KCNB1_PIG
ID KCNB1_PIG Reviewed; 858 AA.
AC O18868;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Potassium voltage-gated channel subfamily B member 1 {ECO:0000250|UniProtKB:Q14721};
DE AltName: Full=Delayed rectifier potassium channel 1 {ECO:0000250|UniProtKB:P15387};
DE Short=DRK1 {ECO:0000250|UniProtKB:P15387};
DE AltName: Full=Voltage-gated potassium channel subunit Kv2.1;
GN Name=KCNB1 {ECO:0000250|UniProtKB:Q14721};
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Lens epithelium;
RA Rae J.L., Shepard A.R.;
RL Submitted (SEP-1997) 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 vascular
RT smooth muscle.";
RL Cell Biochem. Biophys. 42:167-195(2005).
CC -!- FUNCTION: Voltage-gated potassium channel that mediates transmembrane
CC potassium transport in excitable membranes, primarily in the brain, but
CC also in the pancreas and cardiovascular system. Contributes to the
CC regulation of the action potential (AP) repolarization, duration and
CC frequency of repetitive AP firing in neurons, muscle cells and
CC endocrine cells and plays a role in homeostatic attenuation of
CC electrical excitability throughout the brain. Also plays a role in the
CC regulation of exocytosis independently of its electrical function.
CC Forms tetrameric potassium-selective channels through which potassium
CC ions pass in accordance with their electrochemical gradient. The
CC channel alternates between opened and closed conformations in response
CC to the voltage difference across the membrane. Homotetrameric channels
CC mediate a delayed-rectifier voltage-dependent outward potassium current
CC that display rapid activation and slow inactivation in response to
CC membrane depolarization. Can form functional homotetrameric and
CC heterotetrameric channels that contain variable proportions of KCNB2;
CC channel properties depend on the type of alpha subunits that are part
CC of the channel. Can also form functional heterotetrameric channels with
CC other alpha subunits that are non-conducting when expressed alone, such
CC as KCNF1, KCNG1, KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and
CC KCNV1, creating a functionally diverse range of channel complexes (By
CC similarity). Heterotetrameric channel activity formed with KCNS3 show
CC increased 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 of the
CC delayed rectifier potassium channels. In vivo, membranes probably
CC contain a mixture of heteromeric potassium channel complexes, making it
CC difficult to assign currents observed in intact tissues to any
CC particular potassium channel family member. Major contributor to the
CC delayed-rectifier voltage-gated potassium current in neurons of the
CC central nervous system, sympathetic ganglion neurons, neuroendocrine
CC cells, pancreatic beta cells, cardiomyocytes and smooth muscle.
CC Mediates the major part of the somatodendritic delayed-rectifier
CC potassium current in hippocampal and cortical pyramidal neurons and
CC sympathetic superior cervical ganglion (CGC) neurons that acts to slow
CC down periods of firing, especially during high frequency stimulation.
CC Plays a role in the induction of long-term potentiation (LTP) of neuron
CC excitability in the CA3 layer of the hippocampus. Contributes to the
CC regulation of the glucose-induced amplitude and duration of action
CC potentials in pancreatic beta-cells, hence limiting calcium influx and
CC insulin secretion. Plays a role in the regulation of resting membrane
CC potential and contraction in hypoxia-treated pulmonary artery smooth
CC muscle cells. May contribute to the regulation of the duration of both
CC the action potential of cardiomyocytes and the heart ventricular
CC repolarization QT interval. Contributes to the pronounced pro-apoptotic
CC potassium current surge during neuronal apoptotic cell death in
CC response to oxidative injury. May confer neuroprotection in response to
CC hypoxia/ischemic insults by suppressing pyramidal neurons
CC hyperexcitability in hippocampal and cortical regions. Promotes
CC trafficking of KCNG3, KCNH1 and KCNH2 to the cell surface membrane,
CC presumably by forming heterotetrameric channels with these subunits.
CC Plays a role in the calcium-dependent recruitment and release of
CC fusion-competent vesicles from the soma of neurons, neuroendocrine and
CC glucose-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 -!- ACTIVITY 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 G.spatulata.
CC Modestly sensitive to millimolar levels of tetraethylammonium (TEA).
CC Modestly sensitive to millimolar levels of 4-aminopyridine (4-AP).
CC Completely insensitive to toxins such as dendrotoxin (DTX) and
CC charybdotoxin (CTX). {ECO:0000305|PubMed:10414301,
CC 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. After
CC that, inactivate very slowly, i.e within more than 5 sec. Their
CC activation requires low threshold potentials at about -20 to -30 mV
CC with a midpoint activation at about 10 mV. For inactivation, the
CC voltage at half-maximal amplitude is about -20 mV. The time constant
CC for recovery after inactivation is about 1.6 sec. Channels have an
CC unitary conductance of about 8 pS. The voltage-dependence of
CC activation and inactivation and other channel characteristics vary
CC depending on the experimental conditions, the expression system, the
CC presence or absence of ancillary subunits and post-translational
CC modifications. {ECO:0000305|PubMed:10414301,
CC ECO:0000305|PubMed:15858231};
CC -!- SUBUNIT: Homotetramer or heterotetramer with KCNB2. Heterotetramer with
CC non-conducting channel-forming alpha subunits such as KCNF1, KCNG1,
CC KCNG3, KCNG4, KCNH1, KCNH2, KCNS1, KCNS2, KCNS3 and KCNV1. Channel
CC activity is regulated by association with ancillary beta subunits such
CC as AMIGO1, KCNE1, KCNE2 and KCNE3. Self-associates (via N-terminus and
CC C-terminus); self-association is required to regulate trafficking,
CC gating and C-terminal phosphorylation-dependent modulation of the
CC channel. Interacts (via C-terminus) with STX1A (via C-terminus); this
CC decreases the rate of channel activation and increases the rate of
CC channel inactivation in pancreatic beta cells, induces also neuronal
CC apoptosis in response to oxidative injury as well as pore-independent
CC enhancement of exocytosis in neuroendocrine cells, chromaffin cells,
CC pancreatic beta cells and from the soma of dorsal root ganglia (DRG)
CC neurons. Interacts (via N-terminus) with SNAP25; this decreases the
CC rate of channel inactivation in pancreatic beta cells and also
CC increases interaction during neuronal apoptosis in a N-methyl-D-
CC aspartate receptor (NMDAR)-dependent manner. Interacts (via N-terminus
CC and 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. Interacts
CC (via N-terminus and C-terminus) with MYL12B. Interacts (via N-terminus)
CC with PIAS3; this increases the number of functional channels at the
CC cell surface. Interacts with SUMO1. Interacts (via phosphorylated form)
CC with PTPRE; this reduces phosphorylation and channel activity in
CC heterologous cells. {ECO:0000250|UniProtKB:P15387,
CC ECO:0000250|UniProtKB:Q03717, ECO:0000250|UniProtKB:Q14721}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15387}.
CC Perikaryon {ECO:0000250|UniProtKB:P15387}. Cell projection, axon
CC {ECO:0000250|UniProtKB:P15387}. Cell projection, dendrite
CC {ECO:0000250|UniProtKB:P15387}. Membrane; Multi-pass membrane protein.
CC Postsynaptic cell membrane {ECO:0000250|UniProtKB:P15387}. Synapse
CC {ECO:0000250|UniProtKB:P15387}. Synapse, synaptosome
CC {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 clusters
CC in the axon initial segment (AIS), at ankyrin-G-deficient sites, on the
CC surface of neocortical and hippocampal pyramidal neurons. KCNB1-
CC containing AIS clusters localize either in close apposition to smooth
CC endoplasmic reticulum cisternal organelles or with GABA-A receptor-
CC containing synapses of hippocampal and cortical pyramidal neurons,
CC respectively. Localizes to high-density clusters on the cell surface of
CC atrial and ventricular myocytes and at the lateral plasma membrane in
CC epithelial cells. Localizes both to the axial and transverse tubules (T
CC tubule) and sarcolemma in ventricular myocytes. Associated with lipid
CC raft 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 and is
CC characterized by a series of positively charged amino acids at every
CC third position. Channel opening and closing is effected by a
CC conformation change that affects the position and orientation of the
CC voltage-sensor paddle formed by S3 and S4 within the membrane. A
CC transmembrane electric field that is positive inside would push the
CC positively charged S4 segment outwards, thereby opening the pore, while
CC a field that is negative inside would pull the S4 segment inwards and
CC close the pore. Changes in the position and orientation of S4 are then
CC transmitted to the activation gate formed by the inner helix bundle via
CC the S4-S5 linker region. {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 modulation
CC of the channel. The N-terminal cytoplasmic region is important for
CC interaction with other channel-forming alpha subunits and with
CC ancillary beta subunits. The C-terminus is necessary and sufficient for
CC the restricted localization to, and clustering within, both in soma and
CC proximal portions of dendrite of neurons and in lateral membrane of
CC non-neuronal polarized cells. The C-terminus is both necessary and
CC sufficient as a mediator of cholinergic and calcium-stimulated
CC modulation of channel cell membrane clustering localization and
CC activity in 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 the
CC phosphatase PTPRE. CDK5-induced Ser-607 phosphorylation increases in
CC response to acute blockade of neuronal activity. Phosphorylated on Tyr-
CC 128 by Src and on Ser-805 by MAPK14/P38MAPK; phosphorylations are
CC necessary and sufficient for an increase in plasma membrane insertion,
CC apoptotic potassium current surge and completion of the neuronal cell
CC death program. Phosphorylated on Ser-520, Ser-607, Ser-656 and Ser-805
CC by CDK5; phosphorylation is necessary for KCNB1 channel clustering
CC formation. The Ser-607 phosphorylation state differs between KCNB1-
CC containing clusters on the proximal and distal portions of the axon
CC initial segment (AIS). Highly phosphorylated on serine residues in the
CC C-terminal cytoplasmic tail in resting neurons. Phosphorylated in
CC pancreatic beta cells in response to incretin hormones stimulation in a
CC PKA- 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 reach
CC adult levels by P14. Phosphorylation on Ser-457, Ser-541, Ser-567, Ser-
CC 607, Ser-656 and Ser-720 as well as the N-terminal Ser-15 are sensitive
CC to calcineurin-mediated dephosphorylation contributing to the
CC modulation of the voltage-dependent gating properties.
CC Dephosphorylation by phosphatase PTPRE confers neuroprotection by its
CC inhibitory influence on the neuronal apoptotic potassium current surge
CC in a Zn(2+)-dependent manner. Dephosphorylated at Ser-607 by protein
CC phosphatase PPP1CA. Hypoxia-, seizure- or glutamate-induced neuronal
CC activity promote calcium/calcineurin-dependent dephosphorylation
CC resulting in a loss of KCNB1-containing clustering and enhanced channel
CC activity. In response to brain ischemia, Ser-567 and Ser-607 are
CC strongly dephosphorylated while Ser-457 and Ser-720 are less
CC dephosphorylated. In response to brain seizures, phosphorylation levels
CC on Ser-567 and Ser-607 are greatly reduced.
CC Phosphorylated/dephosphorylated by Src or FYN tyrosine-protein kinases
CC and tyrosine phosphatase PTPRE in primary Schwann cells and sciatic
CC 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 signaling
CC pathway, promoting beta cell survival. {ECO:0000250|UniProtKB:P15387}.
CC -!- PTM: Sumoylated on Lys-475, preferentially with SUMO1; sumoylation
CC induces a positive shift in the voltage-dependence of activation and
CC inhibits channel activity. Sumoylation increases the frequency of
CC repetitive action potential firing at the cell surface of hippocampal
CC neurons and decreases its frequency in pancreatic beta cells.
CC Desumoylated by SENP1. {ECO:0000250|UniProtKB:P15387,
CC ECO:0000250|UniProtKB:Q14721}.
CC -!- SIMILARITY: Belongs to the potassium channel family. B (Shab) (TC
CC 1.A.1.2) subfamily. Kv2.1/KCNB1 sub-subfamily. {ECO:0000305}.
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DR EMBL; AF026006; AAB88809.1; -; mRNA.
DR RefSeq; NP_999383.1; NM_214218.1.
DR AlphaFoldDB; O18868; -.
DR SMR; O18868; -.
DR STRING; 9823.ENSSSCP00000007950; -.
DR PaxDb; O18868; -.
DR PeptideAtlas; O18868; -.
DR GeneID; 397433; -.
DR KEGG; ssc:397433; -.
DR CTD; 3745; -.
DR eggNOG; KOG3713; Eukaryota.
DR InParanoid; O18868; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; ISS:UniProtKB.
DR GO; GO:0030425; C:dendrite; ISS:UniProtKB.
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:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
DR GO; GO:0098900; P:regulation of action potential; ISS:UniProtKB.
DR GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
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 Gene3D; 3.30.710.10; -; 1.
DR InterPro; IPR000210; BTB/POZ_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_sf.
DR InterPro; IPR003131; T1-type_BTB.
DR InterPro; IPR028325; VG_K_chnl.
DR InterPro; IPR027359; Volt_channel_dom_sf.
DR PANTHER; PTHR11537; PTHR11537; 1.
DR Pfam; PF02214; BTB_2; 1.
DR Pfam; PF00520; Ion_trans; 1.
DR Pfam; PF03521; Kv2channel; 2.
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 membrane; Cell projection; Exocytosis; Ion channel; Ion transport;
KW Isopeptide bond; Membrane; Phosphoprotein; Postsynaptic cell membrane;
KW Potassium; Potassium channel; Potassium transport; Reference proteome;
KW Synapse; Synaptosome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation; Voltage-gated channel.
FT CHAIN 1..858
FT /note="Potassium voltage-gated channel subfamily B member
FT 1"
FT /id="PRO_0000054044"
FT TOPO_DOM 1..186
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 187..208
FT /note="Helical; Name=Segment S1"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 209..228
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 229..250
FT /note="Helical; Name=Segment S2"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 251..259
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 260..280
FT /note="Helical; Name=Segment S3"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 281..294
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 295..316
FT /note="Helical; Voltage-sensor; Name=Segment S4"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 317..330
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 331..351
FT /note="Helical; Name=Segment S5"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 352..364
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 365..376
FT /note="Helical; Name=Pore helix"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT INTRAMEM 377..384
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 385..391
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TRANSMEM 392..420
FT /note="Helical; Name=Segment S6"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT TOPO_DOM 421..858
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 59..75
FT /note="Self-association"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT REGION 448..481
FT /note="Self-association"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT REGION 474..524
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 537..574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..803
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 839..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 377..382
FT /note="Selectivity filter"
FT /evidence="ECO:0000250|UniProtKB:P63142"
FT COMPBIAS 488..506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 15
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 128
FT /note="Phosphotyrosine; by Src"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 444
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03717"
FT MOD_RES 457
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03717"
FT MOD_RES 484
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 520
FT /note="Phosphoserine; by CDK5; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 541
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 590
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 607
FT /note="Phosphoserine; by CDK5"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 656
FT /note="Phosphoserine; by CDK5; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 720
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 800
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT MOD_RES 805
FT /note="Phosphoserine; by CDK5, MAPK14; in vitro"
FT /evidence="ECO:0000250|UniProtKB:P15387"
FT CROSSLNK 475
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO)"
FT /evidence="ECO:0000250|UniProtKB:P15387"
SQ 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
