Skip to main content
. 2021 May 21;13(11):2513. doi: 10.3390/cancers13112513

Figure 1.

Figure 1

Schematic representation of receptors and their known and putative palmitoylation sites. Signal peptides (SP) are marked in pink, trans-membrane domain (TMD) in blue, and death domain (DD) in red. Intracellular cysteine residues are indicated as known (green) and putative (black) palmitoylation acceptor sites. (A) depicts TNF-R1 (UniProt: P19438). C248 is the sole known palmitoylation site. The TNF-R1 internalization domain (TRID) is marked in green; the neutral sphingomyelinase domain (NSD) is marked in orange. (B) depicts TNF-R2 (UniProt: P20333). Five possible palmitoylation acceptor cysteine residues are indicated. (C) depicts CD95 (UniProt: P25445). C199 is a known human CD95 palmitoylation site. C194 is palmitoylated in murine CD95. (D) depicts DR4/TRAIL-R1 (UniProt: O00220). Cysteine residues 261-263 are known palmitoylation acceptor sites. (E) depicts DR5/TRAIL-R2 (UniProt: O14763) with three putative palmitoylation sites. (F) depicts DR6 (UniProt: O75509). C368 is a known palmitoylation site. (G) Depicts DR3 (UniProt: Q93038). Four possible palmitoylation sites are indicated. A putative internalization domain is marked in green; the putative neutral sphingomyelinase domain (NSD) is marked in orange. (H) depicts CD40 (UniProt: P25942). The sole intracellular cysteine residue 258 is indicated.