Tripartite motif-containing protein 13 (TRIM13)

Tripartite motif-containing protein 13 (TRIM13) is an E3 ubiquitin ligase that is anchored mainly in the endoplasmic reticulum (ER), characterized by a canonical TRIM/RING domain structure: a RING finger domain, two B-box motifs, a coiled-coil region, and a C-terminal transmembrane domain[2][1][3]. TRIM13 regulates ER-associated degradation (ERAD) by ubiquitinating misfolded or regulatory proteins for proteasomal or lysosomal degradation. It also functions in cell cycle regulation, stabilizing key proteins such as cyclin A1 (CCNA1) through ubiquitination and preventing their lysosomal degradation. TRIM13 is implicated as a tumor suppressor, particularly in B-cell chronic lymphocytic leukemia (CLL), where its gene locus (chromosome 13q14) is frequently deleted. Loss or decreased expression of TRIM13 promotes leukemic self-renewal, while its expression can enforce cell cycle entry and exhaust leukemic stem cells. In addition, TRIM13 is involved in innate immune regulation by negatively modulating STING-mediated DNA sensing pathways, controlling inflammatory responses to DNA virus infection, and acting on NF-κB and TBK1-IRF3 signaling pathways. Aberrations in TRIM13 expression are observed in multiple cancers (CLL, AML, myeloma, breast, prostate, lymphoma), with both tumor-suppressing and oncogenic roles described depending on cellular context and disease type[2][1][3].

Other names

E3 ubiquitin-protein ligase TRIM13LEU5RFP2RNF77DLEU5B-cell chronic lymphocytic leukemia tumor suppressor Leu5Leukemia-associated protein 5Putative tumor suppressor RFP2RING finger protein 77CLL-associated RING fingerRet finger protein 2CAR

Protein ubiquitination leading to proteasomal or lysosomal degradation (including modulation of substrates such as MDM2, AKT1, CCNA1, TRAF6, STING); Regulation of signaling pathways (e.g., TBK1-IRF3, NF-κB, TLR2, ERAD-mediated processes)[2][3][1]