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Protein

Potassium voltage-gated channel subfamily A member 2

Gene

Kcna2

Organism
Rattus norvegicus (Rat)
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:12151401, PubMed:21602278, PubMed:24472174). 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:15618540, PubMed:20805574, PubMed:23725331). 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 (PubMed:18003609, PubMed:19713757). In vivo, membranes probably contain a mixture of heteromeric potassium channel complexes, making it difficult to assign currents observed in intact tissues to a 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:1715584, PubMed:16770729, PubMed:17766348, PubMed:18003609, PubMed:18638484, PubMed:19713757, PubMed:20089912). In contrast, a heteromultimer formed by KCNA2 and KCNA4 shows rapid inactivation (PubMed:8495559). Response to toxins that are selective for KCNA1, respectively for KCNA2, suggests that heteromeric potassium channels composed of both KCNA1 and KCNA2 play a role in pacemaking and regulate the output of deep cerebellar nuclear neurons (PubMed:23318870). KCNA2-containing channels play a presynaptic role and prevent hyperexcitability and aberrant action potential firing (PubMed:12777451). 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 (PubMed:16210348). 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 (PubMed:16306173). May contribute to the regulation of neurotransmitter release, such as gamma-aminobutyric acid (GABA) (PubMed:17869444). Contributes to the regulation of the axonal release of the neurotransmitter dopamine (PubMed:21647367). Reduced KCNA2 expression plays a role in the perception of neuropathic pain after peripheral nerve injury, but not acute pain (PubMed:24472174). Plays a role in the regulation of the time spent in non-rapid eye movement (NREM) sleep (By similarity).By similarity20 PublicationsCurated

Enzyme regulationi

Inhibited by 4-aminopyridine (4-AP), dendrotoxin (DTX) and charybdotoxin (CTX), but not by tetraethylammonium (TEA) (PubMed:2555158, PubMed:8495559, PubMed:18638484). Inhibited by tityustoxin-K alpha (TsTX-Kalpha), a toxin that is highly specific for KCNA2 (PubMed:8355670). Inhibited by maurotoxin (PubMed:24472174). Inhibited by kappaM conotoxins kappaM-RIIIJ and kappaM-RIIIK (By similarity).By similarity6 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei252 – 2521Important for normal, slow channel gating1 Publication

GO - Molecular functioni

  1. delayed rectifier potassium channel activity Source: UniProtKB
  2. outward rectifier potassium channel activity Source: RGD
  3. 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. protein homooligomerization Source: InterPro
  5. protein oligomerization Source: RGD
  6. regulation of dopamine secretion Source: UniProtKB
  7. sensory perception of pain Source: UniProtKB
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_199159. Voltage gated Potassium channels.

Names & Taxonomyi

Protein namesi
Recommended name:
Potassium voltage-gated channel subfamily A member 2
Alternative name(s):
RAK
RBK21 Publication
RCK51 Publication
Voltage-gated potassium channel subunit Kv1.2
Gene namesi
Name:Kcna2
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Chromosome 2

Organism-specific databases

RGDi2950. Kcna2.

Subcellular locationi

Cell membrane 17 Publications1 Publication; Multi-pass membrane protein 6 PublicationsCurated. Membrane 9 Publications. Cell projectionaxon 6 Publications. Cell junctionsynapse 1 Publication. Cell junctionsynapsesynaptosome By similarity. Cell junctionsynapsepresynaptic cell membrane By similarity. Cell projectiondendrite By similarity. Endoplasmic reticulum membrane 1 Publication. Cell projectionlamellipodium membrane 1 Publication. Endosome 1 Publication. Perikaryon 1 Publication
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 (PubMed:10896669, PubMed:16770729, PubMed:18003609). Coexpression with KCNA1 inhibits cell surface expression (PubMed:10896669). Surface levels are regulated both by steady-state and stimulus-induced clathrin-dependent endocytosis (PubMed:19403695). Expression at the cell surface is down-regulated in response to CHRM1 activation (PubMed:9635436). Expression at the cell surface is increased in response to the activation of beta-adrenergic receptors and increased cAMP levels (PubMed:18003609). Detected on presynaptic and postsynaptic axon segments (PubMed:12777451).6 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 160160Cytoplasmic3 PublicationsAdd
BLAST
Transmembranei161 – 18222Helical; Name=Segment S13 PublicationsAdd
BLAST
Topological domaini183 – 22139Extracellular3 Publications1 PublicationAdd
BLAST
Transmembranei222 – 24322Helical; Name=Segment S23 PublicationsAdd
BLAST
Topological domaini244 – 25411Cytoplasmic3 PublicationsAdd
BLAST
Transmembranei255 – 27521Helical; Name=Segment S32 PublicationsAdd
BLAST
Topological domaini276 – 28914Extracellular3 PublicationsAdd
BLAST
Transmembranei290 – 31021Helical; Voltage-sensor; Name=Segment S42 PublicationsAdd
BLAST
Topological domaini311 – 32515Cytoplasmic3 PublicationsAdd
BLAST
Transmembranei326 – 34722Helical; Name=Segment S53 PublicationsAdd
BLAST
Topological domaini348 – 36114Extracellular3 PublicationsAdd
BLAST
Intramembranei362 – 37312Helical; Name=Pore helix3 PublicationsAdd
BLAST
Intramembranei374 – 38183 Publications
Topological domaini382 – 3887Extracellular3 Publications
Transmembranei389 – 41729Helical; Name=Segment S63 PublicationsAdd
BLAST
Topological domaini418 – 49982Cytoplasmic1 PublicationCuratedAdd
BLAST

GO - Cellular componenti

  1. axon terminus Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. integral component of membrane Source: GO_Central
  4. integral component of plasma membrane Source: UniProtKB
  5. juxtaparanode region of axon Source: UniProtKB
  6. lamellipodium Source: UniProtKB
  7. neuronal cell body membrane Source: UniProtKB
  8. perikaryon Source: UniProtKB
  9. voltage-gated potassium channel complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

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

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi34 – 341R → L: No effect on channel opening. 1 Publication
Mutagenesisi38 – 381N → A: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi40 – 401S → A: No effect on channel opening. 1 Publication
Mutagenesisi41 – 411G → A: Loss of channel activity. 1 Publication
Mutagenesisi42 – 421L → A: No effect on channel opening. 1 Publication
Mutagenesisi43 – 431R → L: No effect on channel opening. 1 Publication
Mutagenesisi44 – 441F → A: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi45 – 451E → A: Loss of channel activity. 1 Publication
Mutagenesisi46 – 461T → D: Impairs protein folding. Loss of tetramerization. 1 Publication
Mutagenesisi46 – 461T → V or A: No effect on tetramerization. Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi46 – 461T → V: Abolishes interaction with KCNAB2 and strongly reduces cell surface expression. No effect phosphorylation in response to increased cAMP levels. 1 Publication
Mutagenesisi47 – 471Q → A: No effect on channel opening. 1 Publication
Mutagenesisi50 – 501T → A: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi70 – 701D → A: No effect on channel opening. 1 Publication
Mutagenesisi73 – 731R → A: No effect on channel opening. 1 Publication
Mutagenesisi75 – 751E → A: No effect on channel opening. 1 Publication
Mutagenesisi77 – 771F → W: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi79 – 791D → N: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi81 – 811N → A: No effect on channel opening. 1 Publication
Mutagenesisi82 – 821R → A: Loss of channel activity. 1 Publication
Mutagenesisi86 – 861D → A: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi89 – 891L → A: No effect on channel opening. 1 Publication
Mutagenesisi90 – 901Y → A: No effect on channel opening. 1 Publication
Mutagenesisi93 – 931Q → A: Loss of channel activity. 1 Publication
Mutagenesisi97 – 971R → A: No effect on channel opening. 1 Publication
Mutagenesisi99 – 991R → A: No effect on channel opening. 1 Publication
Mutagenesisi102 – 1021V → T: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi103 – 1031N → A: No effect on channel opening. 1 Publication
Mutagenesisi105 – 1051P → A: No effect on channel opening. 1 Publication
Mutagenesisi107 – 1071D → A: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi108 – 1081I → A: No effect on channel opening. 1 Publication
Mutagenesisi111 – 1111E → A: Alters voltage-sensitive channel opening. 1 Publication
Mutagenesisi207 – 2071N → Q: Loss of glycosylation site. 1 Publication
Mutagenesisi252 – 2521T → R: Changes channel gating from a predominantly slow mode to a much more rapid mode. 1 Publication
Mutagenesisi267 – 30236FITLG…LVRVF → YVTIFLTESNKSVLQFQNVR RVVQIFRIM in paddle chimera; changes channel activation to less negative voltage values and renders the channel susceptible to inhibition by the spider toxin VsTx1. 1 PublicationAdd
BLAST
Mutagenesisi356 – 3561S → A: Impairs N-glycosylation and abolishes expression at the cell surface. 1 Publication
Mutagenesisi360 – 3601S → A: No effect on N-glycosylation. Abolishes channel activity of the homotetramer, but retains channel activity in the presence of a beta subunit. 1 Publication
Mutagenesisi381 – 3811V → Y: Confers sensitivity to inhibition by tetraethylammonium (TEA). 1 Publication
Mutagenesisi383 – 3831T → A: Impairs N-glycosylation and abolishes expression at the cell surface. 1 Publication
Mutagenesisi415 – 4151Y → F: Nearly abolishes interaction with CTTN; when associated with F-417. 1 Publication
Mutagenesisi417 – 4171Y → F: Nearly abolishes interaction with CTTN; when associated with F-415. Strongly reduces channel activity. 1 Publication
Mutagenesisi440 – 4401S → A: Strongly reduces cell surface expression. Abolishes phosphorylation in response to increased cAMP levels. 1 Publication
Mutagenesisi449 – 4491S → A: Strongly reduces cell surface expression. Abolishes phosphorylation in response to increased cAMP levels. 1 Publication
Mutagenesisi458 – 4581Y → A: Impairs clustering on axon membranes. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 499499Potassium voltage-gated channel subfamily A member 2PRO_0000053975Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi207 – 2071N-linked (GlcNAc...)1 PublicationSequence Analysis
Lipidationi244 – 2441S-palmitoyl cysteineSequence Analysis
Modified residuei429 – 4291PhosphotyrosineBy similarity
Modified residuei440 – 4401Phosphoserine1 Publication
Modified residuei441 – 4411PhosphoserineBy similarity
Modified residuei449 – 4491Phosphoserine2 Publications
Modified residuei458 – 4581Phosphotyrosine1 Publication

Post-translational modificationi

Phosphorylated on tyrosine residues; phosphorylation increases in response to ischemia (PubMed:14713306). Phosphorylated on tyrosine residues by activated PTK2B/PYK2 (PubMed:7544443). Phosphorylation on tyrosine residues suppresses ion channel activity (PubMed:7544443). Phosphorylated on tyrosine residues in response to CHRM1 activation; this abolishes interaction with CTTN (PubMed:12151401). This is probably due to endocytosis of the phosphorylated channnel subunits. Phosphorylated on serine residues in response to increased cAMP levels; phosphorylation is apparently not catalyzed by PKA (PubMed:18003609).4 Publications
N-glycosylated, with complex, sialylated N-glycans.2 Publications

Keywords - PTMi

Glycoprotein, Lipoprotein, Palmitate, Phosphoprotein

Proteomic databases

PaxDbiP63142.
PRIDEiP63142.

PTM databases

PhosphoSiteiP63142.

Expressioni

Tissue specificityi

Detected in neurons in dorsal root ganglion (PubMed:24472174). Detected in hippocampus neurons (PubMed:21602278). Detected on neurons of the anteroventral cochlear nucleus (PubMed:12777451). Detected in renal arteries (PubMed:12632190). Detected in neurons of the medial nucleus of the trapezoid body (PubMed:12177193). Detected in neurons in the brain cortex (PubMed:14713306). Detected in axon tracts of the corpus callosum, specific terminal fields of the brain cortex neuropil, neurons in the medial entorhinal cortex, and in puncta representing mossy fiber terminals in the hippocampus mossy fiber tract; these puncta correspond to synapses made by dentate granule cells (PubMed:8361540). Detected in paranodal and juxtanodal zones in the central nervous system, including myelinated spinal cord (PubMed:11086297, PubMed:20089912). Detected in the juxtaparanodal region in optic nerve (PubMed:10624965). Detected at nerve terminal plexuses of basket cells in the cerebellum (at protein level) (PubMed:7477295, PubMed:20089912). Detected in brain (PubMed:2722779). Detected in heart atrium and ventricle (PubMed:1715584). Detected in renal arteries (PubMed:12632190).12 Publications

Inductioni

Up-regulated in brain cortex in response to ischemia (at protein level) (PubMed:14713306). Down-regulated in dorsal root ganglion neurons after peripheral nerve injury (at protein level) (PubMed:24472174). Down-regulated in pulmonary artery myocytes in response to chronic moderate hypoxia.3 Publications

Gene expression databases

GenevestigatoriP63142.

Interactioni

Subunit structurei

Homotetramer and heterotetramer with other channel-forming alpha subunits, such as KCNA1, KCNA4, KCNA5, KCNA6 and KCNA7 (PubMed:8495559, PubMed:8361540, PubMed:10896669, PubMed:12777451, PubMed:12632190, PubMed:15618540, PubMed:11007484, PubMed:16002581, PubMed:18004376, PubMed:20534430). Channel activity is regulated by interaction with beta subunits, including KCNAB1 and KCNAB2 (PubMed:18003609, PubMed:19713757, PubMed:16002581, PubMed:18004376, PubMed:20534430, PubMed:20360102, PubMed:23705070). Identified in a complex with KCNA1 and KCNAB2 (PubMed:11086297, PubMed:23318870). Identified in a complex with KCNA5 and KCNAB1 (By similarity). Identified in a complex with KCNA4 and FYN (By similarity). Interacts (via C-terminus) with the PDZ domains of DLG1 and DLG2 (PubMed:7477295). Interacts with DLG4 (via PDZ domain) (PubMed:7477295, PubMed:20089912). Interacts with PTK2B (PubMed:11739373). Interacts (via C-terminus) with CTTN (PubMed:12151401). 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 (PubMed:9635436). Interacts with DRD2 (By similarity). Interacts with SIGMAR1; cocaine consumption leads to increased interaction (By similarity). Interacts with CNTNAP2 (PubMed:10624965). Interacts with ADAM22 (PubMed:20089912).By similarity20 PublicationsCurated

Binary interactionsi

WithEntry#Exp.IntActNotes
DLG4P783522EBI-631446,EBI-80389From a different organism.

Protein-protein interaction databases

BioGridi247501. 5 interactions.
IntActiP63142. 1 interaction.
STRINGi10116.ENSRNOP00000042653.

Structurei

Secondary structure

1
499
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi34 – 396Combined sources
Beta strandi42 – 476Combined sources
Helixi48 – 525Combined sources
Turni58 – 603Combined sources
Helixi62 – 665Combined sources
Turni71 – 744Combined sources
Beta strandi75 – 784Combined sources
Turni82 – 843Combined sources
Helixi85 – 939Combined sources
Helixi106 – 11611Combined sources
Helixi120 – 13011Combined sources
Turni143 – 1453Combined sources
Helixi146 – 1494Combined sources
Turni150 – 1545Combined sources
Beta strandi156 – 1583Combined sources
Helixi160 – 18223Combined sources
Helixi186 – 1894Combined sources
Beta strandi190 – 1923Combined sources
Turni193 – 1964Combined sources
Helixi202 – 2109Combined sources
Helixi221 – 24121Combined sources
Turni249 – 2524Combined sources
Helixi254 – 2618Combined sources
Helixi264 – 2685Combined sources
Turni273 – 2786Combined sources
Helixi281 – 2833Combined sources
Turni284 – 2863Combined sources
Turni291 – 2933Combined sources
Helixi294 – 2985Combined sources
Helixi304 – 3096Combined sources
Helixi312 – 32312Combined sources
Helixi325 – 35127Combined sources
Helixi361 – 37212Combined sources
Beta strandi378 – 3803Combined sources
Helixi385 – 40319Combined sources
Helixi406 – 41813Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DSXX-ray1.60A/B/C/D/E/F/G/H33-119[»]
1QDVX-ray1.60A/B/C/D33-131[»]
1QDWX-ray2.10A/B/C/D/E/F/G/H33-119[»]
2A79X-ray2.90B1-499[»]
2R9RX-ray2.40B/H1-499[»]
3LNMX-ray2.90B/D1-266[»]
B/D303-499[»]
3LUTX-ray2.90B1-499[»]
4JTAX-ray2.50B/Q1-266[»]
B/Q304-499[»]
4JTCX-ray2.56B/H1-266[»]
B/H304-499[»]
4JTDX-ray2.54B/H1-266[»]
B/H304-499[»]
ProteinModelPortaliP63142.
SMRiP63142. Positions 3-421.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP63142.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 125125Tetramerization domain1 PublicationAdd
BLAST
Regioni312 – 32514S4-S5 linker1 PublicationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi374 – 3796Selectivity filterCurated
Motifi497 – 4993PDZ-binding1 Publication

Domaini

The cytoplasmic N-terminus is important for tetramerization. Interactions between the different subunits modulate the gating characteristics (PubMed:11007484). Besides, the cytoplasmic N-terminal domain mediates interaction with RHOA and thus is required for RHOA-mediated endocytosis (PubMed:9635436).3 Publications
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.2 Publications

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP63142.
KOiK04875.
OMAiMTFHTYS.
OrthoDBiEOG7M0NRD.
PhylomeDBiP63142.
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.

Sequencei

Sequence statusi: Complete.

P63142-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MTVATGDPVD 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 ENEDMHGGGV
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
ADERDSQFPS 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):56,701
Last modified:September 13, 2004 - v1
Checksum:iA8FEA6F3F59AF42A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti411 – 4111S → F in AAA19867. (PubMed:1715584)Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04731 mRNA. Translation: AAA40819.1.
X16003 mRNA. Translation: CAA34134.1.
M74449 mRNA. Translation: AAA19867.1.
PIRiA33814.
RefSeqiNP_037102.1. NM_012970.3.
XP_006233194.1. XM_006233132.2.
XP_006233195.1. XM_006233133.2.
XP_006233196.1. XM_006233134.2.
XP_006233197.1. XM_006233135.2.
XP_008759593.1. XM_008761371.1.
UniGeneiRn.10298.
Rn.40779.

Genome annotation databases

EnsembliENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
GeneIDi25468.
KEGGirno:25468.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
J04731 mRNA. Translation: AAA40819.1.
X16003 mRNA. Translation: CAA34134.1.
M74449 mRNA. Translation: AAA19867.1.
PIRiA33814.
RefSeqiNP_037102.1. NM_012970.3.
XP_006233194.1. XM_006233132.2.
XP_006233195.1. XM_006233133.2.
XP_006233196.1. XM_006233134.2.
XP_006233197.1. XM_006233135.2.
XP_008759593.1. XM_008761371.1.
UniGeneiRn.10298.
Rn.40779.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1DSXX-ray1.60A/B/C/D/E/F/G/H33-119[»]
1QDVX-ray1.60A/B/C/D33-131[»]
1QDWX-ray2.10A/B/C/D/E/F/G/H33-119[»]
2A79X-ray2.90B1-499[»]
2R9RX-ray2.40B/H1-499[»]
3LNMX-ray2.90B/D1-266[»]
B/D303-499[»]
3LUTX-ray2.90B1-499[»]
4JTAX-ray2.50B/Q1-266[»]
B/Q304-499[»]
4JTCX-ray2.56B/H1-266[»]
B/H304-499[»]
4JTDX-ray2.54B/H1-266[»]
B/H304-499[»]
ProteinModelPortaliP63142.
SMRiP63142. Positions 3-421.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247501. 5 interactions.
IntActiP63142. 1 interaction.
STRINGi10116.ENSRNOP00000042653.

Chemistry

GuidetoPHARMACOLOGYi539.

PTM databases

PhosphoSiteiP63142.

Proteomic databases

PaxDbiP63142.
PRIDEiP63142.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000050149; ENSRNOP00000042653; ENSRNOG00000018285.
GeneIDi25468.
KEGGirno:25468.

Organism-specific databases

CTDi3737.
RGDi2950. Kcna2.

Phylogenomic databases

eggNOGiCOG1226.
GeneTreeiENSGT00760000118846.
HOGENOMiHOG000231015.
HOVERGENiHBG052230.
InParanoidiP63142.
KOiK04875.
OMAiMTFHTYS.
OrthoDBiEOG7M0NRD.
PhylomeDBiP63142.
TreeFamiTF313103.

Enzyme and pathway databases

ReactomeiREACT_199159. Voltage gated Potassium channels.

Miscellaneous databases

EvolutionaryTraceiP63142.
NextBioi289787.
PROiP63142.

Gene expression databases

GenevestigatoriP63142.

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

  1. "Isolation of a cDNA clone coding for a putative second potassium channel indicates the existence of a gene family."
    McKinnon D.
    J. Biol. Chem. 264:8230-8236(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
  2. "Molecular basis of functional diversity of voltage-gated potassium channels in mammalian brain."
    Stuehmer W., Ruppersberg J.P., Schroerter K.H., Sakmann B., Stocker M., Giese K.P., Perschke A., Baumann A., Pongs O.
    EMBO J. 8:3235-3244(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
    Tissue: Brain.
  3. Ludwig J.
    Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  4. Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    Tissue: Heart atrium.
  5. "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, ENZYME REGULATION.
  6. "Tityustoxin-K alpha, a structurally novel and highly potent K+ channel peptide toxin, interacts with the alpha-dendrotoxin binding site on the cloned Kv1.2 K+ channel."
    Werkman T.R., Gustafson T.A., Rogowski R.S., Blaustein M.P., Rogawski M.A.
    Mol. Pharmacol. 44:430-436(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. "Presynaptic A-current based on heteromultimeric K+ channels detected in vivo."
    Sheng M., Liao Y.J., Jan Y.N., Jan L.Y.
    Nature 365:72-75(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH KCNA4, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  8. "Clustering of Shaker-type K+ channels by interaction with a family of membrane-associated guanylate kinases."
    Kim E., Niethammer M., Rothschild A., Jan Y.N., Sheng M.
    Nature 378:85-88(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH DLG1; DLG2 AND DLG4, TISSUE SPECIFICITY.
  9. "Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions."
    Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., Plowman G.D., Rudy B., Schlessinger J.
    Nature 376:737-745(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
    Tissue: Brain.
  10. "The small GTP-binding protein RhoA regulates a delayed rectifier potassium channel."
    Cachero T.G., Morielli A.D., Peralta E.G.
    Cell 93:1077-1085(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHOA.
  11. "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, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  12. "Subunit composition determines Kv1 potassium channel surface expression."
    Manganas L.N., Trimmer J.S.
    J. Biol. Chem. 275:29685-29693(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, SUBUNIT, INTERACTION WITH KCNAB2; KCNA1 AND KCNA4, GLYCOSYLATION.
  13. "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.
  14. "Signal transduction of physiological concentrations of vasopressin in A7r5 vascular smooth muscle cells. A role for PYK2 and tyrosine phosphorylation of K+ channels in the stimulation of Ca2+ spiking."
    Byron K.L., Lucchesi P.A.
    J. Biol. Chem. 277:7298-7307(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PTK2B, PHOSPHORYLATION.
  15. "Tyrosine phosphorylation of Kv1.2 modulates its interaction with the actin-binding protein cortactin."
    Hattan D., Nesti E., Cachero T.G., Morielli A.D.
    J. Biol. Chem. 277:38596-38606(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, INTERACTION WITH CTTN, SUBCELLULAR LOCATION, TOPOLOGY, MUTAGENESIS OF TYR-415 AND TYR-417.
  16. "Two heteromeric Kv1 potassium channels differentially regulate action potential firing."
    Dodson P.D., Barker M.C., Forsythe I.D.
    J. Neurosci. 22:6953-6961(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, SUBUNIT.
  17. "Enhancement of ischemia-induced tyrosine phosphorylation of Kv1.2 by vascular endothelial growth factor via activation of phosphatidylinositol 3-kinase."
    Qiu M.H., Zhang R., Sun F.Y.
    J. Neurochem. 87:1509-1517(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYPOXIA, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PHOSPHORYLATION.
  18. "Presynaptic rat Kv1.2 channels suppress synaptic terminal hyperexcitability following action potential invasion."
    Dodson P.D., Billups B., Rusznak Z., Szucs G., Barker M.C., Forsythe I.D.
    J. Physiol. (Lond.) 550:27-33(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  19. "Kv channel subunits that contribute to voltage-gated K+ current in renal vascular smooth muscle."
    Fergus D.J., Martens J.R., England S.K.
    Pflugers Arch. 445:697-704(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT, INTERACTION WITH KCNA4, TISSUE SPECIFICITY.
  20. "Subacute hypoxia decreases voltage-activated potassium channel expression and function in pulmonary artery myocytes."
    Hong Z., Weir E.K., Nelson D.P., Olschewski A.
    Am. J. Respir. Cell Mol. Biol. 31:337-343(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HYPOXIA.
  21. "Heteromultimeric Kv1 channels contribute to myogenic control of arterial diameter."
    Plane F., Johnson R., Kerr P., Wiehler W., Thorneloe K., Ishii K., Chen T., Cole W.
    Circ. Res. 96:216-224(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT.
  22. "Kv1 channels selectively prevent dendritic hyperexcitability in rat Purkinje cells."
    Khavandgar S., Walter J.T., Sageser K., Khodakhah K.
    J. Physiol. (Lond.) 569:545-557(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  23. "Mu opioid receptor activation inhibits GABAergic inputs to basolateral amygdala neurons through Kv1.1/1.2 channels."
    Finnegan T.F., Chen S.R., Pan H.L.
    J. Neurophysiol. 95:2032-2041(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  24. "Glycosylation and cell surface expression of Kv1.2 potassium channel are regulated by determinants in the pore region."
    Fujita T., Utsunomiya I., Ren J., Matsushita Y., Kawai M., Sasaki S., Hoshi K., Miyatake T., Taguchi K.
    Neurochem. Res. 31:589-596(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, GLYCOSYLATION AT ASN-207, MUTAGENESIS OF ASN-207; SER-356; SER-360 AND THR-383.
  25. "The glycosylation state of Kv1.2 potassium channels affects trafficking, gating, and simulated action potentials."
    Watanabe I., Zhu J., Sutachan J.J., Gottschalk A., Recio-Pinto E., Thornhill W.B.
    Brain Res. 1144:1-18(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, GLYCOSYLATION.
  26. "An activation gating switch in Kv1.2 is localized to a threonine residue in the S2-S3 linker."
    Rezazadeh S., Kurata H.T., Claydon T.W., Kehl S.J., Fedida D.
    Biophys. J. 93:4173-4186(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF THR-252.
  27. "Kv1.1/1.2 channels are downstream effectors of nitric oxide on synaptic GABA release to preautonomic neurons in the paraventricular nucleus."
    Yang Q., Chen S.R., Li D.P., Pan H.L.
    Neuroscience 149:315-327(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  28. "Homeostatic regulation of Kv1.2 potassium channel trafficking by cyclic AMP."
    Connors E.C., Ballif B.A., Morielli A.D.
    J. Biol. Chem. 283:3445-3453(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-440 AND SER-449, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH KCNAB2, MUTAGENESIS OF THR-46; SER-440 AND SER-449.
  29. "Functional analysis of Kv1.2 and paddle chimera Kv channels in planar lipid bilayers."
    Tao X., MacKinnon R.
    J. Mol. Biol. 382:24-33(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF 267-PHE--PHE-302.
  30. "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: FUNCTION, SUBUNIT, INTERACTION WITH KCNAB1.
  31. "Dual roles for RHOA/RHO-kinase in the regulated trafficking of a voltage-sensitive potassium channel."
    Stirling L., Williams M.R., Morielli A.D.
    Mol. Biol. Cell 20:2991-3002(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  32. Cited for: FUNCTION, SUBCELLULAR LOCATION, ENZYME REGULATION.
  33. "ADAM22, a Kv1 channel-interacting protein, recruits membrane-associated guanylate kinases to juxtaparanodes of myelinated axons."
    Ogawa Y., Oses-Prieto J., Kim M.Y., Horresh I., Peles E., Burlingame A.L., Trimmer J.S., Meijer D., Rasband M.N.
    J. Neurosci. 30:1038-1048(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ADAM22 AND DLG4, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
  34. "Clustering and activity tuning of Kv1 channels in myelinated hippocampal axons."
    Gu C., Gu Y.
    J. Biol. Chem. 286:25835-25847(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, PHOSPHORYLATION AT TYR-458, MUTAGENESIS OF TYR-458.
  35. "Role of Kv1 potassium channels in regulating dopamine release and presynaptic D2 receptor function."
    Martel P., Leo D., Fulton S., Berard M., Trudeau L.E.
    PLoS ONE 6:E20402-E20402(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  36. "Pharmacological characteristics of Kv1.1- and Kv1.2-containing channels are influenced by the stoichiometry and positioning of their alpha subunits."
    Al-Sabi A., Kaza S.K., Dolly J.O., Wang J.
    Biochem. J. 454:101-108(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF VAL-381.
  37. "A defined heteromeric KV1 channel stabilizes the intrinsic pacemaking and regulates the output of deep cerebellar nuclear neurons to thalamic targets."
    Ovsepian S.V., Steuber V., Le Berre M., O'Hara L., O'Leary V.B., Dolly J.O.
    J. Physiol. (Lond.) 591:1771-1791(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, SUBUNIT, IDENTIFICATION IN A COMPLEX WITH KCNA1 AND KCNAB2.
  38. "Impaired neuropathic pain and preserved acute pain in rats overexpressing voltage-gated potassium channel subunit Kv1.2 in primary afferent neurons."
    Fan L., Guan X., Wang W., Zhao J.Y., Zhang H., Tiwari V., Hoffman P.N., Li M., Tao Y.X.
    Mol. Pain 10:8-8(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION.
  39. "The polar T1 interface is linked to conformational changes that open the voltage-gated potassium channel."
    Minor D.L. Jr., Lin Y.-F., Mobley B.C., Avelar A., Jan Y.N., Jan L.Y., Berger J.M.
    Cell 102:657-670(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 33-119 OF WILD-TYPE AND MUTANT VAL-46, FUNCTION, SUBUNIT, REGION, DOMAIN, MUTAGENESIS OF ARG-34; ASN-38; SER-40; GLY-41; LEU-42; ARG-43; PHE-44; GLU-45; THR-46; GLN-47; THR-50; ASP-70; ARG-73; GLU-75; PHE-77; ASP-79; ASN-81; ARG-82; ASP-86; LEU-89; TYR-90; GLN-93; ARG-97; ARG-99; VAL-102; ASN-103; PRO-105; ASP-107; ILE-108 AND GLU-111.
  40. "Crystal structure of a mammalian voltage-dependent Shaker family K+ channel."
    Long S.B., Campbell E.B., Mackinnon R.
    Science 309:897-903(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, INTERACTION WITH KCNAB2.
  41. "Voltage sensor of Kv1.2: structural basis of electromechanical coupling."
    Long S.B., Campbell E.B., Mackinnon R.
    Science 309:903-908(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) IN COMPLEX WITH KCNAB2, DOMAIN.
  42. "Atomic structure of a voltage-dependent K+ channel in a lipid membrane-like environment."
    Long S.B., Tao X., Campbell E.B., MacKinnon R.
    Nature 450:376-382(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF PADDLE CHIMERA MUTANT IN COMPLEX WITH KCNAB2, FUNCTION, SUBUNIT, INTERACTION WITH KCNAB2, SUBCELLULAR LOCATION, TOPOLOGY.
  43. "Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement."
    Chen X., Wang Q., Ni F., Ma J.
    Proc. Natl. Acad. Sci. U.S.A. 107:11352-11357(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) IN COMPLEX WITH KCNAB2, INTERACTION WITH KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.
  44. "A gating charge transfer center in voltage sensors."
    Tao X., Lee A., Limapichat W., Dougherty D.A., MacKinnon R.
    Science 328:67-73(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-266 AND 303-499 IN COMPLEX WITH KCNAB2, SUBUNIT, INTERACTION WITH KCNAB2, SUBCELLULAR LOCATION, TOPOLOGY.
  45. "Structure of a pore-blocking toxin in complex with a eukaryotic voltage-dependent K(+) channel."
    Banerjee A., Lee A., Campbell E., Mackinnon R.
    Elife 2:E00594-E00594(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF PADDLE CHIMERA MUTANT IN COMPLEX WITH KCNAB2 AND CHARYBDOTOXIN, INTERACTION WITH KCNAB2, SUBUNIT, SUBCELLULAR LOCATION, TOPOLOGY.

Entry informationi

Entry nameiKCNA2_RAT
AccessioniPrimary (citable) accession number: P63142
Secondary accession number(s): P15386, Q02010
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 13, 2004
Last sequence update: September 13, 2004
Last modified: February 4, 2015
This is version 106 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. 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.