Target Name: SERPINB11
NCBI ID: G89778
Review Report on SERPINB11 Target / Biomarker Content of Review Report on SERPINB11 Target / Biomarker
SERPINB11
Other Name(s): Serpin B11 (isoform a) | serpin peptidase inhibitor, clade B (ovalbumin), member 11 | Serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 11 | SERPIN11 | EPIPIN | serine (or cysteine) proteinase inhibitor, clade B (ovalbumin), member 11 | SPB11_HUMAN | serpin family B member 11 | Serpin family B member 11, transcript variant 1 | Serpin B11

Understanding SERPINB11: A Protein Involved in Cellular Signaling Pathways

SERPINB11 (Serpin B11 (isoform a)) is a protein that is expressed in various cell types of the body, including blood cells, nerve cells, and epithelial cells. It is a member of the serpin family of proteins, which are known for their role in the regulation of protein-protein interactions and the regulation of cellular signaling pathways.

SERPINB11 is a 11-kDa protein that is expressed in the cytoplasm of various cell types. It is characterized by a single transmembrane domain and a N-terminal extracellular domain that is involved in protein-protein interactions. The extracellular domain of SERPINB11 contains a unique The structural feature is known as a N-terminal hypervariable region (HVR), which is capable of engaging in protein-protein interactions with other proteins.

The N-terminal HVR of SERPINB11 is made up of 25 amino acid residues and is located at the interface between the transmembrane domain and the cytoplasm. It is characterized by the presence of a short peptide that includes the amino acids Asp-21, Asp- 22, Asp-23, Asp-24, Asp-25, and Asp-26. This peptide is known as the N-terminal hypervariable region (HVR) and is responsible for the unique structural features of SERPINB11.

The N-terminal HVR of SERPINB11 is involved in protein-protein interactions with other proteins, including the protein SM autoinhibition (Smin) and the protein coagulation factor VII (CF VII). These interactions are important for the regulation of cellular signaling pathways, including the regulation of cell growth, apoptosis, and inflammation.

In addition to its role in protein-protein interactions, the N-terminal HVR of SERPINB11 is also involved in the regulation of cellular signaling pathways. It is a potent inhibitor of the protein tyrosine phosphatase (PTP) and is capable of inhibiting the activity of multiple transcription factors, including NF-kappa-B, AP-1, and STAT3. This means that it is able to regulate the activity of these transcription factors and thereby influence the expression of genes that are involved in cellular signaling pathways.

SERPINB11 is also involved in the regulation of the actinin-based cytoskeleton, which is a structure that is responsible for maintaining the shape and stability of cells. It is a member of the actinin subfamily of the protein superfamily and is characterized by the presence of a unique N-terminal domain that is involved in the regulation of actinin-based cytoskeleton structure and stability.

In conclusion, SERPINB11 is a unique and important protein that is involved in the regulation of multiple cellular signaling pathways. Its N-terminal HVR is responsible for its unique structural features and its role in protein-protein interactions with other proteins. Further research is needed to fully understand the role of SERPINB11 in cellular signaling pathways and its potential as a drug target.

Protein Name: Serpin Family B Member 11

Functions: Has no serine protease inhibitory activity, probably due to mutations in the scaffold impairing conformational change

The "SERPINB11 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 SERPINB11 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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