BP

GO:0018279

protein N-linked glycosylation via asparagine

The glycosylation of protein via the N4 atom of peptidyl-asparagine forming N4-glycosyl-L-asparagine; the most common form is N-acetylglucosaminyl asparagine; N-acetylgalactosaminyl asparagine and N4 glucosyl asparagine also occur. This modification typically occurs in extracellular peptides with an N-X-(ST) motif. Partial modification has been observed to occur with cysteine, rather than serine or threonine, in the third position; secondary structure features are important, and proline in the second or fourth positions inhibits modification.

IBA

BP

GO:0030968

endoplasmic reticulum unfolded protein response

The series of molecular signals generated as a consequence of the presence of unfolded proteins in the endoplasmic reticulum (ER) or other ER-related stress; results in changes in the regulation of transcription and translation.

IBA

BP

GO:0051084

de novo' posttranslational protein folding

The process of assisting in the correct noncovalent folding of newly formed polypeptides or folding intermediates of polypeptides that have exited the ribosome and/or have been stabilized and transferred by other chaperone proteins. This process could involve several cycles of ATP hydrolysis.

TAS

BP

GO:0071712

ER-associated misfolded protein catabolic process

The chemical reactions and pathways resulting in the breakdown of misfolded proteins transported from the endoplasmic reticulum and targeted to cytoplasmic proteasomes for degradation.

IBA

BP

GO:0097359

UDP-glucosylation

The covalent attachment of a UDP-glucose residue to a substrate molecule.

IEA

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:0005783

endoplasmic reticulum

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).

IDA

CC

GO:0005788

endoplasmic reticulum lumen

The volume enclosed by the membranes of the endoplasmic reticulum.

TAS

CC

GO:0005793

endoplasmic reticulum-Golgi intermediate compartment

A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.

ISS

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

CC

GO:0070062

extracellular exosome

A membrane-bounded vesicle that is released into the extracellular region by fusion of the limiting endosomal membrane of a multivesicular body with the plasma membrane. Extracellular exosomes, also simply called exosomes, have a diameter of about 40-100 nm.

IDA

MF

GO:0003980

UDP-glucose:glycoprotein glucosyltransferase activity

Catalysis of the addition of UDP-glucose on to asparagine-linked (N-linked) oligosaccharides of the form Man7-9GlcNAc2 on incorrectly folded glycoproteins.

IDA|TAS

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:0051082

unfolded protein binding

Interacting selectively and non-covalently with an unfolded protein.

IDA