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Literature summary for 3.4.22.60 extracted from

  • Fernandes-Alnemri, T.; Armstrong, R.C.; Krebs, J.F.; Srinivasula, S.M.; Wang, L.; Bullrich, F.; Fritz, L.C.; Trapani, J.A.; Tomaselli, K.J.; Litwack, G.; Alnemri, E.S.
    In vitro activation of CPP32 and Mch3 by Mch4, a novel human apoptotic cysteine protease containing two FADD-like domains (1996), Proc. Natl. Acad. Sci. USA, 93, 7464-7469.
    View publication on PubMedView publication on EuropePMC
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Organism

Organism UniProt Comment Textmining
Homo sapiens P55210
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification both Mch4 and the serine protease granzyme B cleave proMch3 at a conserved IXXD-S sequence to produce the large and small subunits of the active protease. Mch3 is a target of mature protease in apoptotic cells Homo sapiens