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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | Interleukin-1 beta converting enzyme ( ) (ICE) [ , ] is responsible for the cleavage of the IL-1 beta precursor at an Asp-Ala bond to generate the mature biologically active cytokine. ICE a thiol protease composed of two subunits of 10 (p10) and 20 Kd (p20), both derived by the autocleavage of a 45 Kd precursor (p45). Two residues are implicated in the catalytic mechanism: a cysteine and an histidine. They are located in the P20 subunit after cleavage of the precursor. ICE belongs to a family of peptidases [] which is implicated in programmed cell death (apoptosis) and which has been termed 'caspase' for cysteine aspase. ICE is known as Caspase-1 and the other members of this family [] include:Caspase-2 (ICH-1, NEDD-2).Caspase-3 (also known as apopain, CPP32, Yama), a protease which, at the onset of apoptosis, proteolytically cleaves poly(ADP-ribose) polymerase at an Asp-Gly bond.Caspase-4 (ICH-2, TX, ICErel-II).Caspase-5 (ICH-3, TY, ICErel-III).Caspase-6 (MCH-2).Caspase-7 (MCH-3, ICE-LAP3, CMH-1, SCA-2, LICE2).Caspase-8 (MCH-5, MACH, FLICE).Caspase-9 (MCH-6, ICE-LAP6).Caspase-10 (MCH-4, FLICE2).Caspase-11.Caspase-12.Caspase-13 (ERICE).Caspase-14.Caenorhabditis elegans ced-3 involved in the initiation of apoptosis.Drosophila Ice.This entry represents a conserved region containing the histidine active site. | Name | Peptidase family C14A, His active site |
| Short Name | Caspase_his_AS | Type | Active_site |
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