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Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)

 KCND2_HUMAN             Reviewed;         630 AA.
Q9NZV8; O95012; O95021; Q2TBD3; Q9UBY7; Q9UN98; Q9UNH9;
07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
07-NOV-2003, sequence version 2.
29-SEP-2021, entry version 188.
RecName: Full=Potassium voltage-gated channel subfamily D member 2;
AltName: Full=Voltage-gated potassium channel subunit Kv4.2;
Name=KCND2; Synonyms=KIAA1044;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
PubMed=9843794; DOI=10.1152/ajpheart.1998.275.6.h1963;
Kong W., Po S., Yamagishi T., Ashen M.D., Stetten G., Tomaselli G.F.;
"Isolation and characterization of the human gene encoding Ito: further
diversity by alternative mRNA splicing.";
Am. J. Physiol. 275:H1963-H1970(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=10470851; DOI=10.1093/dnares/6.3.197;
Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A.,
Kotani H., Nomura N., Ohara O.;
"Prediction of the coding sequences of unidentified human genes. XIV. The
complete sequences of 100 new cDNA clones from brain which code for large
proteins in vitro.";
DNA Res. 6:197-205(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND FUNCTION.
PubMed=10551270;
Zhu X.-R., Wulf A., Schwarz M., Isbrandt D., Pongs O.;
"Characterization of human Kv4.2 mediating a rapidly-inactivating transient
voltage-sensitive K+ current.";
Recept. Channels 6:387-400(1999).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
TISSUE=Brain cortex;
PubMed=10729221; DOI=10.1006/geno.2000.6117;
Isbrandt D., Leicher T., Waldschuetz R., Zhu X.-R., Luhmann U., Michel U.,
Sauter K., Pongs O.;
"Gene structures and expression profiles of three human KCND (Kv4)
potassium channels mediating A-type currents I(TO) and I(SA).";
Genomics 64:144-154(2000).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[7]
MUTAGENESIS OF 601-PRO--PRO-604, SUBCELLULAR LOCATION, AND INTERACTION WITH
FLNA AND FLNC.
PubMed=11102480; DOI=10.1523/jneurosci.20-23-08736.2000;
Petrecca K., Miller D.M., Shrier A.;
"Localization and enhanced current density of the Kv4.2 potassium channel
by interaction with the actin-binding protein filamin.";
J. Neurosci. 20:8736-8744(2000).
[8]
INTERACTION WITH KCNIP1.
PubMed=10676964; DOI=10.1038/35000592;
An W.F., Bowlby M.R., Betty M., Cao J., Ling H.-P., Mendoza G.,
Hinson J.W., Mattsson K.I., Strassle B.W., Trimmer J.S., Rhodes K.J.;
"Modulation of A-type potassium channels by a family of calcium sensors.";
Nature 403:553-556(2000).
[9]
INTERACTION WITH KCNIP2.
PubMed=11287421; DOI=10.1074/jbc.m101320200;
Baehring R., Dannenberg J., Peters H.C., Leicher T., Pongs O., Isbrandt D.;
"Conserved Kv4 N-terminal domain critical for effects of Kv channel-
interacting protein 2.2 on channel expression and gating.";
J. Biol. Chem. 276:23888-23894(2001).
[10]
FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND DOMAIN.
PubMed=11507158; DOI=10.1111/j.1469-7793.2001.00065.x;
Baehring R., Boland L.M., Varghese A., Gebauer M., Pongs O.;
"Kinetic analysis of open- and closed-state inactivation transitions in
human Kv4.2 A-type potassium channels.";
J. Physiol. (Lond.) 535:65-81(2001).
[11]
TISSUE SPECIFICITY.
PubMed=12395204; DOI=10.1007/s00395-002-0377-4;
Bertaso F., Sharpe C.C., Hendry B.M., James A.F.;
"Expression of voltage-gated K+ channels in human atrium.";
Basic Res. Cardiol. 97:424-433(2002).
[12]
INTERACTION WITH KCNIP4.
PubMed=11847232; DOI=10.1074/jbc.m200897200;
Morohashi Y., Hatano N., Ohya S., Takikawa R., Watabiki T., Takasugi N.,
Imaizumi Y., Tomita T., Iwatsubo T.;
"Molecular cloning and characterization of CALP/KChIP4, a novel EF-hand
protein interacting with presenilin 2 and voltage-gated potassium channel
subunit Kv4.";
J. Biol. Chem. 277:14965-14975(2002).
[13]
INTERACTION WITH KCNIP3.
PubMed=12451113; DOI=10.1523/jneurosci.22-23-10123.2002;
Schrader L.A., Anderson A.E., Mayne A., Pfaffinger P.J., Sweatt J.D.;
"PKA modulation of Kv4.2-encoded A-type potassium channels requires
formation of a supramolecular complex.";
J. Neurosci. 22:10123-10133(2002).
[14]
FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
PubMed=14695263; DOI=10.1016/s0006-3495(04)74097-7;
Gebauer M., Isbrandt D., Sauter K., Callsen B., Nolting A., Pongs O.,
Baehring R.;
"N-type inactivation features of Kv4.2 channel gating.";
Biophys. J. 86:210-223(2004).
[15]
FUNCTION, INTERACTION WITH DPP10 AND DPP6, AND SUBCELLULAR LOCATION.
PubMed=15454437; DOI=10.1529/biophysj.104.042358;
Jerng H.H., Qian Y., Pfaffinger P.J.;
"Modulation of Kv4.2 channel expression and gating by dipeptidyl peptidase
10 (DPP10).";
Biophys. J. 87:2380-2396(2004).
[16]
INTERACTION WITH KCNIP1 AND KCNIP2, SUBUNIT, AND DOMAIN.
PubMed=15358149; DOI=10.1016/j.bbrc.2004.07.006;
Lin Y.-L., Chen C.Y., Cheng C.P., Chang L.S.;
"Protein-protein interactions of KChIP proteins and Kv4.2.";
Biochem. Biophys. Res. Commun. 321:606-610(2004).
[17]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, DOMAIN, AND ROLE IN DISEASE.
PubMed=16934482; DOI=10.1016/j.nbd.2006.07.001;
Singh B., Ogiwara I., Kaneda M., Tokonami N., Mazaki E., Baba K.,
Matsuda K., Inoue Y., Yamakawa K.;
"A Kv4.2 truncation mutation in a patient with temporal lobe epilepsy.";
Neurobiol. Dis. 24:245-253(2006).
[18]
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).
[19]
REVIEW.
PubMed=18357523; DOI=10.1007/s11064-008-9650-8;
Covarrubias M., Bhattacharji A., De Santiago-Castillo J.A., Dougherty K.,
Kaulin Y.A., Na-Phuket T.R., Wang G.;
"The neuronal Kv4 channel complex.";
Neurochem. Res. 33:1558-1567(2008).
[20]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND MUTAGENESIS OF GLY-309;
ARG-311; ILE-312; LEU-313; GLY-314; TYR-315; THR-316; LEU-317; LYS-318;
SER-319; CYS-320; SER-322; GLU-323; LEU-324; LEU-327; LEU-328; VAL-397;
ILE-398; ALA-399; PRO-401; 402-VAL--VAL-404; PRO-403; ILE-405; VAL-406;
SER-407; ASN-408 AND PHE-409.
PubMed=19171772; DOI=10.1085/jgp.200810073;
Barghaan J., Baehring R.;
"Dynamic coupling of voltage sensor and gate involved in closed-state
inactivation of Kv4.2 channels.";
J. Gen. Physiol. 133:205-224(2009).
[21]
FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, AND INTERACTION WITH KCNIP4.
PubMed=24811166; DOI=10.1074/jbc.m114.563452;
Kitazawa M., Kubo Y., Nakajo K.;
"The stoichiometry and biophysical properties of the Kv4 potassium channel
complex with K+ channel-interacting protein (KChIP) subunits are variable,
depending on the relative expression level.";
J. Biol. Chem. 289:17597-17609(2014).
[22]
STRUCTURE BY ELECTRON MICROSCOPY (21 ANGSTROMS) OF THE KCND2-KCNIP2
COMPLEX, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=14980201; DOI=10.1016/s0896-6273(04)00050-9;
Kim L.A., Furst J., Gutierrez D., Butler M.H., Xu S., Goldstein S.A.,
Grigorieff N.;
"Three-dimensional structure of I(to); Kv4.2-KChIP2 ion channels by
electron microscopy at 21 Angstrom resolution.";
Neuron 41:513-519(2004).
[23]
INTERACTION WITH KCNIP2, FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT.
PubMed=14623880; DOI=10.1074/jbc.m311332200;
Kim L.A., Furst J., Butler M.H., Xu S., Grigorieff N., Goldstein S.A.;
"Ito channels are octameric complexes with four subunits of each Kv4.2 and
K+ channel-interacting protein 2.";
J. Biol. Chem. 279:5549-5554(2004).
[24]
TISSUE SPECIFICITY.
PubMed=15991246; DOI=10.1002/jcp.20453;
Kunz L., Ramsch R., Krieger A., Young K.A., Dissen G.A., Stouffer R.L.,
Ojeda S.R., Mayerhofer A.;
"Voltage-dependent K+ channel acts as sex steroid sensor in endocrine cells
of the human ovary.";
J. Cell. Physiol. 206:167-174(2006).
[25]
INTERACTION WITH KCNIP1.
PubMed=14980207; DOI=10.1016/s0896-6273(04)00049-2;
Scannevin R.H., Wang K., Jow F., Megules J., Kopsco D.C., Edris W.,
Carroll K.C., Lu Q., Xu W., Xu Z., Katz A.H., Olland S., Lin L., Taylor M.,
Stahl M., Malakian K., Somers W., Mosyak L., Bowlby M.R., Chanda P.,
Rhodes K.J.;
"Two N-terminal domains of Kv4 K(+) channels regulate binding to and
modulation by KChIP1.";
Neuron 41:587-598(2004).
[26]
INTERACTION WITH DLG1.
PubMed=19213956; DOI=10.1161/circresaha.108.191007;
El-Haou S., Balse E., Neyroud N., Dilanian G., Gavillet B., Abriel H.,
Coulombe A., Jeromin A., Hatem S.N.;
"Kv4 potassium channels form a tripartite complex with the anchoring
protein SAP97 and CaMKII in cardiac myocytes.";
Circ. Res. 104:758-769(2009).
[27]
VARIANT MET-404, CHARACTERIZATION OF VARIANT MET-404, FUNCTION, AND
SUBCELLULAR LOCATION.
PubMed=24501278; DOI=10.1093/hmg/ddu056;
Lee H., Lin M.C., Kornblum H.I., Papazian D.M., Nelson S.F.;
"Exome sequencing identifies de novo gain of function missense mutation in
KCND2 in identical twins with autism and seizures that slows potassium
channel inactivation.";
Hum. Mol. Genet. 23:3481-3489(2014).
-!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
potassium transport in excitable membranes, primarily in the brain.
Mediates the major part of the dendritic A-type current I(SA) in brain
neurons (By similarity). This current is activated at membrane
potentials that are below the threshold for action potentials. It
regulates neuronal excitability, prolongs the latency before the first
spike in a series of action potentials, regulates the frequency of
repetitive action potential firing, shortens the duration of action
potentials and regulates the back-propagation of action potentials from
the neuronal cell body to the dendrites. Contributes to the regulation
of the circadian rhythm of action potential firing in suprachiasmatic
nucleus neurons, which regulates the circadian rhythm of locomotor
activity (By similarity). Functions downstream of the metabotropic
glutamate receptor GRM5 and plays a role in neuronal excitability and
in nociception mediated by activation of GRM5 (By similarity). Mediates
the transient outward current I(to) in rodent heart left ventricle apex
cells, but not in human heart, where this current is mediated by
another family member. Forms tetrameric potassium-selective channels
through which potassium ions pass in accordance with their
electrochemical gradient (PubMed:10551270, PubMed:15454437,
PubMed:14695263, PubMed:14623880, PubMed:14980201, PubMed:16934482,
PubMed:24811166, PubMed:24501278). The channel alternates between
opened and closed conformations in response to the voltage difference
across the membrane (PubMed:11507158). Can form functional
homotetrameric channels and heterotetrameric channels that contain
variable proportions of KCND2 and KCND3; channel properties depend on
the type of pore-forming alpha subunits that are part of the channel.
In vivo, membranes probably contain a mixture of heteromeric potassium
channel complexes. Interaction with specific isoforms of the regulatory
subunits KCNIP1, KCNIP2, KCNIP3 or KCNIP4 strongly increases expression
at the cell surface and thereby increases channel activity; it
modulates the kinetics of channel activation and inactivation, shifts
the threshold for channel activation to more negative voltage values,
shifts the threshold for inactivation to less negative voltages and
accelerates recovery after inactivation (PubMed:15454437,
PubMed:14623880, PubMed:14980201, PubMed:19171772, PubMed:24501278,
PubMed:24811166). Likewise, interaction with DPP6 or DPP10 promotes
expression at the cell membrane and regulates both channel
characteristics and activity (By similarity).
{ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:10551270, ECO:0000269|PubMed:10729221,
ECO:0000269|PubMed:11507158, ECO:0000269|PubMed:14623880,
ECO:0000269|PubMed:14695263, ECO:0000269|PubMed:14980201,
ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:16934482,
ECO:0000269|PubMed:19171772, ECO:0000269|PubMed:24501278,
ECO:0000269|PubMed:24811166}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels activate rapidly, i.e within a few msec.
After that, they inactivate rapidly, i.e within about 50-100 msec.
The voltage-dependence of activation and inactivation and other
channel characteristics vary depending on the experimental
conditions, the expression system and the presence or absence of
ancillary subunits. Homotetrameric channels have a unitary
conductance of about 4 pS when expressed in a heterologous system.
For the activation of homotetrameric channels expressed in xenopus
oocytes, the voltage at half-maximal amplitude is about -10 mV. The
time constant for inactivation is about 20 msec. For inactivation,
the voltage at half-maximal amplitude is -62 mV. The time constant
for recovery after inactivation is about 70 msec.
{ECO:0000305|PubMed:11507158, ECO:0000305|PubMed:17917103};
-!- SUBUNIT: Homotetramer or heterotetramer with KCND1 or KCND3
(PubMed:14980201, PubMed:16934482, PubMed:24811166). Associates with
the regulatory subunits KCNIP1, KCNIP2, KCNIP3 and KCNIP4
(PubMed:10676964, PubMed:11287421, PubMed:11847232, PubMed:12451113,
PubMed:15358149, PubMed:14623880, PubMed:14980201, PubMed:14980207,
PubMed:24811166). In vivo, probably exists as heteromeric complex
containing variable proportions of KCND1, KCND2, KCND3, KCNIP1, KCNIP2,
KCNIP3, KCNIP4, DPP6 and DPP10 (PubMed:19171772). The tetrameric
channel can associate with up to four regulatory subunits, such as
KCNIP2 or KCNIP4 (PubMed:14623880, PubMed:14980201, PubMed:24811166).
Interaction with four KCNIP4 chains does not reduce interaction with
DPP10 (PubMed:24811166). Interacts with DLG4 and NCS1/FREQ (By
similarity). Interacts with DLG1 (PubMed:19213956). Probably part of a
complex consisting of KCNIP1, KCNIP2 isoform 3 and KCND2
(PubMed:15358149). Interacts with FLNA, FLNC, DPP6 and DPP10
(PubMed:11102480, PubMed:15454437, PubMed:24811166).
{ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:10676964, ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:11287421, ECO:0000269|PubMed:11847232,
ECO:0000269|PubMed:12451113, ECO:0000269|PubMed:14623880,
ECO:0000269|PubMed:14980201, ECO:0000269|PubMed:14980207,
ECO:0000269|PubMed:15358149, ECO:0000269|PubMed:15454437,
ECO:0000269|PubMed:16934482, ECO:0000269|PubMed:19213956,
ECO:0000269|PubMed:24811166, ECO:0000305|PubMed:19171772}.
-!- INTERACTION:
Q9NZV8; Q9NZI2: KCNIP1; NbExp=4; IntAct=EBI-1646745, EBI-2120635;
Q9NZV8; Q9NS61: KCNIP2; NbExp=3; IntAct=EBI-1646745, EBI-1052975;
Q9NZV8; Q9NS61-3: KCNIP2; NbExp=3; IntAct=EBI-1646745, EBI-1053010;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11102480,
ECO:0000269|PubMed:11507158, ECO:0000269|PubMed:14623880,
ECO:0000269|PubMed:14695263, ECO:0000269|PubMed:14980201,
ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:16934482,
ECO:0000269|PubMed:19171772, ECO:0000269|PubMed:24501278,
ECO:0000269|PubMed:24811166}; Multi-pass membrane protein
{ECO:0000269|PubMed:11102480, ECO:0000269|PubMed:14980201,
ECO:0000305}. Cell projection, dendrite {ECO:0000269|PubMed:11102480}.
Cell junction, synapse {ECO:0000250|UniProtKB:Q63881}. Perikaryon
{ECO:0000250|UniProtKB:Q63881}. Cell junction, synapse, postsynaptic
cell membrane {ECO:0000250|UniProtKB:Q63881}. Cell projection,
dendritic spine {ECO:0000250|UniProtKB:Q63881}. Cell junction
{ECO:0000250|UniProtKB:Q63881}. Note=In neurons, primarily detected on
dendrites, dendritic spines and on the neuron cell body, but not on
axons. Localized preferentially at the dendrites of pyramidal cells in
the hippocampus CA1 layer. Detected at GABAergic synapses. Detected at
cell junctions that are distinct from synaptic cell contacts. Detected
in lipid rafts. Detected primarily at the endoplasmic reticulum or
Golgi when expressed by itself (PubMed:15454437). Interaction with
KCNIP1, KCNIP2, KCNIP3 or KCNIP4 promotes expression at the cell
membrane (PubMed:15454437, PubMed:24811166). Interaction with DPP6 or
DPP10 promotes expression at the cell membrane (By similarity).
Internalized from the cell membrane by clathrin-dependent endocytosis
in response to activation of AMPA-selective glutamate receptors and
PKA-mediated phosphorylation at Ser-552. Redistributed from dendritic
spines to the main dendritic shaft in response to activation of AMPA-
selective glutamate receptors and activation of PKA (By similarity).
{ECO:0000250|UniProtKB:Q63881, ECO:0000250|UniProtKB:Q9Z0V2,
ECO:0000269|PubMed:15454437, ECO:0000269|PubMed:24811166}.
-!- TISSUE SPECIFICITY: Detected in ovary, in corpus luteum and in
granulosa and theca cells in the follicle (at protein level)
(PubMed:15991246). Highly expressed throughout the brain
(PubMed:10551270, PubMed:10729221). Detected in amygdala, caudate
nucleus, cerebellum, hippocampus, substantia nigra and thalamus
(PubMed:10551270, PubMed:10729221). Expression is not detectable or
very low in heart, kidney, liver, lung, pancreas and skeletal muscle
(PubMed:10551270, PubMed:10729221). Not detectable in human heart
atrium (PubMed:12395204). {ECO:0000269|PubMed:10551270,
ECO:0000269|PubMed:10729221, ECO:0000269|PubMed:12395204,
ECO:0000269|PubMed:15991246}.
-!- 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}.
-!- DOMAIN: The N-terminal cytoplasmic region can mediate N-type
inactivation by physically blocking the channel (PubMed:14695263). This
probably does not happen in vivo, where the N-terminal region mediates
interaction with regulatory subunits, such as KCNIP1 and KCNIP2
(PubMed:15358149). The zinc binding sites in the N-terminal domain are
important for tetramerization and assembly of a functional channel
complex (By similarity). Most likely, the channel undergoes closed-
state inactivation, where a subtle conformation change would render the
protein less sensitive to activation. {ECO:0000250|UniProtKB:Q63881,
ECO:0000305|PubMed:11507158, ECO:0000305|PubMed:14695263,
ECO:0000305|PubMed:15358149, ECO:0000305|PubMed:18357523}.
-!- DOMAIN: The C-terminal cytoplasmic region is important for normal
expression at the cell membrane and modulates the voltage-dependence of
channel activation and inactivation (PubMed:16934482). It is required
for interaction with KCNIP2, and probably other family members as well
(By similarity). {ECO:0000250|UniProtKB:Q63881,
ECO:0000269|PubMed:16934482}.
-!- PTM: Phosphorylation at Ser-438 in response to MAPK activation is
increased in stimulated dendrites. Interaction with KCNIP2 and DPP6
propomtes phosphorylation by PKA at Ser-552. Phosphorylation at Ser-552
has no effect on interaction with KCNIP3, but is required for the
regulation of channel activity by KCNIP3. Phosphorylation at Ser-552
leads to KCND2 internalization (By similarity). Phosphorylated by MAPK
in response to signaling via the metabotropic glutamate receptor GRM5
(By similarity). Phosphorylation at Ser-616 is required for the down-
regulation of neuronal A-type currents in response to signaling via
GRM5 (By similarity). {ECO:0000250|UniProtKB:Q63881,
ECO:0000250|UniProtKB:Q9Z0V2}.
-!- DISEASE: Note=KNCD2 mutations have been found in a family with autism
and epilepsy and may play a role in disease pathogenesis. Autism is a
complex multifactorial, pervasive developmental disorder characterized
by impairments in reciprocal social interaction and communication,
restricted and stereotyped patterns of interests and activities, and
the presence of developmental abnormalities by 3 years of age. Epilepsy
is characterized by paroxysmal transient disturbances of the electrical
activity of the brain that may be manifested as episodic impairment or
loss of consciousness, abnormal motor phenomena, psychic or sensory
disturbances, or perturbation of the autonomic nervous system.
{ECO:0000269|PubMed:24501278}.
-!- DISEASE: Note=A KCND2 mutation leading to the production of a C-
terminally truncated protein has been identified in a patient with
epilepsy. Epilepsy is characterized by paroxysmal transient
disturbances of the electrical activity of the brain that may be
manifested as episodic impairment or loss of consciousness, abnormal
motor phenomena, psychic or sensory disturbances, or perturbation of
the autonomic nervous system. {ECO:0000269|PubMed:16934482}.
-!- MISCELLANEOUS: The transient neuronal A-type potassium current called
I(SA) is triggered at membrane potentials that are below the threshold
for action potentials. It inactivates rapidly and recovers rapidly from
inactivation. It regulates the firing of action potentials and plays a
role in synaptic integration and plasticity. Potassium channels
containing KCND2 account for about 80% of the neuronal A-type potassium
current. In contrast, the potassium channel responsible for the cardiac
I(to) current differs between species; it is mediated by KCND2 in
rodents. In human and other non-rodents KCND3 may play an equivalent
role. {ECO:0000269|PubMed:10551270, ECO:0000305|PubMed:17917103,
ECO:0000305|PubMed:18357523}.
-!- MISCELLANEOUS: Is specifically and reversibly inhibited by the scorpion
toxin Ts8 (AC P69940). {ECO:0000250|UniProtKB:Q63881}.
-!- SIMILARITY: Belongs to the potassium channel family. D (Shal) (TC
1.A.1.2) subfamily. Kv4.2/KCND2 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA82996.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
---------------------------------------------------------------------------
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Distributed under the Creative Commons Attribution (CC BY 4.0) License
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EMBL; AF121104; AAD22053.1; -; mRNA.
EMBL; AB028967; BAA82996.2; ALT_INIT; mRNA.
EMBL; AJ010969; CAB56841.1; -; mRNA.
EMBL; AF166008; AAF65618.1; -; Genomic_DNA.
EMBL; AF166007; AAF65618.1; JOINED; Genomic_DNA.
EMBL; AC004888; AAC83405.1; -; Genomic_DNA.
EMBL; AC004946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AF142568; AAD52159.1; -; Genomic_DNA.
EMBL; BC110449; AAI10450.1; -; mRNA.
EMBL; BC110450; AAI10451.1; -; mRNA.
CCDS; CCDS5776.1; -.
RefSeq; NP_036413.1; NM_012281.2.
BioGRID; 109953; 19.
ComplexPortal; CPX-3239; Kv4.2-KChIP2 channel complex.
CORUM; Q9NZV8; -.
IntAct; Q9NZV8; 10.
STRING; 9606.ENSP00000333496; -.
ChEMBL; CHEMBL5885; -.
DrugBank; DB06637; Dalfampridine.
DrugBank; DB00280; Disopyramide.
DrugBank; DB00228; Enflurane.
DrugBank; DB00458; Imipramine.
DrugBank; DB01110; Miconazole.
DrugBank; DB01069; Promethazine.
DrugCentral; Q9NZV8; -.
TCDB; 1.A.1.2.5; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q9NZV8; -.
PhosphoSitePlus; Q9NZV8; -.
BioMuta; KCND2; -.
DMDM; 38258257; -.
EPD; Q9NZV8; -.
MassIVE; Q9NZV8; -.
PaxDb; Q9NZV8; -.
PeptideAtlas; Q9NZV8; -.
PRIDE; Q9NZV8; -.
ProteomicsDB; 83521; -.
ABCD; Q9NZV8; 1 sequenced antibody.
Antibodypedia; 31683; 433 antibodies.
DNASU; 3751; -.
Ensembl; ENST00000331113; ENSP00000333496; ENSG00000184408.
GeneID; 3751; -.
KEGG; hsa:3751; -.
UCSC; uc003vjj.2; human.
CTD; 3751; -.
DisGeNET; 3751; -.
GeneCards; KCND2; -.
GeneReviews; KCND2; -.
HGNC; HGNC:6238; KCND2.
HPA; ENSG00000184408; Tissue enriched (brain).
MIM; 605410; gene.
neXtProt; NX_Q9NZV8; -.
OpenTargets; ENSG00000184408; -.
PharmGKB; PA30030; -.
VEuPathDB; HostDB:ENSG00000184408; -.
eggNOG; KOG4390; Eukaryota.
GeneTree; ENSGT00940000155472; -.
HOGENOM; CLU_011722_9_1_1; -.
InParanoid; Q9NZV8; -.
OMA; ETQYNGQ; -.
OrthoDB; 469107at2759; -.
PhylomeDB; Q9NZV8; -.
TreeFam; TF313103; -.
PathwayCommons; Q9NZV8; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
Reactome; R-HSA-5576894; Phase 1 - inactivation of fast Na+ channels.
SIGNOR; Q9NZV8; -.
BioGRID-ORCS; 3751; 8 hits in 1011 CRISPR screens.
ChiTaRS; KCND2; human.
GeneWiki; KCND2; -.
GenomeRNAi; 3751; -.
Pharos; Q9NZV8; Tclin.
PRO; PR:Q9NZV8; -.
Proteomes; UP000005640; Chromosome 7.
RNAct; Q9NZV8; protein.
Bgee; ENSG00000184408; Expressed in caudate nucleus and 151 other tissues.
ExpressionAtlas; Q9NZV8; baseline and differential.
Genevisible; Q9NZV8; HS.
GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
GO; GO:0098982; C:GABA-ergic synapse; IEA:Ensembl.
GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0099060; C:integral component of postsynaptic specialization membrane; IEA:Ensembl.
GO; GO:0031226; C:intrinsic component of plasma membrane; IMP:UniProtKB.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0044853; C:plasma membrane raft; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005250; F:A-type (transient outward) potassium channel activity; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:1905030; F:voltage-gated ion channel activity involved in regulation of postsynaptic membrane potential; IBA:GO_Central.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0001508; P:action potential; TAS:UniProtKB.
GO; GO:0071456; P:cellular response to hypoxia; ISS:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; TAS:UniProtKB.
GO; GO:0045475; P:locomotor rhythm; IEA:Ensembl.
GO; GO:0019228; P:neuronal action potential; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; IEA:Ensembl.
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; IPR003975; K_chnl_volt-dep_Kv4.
InterPro; IPR004055; K_chnl_volt-dep_Kv4.2.
InterPro; IPR024587; K_chnl_volt-dep_Kv4_C.
InterPro; IPR021645; Shal-type_N.
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.
Pfam; PF02214; BTB_2; 1.
Pfam; PF11879; DUF3399; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF11601; Shal-type; 1.
PRINTS; PR01517; KV42CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01497; SHALCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
1: Evidence at protein level;
Autism; Autism spectrum disorder; Cell junction; Cell membrane;
Cell projection; Disease variant; Epilepsy; Ion channel; Ion transport;
Membrane; Metal-binding; Phosphoprotein; Postsynaptic cell membrane;
Potassium; Potassium channel; Potassium transport; Reference proteome;
Synapse; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel; Zinc.
CHAIN 1..630
/note="Potassium voltage-gated channel subfamily D member
2"
/id="PRO_0000054064"
TOPO_DOM 1..182
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 183..204
/note="Helical; Name=Segment S1"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 205..228
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 229..250
/note="Helical; Name=Segment S2"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 251..261
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 262..279
/note="Helical; Name=Segment S3"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 280..286
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 287..306
/note="Helical; Voltage-sensor; Name=Segment S4"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 307..321
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 322..343
/note="Helical; Name=Segment S5"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 344..357
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
INTRAMEM 358..369
/note="Helical; Name=Pore helix"
/evidence="ECO:0000250|UniProtKB:P63142"
INTRAMEM 370..377
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 378..384
/note="Extracellular"
/evidence="ECO:0000250|UniProtKB:P63142"
TRANSMEM 385..413
/note="Helical; Name=Segment S6"
/evidence="ECO:0000250|UniProtKB:P63142"
TOPO_DOM 414..630
/note="Cytoplasmic"
/evidence="ECO:0000250|UniProtKB:P63142"
REGION 2..20
/note="Interaction with KCNIP1, KCNIP2, and other family
members"
/evidence="ECO:0000250|UniProtKB:Q63881"
REGION 71..90
/note="Interaction with KCNIP1"
/evidence="ECO:0000250|UniProtKB:Q63881"
REGION 308..321
/note="S4-S5 linker"
/evidence="ECO:0000250|UniProtKB:P63142"
REGION 474..630
/note="Important for normal channel activation and
inactivation, for interaction with KCNIP2, and probably
other family members as well"
/evidence="ECO:0000250|UniProtKB:Q63881,
ECO:0000305|PubMed:16934482"
REGION 474..489
/note="Required for dendritic targeting"
/evidence="ECO:0000250|UniProtKB:Q63881"
REGION 600..630
/note="Disordered"
/evidence="ECO:0000256|SAM:MobiDB-lite"
MOTIF 370..375
/note="Selectivity filter"
/evidence="ECO:0000250|UniProtKB:P63142"
MOTIF 627..630
/note="PDZ-binding"
/evidence="ECO:0000250|UniProtKB:Q63881"
METAL 105
/note="Zinc; via pros nitrogen"
/evidence="ECO:0000250|UniProtKB:Q63881"
METAL 132
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:Q63881"
METAL 133
/note="Zinc"
/evidence="ECO:0000250|UniProtKB:Q63881"
MOD_RES 38
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q63881"
MOD_RES 438
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q63881"
MOD_RES 548
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q63881"
MOD_RES 552
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9Z0V2"
MOD_RES 572
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9Z0V2"
MOD_RES 575
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9Z0V2"
MOD_RES 602
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q63881"
MOD_RES 607
/note="Phosphothreonine"
/evidence="ECO:0000250|UniProtKB:Q63881"
MOD_RES 616
/note="Phosphoserine"
/evidence="ECO:0000250|UniProtKB:Q9Z0V2"
VARIANT 404
/note="V -> M (probable disease-associated variant found in
a family with atypical autism and severe epilepsy; disrupts
potassium current inactivation; dbSNP:rs587777631)"
/evidence="ECO:0000269|PubMed:24501278"
/id="VAR_072076"
MUTAGEN 309
/note="G->A: Increases peak current amplitude and causes a
negative shift in the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 311
/note="R->A: No effect on peak current amplitude, but
causes a positive shift in the voltage-dependence of
activation. May increase the affinity for the closed-
inactivated state of the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 312
/note="I->A: Increases peak current amplitude and causes a
positive shift in the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 313
/note="L->A: Causes a positive shift in the voltage-
dependence of activation. May decrease the affinity for the
closed-inactivated state of the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 314
/note="G->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 315
/note="Y->A: Increases peak current amplitude but has a
minor effect on the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 316
/note="T->A: Increases peak current amplitude and causes a
positive shift in the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 317
/note="L->A: Increases peak current amplitude and causes a
positive shift in the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 318
/note="K->A: Increases peak current amplitude and causes a
positive shift in the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 319
/note="S->A: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 320
/note="C->A: Increases peak current amplitude and causes a
positive shift in the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 320
/note="C->S: Increases peak current amplitude and slows the
onset of inactivation at low voltage, but has no effect on
the voltage-dependence of activation."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 322
/note="S->A: Increases peak current amplitude and causes a
positive shift in the voltage-dependence of activation. May
increase the affinity for the closed-inactivated state of
the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 323
/note="E->A: Slightly increases peak current amplitude and
causes a negative shift in the voltage-dependence of
activation. May decrease the affinity for the closed-
inactivated state of the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 324
/note="L->A: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 327
/note="L->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 328
/note="L->A: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 329
/note="F->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 397
/note="V->A: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 398
/note="I->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 399
/note="A->V: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 401
/note="P->A: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 402..404
/note="VPV->IPI: Increases pak current amplitude and causes
a positive shift in the voltage-dependence of activation
and steady-state inactivation. May increase the affinity
for the closed-inactivated state of the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 403
/note="P->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 405
/note="I->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 406
/note="V->A: Loss of channel activity."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 407
/note="S->A: Increases peak current amplitude but has no
effect on the voltage-dependence of activation. May
increase the affinity for the closed-inactivated state of
the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 408
/note="N->A: Decreases peak current amplitude and causes a
positive shift in the voltage-dependence of activation. May
increase the affinity for the closed-inactivated state of
the channel."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 409
/note="F->A: May impair protein folding."
/evidence="ECO:0000269|PubMed:19171772"
MUTAGEN 601..604
/note="PTPP->ATAA: Abolishes interaction with FLNC."
/evidence="ECO:0000269|PubMed:11102480"
CONFLICT 450
/note="N -> S (in Ref. 1; AAD22053)"
/evidence="ECO:0000305"
CONFLICT 464
/note="Q -> P (in Ref. 1; AAD22053)"
/evidence="ECO:0000305"
CONFLICT 550
/note="Q -> R (in Ref. 1; AAD22053)"
/evidence="ECO:0000305"
CONFLICT 553
/note="I -> V (in Ref. 1; AAD22053)"
/evidence="ECO:0000305"
SEQUENCE 630 AA; 70537 MW; 0C11E62FFA220421 CRC64;
MAAGVAAWLP FARAAAIGWM PVASGPMPAP PRQERKRTQD ALIVLNVSGT RFQTWQDTLE
RYPDTLLGSS ERDFFYHPET QQYFFDRDPD IFRHILNFYR TGKLHYPRHE CISAYDEELA
FFGLIPEIIG DCCYEEYKDR RRENAERLQD DADTDTAGES ALPTMTARQR VWRAFENPHT
STMALVFYYV TGFFIAVSVI ANVVETVPCG SSPGHIKELP CGERYAVAFF CLDTACVMIF
TVEYLLRLAA APSRYRFVRS VMSIIDVVAI LPYYIGLVMT DNEDVSGAFV TLRVFRVFRI
FKFSRHSQGL RILGYTLKSC ASELGFLLFS LTMAIIIFAT VMFYAEKGSS ASKFTSIPAA
FWYTIVTMTT LGYGDMVPKT IAGKIFGSIC SLSGVLVIAL PVPVIVSNFS RIYHQNQRAD
KRRAQKKARL ARIRAAKSGS ANAYMQSKRN GLLSNQLQSS EDEQAFVSKS GSSFETQHHH
LLHCLEKTTN HEFVDEQVFE ESCMEVATVN RPSSHSPSLS SQQGVTSTCC SRRHKKTFRI
PNANVSGSHQ GSIQELSTIQ IRCVERTPLS NSRSSLNAKM EECVKLNCEQ PYVTTAIISI
PTPPVTTPEG DDRPESPEYS GGNIVRVSAL


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KCNA5_RAT Rat ELISA Kit FOR Potassium voltage-gated channel subfamily A member 5 96T
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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 :
[Kcnd2] Potassium voltage-gated channel subfamily D member 2 (RK5) (Shal1) (Voltage-gated potassium channel subunit Kv4.2)
[KCND2 KIAA1044] Potassium voltage-gated channel subfamily D member 2 (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)
[KCNC1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[KCND3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[Kcnd3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[Kcnd3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[KCND1] Potassium voltage-gated channel subfamily D member 1 (Voltage-gated potassium channel subunit Kv4.1)
[KCND2] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (RAW2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[Kcnc1] Potassium voltage-gated channel subfamily C member 1 (NGK2) (Voltage-gated potassium channel subunit Kv3.1) (Voltage-gated potassium channel subunit Kv4)
[KCND2] Potassium voltage-gated channel subfamily D member 2 (Voltage-gated potassium channel subunit Kv4.2)
[Kcnb1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[Kcnd1] Potassium voltage-gated channel subfamily D member 1 (Voltage-gated potassium channel subunit Kv4.1) (mShal)
[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)
[KCND3] Potassium voltage-gated channel subfamily D member 3 (Voltage-gated potassium channel subunit Kv4.3)
[Kcna5] Potassium voltage-gated channel subfamily A member 5 (Voltage-gated potassium channel subunit Kv1.5) (KV1-5)
[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)
[KCNA5] Potassium voltage-gated channel subfamily A member 5 (HPCN1) (Voltage-gated potassium channel HK2) (Voltage-gated potassium channel subunit Kv1.5)
[KCNQ2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Neuroblastoma-specific potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[Kcnq2] Potassium voltage-gated channel subfamily KQT member 2 (KQT-like 2) (Potassium channel subunit alpha KvLQT2) (Voltage-gated potassium channel subunit Kv7.2)
[KCNH3 KIAA1282] Potassium voltage-gated channel subfamily H member 3 (Brain-specific eag-like channel 1) (BEC1) (Ether-a-go-go-like potassium channel 2) (ELK channel 2) (ELK2) (Voltage-gated potassium channel subunit Kv12.2)
[KCNB1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (h-DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[KCNH6 ERG2] Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (hERG-2) (hERG2) (Voltage-gated potassium channel subunit Kv11.2)
[Kcnh6 Erg2] Potassium voltage-gated channel subfamily H member 6 (Ether-a-go-go-related gene potassium channel 2) (ERG-2) (Eag-related protein 2) (Ether-a-go-go-related protein 2) (Voltage-gated potassium channel subunit Kv11.2)
[KCNH2 ERG ERG1 HERG] Potassium voltage-gated channel subfamily H member 2 (Eag homolog) (Ether-a-go-go-related gene potassium channel 1) (ERG-1) (Eag-related protein 1) (Ether-a-go-go-related protein 1) (H-ERG) (hERG-1) (hERG1) (Voltage-gated potassium channel subunit Kv11.1)
[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)
[KCNB1] Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)
[KCNH5 EAG2] Potassium voltage-gated channel subfamily H member 5 (Ether-a-go-go potassium channel 2) (hEAG2) (Voltage-gated potassium channel subunit Kv10.2)

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