Target Name: TRIM41
NCBI ID: G90933
Review Report on TRIM41 Target / Biomarker Content of Review Report on TRIM41 Target / Biomarker
TRIM41
Other Name(s): TRI41_HUMAN | RING finger-interacting protein with C kinase | E3 ubiquitin-protein ligase TRIM41 | RING-finger protein that interacts with C kinase | Tripartite motif-containing protein 41 | TRIM41 variant 1 | TRIM41a | TRIM41alpha | tripartite motif containing 41 | RINCK | E3 ubiquitin-protein ligase TRIM41 (isoform 1) | Tripartite motif containing 41, transcript variant 1 | RING-type E3 ubiquitin transferase TRIM41

TRIM41: A Potential Drug Target Or Biomarker

TRIM41 (TRI41_HUMAN) is a protein that is expressed in various tissues of the human body, including the brain, lungs, heart, kidneys, and intestines. It is a part of the Tissue Response to Intervention (TRIM) family of proteins, which are involved in various cellular processes in the body, including inflammation, cell survival, and angiogenesis.

TRIM41 has been identified as a potential drug target or biomarker due to its unique structure and biology. The TRIM41 protein is composed of 115 amino acid residues and has a molecular weight of 13.9 kDa. It is characterized by a N-terminal transmembrane domain, a cytoplasmic domain, and a C-terminal T-loop region. The cytoplasmic domain of TRIM41 is rich in conserved hypothetical transmembrane proteins (TMPs), which are involved in various cellular processes, including cell signaling and interactions.

One of the key features of TRIM41 is its ability to interact with various signaling pathways, including TGF-β, NF-kappa-B, and PI3K. These signaling pathways are involved in various cellular processes, including cell growth, differentiation, inflammation, and survival. By interacting with these signaling pathways, TRIM41 plays a role in the regulation of cellular processes that are critical for human health and disease.

TRIM41 has also been shown to be involved in the regulation of cellular apoptosis, which is a critical process for the elimination of damaged or dysfunctional cells. Apoptosis is a natural process that occurs in the body and is important for the maintenance of tissue homeostasis and the regulation of cellular aging. However, aberrant apoptosis can contribute to the development and progression of various diseases, including cancer, neurodegenerative diseases, and systemic diseases.

In addition to its involvement in apoptosis, TRIM41 has also been shown to be involved in the regulation of cellular signaling pathways that are involved in cell growth, differentiation, and angiogenesis. For example, TRIM41 has been shown to be involved in the regulation of theNotch signaling pathway, which is involved in the regulation of cellular growth and differentiation.

TRIM41 has also been shown to be involved in the regulation of the NF-kappa-B signaling pathway, which is involved in the regulation of inflammation and cellular signaling. The NF-kappa-B signaling pathway is a critical pathway that is involved in the regulation of various cellular processes, including inflammation, pain, and survival.

Given its unique structure and biology, TRIM41 has been identified as a potential drug target or biomarker for a variety of diseases. For example, TRIM41 has been shown to be involved in the regulation of cellular signaling pathways that are involved in cancer, neurodegenerative diseases, and systemic diseases. Additionally, TRIM41 has been shown to be involved in the regulation of cellular apoptosis, which is a critical process for the elimination of damaged or dysfunctional cells.

In conclusion, TRIM41 is a protein that has unique structure and biology, and is involved in various cellular processes that are critical for human health and disease. Its potential as a drug target or biomarker makes it an attractive target for research into the regulation of cellular processes that are involved in disease development and progression. Further research is needed to fully understand the role of TRIM41 in cellular processes and its potential as a drug target or biomarker.

Protein Name: Tripartite Motif Containing 41

Functions: E3 ligase that plays essential roles in innate antiviral response (PubMed:28169297, PubMed:29760876, PubMed:29899090, PubMed:31979016). Directly binds to influenza A virus or vesicular stomatitis virus nucleoproteins and targets them for ubiquitination and proteasomal degradation, thereby limiting viral infections (PubMed:29899090, PubMed:31979016, PubMed:28169297). Activates the innate antiviral response by catalyzing monoubiquitination of CGAS, thereby activating CGAS (PubMed:29760876). Also involved in innate antiviral response by mediating 'Lys-63'-linked polyubiquitylation of BCL10 which in turn hubs NEMO for activation of NF-kappa-B and IRF3 pathways (By similarity). Catalyzes the ubiquitin-mediated degradation of other substrates including protein kinase C, ZSCAN21 or TOP3B suggesting additional roles besides its function in immune response (PubMed:17893151, PubMed:33378676)

The "TRIM41 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 TRIM41 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

More Common Targets

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 | TRMT2B | TRMT44 | TRMT5 | TRMT6 | TRMT61A | TRMT61B | TRMT9B | TRMU | TRN-GTT4-1 | TRNA | tRNA splicing endonuclease complex | tRNA(Sec) complex | tRNA-splicing endonuclease complex | tRNA-splicing ligase complex | TRNAU1AP | TRNC | TRND | TRNE | TRNF | TRNG | TRNH