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Protein

Potassium voltage-gated channel subfamily C member 2

Gene

KCNC2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity2 Publications1 Publication

Enzyme regulationi

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).By similarity1 Publication1 Publication

Kineticsi

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.By similarity

1 Publication1 Publication

      GO - Molecular functioni

      GO - Biological processi

      Complete GO annotation...

      Keywords - Molecular functioni

      Ion channel, Potassium channel, Voltage-gated channel

      Keywords - Biological processi

      Ion transport, Potassium transport, Transport

      Keywords - Ligandi

      Potassium

      Enzyme and pathway databases

      ReactomeiREACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
      REACT_75770. Voltage gated Potassium channels.

      Names & Taxonomyi

      Protein namesi
      Recommended name:
      Potassium voltage-gated channel subfamily C member 2Imported
      Alternative name(s):
      Shaw-like potassium channelBy similarity
      Voltage-gated potassium channel Kv3.2By similarity
      Gene namesi
      Name:KCNC2Imported
      OrganismiHomo sapiens (Human)
      Taxonomic identifieri9606 [NCBI]
      Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
      ProteomesiUP000005640 Componenti: Chromosome 12

      Organism-specific databases

      HGNCiHGNC:6234. KCNC2.

      Subcellular locationi

      • Cell membrane 1 Publication; Multi-pass membrane protein Sequence Analysis
      • Membrane By similarity; Multi-pass membrane protein Sequence Analysis
      • Perikaryon By similarity
      • Cell projectionaxon By similarity
      • Cell projectiondendrite By similarity
      • Cell junctionsynapsepostsynaptic cell membrane By similarity
      • Cell junctionsynapsepresynaptic cell membrane By similarity
      • Cell junctionsynapsesynaptosome By similarity
      • Cell junctionsynapse By similarity
      • Apical cell membrane By similarity
      • Basolateral cell membrane By similarity

      • 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 thoughout 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.By similarity

      Topology

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Topological domaini1 – 229229CytoplasmicSequence AnalysisAdd
      BLAST
      Transmembranei230 – 25021Helical; Name=Segment S1Sequence AnalysisAdd
      BLAST
      Transmembranei284 – 30320Helical; Name=Segment S2Sequence AnalysisAdd
      BLAST
      Topological domaini304 – 31310CytoplasmicSequence Analysis
      Transmembranei314 – 33421Helical; Name=Segment S3Sequence AnalysisAdd
      BLAST
      Transmembranei346 – 36823Helical; Voltage-sensor; Name=Segment S4Sequence AnalysisAdd
      BLAST
      Topological domaini369 – 38113CytoplasmicSequence AnalysisAdd
      BLAST
      Transmembranei382 – 40221Helical; Name=Segment S5Sequence AnalysisAdd
      BLAST
      Transmembranei453 – 47321Helical; Name=Segment S6Sequence AnalysisAdd
      BLAST
      Topological domaini474 – 638165CytoplasmicSequence AnalysisAdd
      BLAST

      GO - Cellular componenti

      Complete GO annotation...

      Keywords - Cellular componenti

      Cell junction, Cell membrane, Cell projection, Membrane, Postsynaptic cell membrane, Synapse, Synaptosome

      Pathology & Biotechi

      Organism-specific databases

      PharmGKBiPA35490.

      Chemistry

      DrugBankiDB06637. Dalfampridine.

      Polymorphism and mutation databases

      BioMutaiKCNC2.
      DMDMi74752079.

      PTM / Processingi

      Molecule processing

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Chaini1 – 638638Potassium voltage-gated channel subfamily C member 2PRO_0000310416Add
      BLAST

      Amino acid modifications

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Glycosylationi259 – 2591N-linked (GlcNAc...)Sequence Analysis
      Glycosylationi266 – 2661N-linked (GlcNAc...)Sequence Analysis

      Post-translational modificationi

      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.By similarity

      Keywords - PTMi

      Glycoprotein

      Proteomic databases

      PaxDbiQ96PR1.
      PRIDEiQ96PR1.

      PTM databases

      PhosphoSiteiQ96PR1.

      Expressioni

      Gene expression databases

      BgeeiQ96PR1.
      CleanExiHS_KCNC2.
      ExpressionAtlasiQ96PR1. baseline and differential.
      GenevisibleiQ96PR1. HS.

      Organism-specific databases

      HPAiCAB022571.
      HPA019664.

      Interactioni

      Subunit structurei

      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.By similarity

      Protein-protein interaction databases

      BioGridi109949. 1 interaction.
      STRINGi9606.ENSP00000449253.

      Structurei

      3D structure databases

      ProteinModelPortaliQ96PR1.
      SMRiQ96PR1. Positions 9-480.
      ModBaseiSearch...
      MobiDBiSearch...

      Family & Domainsi

      Region

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Regioni437 – 4426Selectivity filterBy similarity

      Compositional bias

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Compositional biasi56 – 9944Gly/Pro-rich (insert)Add
      BLAST

      Domaini

      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.By similarity

      Sequence similaritiesi

      Keywords - Domaini

      Transmembrane, Transmembrane helix

      Phylogenomic databases

      eggNOGiCOG1226.
      GeneTreeiENSGT00760000118846.
      HOGENOMiHOG000231012.
      HOVERGENiHBG105862.
      InParanoidiQ96PR1.
      KOiK04888.
      OMAiMCLGKDN.
      OrthoDBiEOG7CRTPP.
      PhylomeDBiQ96PR1.
      TreeFamiTF352511.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. BTB/POZ-like.
      IPR011333. BTB/POZ_fold.
      IPR027359. Channel_four-helix_dom.
      IPR005821. Ion_trans_dom.
      IPR003091. K_chnl.
      IPR003968. K_chnl_volt-dep_Kv.
      IPR003974. K_chnl_volt-dep_Kv3.
      IPR003131. T1-type_BTB.
      IPR028325. VG_K_chnl.
      [Graphical view]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01491. KVCHANNEL.
      PR01498. SHAWCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 2 hits.

      Sequences (6)i

      Sequence statusi: Complete.

      This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

      Isoform 1 (identifier: Q96PR1-1) [UniParc]FASTAAdd to basket

      Also known as: Kv3.2b

      This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

      « Hide

              10         20         30         40         50
      MGKIENNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPPGDCLTTA
      60 70 80 90 100
      GDKLQPSPPP LSPPPRAPPL SPGPGGCFEG GAGNCSSRGG RASDHPGGGR
      110 120 130 140 150
      EFFFDRHPGV FAYVLNYYRT GKLHCPADVC GPLFEEELAF WGIDETDVEP
      160 170 180 190 200
      CCWMTYRQHR DAEEALDIFE TPDLIGGDPG DDEDLAAKRL GIEDAAGLGG
      210 220 230 240 250
      PDGKSGRWRR LQPRMWALFE DPYSSRAARF IAFASLFFIL VSITTFCLET
      260 270 280 290 300
      HEAFNIVKNK TEPVINGTSV VLQYEIETDP ALTYVEGVCV VWFTFEFLVR
      310 320 330 340 350
      IVFSPNKLEF IKNLLNIIDF VAILPFYLEV GLSGLSSKAA KDVLGFLRVV
      360 370 380 390 400
      RFVRILRIFK LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI
      410 420 430 440 450
      YYAERVGAQP NDPSASEHTQ FKNIPIGFWW AVVTMTTLGY GDMYPQTWSG
      460 470 480 490 500
      MLVGALCALA GVLTIAMPVP VIVNNFGMYY SLAMAKQKLP RKRKKHIPPA
      510 520 530 540 550
      PQASSPTFCK TELNMACNST QSDTCLGKDN RLLEHNRSVL SGDDSTGSEP
      560 570 580 590 600
      PLSPPERLPI RRSSTRDKNR RGETCFLLTT GDYTCASDGG IRKGYEKSRS
      610 620 630
      LNNIAGLAGN ALRLSPVTSP YNSPCPLRRS RSPIPSIL
      Length:638
      Mass (Da):70,226
      Last modified:December 1, 2001 - v1
      Checksum:i211CAF8395A58C5D
      GO
      Isoform 2 (identifier: Q96PR1-2) [UniParc]FASTAAdd to basket

      Also known as: Kv3.2d

      The sequence of this isoform differs from the canonical sequence as follows:
           594-638: GYEKSRSLNN...RSRSPIPSIL → VLYRIYHGLL...GNRLLLLNVP

      Show »
      Length:629
      Mass (Da):69,534
      Checksum:iBDDBF6DB6FA0A510
      GO
      Isoform 3 (identifier: Q96PR1-3) [UniParc]FASTAAdd to basket

      Also known as: Kv3.2a

      The sequence of this isoform differs from the canonical sequence as follows:
           594-638: GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL → DNCKEVVITGYTQAEARSLT

      Show »
      Length:613
      Mass (Da):67,600
      Checksum:iD6F4DA8E0659682D
      GO
      Isoform 4 (identifier: Q96PR1-4) [UniParc]FASTAAdd to basket

      Also known as: Kv3.2c

      The sequence of this isoform differs from the canonical sequence as follows:
           539-558: VLSGDDSTGSEPPLSPPERL → DNCKEVVITGYTQAEARSLT
           559-638: Missing.

      Show »
      Length:558
      Mass (Da):61,650
      Checksum:i86AC5B2DAF84AF1B
      GO
      Isoform 5 (identifier: Q96PR1-5) [UniParc]FASTAAdd to basket

      The sequence of this isoform differs from the canonical sequence as follows:
           539-593: Missing.

      Note: No experimental confirmation available.
      Show »
      Length:583
      Mass (Da):64,276
      Checksum:i65A3F7DFA2B7448D
      GO
      Isoform 6 (identifier: Q96PR1-6) [UniParc]FASTAAdd to basket

      The sequence of this isoform differs from the canonical sequence as follows:
           595-638: YEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPIPSIL → IRNGHSILHHLDNGTKCHYLRIIF

      Note: No experimental confirmation available.
      Show »
      Length:618
      Mass (Da):68,317
      Checksum:i6C333D045C6325C1
      GO

      Sequence cautioni

      The sequence BAE06076.1 differs from that shown. Reason: Erroneous initiation. Curated

      Experimental Info

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Sequence conflicti31 – 311G → V in AK309245 (PubMed:14702039).Curated
      Sequence conflicti305 – 3051P → S in BAE06076 (Ref. 4) Curated
      Sequence conflicti476 – 4761F → S in BAH11717 (PubMed:14702039).Curated
      Sequence conflicti487 – 4871Q → H in AK309245 (PubMed:14702039).Curated

      Alternative sequence

      Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
      Alternative sequencei539 – 59355Missing in isoform 5. 1 PublicationVSP_044742Add
      BLAST
      Alternative sequencei539 – 55820VLSGD…PPERL → DNCKEVVITGYTQAEARSLT in isoform 4. 2 PublicationsVSP_029269Add
      BLAST
      Alternative sequencei559 – 63880Missing in isoform 4. 2 PublicationsVSP_029270Add
      BLAST
      Alternative sequencei594 – 63845GYEKS…IPSIL → VLYRIYHGLLTAEKGTVEFS HTKDYTGNRLLLLNVP in isoform 2. 1 PublicationVSP_029271Add
      BLAST
      Alternative sequencei594 – 63845GYEKS…IPSIL → DNCKEVVITGYTQAEARSLT in isoform 3. 1 PublicationVSP_029272Add
      BLAST
      Alternative sequencei595 – 63844YEKSR…IPSIL → IRNGHSILHHLDNGTKCHYL RIIF in isoform 6. 1 PublicationVSP_046002Add
      BLAST

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AF268896 mRNA. Translation: AAL27272.1.
      AF268897 mRNA. Translation: AAL27273.1.
      AY243473 mRNA. Translation: AAO89503.1.
      AY118169 mRNA. Translation: AAM81577.1.
      AK094720 mRNA. Translation: BAC04407.1.
      AK294269 mRNA. Translation: BAH11717.1.
      AK309245 mRNA. No translation available.
      AB209994 mRNA. Translation: BAE06076.1. Different initiation.
      AC073525 Genomic DNA. No translation available.
      AC091534 Genomic DNA. No translation available.
      AC130405 Genomic DNA. No translation available.
      CH471054 Genomic DNA. Translation: EAW97287.1.
      CH471054 Genomic DNA. Translation: EAW97288.1.
      CH471054 Genomic DNA. Translation: EAW97289.1.
      CH471054 Genomic DNA. Translation: EAW97291.1.
      BC093635 mRNA. Translation: AAH93635.1.
      BC111991 mRNA. Translation: AAI11992.1.
      CCDSiCCDS58255.1. [Q96PR1-5]
      CCDS58256.1. [Q96PR1-2]
      CCDS58257.1. [Q96PR1-6]
      CCDS9005.1. [Q96PR1-3]
      CCDS9006.1. [Q96PR1-4]
      CCDS9007.1. [Q96PR1-1]
      RefSeqiNP_001247426.1. NM_001260497.1. [Q96PR1-6]
      NP_001247427.1. NM_001260498.1. [Q96PR1-2]
      NP_001247428.1. NM_001260499.1. [Q96PR1-5]
      NP_631874.1. NM_139136.3. [Q96PR1-3]
      NP_631875.1. NM_139137.3. [Q96PR1-1]
      NP_715624.1. NM_153748.2. [Q96PR1-4]
      XP_006719445.1. XM_006719382.2. [Q96PR1-3]
      XP_006719452.1. XM_006719389.2. [Q96PR1-4]
      UniGeneiHs.27214.
      Hs.741918.

      Genome annotation databases

      EnsembliENST00000350228; ENSP00000319877; ENSG00000166006. [Q96PR1-4]
      ENST00000393288; ENSP00000376966; ENSG00000166006. [Q96PR1-6]
      ENST00000540018; ENSP00000438423; ENSG00000166006. [Q96PR1-5]
      ENST00000549446; ENSP00000449253; ENSG00000166006.
      GeneIDi3747.
      KEGGihsa:3747.
      UCSCiuc001sxe.4. human. [Q96PR1-3]
      uc001sxf.4. human. [Q96PR1-4]
      uc001sxg.2. human. [Q96PR1-1]
      uc009zry.4. human. [Q96PR1-2]

      Keywords - Coding sequence diversityi

      Alternative splicing

      Cross-referencesi

      Sequence databases

      Select the link destinations:
      EMBLi
      GenBanki
      DDBJi
      Links Updated
      AF268896 mRNA. Translation: AAL27272.1.
      AF268897 mRNA. Translation: AAL27273.1.
      AY243473 mRNA. Translation: AAO89503.1.
      AY118169 mRNA. Translation: AAM81577.1.
      AK094720 mRNA. Translation: BAC04407.1.
      AK294269 mRNA. Translation: BAH11717.1.
      AK309245 mRNA. No translation available.
      AB209994 mRNA. Translation: BAE06076.1. Different initiation.
      AC073525 Genomic DNA. No translation available.
      AC091534 Genomic DNA. No translation available.
      AC130405 Genomic DNA. No translation available.
      CH471054 Genomic DNA. Translation: EAW97287.1.
      CH471054 Genomic DNA. Translation: EAW97288.1.
      CH471054 Genomic DNA. Translation: EAW97289.1.
      CH471054 Genomic DNA. Translation: EAW97291.1.
      BC093635 mRNA. Translation: AAH93635.1.
      BC111991 mRNA. Translation: AAI11992.1.
      CCDSiCCDS58255.1. [Q96PR1-5]
      CCDS58256.1. [Q96PR1-2]
      CCDS58257.1. [Q96PR1-6]
      CCDS9005.1. [Q96PR1-3]
      CCDS9006.1. [Q96PR1-4]
      CCDS9007.1. [Q96PR1-1]
      RefSeqiNP_001247426.1. NM_001260497.1. [Q96PR1-6]
      NP_001247427.1. NM_001260498.1. [Q96PR1-2]
      NP_001247428.1. NM_001260499.1. [Q96PR1-5]
      NP_631874.1. NM_139136.3. [Q96PR1-3]
      NP_631875.1. NM_139137.3. [Q96PR1-1]
      NP_715624.1. NM_153748.2. [Q96PR1-4]
      XP_006719445.1. XM_006719382.2. [Q96PR1-3]
      XP_006719452.1. XM_006719389.2. [Q96PR1-4]
      UniGeneiHs.27214.
      Hs.741918.

      3D structure databases

      ProteinModelPortaliQ96PR1.
      SMRiQ96PR1. Positions 9-480.
      ModBaseiSearch...
      MobiDBiSearch...

      Protein-protein interaction databases

      BioGridi109949. 1 interaction.
      STRINGi9606.ENSP00000449253.

      Chemistry

      ChEMBLiCHEMBL2362996.
      DrugBankiDB06637. Dalfampridine.
      GuidetoPHARMACOLOGYi549.

      PTM databases

      PhosphoSiteiQ96PR1.

      Polymorphism and mutation databases

      BioMutaiKCNC2.
      DMDMi74752079.

      Proteomic databases

      PaxDbiQ96PR1.
      PRIDEiQ96PR1.

      Protocols and materials databases

      Structural Biology KnowledgebaseSearch...

      Genome annotation databases

      EnsembliENST00000350228; ENSP00000319877; ENSG00000166006. [Q96PR1-4]
      ENST00000393288; ENSP00000376966; ENSG00000166006. [Q96PR1-6]
      ENST00000540018; ENSP00000438423; ENSG00000166006. [Q96PR1-5]
      ENST00000549446; ENSP00000449253; ENSG00000166006.
      GeneIDi3747.
      KEGGihsa:3747.
      UCSCiuc001sxe.4. human. [Q96PR1-3]
      uc001sxf.4. human. [Q96PR1-4]
      uc001sxg.2. human. [Q96PR1-1]
      uc009zry.4. human. [Q96PR1-2]

      Organism-specific databases

      CTDi3747.
      GeneCardsiGC12M075433.
      HGNCiHGNC:6234. KCNC2.
      HPAiCAB022571.
      HPA019664.
      MIMi176256. gene.
      neXtProtiNX_Q96PR1.
      PharmGKBiPA35490.
      GenAtlasiSearch...

      Phylogenomic databases

      eggNOGiCOG1226.
      GeneTreeiENSGT00760000118846.
      HOGENOMiHOG000231012.
      HOVERGENiHBG105862.
      InParanoidiQ96PR1.
      KOiK04888.
      OMAiMCLGKDN.
      OrthoDBiEOG7CRTPP.
      PhylomeDBiQ96PR1.
      TreeFamiTF352511.

      Enzyme and pathway databases

      ReactomeiREACT_18274. Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
      REACT_75770. Voltage gated Potassium channels.

      Miscellaneous databases

      GeneWikiiKCNC2.
      GenomeRNAii3747.
      NextBioi14663.
      PROiQ96PR1.
      SOURCEiSearch...

      Gene expression databases

      BgeeiQ96PR1.
      CleanExiHS_KCNC2.
      ExpressionAtlasiQ96PR1. baseline and differential.
      GenevisibleiQ96PR1. HS.

      Family and domain databases

      Gene3Di1.20.120.350. 1 hit.
      InterProiIPR000210. BTB/POZ-like.
      IPR011333. BTB/POZ_fold.
      IPR027359. Channel_four-helix_dom.
      IPR005821. Ion_trans_dom.
      IPR003091. K_chnl.
      IPR003968. K_chnl_volt-dep_Kv.
      IPR003974. K_chnl_volt-dep_Kv3.
      IPR003131. T1-type_BTB.
      IPR028325. VG_K_chnl.
      [Graphical view]
      PANTHERiPTHR11537. PTHR11537. 1 hit.
      PfamiPF02214. BTB_2. 1 hit.
      PF00520. Ion_trans. 1 hit.
      [Graphical view]
      PRINTSiPR00169. KCHANNEL.
      PR01491. KVCHANNEL.
      PR01498. SHAWCHANNEL.
      SMARTiSM00225. BTB. 1 hit.
      [Graphical view]
      SUPFAMiSSF54695. SSF54695. 2 hits.
      ProtoNetiSearch...

      Publicationsi

      « Hide 'large scale' publications
      1. "Localization of Shaw-related K+ channel genes on mouse and human chromosomes."
        Haas M., Ward D.C., Lee J., Roses A.D., Clarke V., D'Eustachio P., Lau D., Vega-Saenz de Miera E., Rudy B.
        Mamm. Genome 4:711-715(1993) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3).
      2. Isbrandt D., Pongs O.
        Submitted (JUN-2002) to the EMBL/GenBank/DDBJ databases
        Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
        Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
        , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
        Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4; 5 AND 6).
        Tissue: Amygdala and Thalamus.
      4. "Preparation of a set of expression-ready clones of mammalian long cDNAs encoding large proteins by the ORF trap cloning method."
        Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
        Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
        Tissue: Brain.
      5. "The finished DNA sequence of human chromosome 12."
        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.
        Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
        The MGC Project Team
        Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
        Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
        Tissue: Brain.
      8. Cited for: REVIEW.
      9. "Kv3 channels: voltage-gated K+ channels designed for high-frequency repetitive firing."
        Rudy B., McBain C.J.
        Trends Neurosci. 24:517-526(2001) [PubMed] [Europe PMC] [Abstract]
        Cited for: REVIEW.
      10. Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR LOCATION.

      Entry informationi

      Entry nameiKCNC2_HUMAN
      AccessioniPrimary (citable) accession number: Q96PR1
      Secondary accession number(s): B7Z231
      , F5H030, J3KPP5, Q4LE77, Q86W09, Q8N1V9, Q96PR0
      Entry historyi
      Integrated into UniProtKB/Swiss-Prot: November 13, 2007
      Last sequence update: December 1, 2001
      Last modified: July 22, 2015
      This is version 115 of the entry and version 1 of the sequence. [Complete history]
      Entry statusiReviewed (UniProtKB/Swiss-Prot)
      Annotation programChordata Protein Annotation Program
      DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

      Miscellaneousi

      Keywords - Technical termi

      Complete proteome, Reference proteome

      Documents

      1. Human chromosome 12
        Human chromosome 12: entries, gene names and cross-references to MIM
      2. MIM cross-references
        Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
      3. SIMILARITY comments
        Index of protein domains and families

      External Data

      Dasty 3

      Similar proteinsi

      Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
      100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
      90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
      50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.