Recombinant Human E3 ubiquitin-protein ligase TRIM22 (TRIM22)

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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HGNC: 16379

OMIM: 606559

KEGG: hsa:10346

STRING: 9606.ENSP00000369299

UniGene: Hs.501778