Peptide-N(4)-(N-acetyl-beta-glucosaminyl)asparagine amidase; Specifically deglycosylates the denatured form of N-linked glycoproteins in the cytoplasm and assists their proteasome-mediated degradation. Cleaves the beta-aspartyl-glucosamine (GlcNAc) of the glycan and the amide side chain of Asn, converting Asn to Asp. Prefers proteins containing high-mannose over those bearing complex type oligosaccharides. Can recognize misfolded proteins in the endoplasmic reticulum that are exported to the cytosol to be destroyed and deglycosylate them, while it has no activity toward native proteins [...]

Ubiquitin-60S ribosomal protein L40; [Ubiquitin]: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is invol [...]

Regulatory particle non-ATPase 10 (Rpn10) encodes one of the polyubiquitin receptor subunits of the 26S proteasome. It recognizes and binds the polyubiquitin moiety of proteins intended for proteasomal degradation or the ubiquitin-like domain of extraproteasomal ubiquitin receptors.

26S proteasome non-ATPase regulatory subunit 2; Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair; Belongs to the proteasome subunit S2 family.

DNA repair protein Rad23; Rad23 (Rad23) encodes an evolutionarily conserved member of the proteasome-associated proteins. It acts as a shuttle -or bridge- protein helping ubiquitinated proteins to interact with the proteasome, which in turn regulates their turnover.

26S proteasome regulatory subunit 4; Regulatory particle triple-A ATPase 2 (Rpt2) encodes one of six ATPases that form the base of the regulatory 19S cap of the proteasome. The Rpt2 product is involved in the recognition of specific substrates destined for degradation, such as those involved in Notch signalling pathway.

26S proteasome non-ATPase regulatory subunit 14; Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear (By similarity). Belongs to the peptidase M67A family. PSMD14 subfamily.

Polyubiquitin; Ubiquitin exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-48-linked is involved in protein degradatio [...]

Ubiquitin-5E, isoform A; Protein tag; ubiquitin protein ligase binding. It is involved in the biological process described with: ubiquitin-dependent protein catabolic process; protein ubiquitination; modification-dependent protein catabolic process; cellular protein modification process.