Literature summary for 3.4.23.B24 extracted from

Chen, C.Y.; Malchus, N.S.; Hehn, B.; Stelzer, W.; Avci, D.; Langosch, D.; Lemberg, M.K.
Signal peptide peptidase functions in ERAD to cleave the unfolded protein response regulator XBP1u (2014), EMBO J., 33, 2492-2506.

Search for more literature for 3.4.23.B24

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
HEK-293T cell	-	Homo sapiens	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
unfolded protein response regulator XBP1u + H2O	-	Homo sapiens	?	cleavage occurs within a so far unrecognized type II transmembrane domain, which renders XBP1u as an signal peptide peptidase substrate through specific sequence features	?

General Information

General Information	Comment	Organism
physiological function	signal peptide peptidase forms a complex with the ER-associated degradation factor Derlin1 and the E3 ubiquitin ligase TRC8 to cleave the unfolded protein response regulator XBP1u. Cleavage occurs within a so far unrecognized type II transmembrane domain, which renders XBP1u as an signal peptide peptidase substrate through specific sequence features. Additionally, Derlin1 acts in the complex as a substrate receptor by recognizing the luminal tail of XBP1u	Homo sapiens

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Release 2023.1 (January 2023)