Q80UW2
PR
Gene name |
Fbxo2 (Fbs1, Fbx2) |
Protein name |
F-box only protein 2 |
Names |
|
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:230904 |
EC number |
|
Protein Class |
|
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
8 structures for Q80UW2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1UMH | X-ray | 200 A | A | 117-297 | PDB |
| 1UMI | X-ray | 240 A | A | 117-297 | PDB |
| 2E31 | X-ray | 240 A | A | 1-297 | PDB |
| 2E32 | X-ray | 352 A | A/C | 1-297 | PDB |
| 2E33 | X-ray | 270 A | A | 105-297 | PDB |
| 2RJ2 | X-ray | 170 A | A | 117-297 | PDB |
| 5B4N | X-ray | 230 A | A/B | 117-297 | PDB |
| AF-Q80UW2-F1 | Predicted | AlphaFoldDB |
12 variants for Q80UW2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs3388724423 | 69 | T>K | No | EVA | |
| rs3388739092 | 80 | L>V | No | EVA | |
| rs3388724382 | 91 | L>M | No | EVA | |
| rs3388735476 | 99 | E>V | No | EVA | |
| rs3388725770 | 102 | V>L | No | EVA | |
| rs3388720025 | 150 | W>* | No | EVA | |
| rs3395068707 | 151 | R>K | No | EVA | |
| rs3388732984 | 169 | V>F | No | EVA | |
| rs3388733483 | 173 | F>L | No | EVA | |
| rs3388730609 | 224 | T>I | No | EVA | |
| rs3388731832 | 266 | R>C | No | EVA | |
| rs3388730177 | 297 | P>A | No | EVA |
No associated diseases with Q80UW2
7 regional properties for Q80UW2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Dbl homology (DH) domain | 372 - 560 | IPR000219 |
| domain | FYVE zinc finger | 721 - 790 | IPR000306 |
| domain | Pleckstrin homology domain | 589 - 690 | IPR001849-1 |
| domain | Pleckstrin homology domain | 820 - 922 | IPR001849-2 |
| domain | Zinc finger, FYVE-related | 729 - 789 | IPR017455 |
| domain | FGD1, N-terminal PH domain | 590 - 697 | IPR035939 |
| domain | FGD1-4, C-terminal PH domain | 814 - 919 | IPR035941 |
6 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
| 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. |
| endoplasmic reticulum | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). |
| membrane | A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it. |
| SCF ubiquitin ligase complex | A ubiquitin ligase complex in which a cullin from the Cul1 subfamily and a RING domain protein form the catalytic core; substrate specificity is conferred by a Skp1 adaptor and an F-box protein. SCF complexes are involved in targeting proteins for degradation by the proteasome. The best characterized complexes are those from yeast and mammals (with core subunits named Cdc53/Cul1, Rbx1/Hrt1/Roc1). |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| amyloid-beta binding | Binding to an amyloid-beta peptide/protein. |
| carbohydrate binding | Binding to a carbohydrate, which includes monosaccharides, oligosaccharides and polysaccharides as well as substances derived from monosaccharides by reduction of the carbonyl group (alditols), by oxidation of one or more hydroxy groups to afford the corresponding aldehydes, ketones, or carboxylic acids, or by replacement of one or more hydroxy group(s) by a hydrogen atom. Cyclitols are generally not regarded as carbohydrates. |
7 GO annotations of biological process
| Name | Definition |
|---|---|
| glycoprotein catabolic process | The chemical reactions and pathways resulting in the breakdown of a glycoprotein, a protein that contains covalently bound glycose (i.e. monosaccharide) residues; the glycose occurs most commonly as oligosaccharide or fairly small polysaccharide but occasionally as monosaccharide. |
| negative regulation of cell population proliferation | Any process that stops, prevents or reduces the rate or extent of cell proliferation. |
| protein ubiquitination | The process in which one or more ubiquitin groups are added to a protein. |
| regulation of protein ubiquitination | Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein. |
| SCF-dependent proteasomal ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of ubiquitin, with ubiquitin-protein ligation catalyzed by an SCF (Skp1/Cul1/F-box protein) complex, and mediated by the proteasome. |
| ubiquitin-dependent ERAD pathway | The series of steps necessary to target endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. Begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein ubiquitination necessary for correct substrate transfer, transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. |
| ubiquitin-dependent protein catabolic process | The chemical reactions and pathways resulting in the breakdown of a protein or peptide by hydrolysis of its peptide bonds, initiated by the covalent attachment of a ubiquitin group, or multiple ubiquitin groups, to the protein. |
5 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q17QK6 | FBXO2 | F-box only protein 2 | Bos taurus (Bovine) | PR |
| Q8NI29 | FBXO27 | F-box only protein 27 | Homo sapiens (Human) | PR |
| Q9UK22 | FBXO2 | F-box only protein 2 | Homo sapiens (Human) | PR |
| G3X9C2 | Nccrp1 | F-box only protein 50 | Mus musculus (Mouse) | PR |
| Q6DIA9 | Fbxo27 | F-box only protein 27 | Mus musculus (Mouse) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDGDGDPESV | SHPEEASPEE | QPEEAGAEAS | AEEEQLREAE | EEEEAEAVEY | LAELPEPLLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| RVLAELPATE | LVQACRLVCL | RWKELVDGAP | LWLLKCQQEG | LVPEGSADEE | RDHWQQFYFL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SKRRRNLLRN | PCGEEDLEGW | SDVEHGGDGW | RVEELPGDNG | VEFTQDDSVK | KYFASSFEWC |
| 190 | 200 | 210 | 220 | 230 | 240 |
| RKAQVIDLQA | EGYWEELLDT | TQPAIVVKDW | YSGRTDAGSL | YELTVRLLSE | NEDVLAEFAT |
| 250 | 260 | 270 | 280 | 290 | |
| GQVAVPEDGS | WMEISHTFID | YGPGVRFVRF | EHGGQDSVYW | KGWFGARVTN | SSVWVEP |