Target Name: TRIM13
NCBI ID: G10206
Review Report on TRIM13 Target / Biomarker Content of Review Report on TRIM13 Target / Biomarker
TRIM13
Other Name(s): Leukemia-associated protein 5 | CLL-associated RING finger | putative tumor suppressor RFP2 | E3 ubiquitin-protein ligase TRIM13 (isoform 2) | Tripartite motif protein 13 | Tripartite motif-containing 13 | leukemia-associated protein 5 | tripartite motif-containing protein 13 | CAR | LEU5 | Putative tumor suppressor RFP2 | B-cell chronic lymphocytic leukemia tumor suppressor Leu5 | RFP2 | DLEU5 | Tripartite motif containing 13, transcript variant 3 | Tripartite motif containing 13, transcript variant 4 | RNF77 | tripartite motif protein 13 | TRIM13 variant 4 | TRI13_HUMAN | E3 ubiquitin-protein ligase TRIM13 | tripartite motif containing 13 | Ret finger protein 2 | E3 ubiquitin-protein ligase TRIM13 (isoform 1) | Tripartite motif-containing protein 13 | ret finger protein 2 | RING finger protein 77 | RING-type E3 ubiquitin transferase TRIM13 | TRIM13 variant 3

TRIM13: A Potential Drug Target for Leukemia

TRIM13 (Leukemia-associated protein 5) is a protein that is expressed in various tissues of the body, including the bone marrow, where it is a key regulator of hematopoietic stem cells (HSCs) proliferation and differentiation. Researchers have been interested in studying TRIM13 as a potential drug target or biomarker for the treatment of various diseases, including leukemia.

Leukemia is a type of cancer that affects the bone marrow and blood cells. It is characterized by the uncontrolled proliferation of white blood cells, which can lead to the development of different types of leukemia. Treatment for leukemia typically involves chemotherapy, radiation therapy, or bone marrow transplantation. While these treatments can be effective in controlling the symptoms of the disease, they are often not able to completely cure the disease.

TRIM13 is a protein that is expressed in the bone marrow and has been shown to play a key role in the regulation of HSCs proliferation and differentiation. It is made up of 216 amino acids and has a molecular weight of 21.9 kDa. TRIM13 is localized to the N-terminus of its amino acid sequence and is expressed in various tissues of the body, including the bone marrow, spleen, and peripheral blood.

Research has shown that TRIM13 plays a critical role in the regulation of HSCs proliferation and differentiation. It is able to induce the expression of genes that are involved in cell growth and differentiation, as well as regulating the production of factors that can promote the growth and proliferation of HSCs.

One of the potential benefits of TRIM13 as a drug target is that it is able to target a specific protein that is involved in the regulation of cell growth and proliferation. This makes it a potentially attractive target for the development of new treatments for leukemia and other diseases.

Another potential benefit of TRIM13 is that it is a self-replicating protein, which means that it is able to generate new copies of itself in response to certain stimuli. This can potentially make it an effective target for cancer treatments because it is able to generate new copies of itself in response to the presence of a drug or other therapeutic agent.

Research has also shown that TRIM13 is involved in the regulation of the immune response, which is an important aspect of the body's defense against disease. This makes it an potentially promising target for the development of new treatments for leukemia and other diseases because it is able to play a critical role in the immune response.

In conclusion, TRIM13 is a protein that has been shown to play a key role in the regulation of HSCs proliferation and differentiation. As a result, it is an potentially promising target for the development of new treatments for leukemia and other diseases. Further research is needed to fully understand the role of TRIM13 in the immune response and to determine its potential as a drug target.

Protein Name: Tripartite Motif Containing 13

Functions: Endoplasmic reticulum (ER) membrane anchored E3 ligase involved in the retrotranslocation and turnover of membrane and secretory proteins from the ER through a set of processes named ER-associated degradation (ERAD). This process acts on misfolded proteins as well as in the regulated degradation of correctly folded proteins. Enhances ionizing radiation-induced p53/TP53 stability and apoptosis via ubiquitinating MDM2 and AKT1 and decreasing AKT1 kinase activity through MDM2 and AKT1 proteasomal degradation. Regulates ER stress-induced autophagy, and may act as a tumor suppressor (PubMed:22178386). Also plays a role in innate immune response by stimulating NF-kappa-B activity in the TLR2 signaling pathway. Ubiquitinates TRAF6 via the 'Lys-29'-linked polyubiquitination chain resulting in NF-kappa-B activation (PubMed:28087809). Participates as well in T-cell receptor-mediated NF-kappa-B activation (PubMed:25088585). In the presence of TNF, modulates the IKK complex by regulating IKBKG/NEMO ubiquitination leading to the repression of NF-kappa-B (PubMed:25152375)

The "TRIM13 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 TRIM13 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

TRIM14 | TRIM15 | TRIM16 | TRIM16L | TRIM17 | TRIM2 | TRIM21 | TRIM22 | 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