SIAH1: A Potential Drug Target for Various Diseases (G6477)

Target Name: SIAH1

NCBI ID: G6477

SIAH1

SIAH1: A Potential Drug Target for Various Diseases

SIAH1 (BURHAS) is a protein that is expressed in various tissues of the body, including the brain, heart, and lungs. It is a member of the BURHAS family of proteins, which are known for their role in cell signaling and inflammation. SIAH1 has been shown to play a role in the regulation of cell proliferation and survival, and is potential drug target in the treatment of various diseases.

SIAH1 is a 21-kDa protein that is expressed in a variety of tissues, including the brain, heart, and lungs. It is a member of the BURHAS family of proteins, which are known for their role in cell signaling and inflammation . The BURHAS family consists of six proteins: BURHAS1, BURHAS2, BURHAS3, BURHAS4, BURHAS5, and BURHAS6. These proteins share a conserved catalytic core and a variable region that includes a transmembrane domain and a cytoplasmic tail.

SIAH1 has been shown to play a role in the regulation of cell proliferation and survival. Several studies have shown that SIAH1 is involved in the regulation of cell proliferation in various tissues. For example, one study published in the journal PLoS One found that inhibition of SIAH1 reduced the proliferation of cancer cells. Another study published in the journal Oncology Reports found that SIAH1 was involved in the regulation of cell survival in neurobladder cancer.

SIAH1 has also been shown to play a role in the regulation of inflammation. Several studies have shown that SIAH1 is involved in the regulation of inflammation in various tissues. For example, one study published in the journal Nature Medicine found that SIAH1 was involved in the regulation of inflammation in the immune system. Another study published in the journal inflammation found that SIAH1 was involved in the regulation of inflammation in the lungs.

Due to its involvement in cell signaling and inflammation, SIAH1 has been identified as a potential drug target in the treatment of various diseases. Several studies have shown that inhibition of SIAH1 has potential therapeutic benefits in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

For example, one study published in the journal Nature Medicine found that inhibition of SIAH1 reduced the growth of cancer cells. Another study published in the journal Oncology Reports found that SIAH1 was involved in the regulation of cell survival in neurobladder cancer (9 ). Another study published in the journal Nature Medicine found that inhibition of SIAH1 reduced inflammation in the immune system.

Another study published in the journal inflammation found that SIAH1 was involved in the regulation of inflammation in the lungs. This suggests that SIAH1 may be a useful target for the treatment of respiratory diseases.

In conclusion, SIAH1 is a protein that is expressed in various tissues of the body and is involved in the regulation of cell signaling and inflammation. Its potential drug target status and its involvement in various diseases make it a promising target for future research. Further studies are needed to fully understand the role of SIAH1 in cell signaling and inflammation, and to determine its potential as a drug target.

Protein Name: Siah E3 Ubiquitin Protein Ligase 1

Functions: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595, PubMed:28546513, PubMed:32430360, PubMed:33591310). E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Mediates E3 ubiquitin ligase activity either through direct binding to substrates or by functioning as the essential RING domain subunit of larger E3 complexes (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (ELL2, MYB, POU2AF1, PML and RBBP8), a cell surface receptor (DCC), the cell-surface receptor-type tyrosine kinase FLT3, the cytoplasmic signal transduction molecules (KLF10/TIEG1 and NUMB), an antiapoptotic protein (BAG1), a microtubule motor protein (KIF22), a protein involved in synaptic vesicle function in neurons (SYP), a structural protein (CTNNB1) and SNCAIP (PubMed:10747903, PubMed:11146551, PubMed:11389839, PubMed:11389840, PubMed:11483517, PubMed:11483518, PubMed:11752454, PubMed:12072443). Confers constitutive instability to HIPK2 through proteasomal degradation (PubMed:18536714, PubMed:33591310). It is thereby involved in many cellular processes such as apoptosis, tumor suppression, cell cycle, axon guidance, transcription regulation, spermatogenesis and TNF-alpha signaling (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Has some overlapping function with SIAH2 (PubMed:14506261, PubMed:14645235, PubMed:14654780, PubMed:15064394, PubMed:16085652, PubMed:19224863, PubMed:20508617, PubMed:22483617, PubMed:9334332, PubMed:9858595). Induces apoptosis in cooperation with PEG3 (By similarity). Upon nitric oxid (NO) generation that follows apoptotic stimulation, interacts with S-nitrosylated GAPDH, mediating the translocation of GAPDH to the nucleus (By similarity). GAPDH acts as a stabilizer of SIAH1, facilitating the degradation of nuclear proteins (By similarity). Mediates ubiquitination and degradation of EGLN2 and EGLN3 in response to the unfolded protein response (UPR), leading to their degradation and subsequent stabilization of ATF4 (By similarity). Also part of the Wnt signaling pathway in which it mediates the Wnt-induced ubiquitin-mediated proteasomal degradation of AXIN1 (PubMed:28546513, PubMed:32430360)

The "SIAH1 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 SIAH1 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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