TNFRSF9

Human 4-1BB Ligand Receptor, also known as the Tumor Necrosis Factor Receptor Superfamily Member 9, is a 255 amino acid cytokine protein implicated in T-cell activation pathways. After initial synthesis of the peptide, the cytokine is proteolytically cleaved by proteases, thus separating the 23 residue signal sequence from the actual mature 232 residue 4-1BB Receptor sequence. The protein is expressed from the TNFRSF9 gene located at locus 1p36 on chromosome 1. The 4-1BB receptor or TNFRSF9 inherently has high affinity binding for the 4-1BB ligand such that upon binding, the receptor contributes to clonal expansion, survival and development of T-cells. It can also induce proliferation in peripheral monocytes, enhance T-cell apoptosis induced by TCR/CD3 triggered activation and regulate CD28 co-stimulation to promote Th1 cell responses. The expression of this receptor is induced by lymphocyte activation. TRAF adaptor proteins such as TRAF1, TRAF2 and TRAF 3 have been shown to bind to this receptor and transducer the signals leading to activation of NF-κB.

TNFRSF9; 4-1BB; CD137; CDw137; ILA; CD137 antigen; T cell antigen ILA; T-cell antigen 4-1BB homolog; T-cell antigen ILA; homolog of mouse 4-1BB; induced by lymphocyte activation (ILA); interleukin-activated receptor, homolog of mouse Ly63; receptor protein 4-1BB; tumor necrosis factor receptor superfamily member 9;