Target Name: TRIM22
NCBI ID: G10346
Review Report on TRIM22 Target / Biomarker Content of Review Report on TRIM22 Target / Biomarker
TRIM22
Other Name(s): GPSTAF50 | Tripartite motif-containing protein 22 | E3 ubiquitin-protein ligase TRIM22 | Tripartite motif containing 22, transcript variant 2 | Tripartite binding motif 22 | E3 ubiquitin-protein ligase TRIM22 (isoform 2) | stimulated trans-acting factor (50 kDa) | E3 ubiquitin-protein ligase TRIM22 (isoform 1) | OTTHUMP00000069823 | Staf-50 | tripartite motif-containing protein 22 | tripartite motif containing 22 | RNF94 | Tripartite motif-containing 22 protein | tripartite binding motif 22 | RING finger protein 94 | 50 kDa-stimulated trans-acting factor | staf-50 | STAF50 | TRI22_HUMAN | Tripartite motif protein TRIM22 | RING-type E3 ubiquitin transferase TRIM22 | TRIM22 variant 2 | Tripartite motif-containing 22 | TRIM22 variant 1 | tripartite motif protein TRIM22 | Stimulated trans-acting factor (50 kDa) | Tripartite motif containing 22, transcript variant 1

Trim22 (GPSTAF50) as a Potential Drug Target and Biomarker

Abstract:

Trim22, a non-coding RNA molecule, has been identified as a potential drug target and biomarker for various diseases. Its unique structure, function, and regulation have made it an attractive target for drug development. This article will discuss the molecular mechanisms of Trim22, its potential drug targets, and its potential as a biomarker for various diseases.

Introduction:

Trim22 is a non-coding RNA molecule that plays a crucial role in various cellular processes. It is a key regulator of gene expression, and its levels are regulated by several factors, including microRNA (miRNA) and long non-coding RNA (lncRNA) interactions. Trim22 has been shown to participate in various signaling pathways, including cell growth, apoptosis, and inflammation. Its unique structure and function have made it an attractive target for drug development and research.

Drug Targets:

Trim22 has several potential drug targets due to its unique functions and interactions. One of the most promising targets is the inhibition of Trim22, which has been shown to have therapeutic effects on various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

The inhibition of Trim22 has been shown to lead to the downregulation of target genes, including those involved in cell growth, apoptosis, and inflammation. This has led to the inhibition of cell proliferation, apoptosis, and the exacerbation of diseases associated with these processes. Therefore, targeting Trim22 could be an effective way to develop new treatments for various diseases.

Biomarkers:

Trim22 has also been identified as a potential biomarker for various diseases. Its expression levels are regulated by several factors, including miRNA and lncRNA interactions. Therefore, the expression levels of Trim22 can be used as a biomarker for diseases associated with these factors.

For example, Trim22 has been shown to be involved in the regulation of cell apoptosis, which is a crucial factor in neurodegenerative diseases. Its expression levels have been shown to be regulated by microRNA and lncRNA interactions, which could provide new insights into the mechanisms underlying neurodegenerative diseases.

Another example is the regulation of cancer cell growth. Trim22 has been shown to play a role in the regulation of cell cycle progression, which is a crucial factor in cancer development. Therefore, targeting Trim22 could be an effective way to inhibit cancer cell growth and development.

Conclusion:

Trim22 is a non-coding RNA molecule that has a unique structure and function. Its regulation by miRNA and lncRNA interactions makes it an attractive target for drug development and research. Its potential drug targets and biomarkers make it an attractive candidate for the development of new treatments for various diseases. Further research is needed to fully understand its mechanisms and potential clinical applications.

Protein Name: Tripartite Motif Containing 22

Functions: Interferon-induced E3 ubiquitin ligase that plays important roles in innate and adaptive immunity (PubMed:25683609, PubMed:35777501). Restricts the replication of many viruses including HIV-1, encephalomyocarditis virus (EMCV), hepatitis B virus (HBV), hepatitis C virus (HCV) or Zika virus (ZIKV) (PubMed:25683609, PubMed:35777501, PubMed:36042495). Mechanistically, negatively regulates HCV replication by promoting ubiquitination and subsequent degradation of viral NS5A (PubMed:25683609). Acts also by promoting the degradation of Zika virus NS1 and NS3 proteins through proteasomal degradation (PubMed:36042495). Acts as a suppressor of basal HIV-1 LTR-driven transcription by preventing Sp1 binding to the HIV-1 promoter (PubMed:26683615). Plays also a role in antiviral immunity by co-regulating together with NT5C2 the RIGI/NF-kappa-B pathway by promoting 'Lys-63'-linked ubiquitination of RIGI, while NT5C2 is responsible for 'Lys-48'-linked ubiquitination of RIGI (PubMed:36159777). Participates in adaptive immunity by suppressing the amount of MHC class II protein in a negative feedback manner in order to limit the extent of MHC class II induction (PubMed:35777501)

The "TRIM22 Target / Biomarker Review Report" is a customizable review of hundreds up to thousends of related scientific research literature by AI technology, covering specific information about TRIM22 comprehensively, including but not limited to:
•   general information;
•   protein structure and compound binding;
•   protein biological mechanisms;
•   its importance;
•   the target screening and validation;
•   expression level;
•   disease relevance;
•   drug resistance;
•   related combination drugs;
•   pharmacochemistry experiments;
•   related patent analysis;
•   advantages and risks of development, etc.
The report is helpful for project application, drug molecule design, research progress updates, publication of research papers, patent applications, etc. If you are interested to get a full version of this report, please feel free to contact us at BD@silexon.ai

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TRIM23 | TRIM24 | TRIM25 | TRIM26 | TRIM27 | TRIM28 | TRIM29 | TRIM3 | TRIM31 | TRIM32 | TRIM33 | TRIM34 | TRIM35 | TRIM36 | TRIM37 | TRIM38 | TRIM39 | TRIM39-RPP21 | TRIM4 | TRIM40 | TRIM41 | TRIM42 | TRIM43 | TRIM43B | TRIM44 | TRIM45 | TRIM46 | TRIM47 | TRIM48 | TRIM49 | TRIM49B | TRIM49C | TRIM49D2 | TRIM5 | TRIM50 | TRIM51 | TRIM51EP | TRIM51G | TRIM51HP | TRIM52 | TRIM53AP | TRIM54 | TRIM55 | TRIM56 | TRIM58 | TRIM59 | TRIM59-IFT80 | TRIM6 | TRIM6-TRIM34 | TRIM60 | TRIM60P15 | TRIM61 | TRIM62 | TRIM63 | TRIM64 | TRIM64B | TRIM64C | TRIM65 | TRIM66 | TRIM67 | TRIM68 | TRIM69 | TRIM7 | TRIM7-AS2 | TRIM71 | TRIM72 | TRIM73 | TRIM74 | TRIM75 | TRIM77 | TRIM8 | TRIM9 | TRIML1 | TRIML2 | TRIO | TRIOBP | TRIP10 | TRIP11 | TRIP12 | TRIP13 | TRIP4 | TRIP6 | Tripartite motif containing 78, pseudogene | TRIQK | TRIR | TRIT1 | TRL-AAG1-2 | TRL-AAG2-3 | TRL-TAG2-1 | TRMO | TRMT1 | TRMT10A | TRMT10B | TRMT10C | TRMT11 | TRMT112 | TRMT12 | TRMT13 | TRMT1L | TRMT2A