MBTPS2 (S2P) cleaves CREB3

Stable Identifier
Reaction [transition]
Homo sapiens
Locations in the PathwayBrowser
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CREB3 is cleaved by regulated intramembrane proteolysis (RIP) (Raggo et al. 2002, Liang et al. 2006, Eleveld-Trancikova et al. 2010). As inferred from other RIP susbsrates, MBTPS2 (S2P) is believed to cleave CREB3 after MBTPS1 (S1P) cleaves (Raggo et al. 2002). Based on homology with cleavage sites in SREBP (SREBF) homologues, the cleavage site in CREB3 is estimated to be at about amino acid 254 at the cytoplasmic face of the transmembrane domain (Raggo et al. 2002).
Literature References
PubMed ID Title Journal Year
20546900 DC-STAMP interacts with ER-resident transcription factor LUMAN which becomes activated during DC maturation

van Hout-Kuijer, MA, Eleveld-Trancikova, D, Jansen, BJ, Sanecka, A, Adema, GJ, Hendriks, IA, Looman, MW

Mol. Immunol. 2010
16940180 Luman/CREB3 induces transcription of the endoplasmic reticulum (ER) stress response protein Herp through an ER stress response element

Lu, R, Martyn, AC, Dean, JD, Cockram, GP, Kokame, K, Li, Y, Audas, TE, Liang, G

Mol. Cell. Biol. 2006
12138176 Luman, the cellular counterpart of herpes simplex virus VP16, is processed by regulated intramembrane proteolysis

O'Hare, P, Raggo, C, Gobeil, P, Misra, V, Smith-Windsor, E, Stirling, J, Rapin, N

Mol. Cell. Biol. 2002
Catalyst Activity

metalloendopeptidase activity of MBTPS2 [Golgi membrane]

Inferred From
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