Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
1 structures for Q05037
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q05037-F1 | Predicted | AlphaFoldDB |
No variants for Q05037
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q05037 | |||||
No associated diseases with Q05037
4 regional properties for Q05037
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | BTB/POZ domain | 184 - 284 | IPR000210 |
| domain | Potassium channel tetramerisation-type BTB domain | 186 - 274 | IPR003131 |
| domain | Ion transport domain | 318 - 578 | IPR005821 |
| domain | Potassium channel, voltage dependent, Kv1.4, tandem inactivation domain | 1 - 73 | IPR012897 |
5 GO annotations of cellular component
| Name | Definition |
|---|---|
| axon | The long process of a neuron that conducts nerve impulses, usually away from the cell body to the terminals and varicosities, which are sites of storage and release of neurotransmitter. |
| dendritic spine | A small, membranous protrusion from a dendrite that forms a postsynaptic compartment, typically receiving input from a single presynapse. They function as partially isolated biochemical and an electrical compartments. Spine morphology is variable:they can be thin, stubby, mushroom, or branched, with a continuum of intermediate morphologies. They typically terminate in a bulb shape, linked to the dendritic shaft by a restriction. Spine remodeling is though to be involved in synaptic plasticity. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| integral component of plasma membrane | The component of the plasma membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| voltage-gated potassium channel complex | A protein complex that forms a transmembrane channel through which potassium ions may cross a cell membrane in response to changes in membrane potential. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| delayed rectifier potassium channel activity | Enables the transmembrane transfer of a potassium ion by a delayed rectifying voltage-gated channel. A delayed rectifying current-voltage relation is one where channel activation kinetics are time-dependent, and inactivation is slow. |
| potassium ion binding | Binding to a potassium ion (K+). |
| voltage-gated potassium channel activity | Enables the transmembrane transfer of a potassium ion by a voltage-gated channel. A voltage-gated channel is a channel whose open state is dependent on the voltage across the membrane in which it is embedded. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| potassium ion transmembrane transport | A process in which a potassium ion is transported from one side of a membrane to the other. |
| protein homooligomerization | The process of creating protein oligomers, compounds composed of a small number, usually between three and ten, of identical component monomers. Oligomers may be formed by the polymerization of a number of monomers or the depolymerization of a large protein polymer. |
| regulation of ion transmembrane transport | Any process that modulates the frequency, rate or extent of the directed movement of ions from one side of a membrane to the other. |
16 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q4ZHA6 | KCNB2 | Potassium voltage-gated channel subfamily B member 2 | Bos taurus (Bovine) | PR |
| Q7T199 | KCNA10 | Potassium voltage-gated channel subfamily A member 10 | Gallus gallus (Chicken) | PR |
| Q96RP8 | KCNA7 | Potassium voltage-gated channel subfamily A member 7 | Homo sapiens (Human) | PR |
| P22001 | KCNA3 | Potassium voltage-gated channel subfamily A member 3 | Homo sapiens (Human) | PR |
| Q16322 | KCNA10 | Potassium voltage-gated channel subfamily A member 10 | Homo sapiens (Human) | PR |
| Q09470 | KCNA1 | Potassium voltage-gated channel subfamily A member 1 | Homo sapiens (Human) | PR |
| P16389 | KCNA2 | Potassium voltage-gated channel subfamily A member 2 | Homo sapiens (Human) | PR |
| P22459 | KCNA4 | Potassium voltage-gated channel subfamily A member 4 | Homo sapiens (Human) | PR |
| P16390 | Kcna3 | Potassium voltage-gated channel subfamily A member 3 | Mus musculus (Mouse) | PR |
| P16388 | Kcna1 | Potassium voltage-gated channel subfamily A member 1 | Mus musculus (Mouse) | PR |
| Q17ST2 | Kcna7 | Potassium voltage-gated channel subfamily A member 7 | Mus musculus (Mouse) | PR |
| Q61423 | Kcna4 | Potassium voltage-gated channel subfamily A member 4 | Mus musculus (Mouse) | PR |
| P15384 | Kcna3 | Potassium voltage-gated channel subfamily A member 3 | Rattus norvegicus (Rat) | PR |
| P10499 | Kcna1 | Potassium voltage-gated channel subfamily A member 1 | Rattus norvegicus (Rat) | PR |
| P63142 | Kcna2 | Potassium voltage-gated channel subfamily A member 2 | Rattus norvegicus (Rat) | PR |
| P15385 | Kcna4 | Potassium voltage-gated channel subfamily A member 4 | Rattus norvegicus (Rat) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MEVAMVSAES | SGCNSHMPYG | YAAQARARER | ERLAHSRAAA | AAAVAAATAA | VEGGGGSGGS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QHHHHPSRGA | CTSHDPQSGR | GSRRRRRPHP | EKKKVHHRQS | SFPHCSDLMP | SGSEEKILRD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LSEEDEEEDD | EEDEEEEGRF | YYSEEDHGEE | CSYTDLLAQD | DGGGGGGGSG | GGGYSSVRYS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DCCERVVINV | SGLRFETQMK | TLAQFPETLL | GDPEKRTQYF | DPLRNEYFFD | RNRPSFDAIL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YYYQSGGRLK | RPVNVPFDIF | TEEVKFYQLG | EEALLKFRED | EGFVREEEDR | ALPENEFKKQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IWLLFEYPES | SSPARGIAIV | SVLVILISIV | IFCLETLPEF | RDDRDLIMAL | STGGHGGLLN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DTSAPHPENS | GHTIFNDPFF | IVETVCIVWF | SFEFVVRCFA | CPSQALFFKN | IMNIIDIVSI |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LPYFITLGTD | LAQQQGGGNG | QQQQAMSFAI | LRIIRLVRVF | RIFKLSRHSK | GLQILGHTLR |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ASMRELGLLI | FFLFIGVILF | SSAVYFAEAD | EPTTHFQSIP | DAFWWAVVTM | TTVGYGDMKP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ITVGGKIVGS | LCAIAGVLTI | ALPVPVIVSN | FNYFYHRETE | NEEQTQLTQN | AVSCPYLPSN |
| 610 | 620 | 630 | 640 | 650 | |
| LLKKFRSSTS | SSLGDKSEYL | EMEEGVKESL | CAKEKCQGKG | DDSETDKNNV | SNAKAVETDV |