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FBXO2-201 ,FBXO2 ,Q9UK22
  • Uniprot Accession= Q9UK22
  • Ensembl Transcript= ENST00000354287.5
  • Uniprot Name= FBXO2
  • Name= F-box only protein 2
  • Chromosome= chr1
  • Driver status= Not Cancer Driver
  • Number of GO Term: 22
GO term GO name GO namespace GO def
GO:0001540 amyloid-beta binding molecular_function Binding to an amyloid-beta peptide/protein. [GOC:hjd]
GO:0004842 ubiquitin-protein transferase activity molecular_function Catalysis of the transfer of ubiquitin from one protein to another via the reaction X-Ub + Y = Y-Ub + X, where both X-Ub and Y-Ub are covalent linkages. [GOC:BioGRID, GOC:jh2, PMID:9635407]
GO:0005515 protein binding molecular_function Binding to a protein. [GOC:go_curators]
GO:0030246 carbohydrate binding molecular_function 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. [GOC:mah]
GO:0031249 denatured protein binding molecular_function Binding to a denatured protein. [GOC:mlg]
GO:0006508 proteolysis biological_process The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah]
GO:0006516 glycoprotein catabolic process biological_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. [GOC:go_curators, ISBN:0198506732]
GO:0008285 negative regulation of cell population proliferation biological_process Any process that stops, prevents or reduces the rate or extent of cell proliferation. [GOC:go_curators]
GO:0016567 protein ubiquitination biological_process The process in which one or more ubiquitin groups are added to a protein. [GOC:ai]
GO:0031146 SCF-dependent proteasomal ubiquitin-dependent protein catabolic process biological_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. [PMID:15380083]
GO:0031396 regulation of protein ubiquitination biological_process Any process that modulates the frequency, rate or extent of the addition of ubiquitin groups to a protein. [GOC:mah]
GO:0036211 protein modification process biological_process The covalent alteration of one or more amino acids occurring in proteins, peptides and nascent polypeptides (co-translational, post-translational modifications). Includes the modification of charged tRNAs that are destined to occur in a protein (pre-translation modification). [GOC:bf, GOC:jl]
GO:0099576 regulation of protein catabolic process at postsynapse, modulating synaptic transmission biological_process Any process that modulates synaptic transmission by regulating a catabolic process occurring at a postsynapse. [GOC:dos]
GO:0005737 cytoplasm cellular_component The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684]
GO:0005783 endoplasmic reticulum cellular_component 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). [ISBN:0198506732]
GO:0005829 cytosol cellular_component The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl]
GO:0043197 dendritic spine cellular_component 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. [GOC:nln]
GO:0098890 extrinsic component of postsynaptic membrane cellular_component The component of the postsynaptic membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region. [GOC:autophagy, GOC:mf]
GO:0098978 glutamatergic synapse cellular_component A synapse that uses glutamate as a neurotransmitter. [GOC:dos]
GO:0019005 SCF ubiquitin ligase complex cellular_component 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). [PMID:15571813, PMID:15688063]
GO:0061630 ubiquitin protein ligase activity molecular_function Catalysis of the transfer of ubiquitin to a substrate protein via the reaction X-ubiquitin + S = X + S-ubiquitin, where X is either an E2 or E3 enzyme, the X-ubiquitin linkage is a thioester bond, and the S-ubiquitin linkage is an amide bond
GO:0036503 ERAD pathway biological_process The protein catabolic pathway which targets endoplasmic reticulum (ER)-resident proteins for degradation by the cytoplasmic proteasome. It begins with recognition of the ER-resident protein, includes retrotranslocation (dislocation) of the protein from the ER to the cytosol, protein modifications necessary for correct substrate transfer (e.g. ubiquitination), transport of the protein to the proteasome, and ends with degradation of the protein by the cytoplasmic proteasome. [GOC:bf, GOC:PARL, PMID:20940304, PMID:21969857]