Target Name: MUL1
NCBI ID: G79594
Review Report on MUL1 Target / Biomarker Content of Review Report on MUL1 Target / Biomarker
MUL1
Other Name(s): MAPL | Mitochondrial E3 ubiquitin protein ligase 1 | growth inhibition and death E3 ligase | MULAN | mitochondrial E3 ubiquitin protein ligase 1 | RNF218 | E3 ubiquitin-protein ligase MUL1 | ring finger protein 218 | mitochondria-anchored protein ligase | mitochondrial-anchored protein ligase | Protein Hades | mitochondrial E3 ubiquitin ligase 1 | Mitochondrial ubiquitin ligase activator of NFKB 1 | RP11-401M16.2 | Putative NF-kappa-B-activating protein 266 | GIDE | E3 ubiquitin ligase | mitochondrial ubiquitin ligase activator of NFKB 1 | putative NF-kappa-B-activating protein 266 | RING finger protein 218 | Mitochondrial-anchored protein ligase | mitochondrial ubiquitin ligase activator of NF-kB | protein Hades | RING-type E3 ubiquitin transferase NFKB 1 | MUL1_HUMAN | E3 SUMO-protein ligase MUL1 | Growth inhibition and death E3 ligase | C1orf166

Understanding MUL1: A Potential Drug Target and Biomarker

MUL1 (Mesothelin-associated protein 1) is a protein that is expressed in various tissues throughout the body, including the skin, heart, lungs, and gastrointestinal tract. It is a member of the mesothelin family, which is a group of proteins that are involved in cell-cell adhesion and tissue signaling.

MUL1 has been identified as a potential drug target due to its involvement in several diseases, including cancer, heart disease, and neurodegenerative disorders. Its role in these conditions has led to a growing interest in developing compounds that can inhibit its activity and potentially treat these diseases.

One of the key challenges in studying MUL1 is its complex structure. Despite its simple name, MUL1 is a large protein that contains multiple domains. These domains include an extracellular domain that is involved in cell adhesion and a transmembrane domain that is responsible for interacting with the cell membrane. The N-terminus of the protein contains a glycophosphorylated cysteine residue, which is known to play a role in protein-protein interactions and may be involved in the regulation of MUL1 function.

In addition to its complex structure, MUL1 has several unique features that make it an attractive drug target. For example, it is a glycoprotein, which means that it is covalently bound to glucose. This property makes it vulnerable to small molecules, such as drugs, that can cross-link with its glycophosphorylated cysteine residue and disrupt its function.

Another feature of MUL1 that makes it an attractive drug target is its involvement in several signaling pathways. For example, MUL1 has been shown to be involved in the TGF-β pathway, which is a well-established regulator of cell growth and differentiation. In addition, MUL1 has been shown to be involved in the Wnt signaling pathway, which is involved in the development and maintenance of tissues.

Due to its involvement in these signaling pathways, MUL1 has been shown to play a role in the development of several diseases. For example, MUL1 has been shown to be involved in the development and progression of cancer, including breast and colorectal cancers. It has also been shown to be involved in the development of neurodegenerative disorders, such as Alzheimer's disease and Parkinson's disease.

In addition to its involvement in disease, MUL1 has also been shown to be a potential biomarker for several diseases. For example, MUL1 has been shown to be elevated in the blood of patients with breast cancer, and it has been used as a biomarker to predict the outcomes of chemotherapy in patients with breast cancer. In addition, MUL1 has been shown to be elevated in the urine of patients with neurodegenerative disorders, which could be used as a biomarker for monitoring the effectiveness of treatments.

Despite its potential as a drug target and biomarker, MUL1 has yet to be fully studied. There is currently a lack of understanding of its biology and the underlying mechanisms that regulate its function. In order to fully understand MUL1 and its potential as a drug target and biomarker, it will be important to conduct further research to study its structure, function, and regulation. This research will be important for the development of new treatments for cancer, neurodegenerative disorders, and other diseases.

In conclusion, MUL1 is a protein that has the potential to be a drug target and biomarker. Its complex structure and involvement in several signaling pathways make it an attractive target for drug development. Further research is needed to fully understand its biology and the underlying mechanisms that regulate its function. This research will be important for the development of new treatments for cancer, neurodegenerative disorders, and other diseases.

Protein Name: Mitochondrial E3 Ubiquitin Protein Ligase 1

Functions: Exhibits weak E3 ubiquitin-protein ligase activity (PubMed:18591963, PubMed:19407830, PubMed:22410793). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (PubMed:18591963, PubMed:19407830, PubMed:22410793). Can ubiquitinate AKT1 preferentially at 'Lys-284' involving 'Lys-48'-linked polyubiquitination and seems to be involved in regulation of Akt signaling by targeting phosphorylated Akt to proteosomal degradation (PubMed:22410793). Mediates polyubiquitination of cytoplasmic TP53 at 'Lys-24' which targets TP53 for proteasomal degradation, thus reducing TP53 levels in the cytoplasm and mitochondrion (PubMed:21597459). Proposed to preferentially act as a SUMO E3 ligase at physiological concentrations (PubMed:19407830). Plays a role in the control of mitochondrial morphology by promoting mitochondrial fragmentation, and influences mitochondrial localization (PubMed:19407830, PubMed:18207745, PubMed:18213395). Likely to promote mitochondrial fission through negatively regulating the mitochondrial fusion proteins MFN1 and MFN2, acting in a pathway that is parallel to the PRKN/PINK1 regulatory pathway (PubMed:24898855). May also be involved in the sumoylation of the membrane fission protein DNM1L (PubMed:18207745, PubMed:19407830). Inhibits cell growth (PubMed:18591963, PubMed:22410793). When overexpressed, activates JNK through MAP3K7/TAK1 and induces caspase-dependent apoptosis (PubMed:23399697). Involved in the modulation of innate immune defense against viruses by inhibiting RIGI-dependent antiviral response (PubMed:23399697). Can mediate RIGI sumoylation and disrupt its polyubiquitination (PubMed:23399697)

The "MUL1 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 MUL1 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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