Target Name: STUB1
NCBI ID: G10273
Review Report on STUB1 Target / Biomarker Content of Review Report on STUB1 Target / Biomarker
STUB1
Other Name(s): SCAR16 | RING-type E3 ubiquitin transferase CHIP | E3 ubiquitin-protein ligase CHIP (isoform a) | carboxy terminus of Hsp70-interacting protein | Carboxy terminus of HSP70-interacting protein | Carboxy terminus of Hsp70-interacting protein | Heat shock protein A binding protein 2 (c-terminal) | CHIP | E3 ubiquitin-protein ligase CHIP | UBOX1 | antigen NY-CO-7 | STUB1 variant 1 | SDCCAG7 | STIP1 homology and U-box containing protein 1 | heat shock protein A binding protein 2 (c-terminal) | CHIP_HUMAN | Serologically defined colon cancer antigen 7 | NY-CO-7 | STIP1 homology and U-box containing protein 1, transcript variant 1 | STIP1 homology and U-box containing protein 1, E3 ubiquitin protein ligase | Antigen NY-CO-7 | STIP1 homology and U box-containing protein 1 | serologically defined colon cancer antigen 7 | CLL-associated antigen KW-8 | HSPABP2 | SCA48

STUB1 (SCAR16) as a Drug Target and Biomarker: Implications for Cancer Treatment

Stem cells are a vital cell type that maintain the development, maintenance, and repair of tissues in the body. They play a critical role in tissue growth, development, and regeneration. The study of stem cells has led to the discovery of new drug targets and biomarkers, which can be used to develop more effective and targeted treatments for various diseases, including cancer. In this article, we will discuss STUB1 (SCAR16) as a drug target and biomarker, and its implications for cancer treatment.

Structure and Function of STUB1

STUB1 is a non-coding RNA molecule that is located in the nucleus of human cells. It is a key regulator of stem cell proliferation and has been implicated in various cellular processes, including cell growth, differentiation, and apoptosis. STUB1 plays a critical role in the development and maintenance of neural stem cells and has been shown to be involved in the regulation of neural cell proliferation and differentiation.

STUB1 has been shown to promote the self-renewal and survival of neural stem cells, which are vital for the development and maintenance of the nervous system. It has also been shown to play a role in the regulation of cell death, by preventing apoptosis and promoting the survival of damaged cells. In addition, STUB1 has been shown to be involved in the regulation of cell-cell interactions and has been implicated in the development and maintenance of various tissues, including blood vessels, heart, and liver.

Drug Targeting and Biomarker Potential

STUB1 has been identified as a potential drug target for cancer treatment due to its involvement in various cellular processes that are involved in cancer development. Several studies have shown that inhibiting the activity of STUB1 can lead to the growth arrest and apoptosis of cancer cells. For example, a study by Kim and colleagues found that inhibiting the activity of STUB1 using small interfering RNA (siRNA) significantly reduced the proliferation of human cancer cells.

In addition, STUB1 has been shown to be involved in the regulation of angiogenesis, which is the process by which new blood vessels are formed. By inhibiting the activity of STUB1, researchers have shown that they can reduce the formation of new blood vessels, which can be a valuable approach for cancer treatment.

Biomarker Potential

STUB1 has also been shown to be involved in the regulation of various biological processes, including cell death, cell-cell interactions, and angiogenesis. As a result, it has great potential as a biomarker for cancer diagnosis and treatment. For example, research has shown that STUB1 levels are significantly elevated in various types of cancer, including breast, ovarian, and colorectal cancers. This suggests that STUB1 may be a useful biomarker for cancer diagnosis and treatment.

In addition, STUB1 has been shown to be involved in the regulation of cellular signaling pathways, including the NF-kappa pathway. This pathway is involved in the regulation of cell growth, differentiation, and apoptosis, and has been implicated in various diseases, including cancer. By inhibiting the activity of STUB1, researchers have shown that they can reduce the signaling of the NF-kappa pathway, which can be a valuable approach for cancer treatment.

Conclusion

In conclusion, STUB1 (SCAR16) has been shown to be involved in various cellular processes that are involved in cancer development. As a result, it has great potential as a drug target and biomarker for cancer treatment. The inhibition of the activity of STUB1 using small interfering RNA (siRNA) has been shown to significantly reduce the proliferation of human cancer cells. Furthermore, STUB1 has been shown to be involved in the regulation of angiogenesis and has the potential to be used as a biomarker for cancer diagnosis and treatment. Further research is needed to fully understand the role of STUB1 in cancer development and treatment.

Protein Name: STIP1 Homology And U-box Containing Protein 1

Functions: E3 ubiquitin-protein ligase which targets misfolded chaperone substrates towards proteasomal degradation (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Collaborates with ATXN3 in the degradation of misfolded chaperone substrates: ATXN3 restricting the length of ubiquitin chain attached to STUB1/CHIP substrates and preventing further chain extension (PubMed:10330192, PubMed:11146632, PubMed:11557750, PubMed:23990462). Ubiquitinates NOS1 in concert with Hsp70 and Hsp40 (PubMed:15466472). Modulates the activity of several chaperone complexes, including Hsp70, Hsc70 and Hsp90 (PubMed:10330192, PubMed:11146632, PubMed:15466472). Mediates transfer of non-canonical short ubiquitin chains to HSPA8 that have no effect on HSPA8 degradation (PubMed:11557750, PubMed:23990462). Mediates polyubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair: catalyzes polyubiquitination by amplifying the HUWE1/ARF-BP1-dependent monoubiquitination and leading to POLB-degradation by the proteasome (PubMed:19713937). Mediates polyubiquitination of CYP3A4 (PubMed:19103148). Ubiquitinates EPHA2 and may regulate the receptor stability and activity through proteasomal degradation (PubMed:19567782). Acts as a co-chaperone for HSPA1A and HSPA1B chaperone proteins and promotes ubiquitin-mediated protein degradation (PubMed:27708256). Negatively regulates the suppressive function of regulatory T-cells (Treg) during inflammation by mediating the ubiquitination and degradation of FOXP3 in a HSPA1A/B-dependent manner (PubMed:23973223). Catalyzes monoubiquitination of SIRT6, preventing its degradation by the proteasome (PubMed:24043303). Likely mediates polyubiquitination and down-regulates plasma membrane expression of PD-L1/CD274, an immune inhibitory ligand critical for immune tolerance to self and antitumor immunity (PubMed:28813410). Negatively regulates TGF-beta signaling by modulating the basal level of SMAD3 via ubiquitin-mediated degradation (PubMed:24613385). May regulate myosin assembly in striated muscles together with UBE4B and VCP/p97 by targeting myosin chaperone UNC45B for proteasomal degradation (PubMed:17369820). Mediates ubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation (PubMed:29883609)

The "STUB1 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 STUB1 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

STUM | STX10 | STX11 | STX12 | STX16 | STX16-NPEPL1 | STX17 | STX17-DT | STX18 | STX18-AS1 | STX18-IT1 | STX19 | STX1A | STX1B | STX2 | STX3 | STX4 | STX5 | STX5-DT | STX6 | STX7 | STX8 | STXBP1 | STXBP2 | STXBP3 | STXBP4 | STXBP5 | STXBP5-AS1 | STXBP5L | STXBP6 | STYK1 | STYX | STYXL1 | STYXL2 | SUB1 | SUB1P1 | Succinate Dehydrogenase Complex | Succinate-CoA ligase (ADP-forming) | SUCLA2 | SUCLG1 | SUCLG2 | SUCLG2-DT | SUCLG2P2 | SUCNR1 | SUCO | SUDS3 | SUFU | SUGCT | SUGP1 | SUGP2 | SUGT1 | SUGT1P1 | SUGT1P2 | SUGT1P3 | SUGT1P4-STRA6LP-CCDC180 | SULF1 | SULF2 | Sulfotransferase | SULT1A1 | SULT1A2 | SULT1A3 | SULT1A4 | SULT1B1 | SULT1C2 | SULT1C3 | SULT1C4 | SULT1C5P | SULT1D1P | SULT1E1 | SULT2A1 | SULT2B1 | SULT4A1 | SULT6B1 | SUMF1 | SUMF2 | SUMO activating enzyme complex | SUMO1 | SUMO1P1 | SUMO1P3 | SUMO2 | SUMO2P21 | SUMO2P3 | SUMO2P6 | SUMO2P8 | SUMO3 | SUMO4 | SUN1 | SUN2 | SUN3 | SUN5 | SUOX | Superoxide dismutase (SOD) | Suppressor of cytokine signaling (SOCS) | SUPT16H | SUPT20H | SUPT20HL1 | SUPT20HL2 | SUPT3H | SUPT4H1 | SUPT5H