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. 2024 Jan 16;29:13. doi: 10.1186/s11658-023-00528-8

Table 1.

Structural features of TRIM proteins involved in autophagy and apoptosis

Autophagy Apoptosis Autophagy + Apoptosis Classification Domains [N–C]
TRIM1 C-I-2 R-B1-B2-CC-COS-FN3-SPRY
TRIM63 C-II R-B2-CC-COS-ACID
TRIM6, TRIM11, TRIM50 TRIM27 TRIM17, TRIM20, TRIM21, TRIM35, TRIM39, TRIM72 C-IV-1 R-B2-CC-PRY-SPRY
TRIM5 TRIM34 TRIM22 C-IV-2 R-B2-CC-SPRY
TRIM69 C-IV-4 R-CC-PRY-SPRY
TRIM14 TRIM16 C-IV-4? B2-CC-PRY-SPRY
TRIM49 TRIM48 C-IV-5 R-B2-SPRY
TRIM8, TRIM19 C-V-1 R-B1-B2-CC
TRIM31 C-V-2 R-B2-CC
TRIM28 C-VI R-B1-B2-CC-PHD-BROMO
TRIM32 C-VII-3 R-B2-CC-NHL
TRIM37 C-VIII R-B2-CC-MATH
TRIM23 C-IX R-B1-B2CC-ARF
TRIM59 TRIM13 C-XI R-B2-CC-TM

Most TRIM proteins contain a RING-finger domain, one or two B-box (B1 or B2) domains, and a coiled-coil domain

TRIM proteins were classified as C-I to C-XI. TRIM proteins without a RING finger domain (no RING) were unclassified

R, RING-finger domain; B1, B-box domain 1; B2, B-box domain 2; CC, coiled-coil domain; COS, cos box; FN3, fibronectin type III repeat; PRY, PRY domain; SPRY, SPRY domain; ACID, acid-rich region; NHL, NHL domain; PHD, PHD domain; BROMO, bromodomain; MATH, Meprin and TRAF-homology domain; ARF, ADP-ribosylation factor family domain; TM, transmembrane domain. TRIM; Tripartite motif containing, RING, Really interesting new gene, C-I; Class I, N–C; N-terminal-C-terminal domain