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Fig. 1 | Human Genomics

Fig. 1

From: Pan-cancer illumination of TRIM gene family reveals immunology regulation and potential therapeutic implications

Fig. 1

Genetic alterations of TRIM protein family. A Structure and classifications of TRIM family proteins (C-I to UC) are shown. Most TRIM proteins have a RING-finger domain (R), one or two B box zinc-finger domains (B1/B2) and a coiled-coil region (CC) in N-terminal region, and contain one or more carboxyl-terminal domains such as cos-box (COS), fibronectin type III repeat (FN3), PRY domain (PRY), SPRY domain (SPRY), PHD domain (PHD), bromodomain (BR), filamin-type I G domain (FIL), NCL1, HT2A and LIN41 domain (NHL), meprin and TRAF-homology domain (MATH), ADP-ribosylation factor family domain (ARF), and transmembrane region (TM). B Mutation frequency of TRIM proteins in different sub-classes (C-I to UC). Wilcoxon rank sum test, ****p < 0.0001, ***p < 0.001, **p < 0.01, *p < 0.05. C Mutation frequency in different domains of TRIM proteins. D Functional impact scores of mutations in domain versus other regions, evaluated by SIFT, Polyphen-2, CADD and conservation. Wilcoxon rank sum test, ****p < 0.0001, ***p < 0.001, **p < 0.01, *p < 0.05. E The somatic mutations and structure of TRIM16 are shown. Red, protein domains enriched somatic mutations. Blue, other domains. The number in the point represents the number of mutation samples. Mutation information includes mutation location and amino acids before and after mutation. F Proportion of mutations located in domain of interest and other regions for TRIM16. G The somatic mutations and structure of TRIM4. Red, protein domains enriched somatic mutations. Blue, other domains. The number in the point represents the number of mutation samples. Mutation information includes mutation location and amino acids before and after mutation. H Proportion of mutations located in domain of interest and other regions for TRIM4. ****p < 0.0001, ***p < 0.001, **p < 0.01, *p < 0.05

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