RING/FYVE/PHD zinc finger superfamily protein.

Ubiquitin-40S ribosomal protein S27a-3; 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-11-linked is invol [...]

RING/FYVE/PHD zinc finger superfamily protein.

Probable E3 ubiquitin ligase SUD1; Probable E3 ubiquitin ligase acting as a positive post- transcriptional regulator of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity. Might be involved in the quality control that degrades misfolded proteins (By similarity).

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

Alpha-mannosidase I MNS4; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

Alpha-mannosidase I MNS5; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

UDP-glucose:glycoprotein glucosyltransferase; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin- sensing 2 (FLS2) signaling.

Alpha-mannosidase I MNS4; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

Alpha-mannosidase I MNS4; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Alpha-mannosidase I MNS5; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Alpha-mannosidase I MNS4; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

UDP-glucose:glycoprotein glucosyltransferase; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin- sensing 2 (FLS2) signaling.

Alpha-mannosidase I MNS5; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.

Alpha-mannosidase I MNS5; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Alpha-mannosidase I MNS4; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

Alpha-mannosidase I MNS5; Can convert Man(9)GlcNAc(2) and Man(8)GlcNAc(2) into N- glycans with a terminal alpha-1,6-linked Man residue in the C-branch. Functions in the formation of unique N-glycan structures that are specifically recognized by components of the endoplasmic reticulum- associated degradation (ERAD) machinery, which leads to the degradation of misfolded glycoproteins. Most likely generates N-glycan signal on misfolded glycoproteins that is subsequently recognized by OS9. Required for ERAD of the heavily glycosylated and misfolded BRI1 variants BRI1-5 and BRI1-9. Does not [...]

UDP-glucose:glycoprotein glucosyltransferase; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin- sensing 2 (FLS2) signaling.

Ubiquitin-40S ribosomal protein S27a-1; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-2; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-1; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-3; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-2; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-1; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-2; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-3; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-3; 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-11-linked is invol [...]

RING/FYVE/PHD zinc finger superfamily protein.

Ubiquitin-40S ribosomal protein S27a-3; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-1; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-3; 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-11-linked is invol [...]

Ubiquitin-40S ribosomal protein S27a-2; 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-11-linked is invol [...]

Probable E3 ubiquitin ligase SUD1; Probable E3 ubiquitin ligase acting as a positive post- transcriptional regulator of 3-hydroxy-3-methylglutaryl-coenzyme A reductase activity. Might be involved in the quality control that degrades misfolded proteins (By similarity).

RING/FYVE/PHD zinc finger superfamily protein.

UDP-glucose:glycoprotein glucosyltransferase; Recognizes glycoproteins with minor folding defects. Reglucosylates single N-glycans near the misfolded part of the protein, thus providing quality control for protein folding in the endoplasmic reticulum. Reglucosylated proteins are recognized by calreticulin for recycling to the endoplasmic reticulum and refolding or degradation. Required for elongation factor Tu receptor (EFR), but not flagellin- sensing 2 (FLS2) signaling.

Mannosyl-oligosaccharide 1,2-alpha-mannosidase MNS3; Class I alpha-mannosidase essential for early N-glycan processing. Removes preferentially alpha-1,2-linked mannose residues from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2). Involved in root development and cell wall biosynthesis.