Target Name: SIAH2
NCBI ID: G6478
Review Report on SIAH2 Target / Biomarker Content of Review Report on SIAH2 Target / Biomarker
SIAH2
Other Name(s): RING-type E3 ubiquitin transferase SIAH2 | SIAH2_HUMAN | Siah-2 | Siah E3 ubiquitin protein ligase 2 | E3 ubiquitin-protein ligase SIAH2 | siah E3 ubiquitin protein ligase 2 | siah-2 | Seven in absentia homolog 2 | hSiah2 | seven in absentia homolog 2

SIAH2: A Key Protein in Cellular Processes

SIAH2 (RING-type E3 ubiquitin transferase) is a protein that plays a crucial role in the regulation of gene expression and protein stability. It is a key player in the ubiquitin system, a complex protein degradation pathway that is involved in everything from cell division to immune response. SIAH2 is an essential enzyme in this pathway, and its activity is regulated by a variety of factors.

SIAH2 is a 26-kDa protein that is expressed in most tissues and cells. It is a member of the SIAH family of proteins, which are known for their ability to transfer ubiquitin chains to target proteins. SIAH2 has a unique structure, with a N -terminal domain that is rich in conserved amino acid sequences, a central 尾-sheet, and a C-terminal tail that is involved in protein-protein interactions.

SIAH2 functions as an E3 ubiquitin transferase, which means that it transfers a ubiquitin chain from one protein to another. This process is critical for protein stability and degradation, as well as for cell signaling and division. SIAH2 is involved in the regulation of a wide range of cellular processes, including cell growth, apoptosis, and immune response.

One of the key functions of SIAH2 is its role in the regulation of gene expression. SIAH2 has been shown to play a role in the negative regulation of gene expression, by binding to specific DNA sequences and preventing the RNA polymerase from binding to them. This is important for the regulation of stem cell self-renewal and for the development of cancer.

SIAH2 is also involved in the regulation of protein stability and degradation. It has been shown to play a role in the degradation of many proteins, including transcription factors and signaling proteins. This is important for maintaining the levels of these proteins in the cytoplasm, where they are involved in cell signaling and division.

In addition to its role in gene expression and protein stability, SIAH2 is also involved in the regulation of cell signaling and division. It has been shown to play a role in the regulation of cell cycle progression, by binding to specific DNA sequences and preventing the G1-S transition that occurs at the G2 stage. This is important for the regulation of cell division and for the development of cancer.

SIAH2 is also involved in the regulation of immune response. It has been shown to play a role in the regulation of T cell development and function, by binding to specific DNA sequences and preventing the activation of T cells. This is important for the regulation of the immune response and for the development of autoimmune diseases.

Despite its importance in many cellular processes, SIAH2 is a relatively small protein, with only 26 amino acid residues. This makes it a promising target for drug development, as small molecules can often be more effective than larger molecules. Currently, several drugs are being developed against SIAH2, including inhibitors of SIAH2-mediated ubiquitin transferases and antibodies that specifically target SIAH2.

In conclusion, SIAH2 is a key protein involved in the regulation of gene expression, protein stability, and cell signaling and division. Its activity is regulated by a variety of factors, including its structure and interactions with other proteins. Currently, several drugs are being developed against SIAH2, making it an attractive target for drug development. Further research is needed to fully understand the role of SIAH2 in cellular processes and its potential as a drug target.

Protein Name: Siah E3 Ubiquitin Protein Ligase 2

Functions: E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:9334332, PubMed:11483518, PubMed:19224863). 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:9334332, PubMed:11483518, PubMed:19224863). 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:9334332, PubMed:11483518, PubMed:19224863). Triggers the ubiquitin-mediated degradation of many substrates, including proteins involved in transcription regulation (GPS2, POU2AF1, PML, NCOR1), a cell surface receptor (DCC), an antiapoptotic protein (BAG1), and a protein involved in synaptic vesicle function in neurons (SYP) (PubMed:9334332, PubMed:11483518, PubMed:19224863). Mediates ubiquitination and proteasomal degradation of DYRK2 in response to hypoxia (PubMed:22878263). It is thereby involved in apoptosis, tumor suppression, cell cycle, transcription and signaling processes (PubMed:9334332, PubMed:11483518, PubMed:19224863, PubMed:22878263). Has some overlapping function with SIAH1 (PubMed:9334332, PubMed:11483518, PubMed:19224863). Triggers the ubiquitin-mediated degradation of TRAF2, whereas SIAH1 does not (PubMed:12411493). Promotes monoubiquitination of SNCA (PubMed:19224863). Regulates cellular clock function via ubiquitination of the circadian transcriptional repressors NR1D1 and NR1D2 leading to their proteasomal degradation (PubMed:26392558). Plays an important role in mediating the rhythmic degradation/clearance of NR1D1 and NR1D2 contributing to their circadian profile of protein abundance (PubMed:26392558). 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

The "SIAH2 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 SIAH2 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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SIAH3 | Sialidase | Sialyltransferase | SIDT1 | SIDT2 | SIGIRR | SIGLEC1 | SIGLEC10 | SIGLEC11 | SIGLEC12 | SIGLEC14 | SIGLEC15 | SIGLEC16 | SIGLEC17P | SIGLEC5 | SIGLEC6 | SIGLEC7 | SIGLEC8 | SIGLEC9 | SIGLECL1 | sigma Receptor | SIGMAR1 | Signal peptidase complex | Signal recognition particle | Signal recognition particle receptor | Signal Transducers and Activators of Transcription (STAT) | SIK1 | SIK2 | SIK3 | SIKE1 | SIL1 | SILC1 | SIM1 | SIM2 | SIMC1 | SIN3 complex | SIN3A | SIN3B | SINHCAF | SIPA1 | SIPA1L1 | SIPA1L1-AS1 | SIPA1L2 | SIPA1L3 | SIRPA | SIRPAP1 | SIRPB1 | SIRPB2 | SIRPB3P | SIRPD | SIRPG | SIRPG-AS1 | SIRT1 | SIRT2 | SIRT3 | SIRT4 | SIRT5 | SIRT6 | SIRT7 | SIT1 | SIVA1 | SIX1 | SIX2 | SIX3 | SIX3-AS1 | SIX4 | SIX5 | SIX6 | SKA1 | SKA1 complex | SKA2 | SKA2P1 | SKA3 | SKAP1 | SKAP1-AS2 | SKAP2 | Skeletal muscle troponin | SKI | SKIC2 | SKIC3 | SKIC8 | SKIDA1 | SKIL | SKINT1L | SKOR1 | SKOR2 | SKP1 | SKP1P2 | SKP2 | SLA | SLA2 | SLAIN1 | SLAIN2 | SLAM Family Member | SLAMF1 | SLAMF6 | SLAMF6P1 | SLAMF7 | SLAMF8 | SLAMF9