Literature summary for 3.4.21.112 extracted from

Espenshade, P.J.; Cheng, D.; Goldstein, J.L.; Brown, M.S.
Autocatalytic processing of site-1 protease removes propeptide and permits cleavage of sterol regulatory element-binding proteins (1999), J. Biol. Chem., 274, 22795-22804.

Search for more literature for 3.4.21.112

Cloned(Commentary)

Cloned (Comment)	Organism
-	Cricetulus griseus

Protein Variants

Protein Variants	Comment	Organism
S414A	inactive mutant, no autocatalytic processing to generate S1P-C	Cricetulus griseus

Organism

Organism	UniProt	Comment	Textmining
Cricetulus griseus	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
glycoprotein	six potential N-glycosylation sites	Cricetulus griseus
proteolytic modification	protein is inactive and undergoes autocatalytic processing, generating an active form S1P-B, which is further cleaved at an internal RRLL sequence to generate an active S1P-C	Cricetulus griseus

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	initiates a process by which the transcriptionally active N-terminal fragments of SREBPs are released from membranes	Cricetulus griseus	?	-	?
sterol regulatory element-binding protein + H2O	SREBP	Cricetulus griseus	?	-	?

Synonyms

Synonyms	Comment	Organism
S1P	-	Cricetulus griseus

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Release 2023.1 (January 2023)