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 P97838
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P97838-F1 | Predicted | AlphaFoldDB |
No variants for P97838
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P97838 | |||||
No associated diseases with P97838
No regional properties for P97838
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P97838 | |||
10 GO annotations of cellular component
| Name | Definition |
|---|---|
| anchoring junction | A cell junction that mechanically attaches a cell (and its cytoskeleton) to neighboring cells or to the extracellular matrix. |
| cholinergic synapse | A synapse that uses acetylcholine as a 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. |
| glutamatergic synapse | A synapse that uses glutamate as a neurotransmitter. |
| neuromuscular junction | The junction between the axon of a motor neuron and a muscle fiber. In response to the arrival of action potentials, the presynaptic button releases molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane of the muscle fiber, leading to a change in post-synaptic potential. |
| neuronal cell body | The portion of a neuron that includes the nucleus, but excludes cell projections such as axons and dendrites. |
| plasma membrane | The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins. |
| postsynaptic density | An electron dense network of proteins within and adjacent to the postsynaptic membrane of an asymmetric, neuron-neuron synapse. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. |
| postsynaptic specialization | A network of proteins within and adjacent to the postsynaptic membrane. Its major components include neurotransmitter receptors and the proteins that spatially and functionally organize them such as anchoring and scaffolding molecules, signaling enzymes and cytoskeletal components. |
| synapse | The junction between an axon of one neuron and a dendrite of another neuron, a muscle fiber or a glial cell. As the axon approaches the synapse it enlarges into a specialized structure, the presynaptic terminal bouton, which contains mitochondria and synaptic vesicles. At the tip of the terminal bouton is the presynaptic membrane; facing it, and separated from it by a minute cleft (the synaptic cleft) is a specialized area of membrane on the receiving cell, known as the postsynaptic membrane. In response to the arrival of nerve impulses, the presynaptic terminal bouton secretes molecules of neurotransmitters into the synaptic cleft. These diffuse across the cleft and transmit the signal to the postsynaptic membrane. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| amyloid-beta binding | Binding to an amyloid-beta peptide/protein. |
| molecular adaptor activity | The binding activity of a molecule that brings together two or more molecules through a selective, non-covalent, often stoichiometric interaction, permitting those molecules to function in a coordinated way. |
| PDZ domain binding | Binding to a PDZ domain of a protein, a domain found in diverse signaling proteins. |
| protein domain specific binding | Binding to a specific domain of a protein. |
| scaffold protein binding | Binding to a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| modification of synaptic structure | Any process that modifies the structure/morphology of a synapse. |
| protein-containing complex assembly | The aggregation, arrangement and bonding together of a set of macromolecules to form a protein-containing complex. |
| regulation of postsynaptic neurotransmitter receptor activity | Any process that modulates the frequency, rate or extent of neurotransmitter receptor activity involved in synaptic transmission. Modulation may be via an effect on ligand affinity, or effector funtion such as ion selectivity or pore opening/closing in ionotropic receptors. |
| signaling | The entirety of a process in which information is transmitted within a biological system. This process begins with an active signal and ends when a cellular response has been triggered. |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRGYHGDRGS | HPRPARFADQ | QHMDVGPAAR | APYLLGSREA | FSTEPRFCAP | RAGLGHLSPE |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GPLSLSEGPS | SVGPEGGPGG | VGAGGSSSTF | PRMYPGQGPF | DTCEDCVGHP | QGKGATRLLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TFLDQFEKQL | PVQQDGFHTL | PYQRGPAGPG | PGPGSGAAPE | ARSESPSRIR | HLVHSVQKLF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AKSHSLEAPG | KRDYNGPKAE | GRSSSGGDSY | SGPGSGGPPT | SHHHHHHHHH | HHHQSRHGKR |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SKSKDRKGDG | RHQTKATGWW | SSDDNLDSDS | GFLGGRPPGE | PGGPFCLDAP | DGSYRDLSFK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GRSGGSEGRC | LACTGMSMSL | DGQSVKRSAW | HTMMVSQGRD | GYPGAGPGKG | LLGPETKAKA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RTYHYLQVPQ | DDWGGYPTGG | KDGEIPCRRM | RSGSYIKAMG | DEESGDSDGS | PKTSPKALAR |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RFASRRSSSV | DTARINCCVP | PRIHPRSSIP | GYSRSLTTGQ | LSEEFNQQLE | AVCGSVFGEL |
| 490 | 500 | 510 | 520 | 530 | 540 |
| ESQAVDALDL | PGCFRMRSHS | YLRAIQAGCS | QDDDCLPLLA | APASVSGRPG | SSFNFRKAPP |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PIPPGSQAPP | RISITAQSST | DSAHESFTAA | EGPARRCSSA | DGLDGPTMGA | RTLELAPVPP |
| 610 | 620 | 630 | 640 | 650 | 660 |
| RASPKPPTLI | IKTIPGREEL | RSLARQRKWR | PSIGVQVETI | SDSDTENRSR | REFHSIGVQV |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EEDKRRARFK | RSNSVTAGVQ | ADLELEGLAG | LATVATEDKA | LQFGRPFQRQ | ASEPQPGPRA |
| 730 | 740 | 750 | 760 | 770 | 780 |
| PTYSVFRTVH | TQGQWAYREG | YPLPYEPPAT | DGSPGPPPVP | APGPGSGRRD | SWMERGSRSL |
| 790 | 800 | 810 | 820 | 830 | 840 |
| PDSGRTSPCP | RDGEWFIKML | RAEVEKLEHW | CQQMEREAED | YELPEEILEK | IRSAVGSTQL |
| 850 | 860 | 870 | 880 | 890 | 900 |
| LLSQKVQQFF | RLCQQSLDPT | AFPVPTFQDL | AGFWDLLQLS | IEDVTLKFLE | LQQLKANSWK |
| 910 | 920 | 930 | 940 | 950 | 960 |
| LLEPKEEKKV | PPPIPKKPSR | GRGVPVKERS | LDSVDRQRQE | ARKRLLAAKR | AASFRHSSAT |
| 970 | |||||
| ESADSIEIYI | PEAQTRL |