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Q13303 (KCAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 137. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Voltage-gated potassium channel subunit beta-2
Alternative name(s):
K(+) channel subunit beta-2
Kv-beta-2
Short name=hKvbeta2
Gene names
Name:KCNAB2
Synonyms:KCNA2B, KCNK2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. Alters functional properties of Kv1.4. Ref.1

Subunit structure

Forms heteromultimeric complex with alpha subunits. Forms a ternary complex with SQSTM1 and PRKCZ By similarity.

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 By similarity.

Sequence similarities

Belongs to the shaker potassium channel beta subunit family.

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q13303-1)

Also known as: KvB2.1;

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.
Isoform 2 (identifier: Q13303-2)

Also known as: KvB2.2;

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.
Isoform 3 (identifier: Q13303-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-38: MYPESTTGSP...YGSPKRQLQF → MLSMTYSESL...GCTAQRTGMK
     167-167: E → EGDPFSSSKSRTFIIE
Isoform 4 (identifier: Q13303-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1-67: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 367367Voltage-gated potassium channel subunit beta-2
PRO_0000148746

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 Ref.7
Modified residue1241N6-acetyllysine Ref.8

Natural variations

Alternative sequence1 – 6767Missing in isoform 4.
VSP_044311
Alternative sequence1 – 3838MYPES…RQLQF → MLSMTYSESLRSVSSRCHSE WALHPVRQTDTLELQRLREV RAAAQARNMESFLRMHGLSL DGCTAQRTGMK in isoform 3.
VSP_041189
Alternative sequence26 – 3914Missing in isoform 2.
VSP_001054
Alternative sequence1671E → EGDPFSSSKSRTFIIE in isoform 3.
VSP_041190
Natural variant881E → K.
Corresponds to variant rs2229003 [ dbSNP | Ensembl ].
VAR_048747

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (KvB2.1) [UniParc].

Last modified January 1, 1998. Version 2.
Checksum: 91A673F8992140DA

FASTA36741,000
        10         20         30         40         50         60 
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF 

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

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

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

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

       310        320        330        340        350        360 
CTLPQLAIAW CLRNEGVSSV LLGASNADQL MENIGAIQVL PKLSSSIIHE IDSILGNKPY 


SKKDYRS 

« Hide

Isoform 2 (KvB2.2) [UniParc].

Checksum: 7D59C8203AC5606F
Show »

FASTA35339,287
Isoform 3 [UniParc].

Checksum: 3AD46E32E4B200AF
Show »

FASTA41546,527
Isoform 4 [UniParc].

Checksum: 3ADDAAE15216B737
Show »

FASTA30033,657

References

« Hide 'large scale' references
[1]"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 1), FUNCTION.
Tissue: Hippocampus.
[2]McCormack K.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[3]Rae J.L., Shepard A.R.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
Tissue: Lens epithelium.
[4]"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. expand/collapse author list , 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 1; 3 AND 4).
Tissue: Amygdala, Brain and Hippocampus.
[5]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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 1).
Tissue: Brain.
[7]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[8]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[10]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"Crystal structure of human potassium channel Kv beta-subunit (KCNAB2)."
Structural genomics consortium (SGC)
Submitted (JUN-2005) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 36-360 IN COMPLEX WITH NADP.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U33429 mRNA. Translation: AAC50955.1.
AF029749 mRNA. Translation: AAB84170.1.
AF044253 mRNA. Translation: AAB99859.1.
AK124696 mRNA. Translation: BAG54071.1.
AK131252 mRNA. Translation: BAD18431.1.
AK289819 mRNA. Translation: BAF82508.1.
AK315858 mRNA. Translation: BAF98749.1.
AL035406 Genomic DNA. Translation: CAC08512.1.
AL035406 Genomic DNA. Translation: CAI19885.1.
BC126424 mRNA. Translation: AAI26425.1.
BC130413 mRNA. Translation: AAI30414.1.
PIRS66502.
RefSeqNP_001186789.1. NM_001199860.1.
NP_001186790.1. NM_001199861.1.
NP_001186791.1. NM_001199862.1.
NP_001186792.1. NM_001199863.1.
NP_003627.1. NM_003636.3.
NP_742128.1. NM_172130.2.
XP_005263571.1. XM_005263514.1.
UniGeneHs.440497.
Hs.735032.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSXX-ray1.90A39-346[»]
ProteinModelPortalQ13303.
SMRQ13303. Positions 37-359.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114086. 7 interactions.
IntActQ13303. 1 interaction.
MINTMINT-2865320.
STRING9606.ENSP00000164247.

PTM databases

PhosphoSiteQ13303.

Polymorphism databases

DMDM18202496.

Proteomic databases

PaxDbQ13303.
PRIDEQ13303.

Protocols and materials databases

DNASU8514.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000164247; ENSP00000164247; ENSG00000069424. [Q13303-1]
ENST00000341524; ENSP00000340824; ENSG00000069424. [Q13303-1]
ENST00000352527; ENSP00000318772; ENSG00000069424. [Q13303-2]
ENST00000378083; ENSP00000367323; ENSG00000069424. [Q13303-3]
ENST00000378092; ENSP00000367332; ENSG00000069424. [Q13303-2]
ENST00000378097; ENSP00000367337; ENSG00000069424. [Q13303-1]
ENST00000458166; ENSP00000396167; ENSG00000069424. [Q13303-4]
GeneID8514.
KEGGhsa:8514.
UCSCuc001alv.2. human. [Q13303-1]
uc001alw.2. human. [Q13303-2]
uc001aly.2. human. [Q13303-3]

Organism-specific databases

CTD8514.
GeneCardsGC01P006020.
HGNCHGNC:6229. KCNAB2.
HPACAB001975.
HPA030185.
MIM601142. gene.
neXtProtNX_Q13303.
Orphanet1606. 1p36 deletion syndrome.
PharmGKBPA373.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0667.
HOVERGENHBG052216.
KOK04883.
OMAKVFWPTG.
PhylomeDBQ13303.
TreeFamTF324563.

Enzyme and pathway databases

ReactomeREACT_13685. Neuronal System.

Gene expression databases

ArrayExpressQ13303.
BgeeQ13303.
CleanExHS_KCNAB2.
HS_KCNK2.
GenevestigatorQ13303.

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. SSF51430. 1 hit.
TIGRFAMsTIGR01293. Kv_beta. 1 hit.
ProtoNetSearch...

Other

ChiTaRSKCNAB2. human.
EvolutionaryTraceQ13303.
GeneWikiKCNAB2.
GenomeRNAi8514.
NextBio31868.
PROQ13303.
SOURCESearch...

Entry information

Entry nameKCAB2_HUMAN
AccessionPrimary (citable) accession number: Q13303
Secondary accession number(s): A0AVM9 expand/collapse secondary AC list , A8K1A4, B0AZR7, O43659, Q5TG82, Q5TG83, Q6ZNE4, Q99411
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 137 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM