KCAB2_HUMAN
ID KCAB2_HUMAN Reviewed; 367 AA.
AC Q13303; A0AVM9; A8K1A4; B0AZR7; O43659; Q2YD85; Q5TG82; Q5TG83; Q6ZNE4;
AC Q99411;
DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Voltage-gated potassium channel subunit beta-2;
DE EC=1.1.1.- {ECO:0000250|UniProtKB:P62483};
DE AltName: Full=K(+) channel subunit beta-2;
DE AltName: Full=Kv-beta-2;
DE Short=hKvbeta2;
GN Name=KCNAB2; Synonyms=KCNA2B, KCNK2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=7649300; DOI=10.1016/0014-5793(95)00785-8;
RA Mccormack K., McCormack T., Tanouye M.A., Rudy B., Stuehmer W.;
RT "Alternative splicing of the human Shaker K+ channel beta 1 gene and
RT functional expression of the beta 2 gene product.";
RL FEBS Lett. 370:32-36(1995).
RN [2]
RP SEQUENCE REVISION.
RA McCormack K.;
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Amygdala, Brain, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 5).
RC TISSUE=Blood, and Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INTERACTION WITH KCNA1 AND KCNA2, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=11086297;
RX DOI=10.1002/1096-9861(20000101)429:1<166::aid-cne13>3.0.co;2-y;
RA Rasband M.N., Trimmer J.S.;
RT "Subunit composition and novel localization of K+ channels in spinal
RT cord.";
RL J. Comp. Neurol. 429:166-176(2001).
RN [8]
RP MUTAGENESIS OF TYR-90, AND FUNCTION.
RX PubMed=11825900; DOI=10.1074/jbc.m111465200;
RA McCormack K., Connor J.X., Zhou L., Ho L.L., Ganetzky B., Chiu S.Y.,
RA Messing A.;
RT "Genetic analysis of the mammalian K+ channel beta subunit Kvbeta 2
RT (Kcnab2).";
RL J. Biol. Chem. 277:13219-13228(2002).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-124, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, PHOSPHORYLATION AT SER-31 AND SER-112,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21357749; DOI=10.1083/jcb.201007113;
RA Vacher H., Yang J.W., Cerda O., Autillo-Touati A., Dargent B.,
RA Trimmer J.S.;
RT "Cdk-mediated phosphorylation of the Kvbeta2 auxiliary subunit regulates
RT Kv1 channel axonal targeting.";
RL J. Cell Biol. 192:813-824(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9 AND SER-14, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-28, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 36-360 IN COMPLEX WITH NADP.
RG Structural genomics consortium (SGC);
RT "Crystal structure of human potassium channel Kv beta-subunit (KCNAB2).";
RL Submitted (JUN-2005) to the PDB data bank.
CC -!- FUNCTION: Cytoplasmic potassium channel subunit that modulates the
CC characteristics of the channel-forming alpha-subunits (PubMed:7649300,
CC PubMed:11825900). Contributes to the regulation of nerve signaling, and
CC prevents neuronal hyperexcitability (By similarity). Promotes
CC expression of the pore-forming alpha subunits at the cell membrane, and
CC thereby increases channel activity (By similarity). Promotes potassium
CC channel closure via a mechanism that does not involve physical
CC obstruction of the channel pore (PubMed:7649300, PubMed:11825900).
CC Promotes KCNA4 channel closure (PubMed:7649300, PubMed:11825900).
CC Modulates the functional properties of KCNA5 (By similarity). Enhances
CC KCNB2 channel activity (By similarity). Binds NADPH and has NADPH-
CC dependent aldoketoreductase activity (By similarity). Has broad
CC substrate specificity and can catalyze the reduction of methylglyoxal,
CC 9,10-phenanthrenequinone, prostaglandin J2, 4-nitrobenzaldehyde, 4-
CC nitroacetophenone and 4-oxo-trans-2-nonenal (in vitro) (By similarity).
CC {ECO:0000250|UniProtKB:P62482, ECO:0000250|UniProtKB:P62483,
CC ECO:0000269|PubMed:11825900, ECO:0000269|PubMed:7649300}.
CC -!- SUBUNIT: Homotetramer (By similarity). Interaction with tetrameric
CC potassium channel alpha subunits gives rise to a heterooctamer (By
CC similarity). Identified in potassium channel complexes containing
CC KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNAB1 and KCNAB2 (By similarity).
CC Interacts with KCNA1 (PubMed:11086297). Interacts with KCNA2
CC (PubMed:11086297). Interacts with KCNA4 and KCND3 (By similarity).
CC Interacts with KCNA5 (By similarity). Interacts with KCNB2 (By
CC similarity). Interacts (in unphosphorylated form) with MAPRE1 (By
CC similarity). Forms a ternary complex with SQSTM1 and PRKCZ (By
CC similarity). {ECO:0000250|UniProtKB:P62482,
CC ECO:0000250|UniProtKB:P62483, ECO:0000269|PubMed:11086297}.
CC -!- INTERACTION:
CC Q13303; P05067: APP; NbExp=3; IntAct=EBI-948729, EBI-77613;
CC Q13303; P42858: HTT; NbExp=3; IntAct=EBI-948729, EBI-466029;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P62483}.
CC Membrane {ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:21357749};
CC Peripheral membrane protein {ECO:0000305}; Cytoplasmic side
CC {ECO:0000305}. Cell membrane {ECO:0000250|UniProtKB:P62483}; Peripheral
CC membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Cell
CC projection, axon {ECO:0000269|PubMed:11086297}. Synapse, synaptosome
CC {ECO:0000269|PubMed:21357749}. Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:P62483}. Note=Recruited to the cytoplasmic side
CC of the cell membrane via its interaction with pore-forming potassium
CC channel alpha subunits. Associates with microtubules when
CC unphosphorylated. {ECO:0000250|UniProtKB:P62483}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1; Synonyms=KvB2.1;
CC IsoId=Q13303-1; Sequence=Displayed;
CC Name=2; Synonyms=KvB2.2;
CC IsoId=Q13303-2; Sequence=VSP_001054;
CC Name=3;
CC IsoId=Q13303-3; Sequence=VSP_041189, VSP_041190;
CC Name=4;
CC IsoId=Q13303-4; Sequence=VSP_044311;
CC Name=5;
CC IsoId=Q13303-5; Sequence=VSP_057282;
CC -!- TISSUE SPECIFICITY: Detected in myelinated nerve fibers in the spinal
CC cord, in the juxtaparanodal region of the nodes of Ranvier, but also in
CC the paranodal region (PubMed:11086297). Detected in hippocampus (at
CC protein level) (PubMed:21357749). Detected in hippocampus
CC (PubMed:7649300). {ECO:0000269|PubMed:11086297,
CC ECO:0000269|PubMed:21357749, ECO:0000269|PubMed:7649300}.
CC -!- DOMAIN: In contrast to KCNAB1, the shorter N-terminal domain of KCNAB2
CC cannot mediate closure of delayed rectifier potassium channels by
CC physically obstructing the pore. {ECO:0000269|PubMed:7649300}.
CC -!- PTM: Phosphorylated by PRKCZ; may be regulated by incorporation in a
CC complex composed of PRKCZ and SQSTM1. {ECO:0000250|UniProtKB:P62483}.
CC -!- SIMILARITY: Belongs to the shaker potassium channel beta subunit
CC family. {ECO:0000305}.
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DR EMBL; U33429; AAC50955.1; -; mRNA.
DR EMBL; AF029749; AAB84170.1; -; mRNA.
DR EMBL; AF044253; AAB99859.1; -; mRNA.
DR EMBL; AK124696; BAG54071.1; -; mRNA.
DR EMBL; AK131252; BAD18431.1; -; mRNA.
DR EMBL; AK289819; BAF82508.1; -; mRNA.
DR EMBL; AK315858; BAF98749.1; -; mRNA.
DR EMBL; AL035406; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC110351; AAI10352.1; -; mRNA.
DR EMBL; BC126424; AAI26425.1; -; mRNA.
DR EMBL; BC130413; AAI30414.1; -; mRNA.
DR CCDS; CCDS55.1; -. [Q13303-1]
DR CCDS; CCDS55570.1; -. [Q13303-3]
DR CCDS; CCDS55571.1; -. [Q13303-4]
DR CCDS; CCDS56.1; -. [Q13303-2]
DR PIR; S66502; S66502.
DR RefSeq; NP_001186789.1; NM_001199860.1. [Q13303-1]
DR RefSeq; NP_001186790.1; NM_001199861.1. [Q13303-1]
DR RefSeq; NP_001186791.1; NM_001199862.1. [Q13303-3]
DR RefSeq; NP_001186792.1; NM_001199863.1. [Q13303-4]
DR RefSeq; NP_003627.1; NM_003636.3. [Q13303-1]
DR RefSeq; NP_742128.1; NM_172130.2. [Q13303-2]
DR RefSeq; XP_005263571.1; XM_005263514.2. [Q13303-2]
DR RefSeq; XP_011540623.1; XM_011542321.2. [Q13303-5]
DR RefSeq; XP_011540624.1; XM_011542322.2. [Q13303-5]
DR PDB; 1ZSX; X-ray; 1.90 A; A=39-360.
DR PDB; 7EJ1; EM; 3.20 A; A/C/E/G=1-367.
DR PDB; 7EJ2; EM; 3.30 A; A/C/E/G=1-367.
DR PDB; 7WF3; EM; 3.40 A; C/G/I/M=34-361.
DR PDB; 7WF4; EM; 3.40 A; G/I/M/o=34-361.
DR PDBsum; 1ZSX; -.
DR PDBsum; 7EJ1; -.
DR PDBsum; 7EJ2; -.
DR PDBsum; 7WF3; -.
DR PDBsum; 7WF4; -.
DR AlphaFoldDB; Q13303; -.
DR SMR; Q13303; -.
DR BioGRID; 114086; 163.
DR CORUM; Q13303; -.
DR IntAct; Q13303; 26.
DR STRING; 9606.ENSP00000367323; -.
DR DrugBank; DB00228; Enflurane.
DR DrugBank; DB01110; Miconazole.
DR DrugBank; DB01069; Promethazine.
DR iPTMnet; Q13303; -.
DR PhosphoSitePlus; Q13303; -.
DR BioMuta; KCNAB2; -.
DR DMDM; 18202496; -.
DR EPD; Q13303; -.
DR jPOST; Q13303; -.
DR MassIVE; Q13303; -.
DR MaxQB; Q13303; -.
DR PaxDb; Q13303; -.
DR PeptideAtlas; Q13303; -.
DR PRIDE; Q13303; -.
DR ProteomicsDB; 2532; -.
DR ProteomicsDB; 59288; -. [Q13303-1]
DR ProteomicsDB; 59289; -. [Q13303-2]
DR ProteomicsDB; 59290; -. [Q13303-3]
DR ABCD; Q13303; 3 sequenced antibodies.
DR Antibodypedia; 4538; 165 antibodies from 23 providers.
DR DNASU; 8514; -.
DR Ensembl; ENST00000164247.5; ENSP00000164247.1; ENSG00000069424.16. [Q13303-1]
DR Ensembl; ENST00000352527.6; ENSP00000318772.1; ENSG00000069424.16. [Q13303-2]
DR Ensembl; ENST00000378083.8; ENSP00000367323.3; ENSG00000069424.16. [Q13303-3]
DR Ensembl; ENST00000378092.6; ENSP00000367332.2; ENSG00000069424.16. [Q13303-1]
DR Ensembl; ENST00000378097.6; ENSP00000367337.1; ENSG00000069424.16. [Q13303-1]
DR Ensembl; ENST00000428161.6; ENSP00000400285.2; ENSG00000069424.16. [Q13303-1]
DR Ensembl; ENST00000458166.6; ENSP00000396167.2; ENSG00000069424.16. [Q13303-4]
DR Ensembl; ENST00000602612.5; ENSP00000473602.1; ENSG00000069424.16. [Q13303-5]
DR Ensembl; ENST00000666163.1; ENSP00000499370.1; ENSG00000069424.16. [Q13303-2]
DR Ensembl; ENST00000668559.1; ENSP00000499361.1; ENSG00000069424.16. [Q13303-5]
DR Ensembl; ENST00000669250.1; ENSP00000499485.1; ENSG00000069424.16. [Q13303-2]
DR Ensembl; ENST00000671676.1; ENSP00000499496.1; ENSG00000069424.16. [Q13303-1]
DR GeneID; 8514; -.
DR KEGG; hsa:8514; -.
DR MANE-Select; ENST00000378083.8; ENSP00000367323.3; NM_001199862.2; NP_001186791.1. [Q13303-3]
DR UCSC; uc001alv.3; human. [Q13303-1]
DR CTD; 8514; -.
DR DisGeNET; 8514; -.
DR GeneCards; KCNAB2; -.
DR HGNC; HGNC:6229; KCNAB2.
DR HPA; ENSG00000069424; Tissue enhanced (brain).
DR MalaCards; KCNAB2; -.
DR MIM; 601142; gene.
DR neXtProt; NX_Q13303; -.
DR OpenTargets; ENSG00000069424; -.
DR Orphanet; 1606; 1p36 deletion syndrome.
DR PharmGKB; PA373; -.
DR VEuPathDB; HostDB:ENSG00000069424; -.
DR eggNOG; KOG1575; Eukaryota.
DR GeneTree; ENSGT00940000157867; -.
DR InParanoid; Q13303; -.
DR OMA; PPYSLFW; -.
DR OrthoDB; 633642at2759; -.
DR PhylomeDB; Q13303; -.
DR TreeFam; TF324563; -.
DR PathwayCommons; Q13303; -.
DR Reactome; R-HSA-1296072; Voltage gated Potassium channels.
DR Reactome; R-HSA-6798695; Neutrophil degranulation.
DR SignaLink; Q13303; -.
DR BioGRID-ORCS; 8514; 7 hits in 1078 CRISPR screens.
DR ChiTaRS; KCNAB2; human.
DR EvolutionaryTrace; Q13303; -.
DR GeneWiki; KCNAB2; -.
DR GenomeRNAi; 8514; -.
DR Pharos; Q13303; Tbio.
DR PRO; PR:Q13303; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q13303; protein.
DR Bgee; ENSG00000069424; Expressed in Brodmann (1909) area 10 and 167 other tissues.
DR ExpressionAtlas; Q13303; baseline and differential.
DR Genevisible; Q13303; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; ISS:UniProtKB.
DR GO; GO:0044224; C:juxtaparanode region of axon; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:1990031; C:pinceau fiber; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0035579; C:specific granule membrane; TAS:Reactome.
DR GO; GO:0045202; C:synapse; IEA:UniProtKB-SubCell.
DR GO; GO:0070821; C:tertiary granule membrane; TAS:Reactome.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
DR GO; GO:0004033; F:aldo-keto reductase (NADP) activity; ISS:UniProtKB.
DR GO; GO:0015459; F:potassium channel regulator activity; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0005249; F:voltage-gated potassium channel activity; IEA:InterPro.
DR GO; GO:0070995; P:NADPH oxidation; ISS:UniProtKB.
DR GO; GO:0098900; P:regulation of action potential; IBA:GO_Central.
DR GO; GO:1901379; P:regulation of potassium ion transmembrane transport; IDA:UniProtKB.
DR GO; GO:2000008; P:regulation of protein localization to cell surface; ISS:UniProtKB.
DR Gene3D; 3.20.20.100; -; 1.
DR InterPro; IPR005983; K_chnl_volt-dep_bsu_KCNAB.
DR InterPro; IPR005399; K_chnl_volt-dep_bsu_KCNAB-rel.
DR InterPro; IPR005401; K_chnl_volt-dep_bsu_KCNAB2.
DR InterPro; IPR023210; NADP_OxRdtase_dom.
DR InterPro; IPR036812; NADP_OxRdtase_dom_sf.
DR PANTHER; PTHR43150; PTHR43150; 1.
DR Pfam; PF00248; Aldo_ket_red; 1.
DR PRINTS; PR01579; KCNAB2CHANEL.
DR PRINTS; PR01577; KCNABCHANNEL.
DR SUPFAM; SSF51430; SSF51430; 1.
DR TIGRFAMs; TIGR01293; Kv_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Ion channel; Ion transport;
KW Membrane; Methylation; NADP; Oxidoreductase; Phosphoprotein; Potassium;
KW Potassium transport; Reference proteome; Synapse; Synaptosome; Transport;
KW Voltage-gated channel.
FT CHAIN 1..367
FT /note="Voltage-gated potassium channel subunit beta-2"
FT /id="PRO_0000148746"
FT ACT_SITE 90
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:P62483"
FT BINDING 56..57
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 63
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 85
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 90
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 188..189
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 214
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 243..248
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 254
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT BINDING 323..329
FT /ligand="NADP(+)"
FT /ligand_id="ChEBI:CHEBI:58349"
FT /evidence="ECO:0000269|Ref.17"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P62482"
FT MOD_RES 28
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 28
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P62482"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21357749"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:21357749"
FT MOD_RES 124
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..67
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044311"
FT VAR_SEQ 1..38
FT /note="MYPESTTGSPARLSLRQTGSPGMIYSTRYGSPKRQLQF -> MLSMTYSESL
FT RSVSSRCHSEWALHPVRQTDTLELQRLREVRAAAQARNMESFLRMHGLSLDGCTAQRTG
FT MK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041189"
FT VAR_SEQ 26..39
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_001054"
FT VAR_SEQ 167
FT /note="E -> EGDPFSSSKSRTFIIE (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_041190"
FT VAR_SEQ 340..367
FT /note="LPKLSSSIIHEIDSILGNKPYSKKDYRS -> RVRGPAGQRAHPSPSPVQCI
FT LPGSSCVPGSVLGTQDAPVNHQSCAPGELAFQQEQT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_057282"
FT MUTAGEN 90
FT /note="Y->F: No effect on its activity in promoting KCNA4
FT channel closure."
FT /evidence="ECO:0000269|PubMed:11825900"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 48..55
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 59..63
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 66..78
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 94..106
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 110..112
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 114..121
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 126..128
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 129..131
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 133..147
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 152..159
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 162..164
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 166..178
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 181..189
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 192..205
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 218..220
FT /evidence="ECO:0007829|PDB:7EJ2"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 228..236
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 247..252
FT /evidence="ECO:0007829|PDB:1ZSX"
FT TURN 253..257
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 267..269
FT /evidence="ECO:0007829|PDB:7EJ1"
FT HELIX 271..277
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 280..299
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 303..313
FT /evidence="ECO:0007829|PDB:1ZSX"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:7EJ1"
FT STRAND 317..322
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 327..334
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 336..339
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:1ZSX"
FT HELIX 345..355
FT /evidence="ECO:0007829|PDB:1ZSX"
SQ SEQUENCE 367 AA; 41000 MW; 91A673F8992140DA CRC64;
MYPESTTGSP ARLSLRQTGS PGMIYSTRYG SPKRQLQFYR NLGKSGLRVS CLGLGTWVTF
GGQITDEMAE QLMTLAYDNG INLFDTAEVY AAGKAEVVLG NIIKKKGWRR SSLVITTKIF
WGGKAETERG LSRKHIIEGL KASLERLQLE YVDVVFANRP DPNTPMEETV RAMTHVINQG
MAMYWGTSRW SSMEIMEAYS VARQFNLTPP ICEQAEYHMF QREKVEVQLP ELFHKIGVGA
MTWSPLACGI VSGKYDSGIP PYSRASLKGY QWLKDKILSE EGRRQQAKLK ELQAIAERLG
CTLPQLAIAW CLRNEGVSSV LLGASNADQL MENIGAIQVL PKLSSSIIHE IDSILGNKPY
SKKDYRS
