Q13303 (KCAB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	367 AA.
Sequence status	Complete.
Protein existence	Evidence 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.

Ontologies

Keywords
Biological process	Ion transport Potassium transport Transport
Cellular component	Cytoplasm
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	NADP Potassium
Molecular function	Ion channel Voltage-gated channel
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	protein heterooligomerization Inferred from electronic annotation. Source: Compara synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell integral to membrane Inferred from electronic annotation. Source: InterPro juxtaparanode region of axon Inferred from sequence or structural similarity. Source: BHF-UCL plasma membrane Traceable author statement. Source: Reactome
Molecular_function	potassium channel regulator activity Traceable author statement Ref.1. Source: ProtInc voltage-gated potassium channel activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 367

367

Voltage-gated potassium channel subunit beta-2

PRO_0000148746

Regions

Nucleotide binding

56 – 57

2

NADP

Nucleotide binding

188 – 189

2

NADP

Nucleotide binding

243 – 248

6

NADP

Nucleotide binding

323 – 329

7

NADP

Sites

Binding site

63

1

NADP

Binding site

85

1

NADP

Binding site

90

1

NADP

Binding site

214

1

NADP

Binding site

254

1

NADP

Amino acid modifications

Modified residue

9

1

Phosphoserine Ref.7

Modified residue

20

1

Phosphoserine By similarity

Modified residue

25

1

Phosphotyrosine By similarity

Modified residue

124

1

N6-acetyllysine Ref.8

Modified residue

360

1

Phosphotyrosine By similarity

Natural variations

Alternative sequence

1 – 67

67

Missing in isoform 4.

VSP_044311

Alternative sequence

1 – 38

38

MYPES…RQLQF → MLSMTYSESLRSVSSRCHSE WALHPVRQTDTLELQRLREV RAAAQARNMESFLRMHGLSL DGCTAQRTGMK in isoform 3.

VSP_041189

Alternative sequence

26 – 39

14

Missing in isoform 2.

VSP_001054

Alternative sequence

167

1

E → EGDPFSSSKSRTFIIE in isoform 3.

VSP_041190

Natural variant

88

1

E → K.
Corresponds to variant rs2229003 [ dbSNP | Ensembl ].

VAR_048747

Secondary structure

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367

Helix Strand Turn

Details...

Beta strand

39 – 42

4

Beta strand

48 – 55

8

Helix

59 – 63

5

Helix

66 – 78

13

Beta strand

83 – 85

3

Helix

90 – 93

4

Helix

94 – 106

13

Helix

110 – 112

3

Beta strand

114 – 121

8

Helix

126 – 128

3

Beta strand

129 – 131

3

Helix

133 – 147

15

Beta strand

152 – 159

8

Helix

166 – 178

13

Beta strand

181 – 189

9

Helix

192 – 205

14

Beta strand

212 – 216

5

Helix

223 – 226

4

Helix

228 – 236

9

Beta strand

239 – 243

5

Helix

247 – 252

6

Turn

253 – 257

5

Helix

264 – 266

3

Helix

271 – 277

7

Helix

280 – 299

20

Helix

303 – 313

11

Beta strand

317 – 322

6

Helix

327 – 334

8

Helix

336 – 339

4

Helix

340 – 342

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (KvB2.1) [UniParc]. Last modified January 1, 1998. Version 2. Checksum: 91A673F8992140DA	FASTA	367	41,000
	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
	Isoform 2 (KvB2.2) [UniParc]. Checksum: 7D59C8203AC5606F	FASTA	353	39,287
	10 20 30 40 50 60 MYPESTTGSP ARLSLRQTGS PGMIYRNLGK SGLRVSCLGL GTWVTFGGQI TDEMAEQLMT 70 80 90 100 110 120 LAYDNGINLF DTAEVYAAGK AEVVLGNIIK KKGWRRSSLV ITTKIFWGGK AETERGLSRK 130 140 150 160 170 180 HIIEGLKASL ERLQLEYVDV VFANRPDPNT PMEETVRAMT HVINQGMAMY WGTSRWSSME 190 200 210 220 230 240 IMEAYSVARQ FNLTPPICEQ AEYHMFQREK VEVQLPELFH KIGVGAMTWS PLACGIVSGK 250 260 270 280 290 300 YDSGIPPYSR ASLKGYQWLK DKILSEEGRR QQAKLKELQA IAERLGCTLP QLAIAWCLRN 310 320 330 340 350 EGVSSVLLGA SNADQLMENI GAIQVLPKLS SSIIHEIDSI LGNKPYSKKD YRS
	Isoform 3 [UniParc]. Checksum: 3AD46E32E4B200AF	FASTA	415	46,527
	10 20 30 40 50 60 MLSMTYSESL RSVSSRCHSE WALHPVRQTD TLELQRLREV RAAAQARNME SFLRMHGLSL 70 80 90 100 110 120 DGCTAQRTGM KYRNLGKSGL RVSCLGLGTW VTFGGQITDE MAEQLMTLAY DNGINLFDTA 130 140 150 160 170 180 EVYAAGKAEV VLGNIIKKKG WRRSSLVITT KIFWGGKAET ERGLSRKHII EGLKASLERL 190 200 210 220 230 240 QLEYVDVVFA NRPDPNTPME GDPFSSSKSR TFIIEETVRA MTHVINQGMA MYWGTSRWSS 250 260 270 280 290 300 MEIMEAYSVA RQFNLTPPIC EQAEYHMFQR EKVEVQLPEL FHKIGVGAMT WSPLACGIVS 310 320 330 340 350 360 GKYDSGIPPY SRASLKGYQW LKDKILSEEG RRQQAKLKEL QAIAERLGCT LPQLAIAWCL 370 380 390 400 410 RNEGVSSVLL GASNADQLME NIGAIQVLPK LSSSIIHEID SILGNKPYSK KDYRS
	Isoform 4 [UniParc]. Checksum: 3ADDAAE15216B737	FASTA	300	33,657
	10 20 30 40 50 60 MAEQLMTLAY DNGINLFDTA EVYAAGKAEV VLGNIIKKKG WRRSSLVITT KIFWGGKAET 70 80 90 100 110 120 ERGLSRKHII EGLKASLERL QLEYVDVVFA NRPDPNTPME ETVRAMTHVI NQGMAMYWGT 130 140 150 160 170 180 SRWSSMEIME AYSVARQFNL TPPICEQAEY HMFQREKVEV QLPELFHKIG VGAMTWSPLA 190 200 210 220 230 240 CGIVSGKYDS GIPPYSRASL KGYQWLKDKI LSEEGRRQQA KLKELQAIAE RLGCTLPQLA 250 260 270 280 290 300 IAWCLRNEGV SSVLLGASNA DQLMENIGAI QVLPKLSSSI IHEIDSILGN KPYSKKDYRS

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
[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]	"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.

IPI

IPI00021088.
IPI00218374.
IPI00442307.

PIR

S66502.

RefSeq

NP_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.

UniGene

Hs.440497.
Hs.735032.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ZSX	X-ray	1.90	A	39-346	[»]

ProteinModelPortal

Q13303.

ModBase

Search...

Protein-protein interaction databases

IntAct

Q13303. 1 interaction.

MINT

MINT-2865320.

STRING

9606.ENSP00000164247.

PTM databases

PhosphoSite

Q13303.

Polymorphism databases

DMDM

18202496.

Proteomic databases

PaxDb

Q13303.

PRIDE

Q13303.

Protocols and materials databases

DNASU

8514.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000164247; ENSP00000164247; ENSG00000069424.
ENST00000341524; ENSP00000340824; ENSG00000069424.
ENST00000352527; ENSP00000318772; ENSG00000069424.
ENST00000378083; ENSP00000367323; ENSG00000069424.
ENST00000378092; ENSP00000367332; ENSG00000069424.
ENST00000378097; ENSP00000367337; ENSG00000069424.
ENST00000458166; ENSP00000396167; ENSG00000069424.

GeneID

8514.

KEGG

hsa:8514.

UCSC

uc001alv.2. human.
uc001alw.2. human.
uc001aly.2. human.

Organism-specific databases

CTD

8514.

GeneCards

GC01P006020.

HGNC

HGNC:6229. KCNAB2.

HPA

CAB001975.
HPA030185.

MIM

601142. gene.

neXtProt

NX_Q13303.

PharmGKB

PA373.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG0667.

HOVERGEN

HBG052216.

KO

K04883.

OMA

GCTARRT.

PhylomeDB

Q13303.

Enzyme and pathway databases

Reactome

REACT_13685. Neuronal System.

Gene expression databases

ArrayExpress

Q13303.

Bgee

Q13303.

CleanEx

HS_KCNAB2.
HS_KCNK2.

Genevestigator

Q13303.

GermOnline

ENSG00000069424. Homo sapiens.

Family and domain databases

Gene3D

3.20.20.100. 1 hit.

InterPro

IPR001395. 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]

PANTHER

PTHR11732. PTHR11732. 1 hit.
PTHR11732:SF14. PTHR11732:SF14. 1 hit.

Pfam

PF00248. Aldo_ket_red. 1 hit.
[Graphical view]

PRINTS

PR01579. KCNAB2CHANEL.
PR01577. KCNABCHANNEL.

SUPFAM

SSF51430. Aldo/ket_red. 1 hit.

TIGRFAMs

TIGR01293. Kv_beta. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

KCNAB2. human.

EvolutionaryTrace

Q13303.

GenomeRNAi

8514.

NextBio

31868.

SOURCE

Search...

Entry information

Entry name

KCAB2_HUMAN

Accession

Primary (citable) accession number: Q13303
Secondary accession number(s): A0AVM9 , 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:	May 1, 2013
This is version 128 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.