Descriptions
Autoinhibitory domains (AIDs)
Target domain |
147-355 (BAR domain) |
Relief mechanism |
Partner binding |
Assay |
|
Target domain |
147-355 (BAR domain) |
Relief mechanism |
Partner binding |
Assay |
|
Accessory elements
No accessory elements
References
- Karlsen ML et al. (2015) "Structure of Dimeric and Tetrameric Complexes of the BAR Domain Protein PICK1 Determined by Small-Angle X-Ray Scattering", Structure (London, England : 1993), 23, 1258-1270
- Madasu Y et al. (2015) "PICK1 is implicated in organelle motility in an Arp2/3 complex-independent manner", Molecular biology of the cell, 26, 1308-22
Autoinhibited structure

Activated structure

1 structures for Q2T9M1
Entry ID | Method | Resolution | Chain | Position | Source |
---|---|---|---|---|---|
AF-Q2T9M1-F1 | Predicted | AlphaFoldDB |
No variants for Q2T9M1
Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
---|---|---|---|---|---|
No variants for Q2T9M1 |
No associated diseases with Q2T9M1
4 regional properties for Q2T9M1
Type | Name | Position | InterPro Accession |
---|---|---|---|
domain | Homeobox domain | 505 - 569 | IPR001356 |
conserved_site | Homeobox, conserved site | 540 - 563 | IPR017970 |
domain | Homeobox domain, metazoa | 529 - 540 | IPR020479-1 |
domain | Homeobox domain, metazoa | 544 - 563 | IPR020479-2 |
Functions
8 GO annotations of cellular component
Name | Definition |
---|---|
cytoskeleton | A cellular structure that forms the internal framework of eukaryotic and prokaryotic cells. The cytoskeleton includes intermediate filaments, microfilaments, microtubules, the microtrabecular lattice, and other structures characterized by a polymeric filamentous nature and long-range order within the cell. The various elements of the cytoskeleton not only serve in the maintenance of cellular shape but also have roles in other cellular functions, including cellular movement, cell division, endocytosis, and movement of organelles. |
neuron projection | A prolongation or process extending from a nerve cell, e.g. an axon or dendrite. |
perinuclear region of cytoplasm | Cytoplasm situated near, or occurring around, the nucleus. |
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 early endosome | An early endosome of the postsynapse. It acts as the major sorting station on the endocytic pathway, targeting neurotransmitter receptors for degregation or recycling. |
synaptic vesicle | A secretory organelle, typically 50 nm in diameter, of presynaptic nerve terminals; accumulates in high concentrations of neurotransmitters and secretes these into the synaptic cleft by fusion with the 'active zone' of the presynaptic plasma membrane. |
trans-Golgi network membrane | The lipid bilayer surrounding any of the compartments that make up the trans-Golgi network. |
6 GO annotations of molecular function
Name | Definition |
---|---|
actin filament binding | Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits. |
Arp2/3 complex binding | Binding to an Arp2/3 complex, a protein complex that contains two actin-related proteins, Arp2 and Arp3, and five novel proteins (ARPC1-5). |
metal ion binding | Binding to a metal ion. |
phospholipid binding | Binding to a phospholipid, a class of lipids containing phosphoric acid as a mono- or diester. |
protein domain specific binding | Binding to a specific domain of a protein. |
protein kinase C binding | Binding to protein kinase C. |
11 GO annotations of biological process
Name | Definition |
---|---|
cellular response to decreased oxygen levels | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus reflecting a decline in the level of oxygen. |
cellular response to glucose starvation | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of deprivation of glucose. |
dendritic spine maintenance | The organization process that preserves a dendritic spine in a stable functional or structural state. A dendritic spine is a specialized protrusion from a neuronal dendrite and is involved in synaptic transmission. |
dendritic spine organization | A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of a dendritic spine. A dendritic spine is a specialized protrusion from a neuronal dendrite and is involved in synaptic transmission. |
glial cell development | The process aimed at the progression of a glial cell over time, from initial commitment of the cell to a specific fate, to the fully functional differentiated cell. |
intracellular protein transport | The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell. |
long-term synaptic depression | A process that modulates synaptic plasticity such that synapses are changed resulting in the decrease in the rate, or frequency of synaptic transmission at the synapse. |
negative regulation of Arp2/3 complex-mediated actin nucleation | Any process that stops, prevents, or reduces the frequency, rate or extent of actin nucleation mediated by the Arp2/3 complex and interacting proteins. |
positive regulation of receptor internalization | Any process that activates or increases the frequency, rate or extent of receptor internalization. |
receptor clustering | The receptor metabolic process that results in grouping of a set of receptors at a cellular location, often to amplify the sensitivity of a signaling response. |
regulation of Arp2/3 complex-mediated actin nucleation | Any process that modulates the frequency, rate or extent of actin nucleation mediated by the Arp2/3 complex and interacting proteins. |
10 | 20 | 30 | 40 | 50 | 60 |
MFADLGYDIE | EDKLGIPTVP | GKVTLQKDAQ | NLIGISIGGG | AQYCPCLYIV | QVFDNTPAAL |
70 | 80 | 90 | 100 | 110 | 120 |
DGTVAAGDEI | TGVNGRSIKG | KTKVEVAKMI | QEVKGEVTIH | YNKLQADPKQ | GMSLDIVLKK |
130 | 140 | 150 | 160 | 170 | 180 |
VKHRLVENMS | SGTADALGLS | RAILCNDGLV | KRLEELERTA | ELYKGMTEHT | KNLLRAFYEL |
190 | 200 | 210 | 220 | 230 | 240 |
SQTHRAFGDV | FSVIGVREPQ | PAASEAFVKF | ADAHRSIEKF | GIRLLKTIKP | MLTDLNTYLN |
250 | 260 | 270 | 280 | 290 | 300 |
KAIPDTRLTI | KKYLDVKFEY | LSYCLKVKEM | DDEEYSCIAL | GEPLYRVSTG | NYEYRLILRC |
310 | 320 | 330 | 340 | 350 | 360 |
RQEARARFSQ | MRKDVLEKME | LLDQEHVQDI | VLQLQRFVST | MSKYYNDCYS | VLRDADVFPI |
370 | 380 | 390 | 400 | 410 | |
EVDLAHTTLA | YGLSQDEFTD | GEDEEDEDEE | DTAAGEPPRD | SRGAAGPLDK | GGSWCNS |