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Potassium voltage-gated channel subfamily A member 2 (NGK1) (Voltage-gated K( ) channel HuKIV) (Voltage-gated potassium channel HBK5) (Voltage-gated potassium channel subunit Kv1.2)

 KCNA2_HUMAN             Reviewed;         499 AA.
P16389; A0A024R0D3; A8K1Z6; Q86XG6;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
01-FEB-1996, sequence version 2.
23-FEB-2022, entry version 206.
RecName: Full=Potassium voltage-gated channel subfamily A member 2;
AltName: Full=NGK1;
AltName: Full=Voltage-gated K(+) channel HuKIV {ECO:0000303|PubMed:19912772};
AltName: Full=Voltage-gated potassium channel HBK5;
AltName: Full=Voltage-gated potassium channel subunit Kv1.2;
Name=KCNA2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Brain;
PubMed=19912772; DOI=10.1016/1044-7431(90)90004-n;
Ramaswami M., Gautam M., Kamb A., Rudy B., Tanouye M.A., Mathew M.K.;
"Human potassium channel genes: molecular cloning and functional
expression.";
Mol. Cell. Neurosci. 1:214-223(1990).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Substantia nigra {ECO:0000312|EMBL:BAF82750.1};
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Blood;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KCNA4.
PubMed=8495559; DOI=10.1161/01.res.72.6.1326;
Po S., Roberds S., Snyders D.J., Tamkun M.M., Bennett P.B.;
"Heteromultimeric assembly of human potassium channels. Molecular basis of
a transient outward current?";
Circ. Res. 72:1326-1336(1993).
[7]
INTERACTION WITH CNTNAP2.
PubMed=10624965; DOI=10.1016/s0896-6273(00)81049-1;
Poliak S., Gollan L., Martinez R., Custer A., Einheber S., Salzer J.L.,
Trimmer J.S., Shrager P., Peles E.;
"Caspr2, a new member of the neurexin superfamily, is localized at the
juxtaparanodes of myelinated axons and associates with K+ channels.";
Neuron 24:1037-1047(1999).
[8]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=11211111; DOI=10.1007/s004240000406;
Imbrici P., Tucker S.J., D'Adamo M.C., Pessia M.;
"Role of receptor protein tyrosine phosphatase alpha (RPTPalpha) and
tyrosine phosphorylation in the serotonergic inhibition of voltage-
dependent potassium channels.";
Pflugers Arch. 441:257-262(2000).
[9]
SUBCELLULAR LOCATION, INTERACTION WITH KCNA1 AND KCNAB2, SUBUNIT, AND
TISSUE SPECIFICITY.
PubMed=11086297;
DOI=10.1002/1096-9861(20000101)429:1<166::aid-cne13>3.0.co;2-y;
Rasband M.N., Trimmer J.S.;
"Subunit composition and novel localization of K+ channels in spinal
cord.";
J. Comp. Neurol. 429:166-176(2001).
[10]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=16473933; DOI=10.1073/pnas.0511197103;
Inda M.C., DeFelipe J., Munoz A.;
"Voltage-gated ion channels in the axon initial segment of human cortical
pyramidal cells and their relationship with chandelier cells.";
Proc. Natl. Acad. Sci. U.S.A. 103:2920-2925(2006).
[11]
REVIEW.
PubMed=17917103; DOI=10.1007/s12035-007-8001-0;
Baranauskas G.;
"Ionic channel function in action potential generation: current
perspective.";
Mol. Neurobiol. 35:129-150(2007).
[12]
INTERACTION WITH KCNAB1.
PubMed=19713757; DOI=10.4161/chan.3.5.9558;
Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.;
"The molecular basis for the actions of Kvbeta1.2 on the opening and
closing of the Kv1.2 delayed rectifier channel.";
Channels 3:314-322(2009).
[13]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND ACTIVITY REGULATION.
PubMed=20220134; DOI=10.1074/jbc.m109.068486;
Chen P., Dendorfer A., Finol-Urdaneta R.K., Terlau H., Olivera B.M.;
"Biochemical characterization of kappaM-RIIIJ, a Kv1.2 channel blocker:
evaluation of cardioprotective effects of kappaM-conotoxins.";
J. Biol. Chem. 285:14882-14889(2010).
[14]
TISSUE SPECIFICITY.
PubMed=22649228; DOI=10.1523/jneurosci.0719-12.2012;
Zenker J., Poirot O., de Preux Charles A.S., Arnaud E., Medard J.J.,
Lacroix C., Kuntzer T., Chrast R.;
"Altered distribution of juxtaparanodal kv1.2 subunits mediates peripheral
nerve hyperexcitability in type 2 diabetes mellitus.";
J. Neurosci. 32:7493-7498(2012).
[15]
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=23769686; DOI=10.1016/j.neulet.2013.05.048;
Lee J.H., Choi S.H., Lee B.H., Hwang S.H., Kim H.J., Rhee J., Chung C.,
Nah S.Y.;
"Activation of lysophosphatidic acid receptor by gintonin inhibits Kv1.2
channel activity: involvement of tyrosine kinase and receptor protein
tyrosine phosphatase alpha.";
Neurosci. Lett. 548:143-148(2013).
[16]
INVOLVEMENT IN DEE32, AND VARIANT DEE32 GLN-297.
PubMed=25477152; DOI=10.1111/cge.12542;
Pena S.D., Coimbra R.L.;
"Ataxia and myoclonic epilepsy due to a heterozygous new mutation in KCNA2:
proposal for a new channelopathy.";
Clin. Genet. 87:E1-E3(2015).
[17]
INVOLVEMENT IN DEE32, VARIANTS DEE32 THR-263; GLN-297; PHE-298 AND LEU-405,
AND CHARACTERIZATION OF VARIANTS DEE32 THR-263; GLN-297; PHE-298 AND
LEU-405.
PubMed=25751627; DOI=10.1038/ng.3239;
Syrbe S., Hedrich U.B., Riesch E., Djemie T., Mueller S., Moeller R.S.,
Maher B., Hernandez-Hernandez L., Synofzik M., Caglayan H.S., Arslan M.,
Serratosa J.M., Nothnagel M., May P., Krause R., Loeffler H., Detert K.,
Dorn T., Vogt H., Kraemer G., Schoels L., Mullis P.E., Linnankivi T.,
Lehesjoki A.E., Sterbova K., Craiu D.C., Hoffman-Zacharska D., Korff C.M.,
Weber Y.G., Steinlin M., Gallati S., Bertsche A., Bernhard M.K.,
Merkenschlager A., Kiess W., Gonzalez M., Zuechner S., Palotie A., Suls A.,
De Jonghe P., Helbig I., Biskup S., Wolff M., Maljevic S., Schuele R.,
Sisodiya S.M., Weckhuysen S., Lerche H., Lemke J.R.;
"De novo loss- or gain-of-function mutations in KCNA2 cause epileptic
encephalopathy.";
Nat. Genet. 47:393-399(2015).
[18]
VARIANT THR-324.
PubMed=27864847; DOI=10.1002/humu.23149;
Clinical Study Group;
Parrini E., Marini C., Mei D., Galuppi A., Cellini E., Pucatti D.,
Chiti L., Rutigliano D., Bianchini C., Virdo S., De Vita D., Bigoni S.,
Barba C., Mari F., Montomoli M., Pisano T., Rosati A., Guerrini R.;
"Diagnostic targeted resequencing in 349 patients with drug-resistant
pediatric epilepsies identifies causative mutations in 30 different
genes.";
Hum. Mutat. 38:216-225(2017).
[19]
VARIANT DEE32 LYS-236, AND CHARACTERIZATION OF VARIANT DEE32 LYS-236.
PubMed=34576077; DOI=10.3390/ijms22189913;
Imbrici P., Conte E., Blunck R., Stregapede F., Liantonio A., Tosi M.,
D'Adamo M.C., De Luca A., Brankovic V., Zanni G.;
"A novel KCNA2 variant in a patient with non-progressive congenital ataxia
and epilepsy: functional characterization and sensitivity to 4-
aminopyridine.";
Int. J. Mol. Sci. 22:0-0(2021).
-!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
potassium transport in excitable membranes, primarily in the brain and
the central nervous system, but also in the cardiovascular system.
Prevents aberrant action potential firing and regulates neuronal
output. Forms tetrameric potassium-selective channels through which
potassium ions pass in accordance with their electrochemical gradient.
The channel alternates between opened and closed conformations in
response to the voltage difference across the membrane
(PubMed:19912772, PubMed:8495559, PubMed:11211111, PubMed:23769686).
Can form functional homotetrameric channels and heterotetrameric
channels that contain variable proportions of KCNA1, KCNA2, KCNA4,
KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel
properties depend on the type of alpha subunits that are part of the
channel (PubMed:8495559, PubMed:20220134). Channel properties are
modulated by cytoplasmic beta subunits that regulate the subcellular
location of the alpha subunits and promote rapid inactivation of
delayed rectifier potassium channels. In vivo, membranes probably
contain a mixture of heteromeric potassium channel complexes, making it
difficult to assign currents observed in intact tissues to any
particular potassium channel family member. Homotetrameric KCNA2 forms
a delayed-rectifier potassium channel that opens in response to
membrane depolarization, followed by slow spontaneous channel closure
(PubMed:19912772, PubMed:23769686). In contrast, a heteromultimer
formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559).
Regulates neuronal excitability and plays a role as pacemaker in the
regulation of neuronal action potentials (By similarity). KCNA2-
containing channels play a presynaptic role and prevent
hyperexcitability and aberrant action potential firing (By similarity).
Response to toxins that are selective for KCNA2-containing potassium
channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-
containing potassium channels prevent random spontaneous calcium
spikes, suppressing dendritic hyperexcitability without hindering the
generation of somatic action potentials, and thereby play an important
role in motor coordination (By similarity). Plays a role in the
induction of long-term potentiation of neuron excitability in the CA3
layer of the hippocampus (By similarity). May function as down-stream
effector for G protein-coupled receptors and inhibit GABAergic inputs
to basolateral amygdala neurons (By similarity). May contribute to the
regulation of neurotransmitter release, such as gamma-aminobutyric acid
(GABA) (By similarity). Contributes to the regulation of the axonal
release of the neurotransmitter dopamine (By similarity). Reduced KCNA2
expression plays a role in the perception of neuropathic pain after
peripheral nerve injury, but not acute pain (By similarity). Plays a
role in the regulation of the time spent in non-rapid eye movement
(NREM) sleep (By similarity). {ECO:0000250|UniProtKB:P63141,
ECO:0000250|UniProtKB:P63142, ECO:0000269|PubMed:11211111,
ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:20220134,
ECO:0000269|PubMed:23769686, ECO:0000269|PubMed:8495559, ECO:0000305}.
-!- ACTIVITY REGULATION: Inhibited by 4-aminopyridine (4-AP) and
charybdotoxin (CTX), but not by tetraethylammonium (TEA)
(PubMed:19912772). Inhibited by dendrotoxin (DTX) (By similarity).
Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly
specific for KCNA2 (By similarity). Inhibited by maurotoxin (By
similarity). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-
RIIIK; kappaM-RIIIJ has much higher affinity for channels containing
KCNA2 than kappaM-RIIIK, with the exception of heterodimers formed by
KCNA2 and KCNA7 where the opposite is true (PubMed:20220134).
{ECO:0000250|UniProtKB:P63141, ECO:0000250|UniProtKB:P63142,
ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:20220134}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels activate rapidly, i.e within a few msec,
but inactivation is very slow, with only a marginal decrease in
conductance over several seconds. The voltage-dependence of
activation and inactivation and other channel characteristics vary
depending on the experimental conditions, the expression system,
post-translational modifications and the presence or absence of
ancillary subunits. For the activation of homotetrameric channels
expressed in xenopus oocytes, the threshold is at about -30 mV and
the midpoint at about -5 mV. {ECO:0000269|PubMed:19912772};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-forming
alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and KCNA7. Channel
activity is regulated by interaction with the beta subunits, including
KCNAB1 and KCNAB2. Identified in a complex with KCNA1 and KCNAB2
(PubMed:11086297). Identified in a complex with KCNA5 and KCNAB1 (By
similarity). Identified in a complex with KCNA4 and FYN (By
similarity). Interacts with the beta subunit KCNAB1 (PubMed:19713757).
Interacts with PTK2B (By similarity). Interacts (via C-terminus) with
CTTN (By similarity). Interacts (via N-terminal cytoplasmic domain)
with RHOA (GTP-bound form); this regulates channel activity by reducing
location at the cell surface in response to CHRM1 activation (By
similarity). Interacts with DRD2 (By similarity). Interacts with
SIGMAR1; cocaine consumption leads to increased interaction (By
similarity). Interacts with ADAM22 (By similarity). Interacts (via C-
terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity).
Interacts with CNTNAP2 (PubMed:10624965).
{ECO:0000250|UniProtKB:P63141, ECO:0000250|UniProtKB:P63142,
ECO:0000250|UniProtKB:Q09081, ECO:0000269|PubMed:10624965,
ECO:0000269|PubMed:11086297, ECO:0000269|PubMed:19713757,
ECO:0000269|PubMed:8495559, ECO:0000305}.
-!- INTERACTION:
P16389; P49069: CAMLG; NbExp=3; IntAct=EBI-10210559, EBI-1748958;
P16389-2; P49069: CAMLG; NbExp=3; IntAct=EBI-11987131, EBI-1748958;
P16389-2; Q92520: FAM3C; NbExp=3; IntAct=EBI-11987131, EBI-2876774;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11211111,
ECO:0000269|PubMed:19912772, ECO:0000269|PubMed:20220134,
ECO:0000269|PubMed:23769686, ECO:0000269|PubMed:8495559}; Multi-pass
membrane protein {ECO:0000250|UniProtKB:P63142, ECO:0000305}. Membrane
{ECO:0000250|UniProtKB:P63142}. Cell projection, axon
{ECO:0000269|PubMed:16473933}. Cell junction, synapse
{ECO:0000250|UniProtKB:P63142}. Endoplasmic reticulum membrane
{ECO:0000250|UniProtKB:P63142}. Cell projection, lamellipodium membrane
{ECO:0000250|UniProtKB:P63142}. Cell junction, synapse, synaptosome
{ECO:0000250|UniProtKB:P63141}. Cell junction, synapse, presynaptic
cell membrane {ECO:0000250|UniProtKB:P63141}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P63141}. Cell junction, paranodal septate
junction {ECO:0000250|UniProtKB:P63141}. Note=KCNA2 by itself is
detected both at the endoplasmic reticulum and at the cell membrane.
Coexpression with KCNA4 or with beta subunits promotes expression at
the cell membrane. Coexpression with KCNA1 inhibits cell surface
expression. In myelinated peripheral axons, clustered in the
juxtaparadonal region and at an internodal line located along the
mesaxon and below the Schmidt-Lanterman incisures (By similarity).
{ECO:0000250|UniProtKB:P63141, ECO:0000250|UniProtKB:P63142}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P16389-1; Sequence=Displayed;
Name=2;
IsoId=P16389-2; Sequence=VSP_043077;
-!- TISSUE SPECIFICITY: Detected in brain cortex (PubMed:16473933).
Detected in peroneal nerve in the juxtaparanodal regions of the node of
Ranvier; expression is decreased in patients with diabetes mellitus
that suffer from axonal neuropathy (PubMed:22649228). Detected in
paranodal and juxtanodal zones in myelinated spinal cord (at protein
level) (PubMed:11086297). {ECO:0000269|PubMed:11086297,
ECO:0000269|PubMed:16473933, ECO:0000269|PubMed:22649228}.
-!- DOMAIN: The cytoplasmic N-terminus is important for tetramerization.
Interactions between the different subunits modulate the gating
characteristics (By similarity). Besides, the cytoplasmic N-terminal
domain mediates interaction with RHOA and thus is required for RHOA-
mediated endocytosis (By similarity). {ECO:0000250|UniProtKB:P63142}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor and is
characterized by a series of positively charged amino acids at every
third position. Channel opening and closing is effected by a
conformation change that affects the position and orientation of the
voltage-sensor paddle formed by S3 and S4 within the membrane. A
transmembrane electric field that is positive inside would push the
positively charged S4 segment outwards, thereby opening the pore, while
a field that is negative inside would pull the S4 segment inwards and
close the pore. Changes in the position and orientation of S4 are then
transmitted to the activation gate formed by the inner helix bundle via
the S4-S5 linker region. {ECO:0000250|UniProtKB:P63142}.
-!- PTM: Phosphorylated on tyrosine residues; phosphorylation increases in
response to ischemia (By similarity). Phosphorylated on tyrosine
residues by activated PTK2B/PYK2 (By similarity). Phosphorylation on
tyrosine residues suppresses ion channel activity (By similarity).
Phosphorylated on tyrosine residues in response to CHRM1 activation;
this abolishes interaction with CTTN. This is probably due to
endocytosis of the phosphorylated channel subunits (By similarity).
Phosphorylated on serine residues in response to increased cAMP levels;
phosphorylation is apparently not catalyzed by PKA (By similarity).
{ECO:0000250|UniProtKB:P63142}.
-!- PTM: N-glycosylated, with complex, sialylated N-glycans.
{ECO:0000250|UniProtKB:P63142}.
-!- DISEASE: Developmental and epileptic encephalopathy 32 (DEE32)
[MIM:616366]: A form of epileptic encephalopathy, a heterogeneous group
of severe early-onset epilepsies characterized by refractory seizures,
neurodevelopmental impairment, and poor prognosis. Development is
normal prior to seizure onset, after which cognitive and motor delays
become apparent. DEE32 inheritance is autosomal dominant.
{ECO:0000269|PubMed:25477152, ECO:0000269|PubMed:25751627,
ECO:0000269|PubMed:34576077}. Note=The disease is caused by variants
affecting the gene represented in this entry.
-!- MISCELLANEOUS: The delay or D-type current observed in hippocampus
pyramidal neurons is probably mediated by potassium channels containing
KCNA2 plus KCNA1 or other family members. It is activated at about -50
mV, i.e. below the action potential threshold, and is characterized by
slow inactivation, extremely slow recovery from inactivation,
sensitivity to dendrotoxin (DTX) and to 4-aminopyridine (4-AP).
{ECO:0000305|PubMed:17917103}.
-!- SIMILARITY: Belongs to the potassium channel family. A (Shaker) (TC
1.A.1.2) subfamily. Kv1.2/KCNA2 sub-subfamily. {ECO:0000305}.
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; L02752; AAA36141.1; -; mRNA.
EMBL; AK290061; BAF82750.1; -; mRNA.
EMBL; AL365361; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471122; EAW56455.1; -; Genomic_DNA.
EMBL; CH471122; EAW56456.1; -; Genomic_DNA.
EMBL; BC043564; AAH43564.1; -; mRNA.
CCDS; CCDS55625.1; -. [P16389-2]
CCDS; CCDS827.1; -. [P16389-1]
PIR; I77466; I77466.
RefSeq; NP_001191198.1; NM_001204269.1. [P16389-2]
RefSeq; NP_004965.1; NM_004974.3. [P16389-1]
RefSeq; XP_011539698.1; XM_011541396.2. [P16389-1]
RefSeq; XP_011539699.1; XM_011541397.2. [P16389-1]
RefSeq; XP_011539700.1; XM_011541398.2. [P16389-1]
RefSeq; XP_011539701.1; XM_011541399.2. [P16389-1]
RefSeq; XP_011539702.1; XM_011541400.2. [P16389-1]
RefSeq; XP_016856702.1; XM_017001213.1. [P16389-1]
SMR; P16389; -.
BioGRID; 109940; 116.
CORUM; P16389; -.
IntAct; P16389; 3.
STRING; 9606.ENSP00000433109; -.
BindingDB; P16389; -.
ChEMBL; CHEMBL2086; -.
DrugBank; DB06637; Dalfampridine.
DrugBank; DB00228; Enflurane.
DrugBank; DB01110; Miconazole.
DrugBank; DB01069; Promethazine.
DrugCentral; P16389; -.
GuidetoPHARMACOLOGY; 539; -.
TCDB; 1.A.1.2.10; the voltage-gated ion channel (vic) superfamily.
GlyGen; P16389; 1 site.
iPTMnet; P16389; -.
PhosphoSitePlus; P16389; -.
BioMuta; KCNA2; -.
DMDM; 1345813; -.
jPOST; P16389; -.
MassIVE; P16389; -.
MaxQB; P16389; -.
PaxDb; P16389; -.
PeptideAtlas; P16389; -.
PRIDE; P16389; -.
ProteomicsDB; 53349; -. [P16389-1]
ProteomicsDB; 53350; -. [P16389-2]
ABCD; P16389; 3 sequenced antibodies.
Antibodypedia; 4539; 288 antibodies from 31 providers.
DNASU; 3737; -.
Ensembl; ENST00000316361; ENSP00000314520; ENSG00000177301.
Ensembl; ENST00000369770; ENSP00000358785; ENSG00000177301. [P16389-2]
Ensembl; ENST00000485317; ENSP00000433109; ENSG00000177301.
Ensembl; ENST00000633222; ENSP00000487785; ENSG00000177301.
Ensembl; ENST00000638532; ENSP00000491613; ENSG00000177301.
Ensembl; ENST00000638616; ENSP00000491977; ENSG00000177301.
Ensembl; ENST00000675391; ENSP00000502642; ENSG00000177301.
GeneID; 3737; -.
KEGG; hsa:3737; -.
MANE-Select; ENST00000316361.10; ENSP00000314520.4; NM_004974.4; NP_004965.1.
UCSC; uc009wfv.2; human. [P16389-1]
CTD; 3737; -.
DisGeNET; 3737; -.
GeneCards; KCNA2; -.
HGNC; HGNC:6220; KCNA2.
HPA; ENSG00000177301; Tissue enriched (brain).
MalaCards; KCNA2; -.
MIM; 176262; gene.
MIM; 616366; phenotype.
neXtProt; NX_P16389; -.
OpenTargets; ENSG00000177301; -.
Orphanet; 442835; Non-specific early-onset epileptic encephalopathy.
PharmGKB; PA206; -.
VEuPathDB; HostDB:ENSG00000177301; -.
eggNOG; KOG1545; Eukaryota.
GeneTree; ENSGT00940000158688; -.
InParanoid; P16389; -.
OMA; PIFRNDE; -.
OrthoDB; 695337at2759; -.
PhylomeDB; P16389; -.
TreeFam; TF313103; -.
PathwayCommons; P16389; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
SignaLink; P16389; -.
BioGRID-ORCS; 3737; 11 hits in 1031 CRISPR screens.
ChiTaRS; KCNA2; human.
GeneWiki; KCNA2; -.
GenomeRNAi; 3737; -.
Pharos; P16389; Tclin.
PRO; PR:P16389; -.
Proteomes; UP000005640; Chromosome 1.
RNAct; P16389; protein.
Bgee; ENSG00000177301; Expressed in cerebellar vermis and 148 other tissues.
ExpressionAtlas; P16389; baseline and differential.
Genevisible; P16389; HS.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0043194; C:axon initial segment; IEA:Ensembl.
GO; GO:0043679; C:axon terminus; ISS:UniProtKB.
GO; GO:0044305; C:calyx of Held; IEA:Ensembl.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IMP:UniProtKB.
GO; GO:0099056; C:integral component of presynaptic membrane; IEA:Ensembl.
GO; GO:0044224; C:juxtaparanode region of axon; ISS:BHF-UCL.
GO; GO:0030027; C:lamellipodium; ISS:UniProtKB.
GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0033010; C:paranodal junction; IEA:UniProtKB-SubCell.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0019894; F:kinesin binding; IEA:Ensembl.
GO; GO:0015271; F:outward rectifier potassium channel activity; IEA:Ensembl.
GO; GO:0005267; F:potassium channel activity; TAS:ProtInc.
GO; GO:0005249; F:voltage-gated potassium channel activity; IMP:UniProtKB.
GO; GO:0019228; P:neuronal action potential; ISS:UniProtKB.
GO; GO:0021633; P:optic nerve structural organization; IEA:Ensembl.
GO; GO:0097623; P:potassium ion export across plasma membrane; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IMP:UniProtKB.
GO; GO:0006813; P:potassium ion transport; TAS:ProtInc.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0045188; P:regulation of circadian sleep/wake cycle, non-REM sleep; IEA:Ensembl.
GO; GO:0014059; P:regulation of dopamine secretion; ISS:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
Gene3D; 1.20.120.350; -; 1.
Gene3D; 3.30.710.10; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003972; K_chnl_volt-dep_Kv1.
InterPro; IPR004049; K_chnl_volt-dep_Kv1.2.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
PANTHER; PTHR11537:SF23; PTHR11537:SF23; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR01509; KV12CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01496; SHAKERCHANEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Disease variant; Endoplasmic reticulum; Epilepsy; Glycoprotein;
Ion channel; Ion transport; Lipoprotein; Membrane; Palmitate;
Phosphoprotein; Potassium; Potassium channel; Potassium transport;
Reference proteome; Synapse; Synaptosome; Transmembrane;
Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1..499
/note="Potassium voltage-gated channel subfamily A member
2"
/id="PRO_0000053972"
TOPO_DOM 1..160
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 161..182
/note="Helical; Name=Segment S1"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 183..221
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 222..243
/note="Helical; Name=Segment S2"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 244..254
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 255..275
/note="Helical; Name=Segment S3"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 276..289
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 290..310
/note="Helical; Voltage-sensor; Name=Segment S4"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 311..325
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 326..347
/note="Helical; Name=Segment S5"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 348..361
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
INTRAMEM 362..373
/note="Helical; Name=Pore helix"
/evidence="ECO:0000250|UniProtKB:P63142"
INTRAMEM 374..381
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 382..388
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 389..417
/note="Helical; Name=Segment S6"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 418..499
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
REGION 1..125
/note="Tetramerization domain"
/evidence="ECO:0000250|UniProtKB:P63142"
REGION 1..26
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
REGION 312..325
/note="S4-S5 linker"
/evidence="ECO:0000250|UniProtKB:P63142"
MOTIF 374..379
/note="Selectivity filter"
/evidence="ECO:0000250|UniProtKB:P63142"
MOTIF 497..499
/note="PDZ-binding"
/evidence="ECO:0000250|UniProtKB:P63142"
SITE 252
/note="Important for normal, slow channel gating"
/evidence="ECO:0000250|UniProtKB:P63142"
SITE 381
/note="Important for binding with the scorpion
mesomartoxin; when the scorpion mesomartoxin-rKv1.2/KCNA2
interaction is modeled, this residue is close to the 'Y-57'
residue of the toxin"
/evidence="ECO:0000250|UniProtKB:P63142"
MOD_RES 429
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P63141"
MOD_RES 434
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P63141"
MOD_RES 440
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P63141"
MOD_RES 441
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q09081"
MOD_RES 449
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q09081"
MOD_RES 458
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:P63142"
MOD_RES 468
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:P63141"
LIPID 244
/note="S-palmitoyl cysteine"
/evidence="ECO:0000255"
CARBOHYD 207
/note="N-linked (GlcNAc...) asparagine"
/evidence="ECO:0000255"
VAR_SEQ 299..499
/note="VRVFRIFKLSRHSKGLQILGQTLKASMRELGLLIFFLFIGVILFSSAVYFAE
ADERESQFPSIPDAFWWAVVSMTTVGYGDMVPTTIGGKIVGSLCAIAGVLTIALPVPVI
VSNFNYFYHRETEGEEQAQYLQVTSCPKIPSSPDLKKSRSASTISKSDYMEIQEGVNNS
NEDFREENLKTANCTLANTNYVNITKMLTDV -> ERRPLQSQKSKRGRQHLNTSHDCT
LGINLVAGMTVQWTRASGPDDRQTPAVTTLHRMY (in isoform 2)"
/evidence="ECO:0000303|PubMed:15489334"
/id="VSP_043077"
VARIANT 236
/note="E -> K (in DEE32; affects channel activity; mutant
channels display voltage-dependent activation significantly
shifted toward negative potentials compared to wild-type;
no effect on channel sensitivity to 4-aminopyridine)"
/evidence="ECO:0000269|PubMed:34576077"
/id="VAR_085682"
VARIANT 263
/note="I -> T (in DEE32; dominant-negative mutation; loss
of channel function; dbSNP:rs786205231)"
/evidence="ECO:0000269|PubMed:25751627"
/id="VAR_073704"
VARIANT 297
/note="R -> Q (in DEE32; causes a gain of function;
dbSNP:rs786205232)"
/evidence="ECO:0000269|PubMed:25477152,
ECO:0000269|PubMed:25751627"
/id="VAR_073705"
VARIANT 298
/note="L -> F (in DEE32; causes a gain of function;
dbSNP:rs876657390)"
/evidence="ECO:0000269|PubMed:25751627"
/id="VAR_073706"
VARIANT 324
/note="S -> T (probable disease-associated variant found in
a patient with drug-resistant epilepsy)"
/evidence="ECO:0000269|PubMed:27864847"
/id="VAR_078206"
VARIANT 405
/note="P -> L (in DEE32; loss of channel function;
dbSNP:rs876657389)"
/evidence="ECO:0000269|PubMed:25751627"
/id="VAR_073707"
CONFLICT 230
/note="I -> V (in Ref. 2; BAF82750)"
/evidence="ECO:0000305"
SEQUENCE 499 AA; 56717 MW; 4B03F1B46A826C39 CRC64;
MTVATGDPAD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT LAQFPETLLG
DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR PVNVPLDIFS EEIRFYELGE
EAMEMFREDE GYIKEEERPL PENEFQRQVW LLFEYPESSG PARIIAIVSV MVILISIVSF
CLETLPIFRD ENEDMHGSGV TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR
FFACPSKAGF FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE ADERESQFPS
IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL TIALPVPVIV SNFNYFYHRE
TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA STISKSDYME IQEGVNNSNE DFREENLKTA
NCTLANTNYV NITKMLTDV


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Pathways :
WP2197: Endothelin
WP1566: Citrate cycle (TCA cycle)
WP2272: Pathogenic Escherichia coli infection
WP1634: Butanoate metabolism
WP1663: Homologous recombination
WP1680: Oxidative phosphorylation
WP1711: Trinitrotoluene degradation
WP1626: Benzoate degradation via CoA ligation
WP1655: Geraniol degradation
WP1672: Mismatch repair
WP1694: Pyrimidine metabolism
WP1834: Interactions of the immunoglobulin superfamily (IgSF) member proteins
WP2292: Chemokine signaling pathway
WP1614: 1- and 2-Methylnaphthalene degradation
WP1644: DNA replication
WP1671: Methane metabolism
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism

Related Genes :
[KCNA2] Potassium voltage-gated channel subfamily A member 2 (NGK1) (Voltage-gated K(+) channel HuKIV) (Voltage-gated potassium channel HBK5) (Voltage-gated potassium channel subunit Kv1.2)
[KCNA4 KCNA4L] Potassium voltage-gated channel subfamily A member 4 (HPCN2) (Voltage-gated K(+) channel HuKII) (Voltage-gated potassium channel HBK4) (Voltage-gated potassium channel HK1) (Voltage-gated potassium channel subunit Kv1.4)
[KCNA1] Potassium voltage-gated channel subfamily A member 1 (Voltage-gated K(+) channel HuKI) (Voltage-gated potassium channel HBK1) (Voltage-gated potassium channel subunit Kv1.1)
[KCNA5] Potassium voltage-gated channel subfamily A member 5 (HPCN1) (Voltage-gated potassium channel HK2) (Voltage-gated potassium channel subunit Kv1.5)
[KCNA3 HGK5] Potassium voltage-gated channel subfamily A member 3 (HGK5) (HLK3) (HPCN3) (Voltage-gated K(+) channel HuKIII) (Voltage-gated potassium channel subunit Kv1.3)
[Kcna3] Potassium voltage-gated channel subfamily A member 3 (RCK3) (RGK5) (Voltage-gated potassium channel subunit Kv1.3) (Voltage-gated potassium channel subunit Kv3)
[Kcna2] Potassium voltage-gated channel subfamily A member 2 (RAK) (RBK2) (RCK5) (Voltage-gated potassium channel subunit Kv1.2)
[Kcna6] Potassium voltage-gated channel subfamily A member 6 (RCK2) (Voltage-gated potassium channel subunit Kv1.6) (Voltage-gated potassium channel subunit Kv2)
[Kcna2] Potassium voltage-gated channel subfamily A member 2 (MK2) (Voltage-gated potassium channel subunit Kv1.2)
[KCNA2] Potassium voltage-gated channel subfamily A member 2 (KC22) (Voltage-gated potassium channel subunit Kv1.2)
[KCNA2] Potassium voltage-gated channel subfamily A member 2 (CSMK1) (Voltage-gated potassium channel subunit Kv1.2)
[KCNA6] Potassium voltage-gated channel subfamily A member 6 (Voltage-gated potassium channel HBK2) (Voltage-gated potassium channel subunit Kv1.6)
[Kcna5] Potassium voltage-gated channel subfamily A member 5 (Voltage-gated potassium channel subunit Kv1.5) (KV1-5)
[Kcna1] Potassium voltage-gated channel subfamily A member 1 (MBK1) (MKI) (Voltage-gated potassium channel subunit Kv1.1)
[Kcna1] Potassium voltage-gated channel subfamily A member 1 (RBKI) (RCK1) (Voltage-gated potassium channel subunit Kv1.1)
[Kcna4] Potassium voltage-gated channel subfamily A member 4 (RCK4) (RHK1) (RK3) (Voltage-gated potassium channel subunit Kv1.4)
[Kcna4] Potassium voltage-gated channel subfamily A member 4 (Voltage-gated potassium channel subunit Kv1.4)
[Kcna5] Potassium voltage-gated channel subfamily A member 5 (RCK7) (RK4) (Voltage-gated potassium channel subunit Kv1.5)
[KCNA5] Potassium voltage-gated channel subfamily A member 5 (Voltage-gated potassium channel subunit Kv1.5)
[KCNA10] Potassium voltage-gated channel subfamily A member 10 (Voltage-gated potassium channel subunit Kv1.8)
[Kcnb1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[Kcnc2] Potassium voltage-gated channel subfamily C member 2 (Potassium channel voltage-gated Shaw-related subfamily C member 2) (Shaw-like potassium channel) (Voltage-gated potassium channel subunit Kv3.2)
[Kcnd2] Potassium voltage-gated channel subfamily D member 2 (RK5) (Shal1) (Voltage-gated potassium channel subunit Kv4.2)
[Kcnd2 Kiaa1044 MNCb-7013] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcna3] Potassium voltage-gated channel subfamily A member 3 (MK3) (Voltage-gated potassium channel subunit Kv1.3)
[Kcnc2] Potassium voltage-gated channel subfamily C member 2 (Shaw-like potassium channel) (Voltage-gated potassium channel Kv3.2)
[Kcnb1] Potassium voltage-gated channel subfamily B member 1 (Voltage-gated potassium channel subunit Kv2.1) (mShab)
[kcna2] Potassium voltage-gated channel subfamily A member 2 (Voltage-gated potassium channel subunit Kv1.2) (xSHA2)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (RAW2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[KCNA5] Potassium voltage-gated channel subfamily A member 5 (Voltage-gated potassium channel subunit Kv1.5)

Bibliography :