BIRC2

The protein encoded by this gene is a member of a family of proteins that inhibits apoptosis by binding to tumor necrosis factor receptor-associated factors TRAF1 and TRAF2, probably by interfering with activation of ICE-like proteases. This encoded protein inhibits apoptosis induced by serum deprivation and menadione, a potent inducer of free radicals. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jan 2012]

Baculoviral IAP Repeat Containing 2

Multi-functional protein which regulates not only caspases and apoptosis, but also modulates inflammatory signaling and immunity, mitogenic kinase signaling, and cell proliferation, as well as cell invasion and metastasis. Acts as an E3 ubiquitin-protein ligase regulating NF-kappa-B signaling and regulates both canonical and non-canonical NF-kappa-B signaling by acting in opposite directions: acts as a positive regulator of the canonical pathway and suppresses constitutive activation of non-canonical NF-kappa-B signaling. The target proteins for its E3 ubiquitin-protein ligase activity include: RIPK1, RIPK2, RIPK3, RIPK4, CASP3, CASP7, CASP8, TRAF2, DIABLO/SMAC, MAP3K14/NIK, MAP3K5/ASK1, IKBKG/NEMO, IKBKE and MXD1/MAD1. Can also function as an E3 ubiquitin-protein ligase of the NEDD8 conjugation pathway, targeting effector caspases for neddylation and inactivation. Acts as an important regulator of innate immune signaling via regulation of Toll-like receptors (TLRs), Nodlike receptors (NLRs) and RIG-I like receptors (RLRs), collectively referred to as pattern recognition receptors (PRRs). Protects cells from spontaneous formation of the ripoptosome, a large multi-protein complex that has the capability to kill cancer cells in a caspase-dependent and caspase-independent manner. Suppresses ripoptosome formation by ubiquitinating RIPK1 and CASP8. Can stimulate the transcriptional activity of E2F1. Plays a role in the modulation of the cell cycle.

Cell surface receptor signaling pathway Source: ProtInc
I-kappaB kinase/NF-kappaB signaling Source: Reactome
MyD88-independent toll-like receptor signaling pathway Source: Reactome
Necroptotic process Source: Ensembl
Negative regulation of apoptotic process Source: UniProtKB
Negative regulation of necroptotic process Source: GO_Central
Negative regulation of ripoptosome assembly involved in necroptotic process Source: Ensembl
NIK/NF-kappaB signaling Source: UniProtKB
Placenta development Source: Ensembl
Positive regulation of I-kappaB kinase/NF-kappaB signaling Source: UniProtKB
Positive regulation of protein K48-linked ubiquitination Source: UniProtKB
Positive regulation of protein K63-linked ubiquitination Source: UniProtKB
Positive regulation of protein monoubiquitination Source: UniProtKB
Positive regulation of protein ubiquitination Source: GO_Central
Proteasome-mediated ubiquitin-dependent protein catabolic process Source: UniProtKB
Protein deubiquitination Source: Reactome
Protein polyubiquitination Source: UniProtKB
Regulation of apoptotic process Source: UniProtKB
Regulation of cell cycle Source: UniProtKB
Regulation of cell differentiation Source: UniProtKB
Regulation of cell population proliferation Source: UniProtKB
Regulation of cysteine-type endopeptidase activity Source: UniProtKB
Regulation of inflammatory response Source: UniProtKB
Regulation of innate immune response Source: UniProtKB
Regulation of necroptotic process Source: UniProtKB
Regulation of NIK/NF-kappaB signaling Source: Ensembl
Regulation of nucleotide-binding oligomerization domain containing signaling pathway Source: UniProtKB
Regulation of reactive oxygen species metabolic process Source: Ensembl
Regulation of RIG-I signaling pathway Source: UniProtKB
Regulation of toll-like receptor signaling pathway Source: UniProtKB
Regulation of tumor necrosis factor-mediated signaling pathway Source: Reactome
Response to cAMP Source: Ensembl
Response to ethanol Source: Ensembl
Response to hypoxia Source: Ensembl
TRIF-dependent toll-like receptor signaling pathway Source: Reactome
Tumor necrosis factor-mediated signaling pathway Source: Reactome

Cytoplasm; Nucleus. Agents that induce either the extrinsic or intrinsic apoptotic pathways promote its redistribution from the nuclear compartment to the cytoplasmic compartment. Associated with the midbody in telophase cells, and found diffusely in the nucleus of interphase cells.

Auto-ubiquitinated and degraded by the proteasome in apoptotic cells.
Upon stimulation of death receptors, including TNFRSF10B, recruited to receptors and cleaved by caspases. Proteolytic fragments remain associated with the receptors. This cleavage presumably inactivates the protein.