISSUE SPECIFICITY.
  16. "Structure of the cytoplasmic beta subunit-T1 assembly of voltage-dependent K+ channels."
    Gulbis J.M., Zhou M., Mann S., MacKinnon R.
    Science 289:123-127(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 36-367 IN COMPLEX WITH NADP, INTERACTION WITH KCNA1, SUBUNIT.
  17. "Crystal structure of a mammalian voltage-dependent Shaker family K+ channel."
    Long S.B., Campbell E.B., Mackinnon R.
    Science 309:897-903(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 36-367 IN COMPLEX WITH NADP AND KCNA2, SUBUNIT.
  18. "Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment."
    Long S.B., Tao X., Campbell E.B., MacKinnon R.
    Nature 450:376-382(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 36-367 IN COMPLEX WITH NADP AND KCNA2, SUBUNIT.
  19. "Cortisone dissociates the Shaker family K+ channels from their beta subunits."
    Pan Y., Weng J., Kabaleeswaran V., Li H., Cao Y., Bhosle R.C., Zhou M.
    Nat. Chem. Biol. 4:708-714(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.82 ANGSTROMS) OF 36-361 IN COMPLEX WITH KCNA2; CORTISONE AND NADP, SUBUNIT.
  20. "Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement."
    Chen X., Wang Q., Ni F., Ma J.
    Proc. Natl. Acad. Sci. U.S.A. 107:11352-11357(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH KCNA2 AND NADP, SUBUNIT.
  21. "A gating charge transfer center in voltage sensors."
    Tao X., Lee A., Limapichat W., Dougherty D.A., MacKinnon R.
    Science 328:67-73(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 36-367 IN COMPLEX WITH KCNA2 AND NADP, SUBUNIT.
  22. "Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel."
    Banerjee A., Lee A., Campbell E., Mackinnon R.
    Elife 2:E00594-E00594(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 36-367 IN COMPLEX WITH KCNA2 AND NADP, SUBUNIT.

Entry informationi

Entry nameiKCAB2_RAT
AccessioniPrimary (citable) accession number: P62483
Secondary accession number(s): P97381, Q60942, Q64284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: June 24, 2015
This is version 107 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.