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. 2022 Oct 19;11:75. doi: 10.1186/s40164-022-00322-w

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© The Author(s) 2022

Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 1 — Structural classification of TRIM family members. The majority of TRIM proteins contain an N-terminal RING domain, one or two B-box domains (B1, B2) and a coiled-coil domain (CC) and are classified into 11 subfamilies (C-I-C-XI) based on a variable C-terminal domain. There is an additional unclassified group lacking a RING domain. SPRY named from SPla and the RYanodine receptor, PRY-SPRY associated domain, NHL-NCL1, HT2A and LIN41 domain, PHD plant homeodomain, COS cos-box, FN3 fibronectin type III, ARF-ADP ribosylation factor domain, ACID acid-rich region, TM transmembrane region, MATH meprin and TRAF-homology domain, Filamin-filamin-type I G domain, BROMO-bromodomain