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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)DescriptionActionsGraphical viewLength
Binding sitei63NADPCombined sources1 Publication1
Binding sitei85NADPCombined sources1 Publication1
Active sitei90Proton donor/acceptor1 Publication1
Binding sitei90NADP1 Publication1
Binding sitei214NADPCombined sources1 Publication1
Binding sitei254NADPCombined sources1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi56 – 57NADPCombined sources1 Publication2
Nucleotide bindingi188 – 189NADPCombined sources1 Publication2
Nucleotide bindingi243 – 248NADPCombined sources1 Publication6
Nucleotide bindingi262 – 264NADPCombined sources3
Nucleotide bindingi323 – 333NADPCombined sources1 PublicationAdd BLAST11

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

  • 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

ReactomeiR-RNO-1296072. Voltage gated Potassium channels.
R-RNO-6798695. Neutrophil degranulation.

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
Proteomesi
  • UP000002494 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
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi9S → A: Impairs interaction with MAPRE1 and association with microtubules. 1 Publication1
Mutagenesisi20S → A: No effect on interaction with MAPRE1 and association with microtubules. 1 Publication1
Mutagenesisi31S → A: Impairs interaction with MAPRE1 and association with microtubules. 1 Publication1
Mutagenesisi90Y → F: Abolishes enzyme activity, but has no effect on NADPH binding. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001487481 – 367Voltage-gated potassium channel subunit beta-2Add BLAST367

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei9PhosphoserineCombined sources1 Publication1
Modified residuei14PhosphoserineBy similarity1
Modified residuei20PhosphoserineCombined sources1 Publication1
Modified residuei28Asymmetric dimethylarginine; alternateBy similarity1
Modified residuei28Omega-N-methylarginine; alternateBy similarity1
Modified residuei31PhosphoserineBy similarity1
Modified residuei112Phosphoserine1 Publication1
Modified residuei124N6-acetyllysineBy similarity1

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

PaxDbiP62483.
PRIDEiP62483.

PTM databases

iPTMnetiP62483.
PhosphoSitePlusiP62483.

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

BgeeiENSRNOG00000011550.
ExpressionAtlasiP62483. baseline and differential.
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

GO - Molecular functioni

  • ion channel binding Source: RGD

Protein-protein interaction databases

BioGridi248350. 7 interactors.
IntActiP62483. 1 interactor.
STRINGi10116.ENSRNOP00000015840.

Structurei

Secondary structure

1367
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi38 – 42Combined sources5
Beta strandi48 – 55Combined sources8
Helixi59 – 63Combined sources5
Helixi66 – 78Combined sources13
Beta strandi83 – 87Combined sources5
Helixi90 – 93Combined sources4
Helixi94 – 106Combined sources13
Helixi110 – 112Combined sources3
Beta strandi114 – 121Combined sources8
Helixi126 – 128Combined sources3
Beta strandi129 – 132Combined sources4
Helixi133 – 147Combined sources15
Beta strandi152 – 159Combined sources8
Helixi166 – 178Combined sources13
Beta strandi181 – 189Combined sources9
Helixi192 – 204Combined sources13
Beta strandi212 – 216Combined sources5
Helixi223 – 236Combined sources14
Beta strandi239 – 243Combined sources5
Helixi247 – 252Combined sources6
Turni253 – 257Combined sources5
Helixi264 – 266Combined sources3
Helixi271 – 278Combined sources8
Helixi280 – 299Combined sources20
Helixi303 – 312Combined sources10
Beta strandi319 – 322Combined sources4
Helixi327 – 334Combined sources8
Helixi335 – 342Combined sources8
Helixi345 – 355Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
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

eggNOGiKOG1575. Eukaryota.
COG0667. LUCA.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP62483.
KOiK04883.
PhylomeDBiP62483.
TreeFamiTF324563.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
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.
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.
UniGeneiRn.10757.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248350. 7 interactors.
IntActiP62483. 1 interactor.
STRINGi10116.ENSRNOP00000015840.

PTM databases

iPTMnetiP62483.
PhosphoSitePlusiP62483.

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

eggNOGiKOG1575. Eukaryota.
COG0667. LUCA.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiP62483.
KOiK04883.
PhylomeDBiP62483.
TreeFamiTF324563.

Enzyme and pathway databases

ReactomeiR-RNO-1296072. Voltage gated Potassium channels.
R-RNO-6798695. Neutrophil degranulation.

Miscellaneous databases

EvolutionaryTraceiP62483.
PROiP62483.

Gene expression databases

BgeeiENSRNOG00000011550.
ExpressionAtlasiP62483. baseline and differential.
GenevisibleiP62483. RN.

Family and domain databases

CDDicd06660. Aldo_ket_red. 1 hit.
Gene3Di3.20.20.100. 1 hit.
InterProiIPR001395. Aldo/ket_red/Kv-b.
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...

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: November 30, 2016
This is version 117 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

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 one 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.