ID KCNB1_RABIT Reviewed; 858 AA.
AC Q9MZ19;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 06-JUL-2016, entry version 98.
DE RecName: Full=Potassium voltage-gated channel subfamily B member 1 {ECO:0000250|UniProtKB:Q14721};
DE AltName: Full=Voltage-gated potassium channel subunit Kv2.1;
GN Name=KCNB1 {ECO:0000250|UniProtKB:Q14721};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae;
OC Oryctolagus.
OX NCBI_TaxID=9986;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=New Zealand white; TISSUE=Corneal endothelium;
RA Rae J.L.;
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW.
RX PubMed=10414301; DOI=10.1111/j.1749-6632.1999.tb11293.x;
RA Coetzee W.A., Amarillo Y., Chiu J., Chow A., Lau D., McCormack T.,
RA Moreno H., Nadal M.S., Ozaita A., Pountney D., Saganich M.,
RA Vega-Saenz de Miera E., Rudy B.;
RT "Molecular diversity of K+ channels.";
RL Ann. N. Y. Acad. Sci. 868:233-285(1999).
RN [3]
RP REVIEW.
RX PubMed=15858231; DOI=10.1385/CBB:42:2:167;
RA Cox R.H.;
RT "Molecular determinants of voltage-gated potassium currents in
RT vascular smooth muscle.";
RL Cell Biochem. Biophys. 42:167-195(2005).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates
CC transmembrane potassium transport in excitable membranes,
CC primarily in the brain, but also in the pancreas and
CC cardiovascular system. Contributes to the regulation of the action
CC potential (AP) repolarization, duration and frequency of
CC repetitive AP firing in neurons, muscle cells and endocrine cells
CC and plays a role in homeostatic attenuation of electrical
CC excitability throughout the brain. Plays also a role in the
CC regulation of exocytosis independently of its electrical function.
CC Forms tetrameric potassium-selective channels through which
CC potassium ions pass in accordance with their electrochemical
CC gradient. The channel alternates between opened and closed
CC conformations in response to the voltage difference across the
CC membrane. Homotetrameric channels mediate a delayed-rectifier
CC voltage-dependent outward potassium current that display rapid
CC activation and slow inactivation in response to membrane
CC depolarization. Can form functional homotetrameric and
CC heterotetrameric channels that contain variable proportions of
CC KCNB2; channel properties depend on the type of alpha subunits
CC that are part of the channel. Can also form functional
CC heterotetrameric channels with other alpha subunits that are non-
CC conducting when expressed alone, such as KCNF1, KCNG1, KCNG3,
CC KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1, creating a
CC functionally diverse range of channel complexes (By similarity).
CC Heterotetrameric channel activity formed with KCNS3 show increased
CC current amplitude with the threshold for action potential
CC activation shifted towards more negative values in hypoxic-treated
CC pulmonary artery smooth muscle cells. Channel properties are also
CC modulated by cytoplasmic ancillary beta subunits, such as AMIGO1,
CC KCNE1, KCNE2 and KCNE3, slowing activation and inactivation rate
CC of the delayed rectifier potassium channels. In vivo, membranes
CC probably contain a mixture of heteromeric potassium channel
CC complexes, making it difficult to assign currents observed in
CC intact tissues to any particular potassium channel family member.
CC Major contributor to the delayed-rectifier voltage-gated potassium
CC current in neurons of the central nervous system, sympathetic
CC ganglion neurons, neuroendocrine cells, pancreatic beta cells,
CC cardiomyocytes and smooth muscle. Mediates the major part of the
CC somatodendritic delayed-rectifier potassium current in hippocampal
CC and cortical pyramidal neurons and sympathetic superior cervical
CC ganglion (CGC) neurons that acts to slow down periods of firing,
CC especially during high frequency stimulation. Plays a role in the
CC induction of long-term potentiation (LTP) of neuron excitability
CC in the CA3 layer of the hippocampus. Contributes to the regulation
CC of the glucose-induced amplitude and duration of action potentials
CC in pancreatic beta-cells, hence limiting calcium influx and
CC insulin secretion. Plays a role in the regulation of resting
CC membrane potential and contraction in hypoxia-treated pulmonary
CC artery smooth muscle cells. May contribute to the regulation of
CC the duration of both the action potential of cardiomyocytes and
CC the heart ventricular repolarization QT interval. Contributes to
CC the pronounced pro-apoptotic potassium current surge during
CC neuronal apoptotic cell death in response to oxidative injury. May
CC confer neuroprotection in response to hypoxia/ischemic insults by
CC suppressing pyramidal neurons hyperexcitability in hippocampal and
CC cortical regions. Promotes trafficking of KCNG3, KCNH1 and KCNH2
CC to the cell surface membrane, presumably by forming
CC heterotetrameric channels with these subunits. Plays a role in the
CC calcium-dependent recruitment and release of fusion-competent
CC vesicles from the soma of neurons, neuroendocrine and glucose-
CC induced pancreatic beta cells by binding key components of the
CC fusion machinery in a pore-independent manner.
CC {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717,
CC ECO:0000250|UniProtKB:Q14721}.
CC -!- ENZYME REGULATION: Inhibited by 12.7 nM stromatoxin 1 (ScTx1), a
CC spider venom toxin of the tarantula S.calceata. Inhibited by 42 nM
CC hanatoxin 1 (HaTx1), a spider venom toxin of the tarantula
CC G.spatulata. Modestly sensitive to millimolar levels of
CC tetraethylammonium (TEA). Modestly sensitive to millimolar levels
CC of 4-aminopyridine (4-AP). Completely insensitive to toxins such
CC as dendrotoxin (DTX) and charybdotoxin (CTX).
CC {ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=Homotetrameric channels expressed in xenopus oocytes or in
CC mammalian non-neuronal cells display delayed-rectifier voltage-
CC dependent potassium currents which are activated during membrane
CC depolarization, i.e within a risetime of more than 20 msec.
CC After that, inactivate very slowly, i.e within more than 5 sec.
CC Their activation requires low threshold potentials at about -20
CC to -30 mV with a midpoint activation at about 10 mV. For
CC inactivation, the voltage at half-maximal amplitude is about -20
CC mV. The time constant for recovery after inactivation is about
CC 1.6 sec. Channels have an unitary conductance of about 8 pS. The
CC voltage-dependence of activation and inactivation and other
CC channel characteristics vary depending on the experimental
CC conditions, the expression system, the presence or absence of
CC ancillary subunits and post-translational modifications.
CC {ECO:0000305|PubMed:10414301, ECO:0000305|PubMed:15858231};
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCNB2. Heterotetramer
CC with non-conducting channel-forming alpha subunits such as KCNF1,
CC KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1.
CC Channel activity is regulated by association with ancillary beta
CC subunits such as AMIGO1, KCNE1, KCNE2 and KCNE3. Self-associates
CC (via N-terminus and C-terminus); self-association is required to
CC regulate trafficking, gating and C-terminal phosphorylation-
CC dependent modulation of the channel. Interacts (via C-terminus)
CC with STX1A (via C-terminus); this decreases the rate of channel
CC activation and increases the rate of channel inactivation in
CC pancreatic beta cells, induces also neuronal apoptosis in response
CC to oxidative injury as well as pore-independent enhancement of
CC exocytosis in neuroendocrine cells, chromaffin cells, pancreatic
CC beta cells and from the soma of dorsal root ganglia (DRG) neurons.
CC Interacts (via N-terminus) with SNAP25; this decreases the rate of
CC channel inactivation in pancreatic beta cells and also increases
CC interaction during neuronal apoptosis in a N-methyl-D-aspartate
CC receptor (NMDAR)-dependent manner. Interacts (via N-terminus and
CC C-terminus) with VAMP2 (via N-terminus); stimulates channel
CC inactivation rate. Interacts with CREB1; this promotes channel
CC acetylation in response to stimulation by incretin hormones.
CC Interacts (via N-terminus and C-terminus) with MYL12B. Interacts
CC (via N-terminus) with PIAS3; this increases the number of
CC functional channels at the cell surface. Interacts with SUMO1.
CC Interacts (via phosphorylated form) with PTPRE; this reduces
CC phosphorylation and channel activity in heterologous cells.
CC {ECO:0000250|UniProtKB:P15387, ECO:0000250|UniProtKB:Q03717,
CC ECO:0000250|UniProtKB:Q14721}.
CC -!- SUBCELLULAR LOCATION: Cell membrane
CC {ECO:0000250|UniProtKB:P15387}. Perikaryon
CC {ECO:0000250|UniProtKB:P15387}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P15387}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P15387}. Membrane; Multi-pass membrane
CC protein. Cell junction, synapse, postsynaptic cell membrane
CC {ECO:0000250|UniProtKB:P15387}. Cell junction, synapse
CC {ECO:0000250|UniProtKB:P15387}. Cell junction, synapse,
CC synaptosome {ECO:0000250|UniProtKB:P15387}. Lateral cell membrane
CC {ECO:0000250|UniProtKB:P15387}. Cell membrane, sarcolemma
CC {ECO:0000250|UniProtKB:P15387}. Note=Localizes to high-density
CC somatodendritic clusters and non-clustered sites on the surface of
CC neocortical and hippocampal pyramidal neurons in a cortical actin
CC cytoskeleton-dependent manner. Localizes also to high-density
CC clusters in the axon initial segment (AIS), at ankyrin-G-deficient
CC sites, on the surface of neocortical and hippocampal pyramidal
CC neurons. KCNB1-containing AIS clusters localize either in close
CC apposition to smooth endoplasmic reticulum cisternal organelles or
CC with GABA-A receptor-containing synapses of hippocampal and
CC cortical pyramidal neurons, respectively. Localizes to high-
CC density clusters on the cell surface of atrial and ventricular
CC myocytes and at the lateral plasma membrane in epithelial cells.
CC Localizes both to the axial and transverse tubules (T tubule) and
CC sarcolemma in ventricular myocytes. Associated with lipid raft
CC domains. In cortical neurons, apoptotic injuries induce de novo
CC plasma membrane insertion in a SNARE-dependent manner causing an
CC apoptotic potassium current surge. {ECO:0000250|UniProtKB:P15387,
CC ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721}.
CC -!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
CC and is characterized by a series of positively charged amino acids
CC at every third position. Channel opening and closing is effected
CC by a conformation change that affects the position and orientation
CC of the voltage-sensor paddle formed by S3 and S4 within the
CC membrane. A transmembrane electric field that is positive inside
CC would push the positively charged S4 segment outwards, thereby
CC opening the pore, while a field that is negative inside would pull
CC the S4 segment inwards and close the pore. Changes in the position
CC and orientation of S4 are then transmitted to the activation gate
CC formed by the inner helix bundle via the S4-S5 linker region.
CC {ECO:0000250|UniProtKB:P63142}.
CC -!- DOMAIN: The N-terminal and C-terminal cytoplasmic regions mediate
CC homooligomerization; self-association is required to regulate
CC trafficking, gating and C-terminal phosphorylation-dependent
CC modulation of the channel. The N-terminal cytoplasmic region is
CC important for interaction with other channel-forming alpha
CC subunits and with ancillary beta subunits. The C-terminus is
CC necessary and sufficient for the restricted localization to, and
CC clustering within, both in soma and proximal portions of dendrite
CC of neurons and in lateral membrane of non-neuronal polarized
CC cells. The C-terminus is both necessary and sufficient as a
CC mediator of cholinergic and calcium-stimulated modulation of
CC channel cell membrane clustering localization and activity in
CC hippocampal neurons. {ECO:0000250|UniProtKB:P15387,
CC ECO:0000250|UniProtKB:Q14721}.
CC -!- PTM: Phosphorylated. Differential C-terminal phosphorylation on a
CC subset of serines allows graded activity-dependent regulation of
CC channel gating in hippocampal neurons. Ser-607 and Tyr-128 are
CC significant sites of voltage-gated regulation through
CC phosphorylation/dephosphorylation activities. Tyr-128 can be
CC phosphorylated by Src and dephosphorylated by cytoplasmic form of
CC the phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation
CC increases in response to acute blockade of neuronal activity.
CC Phosphorylated on Tyr-128 by Src and on Ser-805 by MAPK14/P38MAPK;
CC phosphorylations are necessary and sufficient for an increase in
CC plasma membrane insertion, apoptotic potassium current surge and
CC completion of the neuronal cell death program. Phosphorylated on
CC Ser-520, Ser-607, Ser-656 and Ser-805 by CDK5; phosphorylation is
CC necessary for KCNB1 channel clustering formation. The Ser-607
CC phosphorylation state differs between KCNB1-containing clusters on
CC the proximal and distal portions of the axon initial segment
CC (AIS). Highly phosphorylated on serine residues in the C-terminal
CC cytoplasmic tail in resting neurons. Phosphorylated in pancreatic
CC beta cells in response to incretin hormones stimulation in a PKA-
CC and RPS6KA5/MSK1-dependent signaling pathway, promoting beta cell
CC survival. Phosphorylation on Ser-567 is reduced during postnatal
CC development with low levels at P2 and P5; levels then increase to
CC reach adult levels by P14. Phosphorylation on Ser-457, Ser-541,
CC Ser-567, Ser-607, Ser-656 and Ser-720 as well as the N-terminal
CC Ser-15 are sensitive to calcineurin-mediated dephosphorylation
CC contributing to the modulation of the voltage-dependent gating
CC properties. Dephosphorylation by phosphatase PTPRE confers
CC neuroprotection by its inhibitory influence on the neuronal
CC apoptotic potassium current surge in a Zn(2+)-dependent manner.
CC Dephosphorylated at Ser-607 by protein phosphatase PPP1CA.
CC Hypoxia-, seizure- or glutamate-induced neuronal activity promote
CC calcium/calcineurin-dependent dephosphorylation resulting in a
CC loss of KCNB1-containing clustering and enhanced channel activity.
CC In response to brain ischemia, Ser-567 and Ser-607 are strongly
CC dephosphorylated while Ser-457 and Ser-720 are less
CC dephosphorylated. In response to brain seizures, phosphorylation
CC levels on Ser-567 and Ser-607 are greatly reduced.
CC Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein
CC kinases and tyrosine phosphatase PTPRE in primary Schwann cells
CC and sciatic nerve tissue. {ECO:0000250|UniProtKB:P15387,
CC ECO:0000250|UniProtKB:Q03717}.
CC -!- PTM: Acetylated. Acetylation occurs in pancreatic beta cells in
CC response to stimulation by incretin hormones in a histone
CC acetyltransferase (HAT)/histone deacetylase (HDAC)-dependent
CC signaling pathway, promoting beta cell survival.
CC {ECO:0000250|UniProtKB:P15387}.
CC -!- PTM: Sumoylated on Lys-474, preferentially with SUMO1; sumoylation
CC induces a positive shift in the voltage-dependence of activation
CC and inhibits channel activity. Sumoylation increases the frequency
CC of repetitive action potential firing at the cell surface of
CC hippocampal neurons and decreases its frequency in pancreatic beta
CC cells. Desumoylated by SENP1. {ECO:0000250|UniProtKB:P15387,
CC ECO:0000250|UniProtKB:Q14721}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab)
CC (TC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. {ECO:0000305}.
DR EMBL; AF266507; AAF77058.1; -; mRNA.
DR RefSeq; NP_001075556.1; NM_001082087.1.
DR UniGene; Ocu.2450; -.
DR ProteinModelPortal; Q9MZ19; -.
DR STRING; 9986.ENSOCUP00000017212; -.
DR GeneID; 100008779; -.
DR KEGG; ocu:100008779; -.
DR CTD; 3745; -.
DR eggNOG; KOG3713; Eukaryota.
DR eggNOG; COG1226; LUCA.
DR HOGENOM; HOG000113206; -.
DR HOVERGEN; HBG052225; -.
DR InParanoid; Q9MZ19; -.
DR KO; K04885; -.
DR Proteomes; UP000001811; Unplaced.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
DR GO; GO:0005622; C:intracellular; IEA:GOC.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032809; C:neuronal cell body membrane; ISS:UniProtKB.
DR GO; GO:0043204; C:perikaryon; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0045211; C:postsynaptic membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0042383; C:sarcolemma; IEA:UniProtKB-SubCell.
DR GO; GO:0008076; C:voltage-gated potassium channel complex; ISS:UniProtKB.
DR GO; GO:0005251; F:delayed rectifier potassium channel activity; ISS:UniProtKB.
DR GO; GO:0046982; F:protein heterodimerization activity; ISS:UniProtKB.
DR GO; GO:0001508; P:action potential; ISS:UniProtKB.
DR GO; GO:0071333; P:cellular response to glucose stimulus; ISS:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; ISS:UniProtKB.
DR GO; GO:0042593; P:glucose homeostasis; ISS:UniProtKB.
DR GO; GO:0007215; P:glutamate receptor signaling pathway; ISS:UniProtKB.
DR GO; GO:0046676; P:negative regulation of insulin secretion; ISS:UniProtKB.
DR GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; ISS:UniProtKB.
DR GO; GO:0033605; P:positive regulation of catecholamine secretion; ISS:UniProtKB.
DR GO; GO:1900454; P:positive regulation of long term synaptic depression; ISS:UniProtKB.
DR GO; GO:0010701; P:positive regulation of norepinephrine secretion; ISS:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISS:UniProtKB.
DR GO; GO:0071805; P:potassium ion transmembrane transport; ISS:UniProtKB.
DR GO; GO:0006813; P:potassium ion transport; ISS:UniProtKB.
DR GO; GO:0051260; P:protein homooligomerization; IEA:InterPro.
DR GO; GO:0072661; P:protein targeting to plasma membrane; ISS:UniProtKB.
DR GO; GO:0098900; P:regulation of action potential; ISS:UniProtKB.
DR GO; GO:2000671; P:regulation of motor neuron apoptotic process; ISS:UniProtKB.
DR GO; GO:0006904; P:vesicle docking involved in exocytosis; ISS:UniProtKB.
DR Gene3D; 1.20.120.350; -; 1.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR027359; Channel_four-helix_dom.
DR InterPro; IPR005821; Ion_trans_dom.
DR InterPro; IPR003968; K_chnl_volt-dep_Kv.
DR InterPro; IPR003973; K_chnl_volt-dep_Kv2.
DR InterPro; IPR004350; K_chnl_volt-dep_Kv2.1.
DR InterPro; IPR011333; SKP1/BTB/POZ.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03521; Kv2channel; 2.
DR PRINTS; PR00169; KCHANNEL.
DR PRINTS; PR01514; KV21CHANNEL.
DR PRINTS; PR01491; KVCHANNEL.
DR PRINTS; PR01495; SHABCHANNEL.
DR SMART; SM00225; BTB; 1.
DR SUPFAM; SSF54695; SSF54695; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Cell projection; Complete proteome;
KW Exocytosis; Ion channel; Ion transport; Isopeptide bond; Membrane;
KW Phosphoprotein; Postsynaptic cell membrane; Potassium;
KW Potassium channel; Potassium transport; Reference proteome; Synapse;
KW Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1 858 Potassium voltage-gated channel subfamily
FT B member 1.
FT /FTId=PRO_0000054045.
FT TOPO_DOM 1 186 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 187 208 Helical; Name=Segment S1.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 209 228 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 229 250 Helical; Name=Segment S2.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 251 259 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 260 280 Helical; Name=Segment S3.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 281 294 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 295 316 Helical; Voltage-sensor; Name=Segment S4.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 317 330 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 331 351 Helical; Name=Segment S5.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 352 364 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT INTRAMEM 365 376 Helical; Name=Pore helix.
FT {ECO:0000250|UniProtKB:P63142}.
FT INTRAMEM 377 384 {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 385 391 Extracellular.
FT {ECO:0000250|UniProtKB:P63142}.
FT TRANSMEM 392 420 Helical; Name=Segment S6.
FT {ECO:0000250|UniProtKB:P63142}.
FT TOPO_DOM 421 858 Cytoplasmic.
FT {ECO:0000250|UniProtKB:P63142}.
FT REGION 59 75 Self-association.
FT {ECO:0000250|UniProtKB:P15387}.
FT REGION 448 481 Self-association.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOTIF 377 382 Selectivity filter.
FT {ECO:0000250|UniProtKB:P63142}.
FT COMPBIAS 517 520 Poly-Ser.
FT COMPBIAS 701 706 Poly-Ala.
FT MOD_RES 15 15 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 128 128 Phosphotyrosine; by Src.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 444 444 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q03717}.
FT MOD_RES 457 457 Phosphoserine.
FT {ECO:0000250|UniProtKB:Q03717}.
FT MOD_RES 484 484 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 496 496 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 503 503 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 519 519 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 520 520 Phosphoserine; by CDK5; in vitro.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 541 541 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 567 567 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 590 590 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 607 607 Phosphoserine; by CDK5.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 656 656 Phosphoserine; by CDK5; in vitro.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 720 720 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 772 772 Phosphoserine.
FT {ECO:0000250|UniProtKB:P15387}.
FT MOD_RES 805 805 Phosphoserine; by CDK5, MAPK14; in vitro.
FT {ECO:0000250|UniProtKB:P15387}.
FT CROSSLNK 475 475 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in SUMO).
FT {ECO:0000250|UniProtKB:P15387}.
CC --------------------------------------------------------------------------
CC The following FT lines are automated annotations from the MyHits database.
CC --------------------------------------------------------------------------
FT MYHIT 189 423 ipfam:Ion_trans [T]
FT MYHIT 653 679 ipfam:Kv2channel [T]
FT MYHIT 33 132 ipfam:BTB_2 [T]
FT MYHIT 467 612 ipfam:Kv2channel [T]
FT MYHIT 31 140 ismart:BTB [T]
SQ SEQUENCE 858 AA; 95373 MW; FDFDCC49B6973C4B CRC64;
MPAGMTKHGS RSASSLPPEP 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 KDAFARSVEM MDIVVEKNGE NLAKKEKVQD
NHLSPNKWKW TKRTLSETSS SKSFETKEQG SPEKARSSSS PQHLNVQQLE DMYNKMAKTQ
SQPVLNTKEA AAQSKPKEEL EMESIPSPVA PLPTRTEGVI DMRSMSSIDS FISCATDFPE
ATRFSHSPLA SLPTKAGGGA APELGWRGAL GASGGRLVEA NPTPDASHGS GFFIESPKSS
MKTNNPLKLR ALKVNFMAGE PGPLLPVLGM YHDPLRTRGG AAAAVAGLEC ATLLDKPVLS
PESSIYTTAS ARTPPRSPEK PTAIAFNFEA GVHQYIDADT DDEGQLLYSV DSSPPKSLHG
GASPKCSIGA RSEKNHFESA PLPTSPKFLR QNCIYSTEGL TGKSLSGQEK CKLGNHISPD
VRVLPGGGAH GSTRDQSL
//
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