Serine-threonine kinase which is a key regulator of TNF- mediated apoptosisnecroptosis and inflammatory pathways. Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival. Has kinase-independent scaffold functions: upon binding of TNF to TNFR1RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survivalin partby activating the canonical NF-kappa-B pathway. Kinase activity is essential to regulate necroptosis and apoptosistwo parallel forms of cell death: upon activation of its protein kinase activityregulates assembly of two death-inducing complexesnamely complex IIa (RIPK1-FADD-CASP8)which drives apoptosisand the complex IIb (RIPK1-RIPK3-MLKL)which drives necroptosis. RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis. In normal conditionsRIPK1 acts as an inhibitor of RIPK3-dependent necroptosisa process mediated by RIPK3 component of complex IIbwhich catalyzes phosphorylation of MLKL upon induction by ZBP1. Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8which cleaves RIPK1 and limits TNF-induced necroptosis. Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8. In addition to apoptosis and necroptosisalso involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokinessuch as interleukin-6 (IL6). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha- dependent mannerand thereby activates the MAP3K5-JNK apoptotic cascade. Required for ZBP1-induced NF-kappa-B activation in response to DNA damage.