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Potassium voltage-gated channel subfamily C member 2 (Shaw-like potassium channel) (Voltage-gated potassium channel Kv3.2)

 KCNC2_HUMAN             Reviewed;         638 AA.
Q96PR1; B7Z231; F5H030; J3KPP5; Q4LE77; Q86W09; Q8N1V9; Q96PR0;
13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
01-DEC-2001, sequence version 1.
18-JUL-2018, entry version 140.
RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|HGNC:HGNC:6234};
AltName: Full=Shaw-like potassium channel {ECO:0000250|UniProtKB:P22462};
AltName: Full=Voltage-gated potassium channel Kv3.2 {ECO:0000250|UniProtKB:P22462};
Name=KCNC2 {ECO:0000312|HGNC:HGNC:6234};
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
PubMed=8111118; DOI=10.1007/BF00357794;
Haas M., Ward D.C., Lee J., Roses A.D., Clarke V., D'Eustachio P.,
Lau D., Vega-Saenz de Miera E., Rudy B.;
"Localization of Shaw-related K+ channel genes on mouse and human
chromosomes.";
Mamm. Genome 4:711-715(1993).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Isbrandt D., Pongs O.;
Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
TISSUE=Amygdala, and Thalamus;
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).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M.,
Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.;
"Preparation of a set of expression-ready clones of mammalian long
cDNAs encoding large proteins by the ORF trap cloning method.";
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16541075; DOI=10.1038/nature04569;
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M.,
Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B.,
Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D.,
Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z.,
Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z.,
Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H.,
Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H.,
Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V.,
Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J.,
Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A.,
Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M.,
Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E.,
Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M.,
Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R.,
Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J.,
Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C.,
Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M.,
Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M.,
Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P.,
Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L.,
Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E.,
Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C.,
Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F.,
Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M.,
Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S.,
Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D.,
Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I.,
Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T.,
Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S.,
Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D.,
Kucherlapati R., Weinstock G., Gibbs R.A.;
"The finished DNA sequence of human chromosome 12.";
Nature 440:346-351(2006).
[6]
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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
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).
[8]
REVIEW.
PubMed=10414303; DOI=10.1111/j.1749-6632.1999.tb11295.x;
Rudy B., Chow A., Lau D., Amarillo Y., Ozaita A., Saganich M.,
Moreno H., Nadal M.S., Hernandez-Pineda R., Hernandez-Cruz A.,
Erisir A., Leonard C., Vega-Saenz de Miera E.;
"Contributions of Kv3 channels to neuronal excitability.";
Ann. N. Y. Acad. Sci. 868:304-343(1999).
[9]
REVIEW.
PubMed=11506885; DOI=10.1016/S0166-2236(00)01892-0;
Rudy B., McBain C.J.;
"Kv3 channels: voltage-gated K+ channels designed for high-frequency
repetitive firing.";
Trends Neurosci. 24:517-526(2001).
[10]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, AND
SUBCELLULAR LOCATION.
PubMed=15709110; DOI=10.1124/mol.105.011064;
Yan L., Herrington J., Goldberg E., Dulski P.M., Bugianesi R.M.,
Slaughter R.S., Banerjee P., Brochu R.M., Priest B.T.,
Kaczorowski G.J., Rudy B., Garcia M.L.;
"Stichodactyla helianthus peptide, a pharmacological tool for studying
Kv3.2 channels.";
Mol. Pharmacol. 67:1513-1521(2005).
[11]
CHROMOSOMAL REARRANGEMENT.
PubMed=23475819; DOI=10.1136/jnnp-2012-304555;
Rajakulendran S., Roberts J., Koltzenburg M., Hanna M.G., Stewart H.;
"Deletion of chromosome 12q21 affecting KCNC2 and ATXN7L3B in a family
with neurodevelopmental delay and ataxia.";
J. Neurol. Neurosurg. Psych. 84:1255-1257(2013).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain. Contributes to the regulation of the fast
action potential repolarization and in sustained high-frequency
firing in neurons of the central nervous system. Homotetramer
channels mediate delayed-rectifier voltage-dependent potassium
currents that activate rapidly at high-threshold voltages and
inactivate slowly. Forms tetrameric 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:15709110). Can form functional homotetrameric and
heterotetrameric channels that contain variable proportions of
KCNC1, and possibly other family members as well; channel
properties depend on the type of alpha subunits that are part of
the channel. Channel properties may be modulated either by the
association with ancillary subunits, such as KCNE1, KCNE2 or KCNE3
or indirectly by nitric oxide (NO) through a cGMP- and PKG-
mediated signaling cascade, slowing channel activation and
deactivation of delayed rectifier potassium channels (By
similarity). Contributes to fire sustained trains of very brief
action potentials at high frequency in retinal ganglion cells,
thalamocortical and suprachiasmatic nucleus (SCN) neurons and in
hippocampal and neocortical interneurons (PubMed:15709110).
Sustained maximal action potential firing frequency in inhibitory
hippocampal interneurons is negatively modulated by histamine H2
receptor activation in a cAMP- and protein kinase (PKA)
phosphorylation-dependent manner. Plays a role in maintaining the
fidelity of synaptic transmission in neocortical GABAergic
interneurons by generating action potential (AP) repolarization at
nerve terminals, thus reducing spike-evoked calcium influx and
GABA neurotransmitter release. Required for long-range
synchronization of gamma oscillations over distance in the
neocortex. Contributes to the modulation of the circadian rhythm
of spontaneous action potential firing in suprachiasmatic nucleus
(SCN) neurons in a light-dependent manner (By similarity).
{ECO:0000250|UniProtKB:P22462, ECO:0000250|UniProtKB:Q14B80,
ECO:0000269|PubMed:15709110, ECO:0000305|PubMed:10414303,
ECO:0000305|PubMed:11506885}.
-!- ENZYME REGULATION: Inhibited by Stichodactyla helianthus peptide
ShK (PubMed:15709110). Inhibited by millimolar levels of
tetraethylammonium (TEA). Contrary to other channels, inhibited
only by millimolar levels of 4-aminopyridine (4-AP) (By
similarity). {ECO:0000250|UniProtKB:P22462,
ECO:0000269|PubMed:15709110, ECO:0000305|PubMed:10414303}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels expressed in xenopus oocytes or in
mammalian non-neuronal cells display delayed-rectifier voltage-
dependent potassium currents, that are rapidly activated during
membrane depolarization, i.e within a risetime of a few msec.
After that, inactivates very slowly, i.e within about >800 msec.
Their activation requires a threshold potential at about -10 mV,
with a midpoint activation at about 12.1 mV and a steepness
parameter of about 8.4 mV. The voltage-dependence of activation
and inactivation and other channel characteristics vary
depending on the experimental conditions, the expression system,
the presence or absence of ancillary subunits and post-
translational modifications. {ECO:0000250|UniProtKB:P22462,
ECO:0000269|PubMed:15709110, ECO:0000305|PubMed:10414303};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNC1. Interacts with KCNC1.
Homotetramer or heterotetramer channel activity is regulated by
association with modulating ancillary subunits such as KCNE1,
KCNE2 and KCNE3, creating a functionally diverse range of channel
complexes. Interacts with KCNE1, KCNE2 and KCNE3.
{ECO:0000250|UniProtKB:P22462, ECO:0000250|UniProtKB:Q14B80}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15709110};
Multi-pass membrane protein {ECO:0000255}. Membrane
{ECO:0000250|UniProtKB:Q14B80}; Multi-pass membrane protein
{ECO:0000255}. Perikaryon {ECO:0000250|UniProtKB:Q14B80}. Cell
projection, axon {ECO:0000250|UniProtKB:Q14B80}. Cell projection,
dendrite {ECO:0000250|UniProtKB:Q14B80}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:Q14B80}. Cell
junction, synapse, presynaptic cell membrane
{ECO:0000250|UniProtKB:Q14B80}. Cell junction, synapse,
synaptosome {ECO:0000250|UniProtKB:P22462}. Cell junction, synapse
{ECO:0000250|UniProtKB:P22462}. Apical cell membrane
{ECO:0000250|UniProtKB:P22462}. Basolateral cell membrane
{ECO:0000250|UniProtKB:P22462}. Note=Colocalizes with parvalbumin
in globus pallidus neurons. Localizes in thalamocortical axons and
synapses. Localizes on the surface of cell somata, proximal
dendrites and axonal membranes. Also detected throughout the
neuropil. Localized in starburst cell somata and proximal dendrite
processes. Colocalized with GABA in presynaptic terminals.
Clustered in patches in somatic and proximal dendritic membrane as
well as in axons and presnypatic terminals of GABAergic
interneurons; some of these patches are found near postsynaptic
sites. {ECO:0000250|UniProtKB:P22462,
ECO:0000250|UniProtKB:Q14B80}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Kv3.2b;
IsoId=Q96PR1-1; Sequence=Displayed;
Name=2; Synonyms=Kv3.2d;
IsoId=Q96PR1-2; Sequence=VSP_029271;
Name=3; Synonyms=Kv3.2a;
IsoId=Q96PR1-3; Sequence=VSP_029272;
Name=4; Synonyms=Kv3.2c;
IsoId=Q96PR1-4; Sequence=VSP_029269, VSP_029270;
Name=5;
IsoId=Q96PR1-5; Sequence=VSP_044742;
Note=No experimental confirmation available.;
Name=6;
IsoId=Q96PR1-6; Sequence=VSP_046002;
Note=No experimental confirmation available.;
-!- 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 by PKA in cortical synaptosomes. cAMP-
dependent phosphorylation inhibits channel activity (By
similarity). Histamine H2 receptor- and PKA-induced
phosphorylation extends action potential spike duration, reduces
action potential spike amplitude, sustains maximum firing
frequency in hippocampal interneurons; also reduces the incidence
of high-frequency oscillations in hippocampal CA3 pyramidal cell
layers. {ECO:0000250|UniProtKB:P22462,
ECO:0000250|UniProtKB:Q14B80}.
-!- DISEASE: Note=A chromosomal aberration involving KCNC2 has been
found in a mother and her two children with varying degrees of
neurodevelopmental delay and cerebellar ataxia. One child also
exhibits episodes of unresponsiveness suggestive of absence
seizures and facial dysmorphism. Deletion at 12q21.1 deletes exons
3-5 of KCNC2. {ECO:0000269|PubMed:23475819}.
-!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAE06076.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF268896; AAL27272.1; -; mRNA.
EMBL; AF268897; AAL27273.1; -; mRNA.
EMBL; AY243473; AAO89503.1; -; mRNA.
EMBL; AY118169; AAM81577.1; -; mRNA.
EMBL; AK094720; BAC04407.1; -; mRNA.
EMBL; AK294269; BAH11717.1; -; mRNA.
EMBL; AK309245; -; NOT_ANNOTATED_CDS; mRNA.
EMBL; AB209994; BAE06076.1; ALT_INIT; mRNA.
EMBL; AC073525; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC091534; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC130405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471054; EAW97287.1; -; Genomic_DNA.
EMBL; CH471054; EAW97288.1; -; Genomic_DNA.
EMBL; CH471054; EAW97289.1; -; Genomic_DNA.
EMBL; CH471054; EAW97291.1; -; Genomic_DNA.
EMBL; BC093635; AAH93635.1; -; mRNA.
EMBL; BC111991; AAI11992.1; -; mRNA.
CCDS; CCDS58255.1; -. [Q96PR1-5]
CCDS; CCDS58256.1; -. [Q96PR1-2]
CCDS; CCDS58257.1; -. [Q96PR1-6]
CCDS; CCDS9005.1; -. [Q96PR1-3]
CCDS; CCDS9006.1; -. [Q96PR1-4]
CCDS; CCDS9007.1; -. [Q96PR1-1]
RefSeq; NP_001247426.1; NM_001260497.1. [Q96PR1-6]
RefSeq; NP_001247427.1; NM_001260498.1. [Q96PR1-2]
RefSeq; NP_001247428.1; NM_001260499.1. [Q96PR1-5]
RefSeq; NP_631874.1; NM_139136.3. [Q96PR1-3]
RefSeq; NP_631875.1; NM_139137.3. [Q96PR1-1]
RefSeq; NP_715624.1; NM_153748.2. [Q96PR1-4]
RefSeq; XP_006719445.1; XM_006719382.3. [Q96PR1-3]
UniGene; Hs.27214; -.
UniGene; Hs.741918; -.
ProteinModelPortal; Q96PR1; -.
BioGrid; 109949; 1.
STRING; 9606.ENSP00000449253; -.
ChEMBL; CHEMBL2362996; -.
DrugBank; DB06637; Dalfampridine.
GuidetoPHARMACOLOGY; 549; -.
iPTMnet; Q96PR1; -.
PhosphoSitePlus; Q96PR1; -.
BioMuta; KCNC2; -.
DMDM; 74752079; -.
EPD; Q96PR1; -.
PaxDb; Q96PR1; -.
PeptideAtlas; Q96PR1; -.
PRIDE; Q96PR1; -.
ProteomicsDB; 77738; -.
ProteomicsDB; 77739; -. [Q96PR1-2]
ProteomicsDB; 77740; -. [Q96PR1-3]
ProteomicsDB; 77741; -. [Q96PR1-4]
TopDownProteomics; Q96PR1-4; -. [Q96PR1-4]
Ensembl; ENST00000298972; ENSP00000298972; ENSG00000166006. [Q96PR1-3]
Ensembl; ENST00000350228; ENSP00000319877; ENSG00000166006. [Q96PR1-4]
Ensembl; ENST00000393288; ENSP00000376966; ENSG00000166006. [Q96PR1-6]
Ensembl; ENST00000540018; ENSP00000438423; ENSG00000166006. [Q96PR1-5]
Ensembl; ENST00000548513; ENSP00000449941; ENSG00000166006. [Q96PR1-3]
Ensembl; ENST00000549446; ENSP00000449253; ENSG00000166006. [Q96PR1-1]
Ensembl; ENST00000550433; ENSP00000448301; ENSG00000166006. [Q96PR1-2]
GeneID; 3747; -.
KEGG; hsa:3747; -.
UCSC; uc001sxe.5; human. [Q96PR1-1]
CTD; 3747; -.
DisGeNET; 3747; -.
EuPathDB; HostDB:ENSG00000166006.12; -.
GeneCards; KCNC2; -.
HGNC; HGNC:6234; KCNC2.
HPA; CAB022571; -.
HPA; HPA019664; -.
MIM; 176256; gene.
neXtProt; NX_Q96PR1; -.
OpenTargets; ENSG00000166006; -.
PharmGKB; PA35490; -.
eggNOG; KOG3713; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231012; -.
HOVERGEN; HBG105862; -.
InParanoid; Q96PR1; -.
KO; K04888; -.
OMA; DLNMACN; -.
OrthoDB; EOG091G0EJL; -.
PhylomeDB; Q96PR1; -.
TreeFam; TF352511; -.
Reactome; R-HSA-1296072; Voltage gated Potassium channels.
Reactome; R-HSA-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
ChiTaRS; KCNC2; human.
GeneWiki; KCNC2; -.
GenomeRNAi; 3747; -.
PRO; PR:Q96PR1; -.
Proteomes; UP000005640; Chromosome 12.
Bgee; ENSG00000166006; -.
CleanEx; HS_KCNC2; -.
ExpressionAtlas; Q96PR1; baseline and differential.
Genevisible; Q96PR1; HS.
GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
GO; GO:0030673; C:axolemma; IEA:Ensembl.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0016020; C:membrane; ISS:UniProtKB.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; ISS:UniProtKB.
GO; GO:0043195; C:terminal bouton; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IEA:Ensembl.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0005249; F:voltage-gated potassium channel activity; ISS:UniProtKB.
GO; GO:0071242; P:cellular response to ammonium ion; IEA:Ensembl.
GO; GO:0071732; P:cellular response to nitric oxide; ISS:UniProtKB.
GO; GO:0097237; P:cellular response to toxic substance; IEA:Ensembl.
GO; GO:0021759; P:globus pallidus development; IEA:Ensembl.
GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; ISS:UniProtKB.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IEA:Ensembl.
GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; ISS:UniProtKB.
GO; GO:0050796; P:regulation of insulin secretion; TAS:Reactome.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0045471; P:response to ethanol; IEA:Ensembl.
GO; GO:0009642; P:response to light intensity; IEA:Ensembl.
GO; GO:0032026; P:response to magnesium ion; IEA:Ensembl.
GO; GO:1990089; P:response to nerve growth factor; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003974; K_chnl_volt-dep_Kv3.
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; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01498; SHAWCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 2.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Chromosomal rearrangement; Complete proteome; Glycoprotein;
Ion channel; Ion transport; Membrane; Phosphoprotein;
Postsynaptic cell membrane; Potassium; Potassium channel;
Potassium transport; Reference proteome; Synapse; Synaptosome;
Transmembrane; Transmembrane helix; Transport; Voltage-gated channel.
CHAIN 1 638 Potassium voltage-gated channel subfamily
C member 2.
/FTId=PRO_0000310416.
TOPO_DOM 1 229 Cytoplasmic. {ECO:0000255}.
TRANSMEM 230 250 Helical; Name=Segment S1. {ECO:0000255}.
TRANSMEM 284 303 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 304 313 Cytoplasmic. {ECO:0000255}.
TRANSMEM 314 334 Helical; Name=Segment S3. {ECO:0000255}.
TRANSMEM 346 368 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 369 381 Cytoplasmic. {ECO:0000255}.
TRANSMEM 382 402 Helical; Name=Segment S5. {ECO:0000255}.
TRANSMEM 453 473 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 474 638 Cytoplasmic. {ECO:0000255}.
REGION 437 442 Selectivity filter. {ECO:0000250}.
COMPBIAS 56 99 Gly/Pro-rich (insert).
MOD_RES 600 600 Phosphoserine.
{ECO:0000250|UniProtKB:Q14B80}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 539 593 Missing (in isoform 5).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044742.
VAR_SEQ 539 558 VLSGDDSTGSEPPLSPPERL -> DNCKEVVITGYTQAEAR
SLT (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_029269.
VAR_SEQ 559 638 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_029270.
VAR_SEQ 594 638 GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPI
PSIL -> VLYRIYHGLLTAEKGTVEFSHTKDYTGNRLLLL
NVP (in isoform 2).
{ECO:0000303|PubMed:8111118}.
/FTId=VSP_029271.
VAR_SEQ 594 638 GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPI
PSIL -> DNCKEVVITGYTQAEARSLT (in isoform
3). {ECO:0000303|PubMed:8111118}.
/FTId=VSP_029272.
VAR_SEQ 595 638 YEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIP
SIL -> IRNGHSILHHLDNGTKCHYLRIIF (in
isoform 6).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_046002.
CONFLICT 31 31 G -> V (in Ref. 3; AK309245).
{ECO:0000305}.
CONFLICT 305 305 P -> S (in Ref. 4; BAE06076).
{ECO:0000305}.
CONFLICT 476 476 F -> S (in Ref. 3; BAH11717).
{ECO:0000305}.
CONFLICT 487 487 Q -> H (in Ref. 3; AK309245).
{ECO:0000305}.
SEQUENCE 638 AA; 70226 MW; 211CAF8395A58C5D CRC64;
MGKIENNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPPGDCLTTA GDKLQPSPPP
LSPPPRAPPL SPGPGGCFEG GAGNCSSRGG RASDHPGGGR EFFFDRHPGV FAYVLNYYRT
GKLHCPADVC GPLFEEELAF WGIDETDVEP CCWMTYRQHR DAEEALDIFE TPDLIGGDPG
DDEDLAAKRL GIEDAAGLGG PDGKSGRWRR LQPRMWALFE DPYSSRAARF IAFASLFFIL
VSITTFCLET HEAFNIVKNK TEPVINGTSV VLQYEIETDP ALTYVEGVCV VWFTFEFLVR
IVFSPNKLEF IKNLLNIIDF VAILPFYLEV GLSGLSSKAA KDVLGFLRVV RFVRILRIFK
LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI YYAERVGAQP NDPSASEHTQ
FKNIPIGFWW AVVTMTTLGY GDMYPQTWSG MLVGALCALA GVLTIAMPVP VIVNNFGMYY
SLAMAKQKLP RKRKKHIPPA PQASSPTFCK TELNMACNST QSDTCLGKDN RLLEHNRSVL
SGDDSTGSEP PLSPPERLPI RRSSTRDKNR RGETCFLLTT GDYTCASDGG IRKGYEKSRS
LNNIAGLAGN ALRLSPVTSP YNSPCPLRRS RSPIPSIL


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