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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

Accessory potassium channel protein which modulates the activity of the pore-forming alpha subunit.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631NADP1 Publication
Binding sitei85 – 851NADP1 Publication
Binding sitei90 – 901NADP1 Publication
Binding sitei214 – 2141NADP1 Publication
Binding sitei254 – 2541NADP1 Publication

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi56 – 572NADP1 Publication
Nucleotide bindingi188 – 1892NADP1 Publication
Nucleotide bindingi243 – 2486NADP1 Publication
Nucleotide bindingi323 – 3297NADP1 Publication

GO - Molecular functioni

  1. voltage-gated potassium channel activity Source: InterPro

GO - Biological processi

  1. hematopoietic progenitor cell differentiation Source: Ensembl
  2. protein heterooligomerization Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Ion channel, Voltage-gated channel

Keywords - Biological processi

Ion transport, Potassium transport, Transport

Keywords - Ligandi

NADP, Potassium

Enzyme and pathway databases

ReactomeiREACT_199159. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-2
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: Chromosome 5

Organism-specific databases

RGDi61828. Kcnab2.

Subcellular locationi

Cytoplasm Curated

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. integral component of membrane Source: InterPro
  3. juxtaparanode region of axon Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

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 – 91PhosphoserineBy similarity
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

Gene expression databases

GenevestigatoriP62483.

Interactioni

Subunit structurei

Forms heteromultimeric complex with alpha subunits. Forms a ternary complex with SQSTM1 and PRKCZ.1 Publication

Protein-protein interaction databases

BioGridi248350. 7 interactions.
IntActiP62483. 1 interaction.

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

Alteration of functional properties of alpha subunit is mediated through N-terminal domain of beta subunit.Curated

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.

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_199159. Voltage gated Potassium channels.

Miscellaneous databases

EvolutionaryTraceiP62483.
NextBioi289815.
PROiP62483.

Gene expression databases

GenevestigatoriP62483.

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. "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.
  3. "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.
  4. "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, INTERACTION WITH KCNA1, TETRAMERIZATION.
  5. "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.

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: January 7, 2015
This is version 102 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.