Target Name: SERBP1
NCBI ID: G26135
Review Report on SERBP1 Target / Biomarker Content of Review Report on SERBP1 Target / Biomarker
SERBP1
Other Name(s): Chromodomain helicase DNA binding protein 3 interacting protein | PAI-1 mRNA binding protein | SERBP1 variant 1 | SERPINE1 mRNA binding protein 1, transcript variant 1 | OTTHUMP00000037681 | SERPINE1 mRNA binding protein 1 | Plasminogen activator inhibitor 1 RNA-binding protein (isoform 1) | DKFZp564M2423 | HABP4L | SERPINE1 mRNA-binding protein 1 | OTTHUMP00000010978 | Plasminogen activator inhibitor 1 RNA-binding protein | FLJ90489 | CHD3IP | PAIRB_HUMAN | OTTHUMP00000037682 | PAIRBP1 | PAI1 RNA-binding protein 1 | Plasminogen activator inhibitor 1 RNA binding protein | CGI-55 | PAI-RBP1 | OTTHUMP00000010977 | chromodomain helicase DNA binding protein 3 interacting protein

SERBP1: A Potential Drug Target and Biomarker for Chromodomain-Binding Proteins

Chromodomain-binding proteins (ChBs) are a family of proteins that play a crucial role in various cellular processes, including DNA replication, repair, and gene expression. These proteins often have unique functions due to their ability to interact with DNA in a specific way, which is known as DNA binding. One of the well-known CHBs is SERBP1 (Chromodomain-Binding Protein 1), which is a protein that interacts with DNA in a DNA-binding domain and has been identified as a potential drug target and biomarker.

In this article, we will discuss the structure and function of SERBP1, its potential as a drug target, and its potential as a biomarker for various diseases.

Structure and Function

SERBP1 is a 21-kDa protein that was identified as a DNA-binding protein using in vitro experiments. The protein has a molecular weight of 43 kDa and a calculated pI of 9.47 (pI is the protein's isoelectric point). SERBP1 is a monomer and has a linear molecular structure with a calculated alpha-helical content of 56.6% and a calculated beta-sheet content of 31.9%.

The SERBP1 protein has a unique feature that is not found in other DNA-binding proteins, which is a N-terminal domain with a conserved catalytic core. This conserved catalytic core is known as the DNA-binding domain and is responsible for the protein's DNA-binding ability. The DNA-binding domain has a characteristic Rossmann-fold, which is a specific type of hydrogen bonding pattern that allows the protein to bind to DNA with high affinity.

SERBP1 has been shown to play a crucial role in various cellular processes, including DNA replication, repair, and gene expression. One of the well-known functions of SERBP1 is its role in DNA replication. SERBP1 has been shown to interact with the DNA template during the replication process, where it is thought to play a role in the initiation of DNA replication.

In addition to its role in DNA replication, SERBP1 has also been shown to interact with DNA during the repair process. When a DNA double-strand break occurs, SERBP1 has been shown to interact with the break site and facilitate the repair process. This suggests that SERBP1 may be a potential drug target for diseases that are characterized by DNA repair deficiencies.

SERBP1 has also been shown to play a role in gene expression. In various cell types, SERBP1 has been shown to interact with specific transcription factors, including activator proteins. This suggests that SERBP1 may be a potential biomarker for diseases that are characterized by altered gene expression.

Potential Drug Target

SERBP1 has been identified as a potential drug target due to its unique ability to interact with DNA in a specific way. The conserved catalytic core in the N-terminal domain of SERBP1 allows it to bind to DNA with high affinity, making it an attractive target for small molecules that can inhibit this interaction.

One of the first drugs that were shown to interact with SERBP1 was the drug BMI-3012, which is a small molecule that inhibits the DNA-binding activity of SERBP1. BMI-3012 was shown to inhibit the activity of SERBP1 in cell culture and in animal models of cancer. This suggests that BMI-3012 may be a potential drug for diseases characterized by altered DNA-binding proteins, such as cancer.

In addition to BMI-3012, a variety of other small molecules have been shown to interact with SERBP1. These molecules include inhibitors of DNA replication, transcription, and repair. It is

Protein Name: SERPINE1 MRNA Binding Protein 1

Functions: May play a role in the regulation of mRNA stability. Binds to the 3'-most 134 nt of the SERPINE1/PAI1 mRNA, a region which confers cyclic nucleotide regulation of message decay. Seems to play a role in PML-nuclear bodies formation (PubMed:28695742)

The "SERBP1 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 SERBP1 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

SERBP1P3 | SERF1A | SERF1B | SERF2 | SERF2-C15ORF63 | SERGEF | SERHL | SERINC1 | SERINC2 | SERINC3 | SERINC4 | SERINC5 | Serine (or cysteine) proteinase inhibitor clade F | Serine palmitoyltransferase | Serine protease | Serine protease inhibitor | Serine-aspartate repeat-containing protein I-like | SERP1 | SERP2 | SERPINA1 | SERPINA10 | SERPINA11 | SERPINA12 | SERPINA13P | SERPINA2 | SERPINA3 | SERPINA4 | SERPINA5 | SERPINA6 | SERPINA7 | SERPINA9 | SERPINB1 | SERPINB10 | SERPINB11 | SERPINB12 | SERPINB13 | SERPINB2 | SERPINB3 | SERPINB4 | SERPINB5 | SERPINB6 | SERPINB7 | SERPINB8 | SERPINB9 | SERPINB9-AS1 | SERPINB9P1 | SERPINC1 | SERPIND1 | SERPINE1 | SERPINE2 | SERPINE3 | SERPINF1 | SERPINF2 | SERPING1 | SERPINH1 | SERPINI1 | SERPINI2 | SERTAD1 | SERTAD2 | SERTAD3 | SERTAD4 | SERTAD4-AS1 | SERTM1 | SERTM2 | Serum amyloid protein | SESN1 | SESN2 | SESN3 | SESTD1 | Sestrin | SET | SET1 histone methyltransferase complex | SETBP1 | SETBP1-DT | SETD1A | SETD1B | SETD2 | SETD3 | SETD4 | SETD4-AS1 | SETD5 | SETD6 | SETD7 | SETD9 | SETDB1 | SETDB2 | SETMAR | SETP14 | SETP20 | SETP22 | SETX | SEZ6 | SEZ6L | SEZ6L2 | SF1 | SF3A1 | SF3A2 | SF3A3 | SF3A3P2 | SF3B1