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Protein

Potassium voltage-gated channel subfamily A member 2

Gene

KCNA2

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 and the central nervous system, but also in the cardiovascular system. Prevents aberrant action potential firing and regulates neuronal output. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response to the voltage difference across the membrane (PubMed:19912772, PubMed:8495559, PubMed:11211111, PubMed:23769686). Can form functional homotetrameric channels and heterotetrameric channels that contain variable proportions of KCNA1, KCNA2, KCNA4, KCNA5, KCNA6, KCNA7, and possibly other family members as well; channel properties depend on the type of alpha subunits that are part of the channel (PubMed:8495559, PubMed:20220134). Channel properties are modulated by cytoplasmic beta subunits that regulate the subcellular location of the alpha subunits and promote rapid inactivation of delayed rectifier potassium channels. In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to any particular potassium channel family member. Homotetrameric KCNA2 forms a delayed-rectifier potassium channel that opens in response to membrane depolarization, followed by slow spontaneous channel closure (PubMed:19912772, PubMed:23769686). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559). Regulates neuronal excitability and plays a role as pacemaker in the regulation of neuronal action potentials (By similarity). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (By similarity). Response to toxins that are selective for KCNA2-containing potassium channels suggests that in Purkinje cells, dendritic subthreshold KCNA2-containing potassium channels prevent random spontaneous calcium spikes, suppressing dendritic hyperexcitability without hindering the generation of somatic action potentials, and thereby play an important role in motor coordination (By similarity). Plays a role in the induction of long-term potentiation of neuron excitability in the CA3 layer of the hippocampus (By similarity). May function as down-stream effector for G protein-coupled receptors and inhibit GABAergic inputs to basolateral amygdala neurons (By similarity). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (By similarity). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (By similarity). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (By similarity). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (By similarity).By similarityCurated5 Publications

Enzyme regulationi

Inhibited by 4-aminopyridine (4-AP) and charybdotoxin (CTX), but not by tetraethylammonium (TEA) (PubMed:19912772). Inhibited by dendrotoxin (DTX) (By similarity). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly specific for KCNA2 (By similarity). Inhibited by maurotoxin (By similarity). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-RIIIK; kappaM-RIIIJ has much higher affinity for channels containing KCNA2 than kappaM-RIIIK, with the exception of heterodimers formed by KCNA2 and KCNA7 where the opposite is true (PubMed:20220134).By similarity2 Publications

Kineticsi

Homotetrameric channels activate rapidly, i.e within a few msec, but inactivation is very slow, with only a marginal decrease in conductance over several seconds. The voltage-dependence of activation and inactivation and other channel characteristics vary depending on the experimental conditions, the expression system, post-translational modifications and the presence or absence of ancillary subunits. For the activation of homotetrameric channels expressed in xenopus oocytes, the threshold is at about -30 mV and the midpoint at about -5 mV.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei252 – 2521Important for normal, slow channel gatingBy similarity

    GO - Molecular functioni

    1. delayed rectifier potassium channel activity Source: UniProtKB
    2. outward rectifier potassium channel activity Source: Ensembl
    3. potassium channel activity Source: ProtInc
    4. voltage-gated potassium channel activity Source: UniProtKB

    GO - Biological processi

    1. neuronal action potential Source: UniProtKB
    2. optic nerve structural organization Source: Ensembl
    3. potassium ion transmembrane transport Source: UniProtKB
    4. potassium ion transport Source: ProtInc
    5. protein homooligomerization Source: InterPro
    6. regulation of dopamine secretion Source: UniProtKB
    7. sensory perception of pain Source: UniProtKB
    8. synaptic transmission Source: Reactome
    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_75770. Voltage gated Potassium channels.

    Protein family/group databases

    TCDBi1.A.1.2.10. the voltage-gated ion channel (vic) superfamily.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Potassium voltage-gated channel subfamily A member 2
    Alternative name(s):
    NGK1
    Voltage-gated K(+) channel HuKIV1 Publication
    Voltage-gated potassium channel HBK5
    Voltage-gated potassium channel subunit Kv1.2
    Gene namesi
    Name:KCNA2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640 Componenti: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:6220. KCNA2.

    Subcellular locationi

    1. Cell membrane 5 Publications; Multi-pass membrane protein By similarityCurated
    2. Membrane By similarity
    3. Cell projectionaxon 1 Publication
    4. Cell junctionsynapse By similarity
    5. Endoplasmic reticulum membrane By similarity
    6. Cell projectionlamellipodium membrane By similarity
    7. Cell junctionsynapsesynaptosome By similarity
    8. Cell junctionsynapsepresynaptic cell membrane By similarity
    9. Cell projectiondendrite By similarity

    10. Note: KCNA2 by itself is detected both at the endoplasmic reticulum and at the cell membrane. Coexpression with KCNA4 or with beta subunits promotes expression at the cell membrane. Coexpression with KCNA1 inhibits cell surface expression.By similarity

    Topology

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 160160CytoplasmicBy similarityAdd
    BLAST
    Transmembranei161 – 18222Helical; Name=Segment S1By similarityAdd
    BLAST
    Topological domaini183 – 22139ExtracellularBy similarityAdd
    BLAST
    Transmembranei222 – 24322Helical; Name=Segment S2By similarityAdd
    BLAST
    Topological domaini244 – 25411CytoplasmicBy similarityAdd
    BLAST
    Transmembranei255 – 27521Helical; Name=Segment S3By similarityAdd
    BLAST
    Topological domaini276 – 28914ExtracellularBy similarityAdd
    BLAST
    Transmembranei290 – 31021Helical; Voltage-sensor; Name=Segment S4By similarityAdd
    BLAST
    Topological domaini311 – 32515CytoplasmicBy similarityAdd
    BLAST
    Transmembranei326 – 34722Helical; Name=Segment S5By similarityAdd
    BLAST
    Topological domaini348 – 36114ExtracellularBy similarityAdd
    BLAST
    Intramembranei362 – 37312Helical; Name=Pore helixBy similarityAdd
    BLAST
    Intramembranei374 – 3818By similarity
    Topological domaini382 – 3887ExtracellularBy similarity
    Transmembranei389 – 41729Helical; Name=Segment S6By similarityAdd
    BLAST
    Topological domaini418 – 49982CytoplasmicBy similarityAdd
    BLAST

    GO - Cellular componenti

    1. axon Source: UniProtKB
    2. axon terminus Source: UniProtKB
    3. cell junction Source: UniProtKB-KW
    4. dendrite Source: UniProtKB
    5. endoplasmic reticulum membrane Source: UniProtKB-SubCell
    6. integral component of membrane Source: GO_Central
    7. integral component of plasma membrane Source: UniProtKB
    8. juxtaparanode region of axon Source: BHF-UCL
    9. lamellipodium Source: UniProtKB
    10. lamellipodium membrane Source: UniProtKB-SubCell
    11. neuronal cell body membrane Source: UniProtKB
    12. perikaryon Source: UniProtKB
    13. plasma membrane Source: Reactome
    14. presynaptic membrane Source: UniProtKB-SubCell
    15. voltage-gated potassium channel complex Source: UniProtKB
    Complete GO annotation...

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Endoplasmic reticulum, Membrane, Synapse, Synaptosome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA206.

    Chemistry

    DrugBankiDB06637. Dalfampridine.

    Polymorphism and mutation databases

    BioMutaiKCNA2.
    DMDMi1345813.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 499499Potassium voltage-gated channel subfamily A member 2PRO_0000053972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Lipidationi244 – 2441S-palmitoyl cysteineSequence Analysis
    Modified residuei429 – 4291PhosphotyrosineBy similarity
    Modified residuei440 – 4401PhosphoserineBy similarity
    Modified residuei441 – 4411PhosphoserineBy similarity
    Modified residuei449 – 4491PhosphoserineBy similarity
    Modified residuei458 – 4581PhosphotyrosineBy similarity

    Post-translational modificationi

    Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (By similarity). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (By similarity). Phosphorylation on tyrosine residues suppresses ion channel activity (By similarity). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN. This is probably due to endocytosis of the phosphorylated channnel subunits (By similarity). Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (By similarity).By similarity
    N-glycosylated, with complex, sialylated N-glycans.By similarity

    Keywords - PTMi

    Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

    Proteomic databases

    MaxQBiP16389.
    PaxDbiP16389.
    PRIDEiP16389.

    PTM databases

    PhosphoSiteiP16389.

    Expressioni

    Tissue specificityi

    Detected in brain cortex (PubMed:16473933). Detected in peroneal nerve in the juxtaparanodal regions of the node of Ranvier; expression is decreased in patients with diabetes mellitus that suffer from axonal neuropathy (PubMed:22649228). Detected in paranodal and juxtanodal zones in myelinated spinal cord (at protein level) (PubMed:11086297).3 Publications

    Gene expression databases

    BgeeiP16389.
    CleanExiHS_KCNA2.
    ExpressionAtlasiP16389. baseline and differential.
    GenevestigatoriP16389.

    Organism-specific databases

    HPAiCAB001976.

    Interactioni

    Subunit structurei

    Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and KCNA7. Channel activity is regulated by interaction with the beta subunits, including KCNAB1 and KCNAB2. Identified in a complex with KCNA1 and KCNAB2 (PubMed:11086297). Identified in a complex with KCNA5 and KCNAB1 (By similarity). Identified in a complex with KCNA4 and FYN (By similarity). Interacts with the beta subunit KCNAB1 (PubMed:19713757). Interacts with PTK2B (By similarity). Interacts (via C-terminus) with CTTN (By similarity). Interacts (via N-terminal cytoplasmic domain) with RHOA (GTP-bound form); this regulates channel activity by reducing location at the cell surface in response to CHRM1 activation (By similarity). Interacts with DRD2 (By similarity). Interacts with SIGMAR1; cocaine consumption leads to increased interaction (By similarity). Interacts with ADAM22 (By similarity). Interacts (via C-terminus) with the PDZ domains of DLG1, DLG2 and DLG4 (By similarity). Interacts with CNTNAP2 (PubMed:10624965).By similarityCurated4 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    CAMLGP490693EBI-10210559,EBI-1748958

    Protein-protein interaction databases

    BioGridi109940. 17 interactions.
    IntActiP16389. 1 interaction.
    STRINGi9606.ENSP00000314520.

    Structurei

    3D structure databases

    ProteinModelPortaliP16389.
    SMRiP16389. Positions 3-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 125125Tetramerization domainBy similarityAdd
    BLAST
    Regioni312 – 32514S4-S5 linkerBy similarityAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi374 – 3796Selectivity filterBy similarity
    Motifi497 – 4993PDZ-bindingBy similarity

    Domaini

    The cytoplasmic N-terminus is important for tetramerization. Interactions between the different subunits modulate the gating characteristics (By similarity). Besides, the cytoplasmic N-terminal domain mediates interaction with RHOA and thus is required for RHOA-mediated endocytosis (By similarity).By similarity
    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.
    HOGENOMiHOG000231015.
    HOVERGENiHBG052230.
    InParanoidiP16389.
    KOiK04875.
    OMAiMTFHTYS.
    OrthoDBiEOG7M0NRD.
    PhylomeDBiP16389.
    TreeFamiTF313103.

    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.
    IPR003972. K_chnl_volt-dep_Kv1.
    IPR004049. K_chnl_volt-dep_Kv1.2.
    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.
    PR01509. KV12CHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

    Isoform 1 (identifier: P16389-1) [UniParc]FASTAAdd to basket

    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
    MTVATGDPAD EAAALPGHPQ DTYDPEADHE CCERVVINIS GLRFETQLKT
    60 70 80 90 100
    LAQFPETLLG DPKKRMRYFD PLRNEYFFDR NRPSFDAILY YYQSGGRLRR
    110 120 130 140 150
    PVNVPLDIFS EEIRFYELGE EAMEMFREDE GYIKEEERPL PENEFQRQVW
    160 170 180 190 200
    LLFEYPESSG PARIIAIVSV MVILISIVSF CLETLPIFRD ENEDMHGSGV
    210 220 230 240 250
    TFHTYSNSTI GYQQSTSFTD PFFIVETLCI IWFSFEFLVR FFACPSKAGF
    260 270 280 290 300
    FTNIMNIIDI VAIIPYFITL GTELAEKPED AQQGQQAMSL AILRVIRLVR
    310 320 330 340 350
    VFRIFKLSRH SKGLQILGQT LKASMRELGL LIFFLFIGVI LFSSAVYFAE
    360 370 380 390 400
    ADERESQFPS IPDAFWWAVV SMTTVGYGDM VPTTIGGKIV GSLCAIAGVL
    410 420 430 440 450
    TIALPVPVIV SNFNYFYHRE TEGEEQAQYL QVTSCPKIPS SPDLKKSRSA
    460 470 480 490
    STISKSDYME IQEGVNNSNE DFREENLKTA NCTLANTNYV NITKMLTDV
    Length:499
    Mass (Da):56,717
    Last modified:February 1, 1996 - v2
    Checksum:i4B03F1B46A826C39
    GO
    Isoform 2 (identifier: P16389-2) [UniParc]FASTAAdd to basket

    The sequence of this isoform differs from the canonical sequence as follows:
         299-499: VRVFRIFKLS...VNITKMLTDV → ERRPLQSQKS...PAVTTLHRMY

    Note: No experimental confirmation available.

    Show »
    Length:356
    Mass (Da):40,966
    Checksum:i9917ABBFCCCF7411
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti230 – 2301I → V in BAF82750 (PubMed:14702039).Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei299 – 499201VRVFR…MLTDV → ERRPLQSQKSKRGRQHLNTS HDCTLGINLVAGMTVQWTRA SGPDDRQTPAVTTLHRMY in isoform 2. 1 PublicationVSP_043077Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L02752 mRNA. Translation: AAA36141.1.
    AK290061 mRNA. Translation: BAF82750.1.
    AL365361 Genomic DNA. Translation: CAH71982.1.
    CH471122 Genomic DNA. Translation: EAW56455.1.
    CH471122 Genomic DNA. Translation: EAW56456.1.
    BC043564 mRNA. Translation: AAH43564.1.
    CCDSiCCDS55625.1. [P16389-2]
    CCDS827.1. [P16389-1]
    PIRiI77466.
    RefSeqiNP_001191198.1. NM_001204269.1. [P16389-2]
    NP_004965.1. NM_004974.3. [P16389-1]
    UniGeneiHs.248139.
    Hs.657199.
    Hs.731191.

    Genome annotation databases

    EnsembliENST00000316361; ENSP00000314520; ENSG00000177301. [P16389-1]
    ENST00000369770; ENSP00000358785; ENSG00000177301. [P16389-2]
    ENST00000485317; ENSP00000433109; ENSG00000177301. [P16389-1]
    GeneIDi3737.
    KEGGihsa:3737.
    UCSCiuc009wfv.2. human. [P16389-2]
    uc009wfw.3. human. [P16389-1]

    Polymorphism and mutation databases

    BioMutaiKCNA2.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    L02752 mRNA. Translation: AAA36141.1.
    AK290061 mRNA. Translation: BAF82750.1.
    AL365361 Genomic DNA. Translation: CAH71982.1.
    CH471122 Genomic DNA. Translation: EAW56455.1.
    CH471122 Genomic DNA. Translation: EAW56456.1.
    BC043564 mRNA. Translation: AAH43564.1.
    CCDSiCCDS55625.1. [P16389-2]
    CCDS827.1. [P16389-1]
    PIRiI77466.
    RefSeqiNP_001191198.1. NM_001204269.1. [P16389-2]
    NP_004965.1. NM_004974.3. [P16389-1]
    UniGeneiHs.248139.
    Hs.657199.
    Hs.731191.

    3D structure databases

    ProteinModelPortaliP16389.
    SMRiP16389. Positions 3-421.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi109940. 17 interactions.
    IntActiP16389. 1 interaction.
    STRINGi9606.ENSP00000314520.

    Chemistry

    BindingDBiP16389.
    ChEMBLiCHEMBL2086.
    DrugBankiDB06637. Dalfampridine.
    GuidetoPHARMACOLOGYi539.

    Protein family/group databases

    TCDBi1.A.1.2.10. the voltage-gated ion channel (vic) superfamily.

    PTM databases

    PhosphoSiteiP16389.

    Polymorphism and mutation databases

    BioMutaiKCNA2.
    DMDMi1345813.

    Proteomic databases

    MaxQBiP16389.
    PaxDbiP16389.
    PRIDEiP16389.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsembliENST00000316361; ENSP00000314520; ENSG00000177301. [P16389-1]
    ENST00000369770; ENSP00000358785; ENSG00000177301. [P16389-2]
    ENST00000485317; ENSP00000433109; ENSG00000177301. [P16389-1]
    GeneIDi3737.
    KEGGihsa:3737.
    UCSCiuc009wfv.2. human. [P16389-2]
    uc009wfw.3. human. [P16389-1]

    Organism-specific databases

    CTDi3737.
    GeneCardsiGC01M111137.
    HGNCiHGNC:6220. KCNA2.
    HPAiCAB001976.
    MIMi176262. gene.
    neXtProtiNX_P16389.
    PharmGKBiPA206.
    GenAtlasiSearch...

    Phylogenomic databases

    eggNOGiCOG1226.
    GeneTreeiENSGT00760000118846.
    HOGENOMiHOG000231015.
    HOVERGENiHBG052230.
    InParanoidiP16389.
    KOiK04875.
    OMAiMTFHTYS.
    OrthoDBiEOG7M0NRD.
    PhylomeDBiP16389.
    TreeFamiTF313103.

    Enzyme and pathway databases

    ReactomeiREACT_75770. Voltage gated Potassium channels.

    Miscellaneous databases

    GeneWikiiKCNA2.
    GenomeRNAii3737.
    NextBioi14627.
    PROiP16389.
    SOURCEiSearch...

    Gene expression databases

    BgeeiP16389.
    CleanExiHS_KCNA2.
    ExpressionAtlasiP16389. baseline and differential.
    GenevestigatoriP16389.

    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.
    IPR003972. K_chnl_volt-dep_Kv1.
    IPR004049. K_chnl_volt-dep_Kv1.2.
    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.
    PR01509. KV12CHANNEL.
    PR01491. KVCHANNEL.
    PR01496. SHAKERCHANEL.
    SMARTiSM00225. BTB. 1 hit.
    [Graphical view]
    SUPFAMiSSF54695. SSF54695. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Human potassium channel genes: molecular cloning and functional expression."
      Ramaswami M., Gautam M., Kamb A., Rudy B., Tanouye M.A., Mathew M.K.
      Mol. Cell. Neurosci. 1:214-223(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
      Tissue: Brain.
    2. "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].
      Tissue: Substantia nigraImported.
    3. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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 2).
      Tissue: Blood.
    6. "Heteromultimeric assembly of human potassium channels. Molecular basis of a transient outward current?"
      Po S., Roberds S., Snyders D.J., Tamkun M.M., Bennett P.B.
      Circ. Res. 72:1326-1336(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNA4.
    7. "Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels."
      Poliak S., Gollan L., Martinez R., Custer A., Einheber S., Salzer J.L., Trimmer J.S., Shrager P., Peles E.
      Neuron 24:1037-1047(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH CNTNAP2.
    8. "Role of receptor protein tyrosine phosphatase alpha (RPTPalpha) and tyrosine phosphorylation in the serotonergic inhibition of voltage-dependent potassium channels."
      Imbrici P., Tucker S.J., D'Adamo M.C., Pessia M.
      Pflugers Arch. 441:257-262(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    9. "Subunit composition and novel localization of K+ channels in spinal cord."
      Rasband M.N., Trimmer J.S.
      J. Comp. Neurol. 429:166-176(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH KCNA1 AND KCNAB2, SUBUNIT, TISSUE SPECIFICITY.
    10. "Voltage-gated ion channels in the axon initial segment of human cortical pyramidal cells and their relationship with chandelier cells."
      Inda M.C., DeFelipe J., Munoz A.
      Proc. Natl. Acad. Sci. U.S.A. 103:2920-2925(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    11. "Ionic channel function in action potential generation: current perspective."
      Baranauskas G.
      Mol. Neurobiol. 35:129-150(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.
    12. "The molecular basis for the actions of Kvbeta1.2 on the opening and closing of the Kv1.2 delayed rectifier channel."
      Peters C.J., Vaid M., Horne A.J., Fedida D., Accili E.A.
      Channels 3:314-322(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KCNAB1.
    13. "Biochemical characterization of kappaM-RIIIJ, a Kv1.2 channel blocker: evaluation of cardioprotective effects of kappaM-conotoxins."
      Chen P., Dendorfer A., Finol-Urdaneta R.K., Terlau H., Olivera B.M.
      J. Biol. Chem. 285:14882-14889(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, ENZYME REGULATION.
    14. "Altered distribution of juxtaparanodal kv1.2 subunits mediates peripheral nerve hyperexcitability in type 2 diabetes mellitus."
      Zenker J., Poirot O., de Preux Charles A.S., Arnaud E., Medard J.J., Lacroix C., Kuntzer T., Chrast R.
      J. Neurosci. 32:7493-7498(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    15. "Activation of lysophosphatidic acid receptor by gintonin inhibits Kv1.2 channel activity: involvement of tyrosine kinase and receptor protein tyrosine phosphatase alpha."
      Lee J.H., Choi S.H., Lee B.H., Hwang S.H., Kim H.J., Rhee J., Chung C., Nah S.Y.
      Neurosci. Lett. 548:143-148(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.

    Entry informationi

    Entry nameiKCNA2_HUMAN
    AccessioniPrimary (citable) accession number: P16389
    Secondary accession number(s): A0A024R0D3, A8K1Z6, Q86XG6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1990
    Last sequence update: February 1, 1996
    Last modified: April 29, 2015
    This is version 150 of the entry and version 2 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

    Miscellaneous

    The delay or D-type current observed in hippocampus pyramidal neurons is probably mediated by potassium channels containing KCNA2 plus KCNA1 or other family members. It is activated at about -50 mV, i.e. below the action potential threshold, and is characterized by slow inactivation, extremely slow recovery from inactivation, sensitivity to dendrotoxin (DTX) and to 4-aminopyridine (4-AP).1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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.