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Protein

Voltage-gated potassium channel subunit beta-2

Gene

KCNAB2

Organism
Homo sapiens (Human)
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:7649300, PubMed:11825900). 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 (By similarity). Promotes potassium channel closure via a mechanism that does not involve physical obstruction of the channel pore (PubMed:7649300, PubMed:11825900). Promotes KCNA4 channel closure (PubMed:7649300, PubMed:11825900). Modulates the functional properties of KCNA5 (By similarity). Enhances KCNB2 channel activity (By similarity). Binds NADPH and has NADPH-dependent aldoketoreductase activity (By similarity). 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) (By similarity).By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei63 – 631NADP1 Publication
Binding sitei85 – 851NADP1 Publication
Active sitei90 – 901Proton donor/acceptorBy similarity
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

GO - Biological processi

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

BioCyciRETL1328306-WGS:GSTH-2009-MONOMER.
ReactomeiREACT_75770. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Voltage-gated potassium channel subunit beta-2 (EC:1.1.1.-By similarity)
Alternative name(s):
K(+) channel subunit beta-2
Kv-beta-2
Short name:
hKvbeta2
Gene namesi
Name:KCNAB2
Synonyms:KCNA2B, KCNK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:6229. KCNAB2.

Subcellular locationi

GO - Cellular componenti

  • 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
  • membrane Source: UniProtKB
  • pinceau fiber Source: UniProtKB
  • plasma membrane Source: Reactome
  • synapse Source: UniProtKB-KW
  • voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi90 – 901Y → F: No effect on its activity in promoting KCNA4 channel closure. 1 Publication

Organism-specific databases

Orphaneti1606. 1p36 deletion syndrome.
PharmGKBiPA373.

Polymorphism and mutation databases

BioMutaiKCNAB2.
DMDMi18202496.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 367367Voltage-gated potassium channel subunit beta-2PRO_0000148746Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei9 – 91Phosphoserine1 Publication
Modified residuei20 – 201PhosphoserineBy similarity
Modified residuei31 – 311Phosphoserine1 Publication
Modified residuei112 – 1121Phosphoserine1 Publication
Modified residuei124 – 1241N6-acetyllysine1 Publication

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ13303.
PaxDbiQ13303.
PRIDEiQ13303.

PTM databases

PhosphoSiteiQ13303.

Expressioni

Tissue specificityi

Detected in myelinated nerve fibers in the spinal cord, in the juxtaparanodal region of the nodes of Ranvier, but also in the paranodal region (PubMed:11086297). Detected in hippocampus (at protein level) (PubMed:21357749). Detected in hippocampus (PubMed:7649300).3 Publications

Gene expression databases

BgeeiQ13303.
CleanExiHS_KCNAB2.
HS_KCNK2.
ExpressionAtlasiQ13303. baseline and differential.
GenevestigatoriQ13303.

Organism-specific databases

HPAiCAB001975.
HPA030185.

Interactioni

Subunit structurei

Homotetramer (By similarity). Interaction with tetrameric potassium channel alpha subunits gives rise to a heterooctamer (By similarity). Identified in potassium channel complexes containing KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity). Interacts with KCNA1 (PubMed:11086297). Interacts with KCNA2 (PubMed:11086297). Interacts with KCNA4 and KCND3 (By similarity). Interacts with KCNA5 (By similarity). Interacts with KCNB2 (By similarity). Interacts (in unphosphorylated form) with MAPRE1 (By similarity). Forms a ternary complex with SQSTM1 and PRKCZ (By similarity).By similarity1 Publication

Protein-protein interaction databases

BioGridi114086. 20 interactions.
IntActiQ13303. 1 interaction.
MINTiMINT-2865320.
STRINGi9606.ENSP00000164247.

Structurei

Secondary structure

1
367
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi39 – 424Combined sources
Beta strandi48 – 558Combined sources
Helixi59 – 635Combined sources
Helixi66 – 7813Combined sources
Beta strandi83 – 853Combined sources
Helixi90 – 934Combined sources
Helixi94 – 10613Combined sources
Helixi110 – 1123Combined sources
Beta strandi114 – 1218Combined sources
Helixi126 – 1283Combined sources
Beta strandi129 – 1313Combined sources
Helixi133 – 14715Combined sources
Beta strandi152 – 1598Combined sources
Helixi166 – 17813Combined sources
Beta strandi181 – 1899Combined sources
Helixi192 – 20514Combined sources
Beta strandi212 – 2165Combined sources
Helixi223 – 2264Combined sources
Helixi228 – 2369Combined sources
Beta strandi239 – 2435Combined sources
Helixi247 – 2526Combined sources
Turni253 – 2575Combined sources
Helixi264 – 2663Combined sources
Helixi271 – 2777Combined sources
Helixi280 – 29920Combined sources
Helixi303 – 31311Combined sources
Beta strandi317 – 3226Combined sources
Helixi327 – 3348Combined sources
Helixi336 – 3394Combined sources
Helixi340 – 3423Combined sources
Helixi345 – 35511Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSXX-ray1.90A39-360[»]
ProteinModelPortaliQ13303.
SMRiQ13303. Positions 37-359.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ13303.

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.1 Publication

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiQ13303.
KOiK04883.
OMAiQCKASLA.
PhylomeDBiQ13303.
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.

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q13303-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS
60 70 80 90 100
CLGLGTWVTF GGQITDEMAE QLMTLAYDNG 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
VARQFNLTPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA MTWSPLACGI
260 270 280 290 300
VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
310 320 330 340 350
CTLPQLAIAW CLRNEGVSSV LLGASNADQL MENIGAIQVL PKLSSSIIHE
360
IDSILGNKPY SKKDYRS
Length:367
Mass (Da):41,000
Last modified:January 1, 1998 - v2
Checksum:i91A673F8992140DA
GO
Isoform 2 (identifier: Q13303-2) [UniParc]FASTAAdd to basket

Also known as: KvB2.2

The sequence of this isoform differs from the canonical sequence as follows:
     26-39: Missing.

Show »
Length:353
Mass (Da):39,287
Checksum:i7D59C8203AC5606F
GO
Isoform 3 (identifier: Q13303-3) [UniParc]FASTAAdd to basket

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

Show »
Length:415
Mass (Da):46,527
Checksum:i3AD46E32E4B200AF
GO
Isoform 4 (identifier: Q13303-4) [UniParc]FASTAAdd to basket

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

Show »
Length:300
Mass (Da):33,657
Checksum:i3ADDAAE15216B737
GO
Isoform 5 (identifier: Q13303-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     340-367: LPKLSSSIIHEIDSILGNKPYSKKDYRS → RVRGPAGQRA...GELAFQQEQT

Note: No experimental confirmation available.

Show »
Length:395
Mass (Da):43,560
Checksum:i4E6CED2B3028BBB0
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti88 – 881E → K.
Corresponds to variant rs2229003 [ dbSNP | Ensembl ].
VAR_048747

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 6767Missing in isoform 4. 1 PublicationVSP_044311Add
BLAST
Alternative sequencei1 – 3838MYPES…RQLQF → MLSMTYSESLRSVSSRCHSE WALHPVRQTDTLELQRLREV RAAAQARNMESFLRMHGLSL DGCTAQRTGMK in isoform 3. 1 PublicationVSP_041189Add
BLAST
Alternative sequencei26 – 3914Missing in isoform 2. 1 PublicationVSP_001054Add
BLAST
Alternative sequencei167 – 1671E → EGDPFSSSKSRTFIIE in isoform 3. 1 PublicationVSP_041190
Alternative sequencei340 – 36728LPKLS…KDYRS → RVRGPAGQRAHPSPSPVQCI LPGSSCVPGSVLGTQDAPVN HQSCAPGELAFQQEQT in isoform 5. 1 PublicationVSP_057282Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC110351 mRNA. Translation: AAI10352.1.
BC126424 mRNA. Translation: AAI26425.1.
BC130413 mRNA. Translation: AAI30414.1.
CCDSiCCDS55.1. [Q13303-1]
CCDS55570.1. [Q13303-3]
CCDS55571.1. [Q13303-4]
CCDS56.1. [Q13303-2]
PIRiS66502.
RefSeqiNP_001186789.1. NM_001199860.1. [Q13303-1]
NP_001186790.1. NM_001199861.1. [Q13303-1]
NP_001186791.1. NM_001199862.1. [Q13303-3]
NP_001186792.1. NM_001199863.1. [Q13303-4]
NP_003627.1. NM_003636.3. [Q13303-1]
NP_742128.1. NM_172130.2. [Q13303-2]
XP_005263570.1. XM_005263513.3. [Q13303-5]
XP_005263571.1. XM_005263514.1. [Q13303-2]
UniGeneiHs.440497.
Hs.735032.

Genome annotation databases

EnsembliENST00000164247; 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]
ENST00000602612; ENSP00000473602; ENSG00000069424. [Q13303-5]
GeneIDi8514.
KEGGihsa:8514.
UCSCiuc001alu.3. human.
uc001alv.2. human. [Q13303-1]
uc001alw.2. human. [Q13303-2]
uc001aly.2. human. [Q13303-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
BC110351 mRNA. Translation: AAI10352.1.
BC126424 mRNA. Translation: AAI26425.1.
BC130413 mRNA. Translation: AAI30414.1.
CCDSiCCDS55.1. [Q13303-1]
CCDS55570.1. [Q13303-3]
CCDS55571.1. [Q13303-4]
CCDS56.1. [Q13303-2]
PIRiS66502.
RefSeqiNP_001186789.1. NM_001199860.1. [Q13303-1]
NP_001186790.1. NM_001199861.1. [Q13303-1]
NP_001186791.1. NM_001199862.1. [Q13303-3]
NP_001186792.1. NM_001199863.1. [Q13303-4]
NP_003627.1. NM_003636.3. [Q13303-1]
NP_742128.1. NM_172130.2. [Q13303-2]
XP_005263570.1. XM_005263513.3. [Q13303-5]
XP_005263571.1. XM_005263514.1. [Q13303-2]
UniGeneiHs.440497.
Hs.735032.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZSXX-ray1.90A39-360[»]
ProteinModelPortaliQ13303.
SMRiQ13303. Positions 37-359.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114086. 20 interactions.
IntActiQ13303. 1 interaction.
MINTiMINT-2865320.
STRINGi9606.ENSP00000164247.

PTM databases

PhosphoSiteiQ13303.

Polymorphism and mutation databases

BioMutaiKCNAB2.
DMDMi18202496.

Proteomic databases

MaxQBiQ13303.
PaxDbiQ13303.
PRIDEiQ13303.

Protocols and materials databases

DNASUi8514.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000164247; 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]
ENST00000602612; ENSP00000473602; ENSG00000069424. [Q13303-5]
GeneIDi8514.
KEGGihsa:8514.
UCSCiuc001alu.3. human.
uc001alv.2. human. [Q13303-1]
uc001alw.2. human. [Q13303-2]
uc001aly.2. human. [Q13303-3]

Organism-specific databases

CTDi8514.
GeneCardsiGC01P006020.
HGNCiHGNC:6229. KCNAB2.
HPAiCAB001975.
HPA030185.
MIMi601142. gene.
neXtProtiNX_Q13303.
Orphaneti1606. 1p36 deletion syndrome.
PharmGKBiPA373.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0667.
GeneTreeiENSGT00550000074567.
HOGENOMiHOG000250283.
HOVERGENiHBG052216.
InParanoidiQ13303.
KOiK04883.
OMAiQCKASLA.
PhylomeDBiQ13303.
TreeFamiTF324563.

Enzyme and pathway databases

BioCyciRETL1328306-WGS:GSTH-2009-MONOMER.
ReactomeiREACT_75770. Voltage gated Potassium channels.

Miscellaneous databases

ChiTaRSiKCNAB2. human.
EvolutionaryTraceiQ13303.
GeneWikiiKCNAB2.
GenomeRNAii8514.
NextBioi31868.
PROiQ13303.
SOURCEiSearch...

Gene expression databases

BgeeiQ13303.
CleanExiHS_KCNAB2.
HS_KCNK2.
ExpressionAtlasiQ13303. baseline and differential.
GenevestigatoriQ13303.

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

« Hide 'large scale' publications
  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 SPECIFICITY.
    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] (ISOFORMS 1 AND 5).
    Tissue: Blood and Brain.
  7. "Subunit composition and novel localization of K+ channels in spinal cord."
    Rasband M.N., Trimmer J.S.
    J. Comp. Neurol. 429:166-176(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH KCNA1 AND KCNA2, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Genetic analysis of the mammalian K+ channel beta subunit Kvbeta 2 (Kcnab2)."
    McCormack K., Connor J.X., Zhou L., Ho L.L., Ganetzky B., Chiu S.Y., Messing A.
    J. Biol. Chem. 277:13219-13228(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF TYR-90, FUNCTION.
  9. "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.
  10. "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].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates Kv1 channel axonal targeting."
    Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B., Trimmer J.S.
    J. Cell Biol. 192:813-824(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-31 AND SER-112, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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.

Entry informationi

Entry nameiKCAB2_HUMAN
AccessioniPrimary (citable) accession number: Q13303
Secondary accession number(s): A0AVM9
, A8K1A4, B0AZR7, O43659, Q2YD85, Q5TG82, Q5TG83, Q6ZNE4, Q99411
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: January 1, 1998
Last modified: April 29, 2015
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.