Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Potassium voltage-gated channel subfamily B member 1 (Delayed rectifier potassium channel 1) (DRK1) (Voltage-gated potassium channel subunit Kv2.1)

 KCNB1_PIG               Reviewed;         858 AA.
O18868;
25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-JAN-1998, sequence version 1.
28-FEB-2018, entry version 112.
RecName: Full=Potassium voltage-gated channel subfamily B member 1 {ECO:0000250|UniProtKB:Q14721};
AltName: Full=Delayed rectifier potassium channel 1 {ECO:0000250|UniProtKB:P15387};
Short=DRK1 {ECO:0000250|UniProtKB:P15387};
AltName: Full=Voltage-gated potassium channel subunit Kv2.1;
Name=KCNB1 {ECO:0000250|UniProtKB:Q14721};
Sus scrofa (Pig).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Suina; Suidae;
Sus.
NCBI_TaxID=9823;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lens epithelium;
Rae J.L., Shepard A.R.;
Submitted (SEP-1997) to the EMBL/GenBank/DDBJ databases.
[2]
REVIEW.
PubMed=10414301; DOI=10.1111/j.1749-6632.1999.tb11293.x;
Coetzee W.A., Amarillo Y., Chiu J., Chow A., Lau D., McCormack T.,
Moreno H., Nadal M.S., Ozaita A., Pountney D., Saganich M.,
Vega-Saenz de Miera E., Rudy B.;
"Molecular diversity of K+ channels.";
Ann. N. Y. Acad. Sci. 868:233-285(1999).
[3]
REVIEW.
PubMed=15858231; DOI=10.1385/CBB:42:2:167;
Cox R.H.;
"Molecular determinants of voltage-gated potassium currents in
vascular smooth muscle.";
Cell Biochem. Biophys. 42:167-195(2005).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain, but also in the pancreas and
cardiovascular system. Contributes to the regulation of the action
potential (AP) repolarization, duration and frequency of
repetitive AP firing in neurons, muscle cells and endocrine cells
and plays a role in homeostatic attenuation of electrical
excitability throughout the brain. Plays also a role in the
regulation of exocytosis independently of its electrical function.
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. Homotetrameric channels mediate a delayed-rectifier
voltage-dependent outward potassium current that display rapid
activation and slow inactivation in response to membrane
depolarization. Can form functional homotetrameric and
heterotetrameric channels that contain variable proportions of
KCNB2; channel properties depend on the type of alpha subunits
that are part of the channel. Can also form functional
heterotetrameric channels with other alpha subunits that are non-
conducting when expressed alone, such as KCNF1, KCNG1, KCNG3,
KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a
functionally diverse range of channel complexes (By similarity).
Heterotetrameric channel activity formed with KCNS3 show increased
current amplitude with the threshold for action potential
activation shifted towards more negative values in hypoxic-treated
pulmonary artery smooth muscle cells. Channel properties are also
modulated by cytoplasmic ancillary beta subunits, such as AMIGO1,
KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate
of the 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.
Major contributor to the delayed-rectifier voltage-gated potassium
current in neurons of the central nervous system, sympathetic
ganglion neurons, neuroendocrine cells, pancreatic beta cells,
cardiomyocytes and smooth muscle. Mediates the major part of the
somatodendritic delayed-rectifier potassium current in hippocampal
and cortical pyramidal neurons and sympathetic superior cervical
ganglion (CGC) neurons that acts to slow down periods of firing,
especially during high frequency stimulation. Plays a role in the
induction of long-term potentiation (LTP) of neuron excitability
in the CA3 layer of the hippocampus. Contributes to the regulation
of the glucose-induced amplitude and duration of action potentials
in pancreatic beta-cells, hence limiting calcium influx and
insulin secretion. Plays a role in the regulation of resting
membrane potential and contraction in hypoxia-treated pulmonary
artery smooth muscle cells. May contribute to the regulation of
the duration of both the action potential of cardiomyocytes and
the heart ventricular repolarization QT interval. Contributes to
the pronounced pro-apoptotic potassium current surge during
neuronal apoptotic cell death in response to oxidative injury. May
confer neuroprotection in response to hypoxia/ischemic insults by
suppressing pyramidal neurons hyperexcitability in hippocampal and
cortical regions. Promotes trafficking of KCNG3, KCNH1 and KCNH2
to the cell surface membrane, presumably by forming
heterotetrameric channels with these subunits. Plays a role in the
calcium-dependent recruitment and release of fusion-competent
vesicles from the soma of neurons, neuroendocrine and glucose-
induced pancreatic beta cells by binding key components of the
fusion machinery in a pore-independent manner.
{ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717,
ECO:0000250|UniProtKB:Q14721}.
-!- ENZYME REGULATION: Inhibited by 12.7 nM stromatoxin 1 (ScTx1), a
spider venom toxin of the tarantula S.calceata. Inhibited by 42 nM
hanatoxin 1 (HaTx1), a spider venom toxin of the tarantula
G.spatulata. Modestly sensitive to millimolar levels of
tetraethylammonium (TEA). Modestly sensitive to millimolar levels
of 4-aminopyridine (4-AP). Completely insensitive to toxins such
as dendrotoxin (DTX) and charybdotoxin (CTX).
{ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels expressed in xenopus oocytes or in
mammalian non-neuronal cells display delayed-rectifier voltage-
dependent potassium currents which are activated during membrane
depolarization, i.e within a risetime of more than 20 msec.
After that, inactivate very slowly, i.e within more than 5 sec.
Their activation requires low threshold potentials at about -20
to -30 mV with a midpoint activation at about 10 mV. For
inactivation, the voltage at half-maximal amplitude is about -20
mV. The time constant for recovery after inactivation is about
1.6 sec. Channels have an unitary conductance of about 8 pS. The
voltage-dependence of activation and inactivation and other
channel characteristics vary depending on the experimental
conditions, the expression system, the presence or absence of
ancillary subunits and post-translational modifications.
{ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231};
-!- SUBUNIT: Homotetramer or heterotetramer with KCNB2. Heterotetramer
with non-conducting channel-forming alpha subunits such as KCNF1,
KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1.
Channel activity is regulated by association with ancillary beta
subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3. Self-associates
(via N-terminus and C-terminus); self-association is required to
regulate trafficking, gating and C-terminal phosphorylation-
dependent modulation of the channel. Interacts (via C-terminus)
with STX1A (via C-terminus); this decreases the rate of channel
activation and increases the rate of channel inactivation in
pancreatic beta cells, induces also neuronal apoptosis in response
to oxidative injury as well as pore-independent enhancement of
exocytosis in neuroendocrine cells, chromaffin cells, pancreatic
beta cells and from the soma of dorsal root ganglia (DRG) neurons.
Interacts (via N-terminus) with SNAP25; this decreases the rate of
channel inactivation in pancreatic beta cells and also increases
interaction during neuronal apoptosis in a N-methyl-D-aspartate
receptor (NMDAR)-dependent manner. Interacts (via N-terminus and
C-terminus) with VAMP2 (via N-terminus); stimulates channel
inactivation rate. Interacts with CREB1; this promotes channel
acetylation in response to stimulation by incretin hormones.
Interacts (via N-terminus and C-terminus) with MYL12B. Interacts
(via N-terminus) with PIAS3; this increases the number of
functional channels at the cell surface. Interacts with SUMO1.
Interacts (via phosphorylated form) with PTPRE; this reduces
phosphorylation and channel activity in heterologous cells.
{ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717,
ECO:0000250|UniProtKB:Q14721}.
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:P15387}. Perikaryon
{ECO:0000250|UniProtKB:P15387}. Cell projection, axon
{ECO:0000250|UniProtKB:P15387}. Cell projection, dendrite
{ECO:0000250|UniProtKB:P15387}. Membrane; Multi-pass membrane
protein. Cell junction, synapse, postsynaptic cell membrane
{ECO:0000250|UniProtKB:P15387}. Cell junction, synapse
{ECO:0000250|UniProtKB:P15387}. Cell junction, synapse,
synaptosome {ECO:0000250|UniProtKB:P15387}. Lateral cell membrane
{ECO:0000250|UniProtKB:P15387}. Cell membrane, sarcolemma
{ECO:0000250|UniProtKB:P15387}. Note=Localizes to high-density
somatodendritic clusters and non-clustered sites on the surface of
neocortical and hippocampal pyramidal neurons in a cortical actin
cytoskeleton-dependent manner. Localizes also to high-density
clusters in the axon initial segment (AIS), at ankyrin-G-deficient
sites, on the surface of neocortical and hippocampal pyramidal
neurons. KCNB1-containing AIS clusters localize either in close
apposition to smooth endoplasmic reticulum cisternal organelles or
with GABA-A receptor-containing synapses of hippocampal and
cortical pyramidal neurons, respectively. Localizes to high-
density clusters on the cell surface of atrial and ventricular
myocytes and at the lateral plasma membrane in epithelial cells.
Localizes both to the axial and transverse tubules (T tubule) and
sarcolemma in ventricular myocytes. Associated with lipid raft
domains. In cortical neurons, apoptotic injuries induce de novo
plasma membrane insertion in a SNARE-dependent manner causing an
apoptotic potassium current surge. {ECO:0000250|UniProtKB:P15387,
ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- DOMAIN: The N-terminal and C-terminal cytoplasmic regions mediate
homooligomerization; self-association is required to regulate
trafficking, gating and C-terminal phosphorylation-dependent
modulation of the channel. The N-terminal cytoplasmic region is
important for interaction with other channel-forming alpha
subunits and with ancillary beta subunits. The C-terminus is
necessary and sufficient for the restricted localization to, and
clustering within, both in soma and proximal portions of dendrite
of neurons and in lateral membrane of non-neuronal polarized
cells. The C-terminus is both necessary and sufficient as a
mediator of cholinergic and calcium-stimulated modulation of
channel cell membrane clustering localization and activity in
hippocampal neurons. {ECO:0000250|UniProtKB:P15387,
ECO:0000250|UniProtKB:Q14721}.
-!- PTM: Phosphorylated. Differential C-terminal phosphorylation on a
subset of serines allows graded activity-dependent regulation of
channel gating in hippocampal neurons. Ser-607 and Tyr-128 are
significant sites of voltage-gated regulation through
phosphorylation/dephosphorylation activities. Tyr-128 can be
phosphorylated by Src and dephosphorylated by cytoplasmic form of
the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation
increases in response to acute blockade of neuronal activity.
Phosphorylated on Tyr-128 by Src and on Ser-805 by MAPK14/P38MAPK;
phosphorylations are necessary and sufficient for an increase in
plasma membrane insertion, apoptotic potassium current surge and
completion of the neuronal cell death program. Phosphorylated on
Ser-520, Ser-607, Ser-656 and Ser-805 by CDK5; phosphorylation is
necessary for KCNB1 channel clustering formation. The Ser-607
phosphorylation state differs between KCNB1-containing clusters on
the proximal and distal portions of the axon initial segment
(AIS). Highly phosphorylated on serine residues in the C-terminal
cytoplasmic tail in resting neurons. Phosphorylated in pancreatic
beta cells in response to incretin hormones stimulation in a
PKA- and RPS6KA5/MSK1-dependent signaling pathway, promoting beta
cell survival. Phosphorylation on Ser-567 is reduced during
postnatal development with low levels at P2 and P5; levels then
increase to reach adult levels by P14. Phosphorylation on Ser-457,
Ser-541, Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-
terminal Ser-15 are sensitive to calcineurin-mediated
dephosphorylation contributing to the modulation of the voltage-
dependent gating properties. Dephosphorylation by phosphatase
PTPRE confers neuroprotection by its inhibitory influence on the
neuronal apoptotic potassium current surge in a Zn(2+)-dependent
manner. Dephosphorylated at Ser-607 by protein phosphatase PPP1CA.
Hypoxia-, seizure- or glutamate-induced neuronal activity promote
calcium/calcineurin-dependent dephosphorylation resulting in a
loss of KCNB1-containing clustering and enhanced channel activity.
In response to brain ischemia, Ser-567 and Ser-607 are strongly
dephosphorylated while Ser-457 and Ser-720 are less
dephosphorylated. In response to brain seizures, phosphorylation
levels on Ser-567 and Ser-607 are greatly reduced.
Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein
kinases and tyrosine phosphatase PTPRE in primary Schwann cells
and sciatic nerve tissue. {ECO:0000250|UniProtKB:P15387,
ECO:0000250|UniProtKB:Q03717}.
-!- PTM: Acetylated. Acetylation occurs in pancreatic beta cells in
response to stimulation by incretin hormones in a histone
acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent
signaling pathway, promoting beta cell survival.
{ECO:0000250|UniProtKB:P15387}.
-!- PTM: Sumoylated on Lys-475, preferentially with SUMO1; sumoylation
induces a positive shift in the voltage-dependence of activation
and inhibits channel activity. Sumoylation increases the frequency
of repetitive action potential firing at the cell surface of
hippocampal neurons and decreases its frequency in pancreatic beta
cells. Desumoylated by SENP1. {ECO:0000250|UniProtKB:P15387,
ECO:0000250|UniProtKB:Q14721}.
-!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF026006; AAB88809.1; -; mRNA.
RefSeq; NP_999383.1; NM_214218.1.
UniGene; Ssc.16142; -.
ProteinModelPortal; O18868; -.
STRING; 9823.ENSSSCP00000007950; -.
PaxDb; O18868; -.
PeptideAtlas; O18868; -.
PRIDE; O18868; -.
GeneID; 397433; -.
KEGG; ssc:397433; -.
CTD; 3745; -.
eggNOG; KOG3713; Eukaryota.
eggNOG; COG1226; LUCA.
HOGENOM; HOG000113206; -.
HOVERGEN; HBG052225; -.
InParanoid; O18868; -.
KO; K04885; -.
Proteomes; UP000008227; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; ISS:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central.
GO; GO:0001508; P:action potential; ISS:UniProtKB.
GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
GO; GO:0033605; P:positive regulation of catecholamine secretion; ISS:UniProtKB.
GO; GO:1900454; P:positive regulation of long term synaptic depression; ISS:UniProtKB.
GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB.
GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0098900; P:regulation of action potential; ISS:UniProtKB.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:2000671; P:regulation of motor neuron apoptotic process; ISS:UniProtKB.
GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:UniProtKB.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003973; K_chnl_volt-dep_Kv2.
InterPro; IPR004350; K_chnl_volt-dep_Kv2.1.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
Pfam; PF03521; Kv2channel; 2.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01514; KV21CHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01495; SHABCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 1.
2: Evidence at transcript level;
Cell junction; Cell membrane; Cell projection; Complete proteome;
Exocytosis; Ion channel; Ion transport; Isopeptide bond; Membrane;
Phosphoprotein; Postsynaptic cell membrane; Potassium;
Potassium channel; Potassium transport; Reference proteome; Synapse;
Synaptosome; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; Voltage-gated channel.
CHAIN 1 858 Potassium voltage-gated channel subfamily
B member 1.
/FTId=PRO_0000054044.
TOPO_DOM 1 186 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 187 208 Helical; Name=Segment S1.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 209 228 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 229 250 Helical; Name=Segment S2.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 251 259 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 260 280 Helical; Name=Segment S3.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 281 294 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 295 316 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 317 330 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 331 351 Helical; Name=Segment S5.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 352 364 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 365 376 Helical; Name=Pore helix.
{ECO:0000250|UniProtKB:P63142}.
INTRAMEM 377 384 {ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 385 391 Extracellular.
{ECO:0000250|UniProtKB:P63142}.
TRANSMEM 392 420 Helical; Name=Segment S6.
{ECO:0000250|UniProtKB:P63142}.
TOPO_DOM 421 858 Cytoplasmic.
{ECO:0000250|UniProtKB:P63142}.
REGION 59 75 Self-association.
{ECO:0000250|UniProtKB:P15387}.
REGION 448 481 Self-association.
{ECO:0000250|UniProtKB:P15387}.
MOTIF 377 382 Selectivity filter.
{ECO:0000250|UniProtKB:P63142}.
COMPBIAS 517 520 Poly-Ser.
COMPBIAS 701 706 Poly-Ala.
MOD_RES 15 15 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 128 128 Phosphotyrosine; by Src.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 444 444 Phosphoserine.
{ECO:0000250|UniProtKB:Q03717}.
MOD_RES 457 457 Phosphoserine.
{ECO:0000250|UniProtKB:Q03717}.
MOD_RES 484 484 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 496 496 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 503 503 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 519 519 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 520 520 Phosphoserine; by CDK5; in vitro.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 541 541 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 567 567 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 590 590 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 607 607 Phosphoserine; by CDK5.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 656 656 Phosphoserine; by CDK5; in vitro.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 720 720 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 800 800 Phosphoserine.
{ECO:0000250|UniProtKB:P15387}.
MOD_RES 805 805 Phosphoserine; by CDK5, MAPK14; in vitro.
{ECO:0000250|UniProtKB:P15387}.
CROSSLNK 475 475 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000250|UniProtKB:P15387}.
SEQUENCE 858 AA; 96118 MW; A9E24C3A8E13B491 CRC64;
MPAGMTKHGS RSTSSLPPEP MEIVRSKACS RRVRLNVGGL AHEVLWRTLD RLPRTRLGKL
RDCNTHDSLL EVCDDYSLDD NEYFFDRHPG AFTSILNFYR TGRLHMMEEM CALSFSQELD
YWGIDEIYLE SCCQARYHQK KEQMNEELKR EAETLREREG EEFDNTCCAE KRKKLWDLLE
KPNSSVAAKI LAIISIMFIV LSTIALSLNT LPELQSLDEF GQTTDNPQLA HVEAVCIAWF
TMEYLLRFLS SPKKWKFFKG PLNAIDLLAI LPYYVTIFLT ESNKSVLQFQ NVRRVVQIFR
IMRILRILKL ARHSTGLQSL GFTLRRSYNE LGLLILFLAM GIMIFSSLVF FAEKDEDDTK
FKSIPASFWW ATITMTTVGY GDIYPKTLLG KIVGGLCCIA GVLVIALPIP IIVNNFSEFY
KEQKRQEKAI KRREALERAK RNGSIVSMNM KDAFPRSIEM MDIVVEKNVE NMGQKDKVQD
NHLSPNKWKW TKRTLSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYNKMAKTQ
SQPILNTKES ATQSKPKEEL EMESIPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
ATRFSHSPLA SLPSKSGGSM APEVGWRGAL GATGGRFVEA NPTPDASHHS TFFIESPKSS
MKTTNPLKLR ALKVNFMEGD PSPLVPVLGM YHDPLRNRGG AAAAVAGLEC ATLLDRPVLS
PESSIYTTAS ARTPPRSPEK HTAIAFNFEA GIHQYIDADT DDEGQVLYSV DSSPPKSLHG
STSPKFSIGT RSEKNHFESS PLPTSPKFLR QNCIYSTEAL TGKAPSGQEK CKLENHISPD
VRVLPGGGAH GSTRDQSI


Related products :

Catalog number Product name Quantity
28-297 This gene encodes a member of the potassium channel, voltage-gated, subfamily H. This member is a pore-forming (alpha) subunit of a voltage-gated non-inactivating delayed rectifier potassium channel. 0.1 mg
18-003-42663 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.05 mg Aff Pur
18-003-42664 Potassium voltage-gated channel subfamily KQT member 2 - Voltage-gated potassium channel subunit Kv7.2; Neuroblastoma-specific potassium channel subunit alpha KvLQT2; KQT-like 2 Polyclonal 0.1 mg Protein A
18-662-20074 Potassium voltage-gated channel subfamily C member 1 - Voltage-gated potassium channel subunit Kv3.1; Kv4; NGK2; RAW2 Polyclonal 0.1 ml
18-662-20009 Potassium voltage-gated channel subfamily B member 2 - Voltage-gated potassium channel subunit Kv2.2; CDRK Polyclonal 0.1 ml
18-003-43133 Potassium voltage-gated channel subfamily G member 1 - Voltage-gated potassium channel subunit Kv6.1; kH2 Polyclonal 0.05 mg Aff Pur
18-003-42629 Potassium voltage-gated channel subfamily D member 3 - Voltage-gated potassium channel subunit Kv4.3 Polyclonal 0.1 mg Protein A
Y062354 Anti-Potassium Channel Kv<_SUB>1.6 (Voltage-gated, Delayed-Rectifier Potassium Channel; RCK2; KV2) produced in rabbit Antibody 100ul
KCNT2 KCNS3 Gene potassium voltage-gated channel, delayed-rectifier, subfamily S, member 3
201-20-2921 KCNS2{potassium voltage-gated channel, delayed-rectifier, subfamily S, member 2}rabbit.pAb 0.2ml
KCNS3 KCNS1 Gene potassium voltage-gated channel, delayed-rectifier, subfamily S, member 1
KCNT1 KCNS2 Gene potassium voltage-gated channel, delayed-rectifier, subfamily S, member 2
18-003-42631 Cyclic GMP gated potassium channel - Potassium voltage-gated channel. shaker-related subfamily. member 10 Polyclonal 0.1 mg Protein A
CSB-EL012097RA Rat potassium voltage-gated channel, delayed-rectifier, subfamily S, member 3 (KCNS3) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL012095RA Rat potassium voltage-gated channel, delayed-rectifier, subfamily S, member 1 (KCNS1) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL012096RA Rat potassium voltage-gated channel, delayed-rectifier, subfamily S, member 2 (KCNS2) ELISA kit, Species Rat, Sample Type serum, plasma 96T
CSB-EL012097HU Human potassium voltage-gated channel, delayed-rectifier, subfamily S, member 3 (KCNS3) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL012097RB Rabbit potassium voltage-gated channel, delayed-rectifier, subfamily S, member 3 (KCNS3) ELISA kit, Species Rabbit, Sample Type serum, plasma 96T
CSB-EL012095HU Human potassium voltage-gated channel, delayed-rectifier, subfamily S, member 1 (KCNS1) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL012096HU Human potassium voltage-gated channel, delayed-rectifier, subfamily S, member 2 (KCNS2) ELISA kit, Species Human, Sample Type serum, plasma 96T
CSB-EL012095MO Mouse potassium voltage-gated channel, delayed-rectifier, subfamily S, member 1 (KCNS1) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL012096MO Mouse potassium voltage-gated channel, delayed-rectifier, subfamily S, member 2 (KCNS2) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL012095RH Monkey potassium voltage-gated channel, delayed-rectifier, subfamily S, member 1 (KCNS1) ELISA kit, Species Monkey, Sample Type serum, plasma 96T
CSB-EL012097MO Mouse potassium voltage-gated channel, delayed-rectifier, subfamily S, member 3 (KCNS3) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-PA012096GA01HU Rabbit anti-human potassium voltage-gated channel, delayed-rectifier, subfamily S, member 2 polyclonal Antibody Primary antibody Host:Rabbit IgG 150ul


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur