1. Upregulation of TRIM22 triggers the expression and oligomerization of Bak and subsequently leads to cytochrome c release in a caspase-9- and caspase-3-dependent manner. Both the RING domain and the SPRY domain of the TRIM22 molecule are associated with its pro-apoptotic function. PMID: 28079123
2. miR-215 facilitated HCV replication via inactivation of the NF-kappaB pathway by inhibiting TRIM22, providing a novel potential target for HCV infection. PMID: 29749134
3. Suppression of interferon-mediated anti-HBV response by single CpG methylation in the 5'-UTR of TRIM22. PMID: 28341749
4. Wthis study identified a genetic variation (rs7935564 G allele) in TRIM22 gene, which encodes TRIM22 protein acting like a HIV restriction factor, as being associated with good response to dendritic cell-based immunotherapy PMID: 27704462
5. TRIM5 and TRIM22 single nucleotide polymorphisms are associated to increased odds of significant liver fibrosis and sustained virological response after pegIFNalpha/RBV therapy in human immunodeficiency virus/hepatitis C virus coinfected patients. PMID: 27590274
6. Infant with severe IBD characterized by granulomatous colitis and severe perianal disease, we identified a homozygous variant of TRIM22 that affects the ability of its product to regulate NOD2. PMID: 26836588
7. Interferon-alpha-induced TRIM22 interrupts hepatitis c virus replication by ubiquitinating NS5A. PMID: 25683609
8. regulation of FoxO4 protein expression and cell survival by TRIM22 controls TLR3-mediated IFN type I gene induction, preventing excessive antiviral response through dsRNA-induced apoptosis. PMID: 26237181
9. TRIM22 could interact with IkappaB kinase (IKK)alpha but not IKKbeta and could increase the level and phosphorylation of IKKalpha through its really interesting new gene (RING) and spla-ryanodine receptor (SPRY) domains. PMID: 25510414
10. Demonstrated that TRIM22 acts as a negative regulator of HIV-1 replication via inhibition of basal Sp1-driven proviral transcription. PMID: 26683615
11. propose that TRIM22 is a direct target gene of PR and that it can mediate progesterone actions in uterine cells PMID: 26316153
12. Data show that capsid protein p24-DsRed-Monomer was co-localized with tripartite motif containing 22 (TRIM22)-EGFP in HEK293T cells. PMID: 26271984
13. A number of putative structural and functional residues, including several sites that undergo post-translational modification, were also identified in TRIM22. PMID: 24983760
14. our data characterize the extensive genetic variation in TRIM22 and identify rs1063303:G>C as a highly prevalent SNP that influences its function. PMID: 24863734
15. Upregulation of TRIM22 may be associated with responsiveness to Peg-IFNalpha-2a/RBV combination therapy in hepatitis C. PMID: 24889558
16. TRIM5alpha and TRIM22 have differential transcriptional regulation and distinct anti-HIV roles according to infection phase. PMID: 24478420
17. Data report that markers in two TRIMs, TRIM5 and TRIM22 and a marker in BST2, associated statistically with the risk of getting MS. PMID: 24066097
18. TRIM22 genetic diversity affects HIV-1 replication in vitro and it is a potentially novel determinant of HIV-1 disease severity PMID: 23921607
19. this study shows that TRIM22 is greatly under-expressed in breast cancer. p53 dysfunction may be one of the mechanisms for TRIM22 down-regulation. PMID: 24183724
20. These data indicate that overexpression of TRIM22 may negatively regulate the TRAF6-stimulated NF-kappaB pathway by interacting with and degrading TAB2. PMID: 23818111
21. p300 contributed to both IFN-gamma- and IRF-1-mediated TRIM22 transcription independent of its histone acetyltransferase activity, however, it was required for the recruitment of RNA polymerase II to TRIM22 promoter region. PMID: 23670564
22. Restriction of influenza A virus replication was accounted for by the interaction between TRIM22 and the viral nucleoprotein (NP), resulting in its polyubiquitination and degradation in a proteasome-dependent manner PMID: 23408607
23. TRIM22 to repress protein translation preferably of some specific mRNAs. TRIM22 represses translation by inhibiting the binding of eIF4E to eIF4G, suggesting a mechanism for regulation of protein translation PMID: 22509910
24. BRG1-mediated chromatin remodeling is critical for the IFN-gamma-inducibility of TRIM22 gene. PMID: 21683060
25. These data suggested that TRIM22 was a positive regulator of NF-kappaB-mediated transcription. PMID: 21651891
26. Nuclear TRIM22 significantly impairs HIV-1 replication, likely by interfering with Tat- and NF-kappaB-independent long-terminal-repeat-driven transcription. PMID: 21345949
27. TRIM22 inhibits HIV-1 particle production by interfering with the trafficking of Gag to the plasma membrane and is a key player in the antiviral activity of the Type I interferon response to HIV-1. PMID: 18389079
28. These data suggest concordance between type 1 IFN and TRIM22 in PBMCs and that TRIM22 likely acts as an antiviral effector in HIV-1 infection. PMID: 20980524
29. REVIEW: current knowledge on the anti-retroviral effects of TRIM5 alpha and TRIM22 PMID: 19943174
30. endogenous TRIM22 is localized to both nucleus and cytosol in primary human mononuclear cells, as well as in the human osteosarcoma cell line U2OS PMID: 20006605
31. Specific polymorphisms in tripartite motif22 (TRIM22) genes were significantly associated with rubella vaccine humoral immunity PMID: 20001730
32. May be involved in proliferation and/or differentiation of leukemic cells. PMID: 15064739
33. Overexpression of Staf50 inhibited the HIV-1 infection between 50% and 90% in 293 T CD4/CCR5 as well as in monocyte-derived macrophages. PMID: 16926043
34. These data suggest a more complex role for TRIM22 during T lymphocyte activation than merely as an antiproliferative factor. PMID: 17970695
35. A novel property of TRIM22, E3 ubiquitin ligase activity, was demonstrated. PMID: 18656448
36. Study shows that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain. PMID: 19212762
37. TRIM22 is an E3 Ubiquitin ligase whose expression leads to antiviral effects towards Encephalomyocarditis virus infections in HeLa cells. [TRIM22] PMID: 19218198
38. Deletion of putative nuclear localization signal abolished TRIM22 localization and nuclear body (NB) formation, the B30.2/SplA and ryanodine receptor (SPRY) domain, and residues 491-494 specifically are essential for nuclear localization and NB formation. PMID: 19481078
39. TRIM22-mediated anti-hepatitis B virus activity dependent on the nuclear-located RING domain PMID: 19585648

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Cytoplasm. Nucleus. Nucleus speckle. Nucleus, Cajal body. Note=Localizes predominantly to the nucleus, found in cytoplasm to some extent. Forms distinct nuclear bodies that undergo dynamic changes during cell cycle progression. Nuclear bodies start to form in the early G0/G1 phase but become speckle-like in the S-phase and completely dispersed in mitosis. 35% of TRIM22 nuclear bodies overlap or are found adjacent to Cajal bodies.

TRIM/RBCC family

Strongly expressed in peripheral blood leukocytes, spleen, thymus, and ovary. Expressed at basal levels in other tissues.

HGNC: 16379

OMIM: 606559

KEGG: hsa:10346

STRING: 9606.ENSP00000369299

UniGene: Hs.501778