InterPro domain: IPR025735

RIP proteins are receptor-interacting serine/threonine-protein kinases or cell death proteins [ 1 ]. The RHIM (RIP homotypic interaction motif) domain is involved in virus recognition. It is necessary for the recruitment of RIP and RIP3 by the IFN-inducible protein DNA-dependent activator of IRFs (DAI), also known as DLM-1 or Z-DNA binding protein (ZBP1). Both RIP kinases contribute to DAI-induced NF-kappaB activation. RIP3 undergoes auto phosphorylation on binding to DAI [ 2 ].

The RHIM domain is also located at the C terminus of TIR-domain-containing adapter-inducing IFN-beta (TRIF). It is essential for TRIF-induced apoptosis, and has been shown to contribute to TRIF-induced NF-kappaB activation [ 3 ].

1. Identification of a novel homotypic interaction motif required for the phosphorylation of receptor-interacting protein (RIP) by RIP3. J. Biol. Chem. 277, 9505-11
2. DAI/ZBP1 recruits RIP1 and RIP3 through RIP homotypic interaction motifs to activate NF-kappaB. EMBO Rep. 10, 916-22
3. Apoptosis induced by the toll-like receptor adaptor TRIF is dependent on its receptor interacting protein homotypic interaction motif. J. Immunol. 174, 4942-52