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P62483 (KCAB2_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Voltage-gated potassium channel subunit beta-2
Alternative name(s):
K(+) channel subunit beta-2
Kv-beta-2
Gene names
Name:Kcnab2
Synonyms:Ckbeta2, Kcnb3
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length367 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Subunit structure

Forms heteromultimeric complex with alpha subunits. Forms a ternary complex with SQSTM1 and PRKCZ. Ref.4

Subcellular location

Cytoplasm Potential.

Domain

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

Post-translational modification

Phosphorylated by PRKCZ; may be regulated by incorporation in a complex composed of PRKCZ and SQSTM1. Ref.2

Sequence similarities

Belongs to the shaker potassium channel beta subunit family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Kcna1P104991EBI-771110,EBI-631463

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Voltage-gated potassium channel subunit beta-2
PRO_0000148748

Regions

Nucleotide binding56 – 572NADP
Nucleotide binding188 – 1892NADP
Nucleotide binding243 – 2486NADP
Nucleotide binding323 – 3297NADP

Sites

Binding site631NADP
Binding site851NADP
Binding site901NADP
Binding site2141NADP
Binding site2541NADP

Amino acid modifications

Modified residue91Phosphoserine By similarity
Modified residue201Phosphoserine By similarity
Modified residue251Phosphotyrosine By similarity
Modified residue1241N6-acetyllysine By similarity
Modified residue3601Phosphotyrosine By similarity

Secondary structure

1 ...................................................... 367
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P62483 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 5303FD1411B324FC

FASTA36741,021
        10         20         30         40         50         60 
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF 

        70         80         90        100        110        120 
GGQITDEMAE HLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF 

       130        140        150        160        170        180 
WGGKAETERG LSRKHIIEGL KASLERLQLE YVDVVFANRP DPNTPMEETV RAMTHVINQG 

       190        200        210        220        230        240 
MAMYWGTSRW SSMEIMEAYS VARQFNLIPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA 

       250        260        270        280        290        300 
MTWSPLACGI VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG 

       310        320        330        340        350        360 
CTLPQLAIAW CLRNEGVSSV LLGASNAEQL MENIGAIQVL PKLSSSIVHE IDSILGNKPY 


SKKDYRS

« Hide

References

[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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		X76724 mRNA. Translation: CAA54142.1.
IPIIPI00211012.
PIRS45312.
RefSeqNP_059000.1. NM_017304.2.
UniGeneRn.10757.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP62483.
SMRP62483. Positions 36-361.
ModBaseSearch...

Protein-protein interaction databases

IntActP62483. 1 interaction.

PTM databases

PhosphoSiteP62483.

Proteomic databases

PaxDbP62483.
PRIDEP62483.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000015840; ENSRNOP00000015840; ENSRNOG00000011550.
GeneID29738.
KEGGrno:29738.
UCSCRGD:61828. rat.

Organism-specific databases

CTD8514.
RGD61828. Kcnab2.

Phylogenomic databases

eggNOGCOG0667.
GeneTreeENSGT00550000074567.
HOGENOMHOG000250283.
HOVERGENHBG052216.
KOK04883.
OMAGCTARRT.
OrthoDBEOG476K0F.

Gene expression databases

GenevestigatorP62483.
GermOnlineENSRNOG00000011550. Rattus norvegicus.

Family and domain databases

Gene3D3.20.20.100. 1 hit.
InterProIPR001395. 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]
PANTHERPTHR11732. PTHR11732. 1 hit.
PTHR11732:SF14. PTHR11732:SF14. 1 hit.
PfamPF00248. Aldo_ket_red. 1 hit.
[Graphical view]
PRINTSPR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.
SUPFAMSSF51430. Aldo/ket_red. 1 hit.
TIGRFAMsTIGR01293. Kv_beta. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP62483.
NextBio289815.

Entry information

Entry nameKCAB2_RAT
AccessionPrimary (citable) accession number: P62483
Secondary accession number(s): P97381, Q60942, Q64284
Entry history
Integrated into UniProtKB/Swiss-Prot: July 5, 2004
Last sequence update: July 5, 2004
Last modified: May 1, 2013
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents