AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

GM09977p; Nucleic acid binding.

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

Derlin-1; May be involved in the degradation process of specific misfolded endoplasmic reticulum (ER) luminal proteins. May also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation.

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

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 [...]

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

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.

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

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 [...]

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

Ubiquitin-40S ribosomal protein S27a; 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 involve [...]

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

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.

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

Transitional endoplasmic reticulum ATPase TER94; Necessary for the fragmentation of Golgi stacks during mitosis and for their reassembly after mitosis. Involved in the formation of the transitional endoplasmic reticulum (tER). The transfer of membranes from the endoplasmic reticulum to the Golgi apparatus occurs via 50-70 nm transition vesicles which derive from part-rough, part-smooth transitional elements of the endoplasmic reticulum (tER). Vesicle budding from the tER is an ATP-dependent process. Involved in the ubiquitin-proteasome system. Important for oskar mRNA localization and/ [...]

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

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.

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

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 [...]

Uncharacterized protein, isoform A; Myosin binding; mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity. It is involved in the biological process described with: protein deglycosylation.

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 [...]

Uncharacterized protein, isoform A; Myosin binding; mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity. It is involved in the biological process described with: protein deglycosylation.

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 [...]

Uncharacterized protein, isoform A; Myosin binding; mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity. It is involved in the biological process described with: protein deglycosylation.

Ubiquitin-40S ribosomal protein S27a; 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 involve [...]

Uncharacterized protein, isoform A; Myosin binding; mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity. It is involved in the biological process described with: protein deglycosylation.

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.

Uncharacterized protein, isoform A; Myosin binding; mannosyl-glycoprotein endo-beta-N-acetylglucosaminidase activity. It is involved in the biological process described with: protein deglycosylation.

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 [...]

GM09977p; Nucleic acid binding.

AT15685p; Ubiquitin binding; polyubiquitin modification-dependent protein binding; damaged DNA binding; proteasome binding. It is involved in the biological process described with: nucleotide-excision repair; proteasome-mediated ubiquitin-dependent protein catabolic process.

GM09977p; Nucleic acid binding.

Derlin-1; May be involved in the degradation process of specific misfolded endoplasmic reticulum (ER) luminal proteins. May also involved in endoplasmic reticulum stress-induced pre-emptive quality control, a mechanism that selectively attenuates the translocation of newly synthesized proteins into the endoplasmic reticulum and reroutes them to the cytosol for proteasomal degradation.

GM09977p; Nucleic acid binding.

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 [...]

GM09977p; Nucleic acid binding.

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.

GM09977p; Nucleic acid binding.

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 [...]