BP

GO:0006605

protein targeting

The process of targeting specific proteins to particular regions of the cell, typically membrane-bounded subcellular organelles. Usually requires an organelle specific protein sequence motif.

IEA

BP

GO:0006621

protein retention in ER lumen

The retention in the endoplasmic reticulum (ER) lumen of soluble resident proteins. Sorting receptors retrieve proteins with ER localization signals, such as KDEL and HDEL sequences or some transmembrane domains, that have escaped to the cis-Golgi network and return them to the ER. Abnormally folded proteins and unassembled subunits are also selectively retained in the ER.

IDA

BP

GO:0016567

protein ubiquitination

The process in which one or more ubiquitin groups are added to a protein.

IMP

BP

GO:0030433

ER-associated ubiquitin-dependent protein catabolic process

The chemical reactions and pathways resulting in the breakdown of proteins transported from the endoplasmic reticulum and targeted to cytoplasmic proteasomes for degradation. This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins.

IMP

BP

GO:0034976

response to endoplasmic reticulum stress

Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stress acting at the endoplasmic reticulum. ER stress usually results from the accumulation of unfolded or misfolded proteins in the ER lumen.

IDA

BP

GO:0042787

protein ubiquitination involved in ubiquitin-dependent protein catabolic process

The process in which a ubiquitin group, or multiple groups, are covalently attached to the target protein, thereby initiating the degradation of that protein.

IMP

BP

GO:1904153

negative regulation of retrograde protein transport, ER to cytosol

Any process that stops, prevents or reduces the frequency, rate or extent of retrograde protein transport, ER to cytosol.

IMP

BP

GO:1904380

endoplasmic reticulum mannose trimming

Any protein alpha-1,2-demannosylation that takes place in the endoplasmic reticulum quality control compartment (ERQC).

TAS

CC

GO:0000836

Hrd1p ubiquitin ligase complex

A multiprotein complex that recognizes and ubiquitinates proteins with misfolded luminal and membrane domains during ER-associated protein degradation (ERAD). In S. cerevisiae, this complex contains the ubiquitin ligase Hrd1p. In mammals, this complex contains the ubiquitin ligase HRD1 (Synoviolin) or AMFR (gp78).

IDA|NAS

CC

GO:0005788

endoplasmic reticulum lumen

The volume enclosed by the membranes of the endoplasmic reticulum.

IDA

CC

GO:0005789

endoplasmic reticulum membrane

The lipid bilayer surrounding the endoplasmic reticulum.

TAS

CC

GO:0044322

endoplasmic reticulum quality control compartment

A subcompartment of the endoplasmic reticulum in which proteins with improper or incorrect folding accumulate. Enzymes in this compartment direct proteins with major folding problems to translocation to the cytosol and degradation, and proteins with minor folding problems to the ER, to interact with chaperon proteins.

IEA

MF

GO:0001948

glycoprotein binding

Interacting selectively and non-covalently with a glycoprotein, a protein that contains covalently bound glycose (monosaccharide) residues. These also include proteoglycans.

IDA

MF

GO:0002020

protease binding

Interacting selectively and non-covalently with any protease or peptidase.

IEA

MF

GO:0005515

protein binding

Interacting selectively and non-covalently with any protein or protein complex (a complex of two or more proteins that may include other nonprotein molecules).

IPI

MF

GO:0030246

carbohydrate binding

Interacting selectively and non-covalently with any 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.

IEA