FUNCTION Apoptosis regulator protein which may function as a crucial link between cell survival and cell death pathways in mammalian cells (PubMed:31046799). Acts as an inhibitor of TNFRSF6 mediated apoptosis. A proteolytic fragment (p43) is likely retained in the death-inducing signaling complex (DISC) thereby blocking further recruitment and processing of caspase-8 at the complex. Full length and shorter isoforms have been shown either to induce apoptosis or to reduce TNFRSF-triggered apoptosis. Lacks enzymatic (caspase) activity.SUBUNIT TNFRSF6 stimulation triggers recruitment to the death-inducing signaling complex (DISC) formed by TNFRSF6, FADD and CASP8 (PubMed:9880531). A proteolytic fragment (p43) stays associated with the DISC (PubMed:9880531). Also interacts with FADD, CASP8, CASP3, TRAF1, TRAF2 and Bcl-X(L) (in vitro) (PubMed:9208847, PubMed:9326610). Interacts with RIPK1 (By similarity) (PubMed:9208847, PubMed:9326610, PubMed:9880531). Interacts with GMEB1 (PubMed:31046799).SUBUNIT (Microbial infection) Interacts with HBV protein X.INTERACTION Widely expressed. Higher expression in skeletal muscle, pancreas, heart, kidney, placenta, and peripheral blood leukocytes. Also detected in diverse cell lines. Isoform 8 is predominantly expressed in testis and skeletal muscle.INDUCTION Repressed by IL2/interleukin-2 after TCR stimulation, during progression to the S phase of the cell cycle.DOMAIN The caspase domain lacks the active site residues involved in catalysis.PTM Proteolytically processed by CASP8 generating subunit p43 and p12.PTM Deubiquitinated by USP40, leading to stabilization.MISCELLANEOUS May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.SIMILARITY Belongs to the peptidase C14A family.
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