Target Name: HSP90B1
NCBI ID: G7184
Other Name(s): HEL-S-125m | HEL35 | GRP94 | heat shock protein 90 kDa beta member 1 | heat shock protein 90kDa beta family member 1 | Heat shock protein 90 beta family member 1 | Tumor rejection antigen (gp96) 1 | gp96 homolog | Tumor rejection antigen-1 (gp96) | GRP-94 | heat shock protein 90 beta family member 1 | ENPL_HUMAN | Heat shock protein 90kDa beta, member 1 | endothelial cell (HBMEC) glycoprotein | Endothelial cell (HBMEC) glycoprotein | Tumor rejection antigen 1 | ECGP | tumor rejection antigen 1 | epididymis luminal protein 35 | Heat shock protein 90 kDa beta member 1 | stress-inducible tumor rejection antigen gp96 | GP96 | Endoplasmin | Glucose regulated protein, 94 kDa | 94 kDa glucose-regulated protein | heat shock protein 90kDa beta (Grp94), member 1 | tumor rejection antigen (gp96) 1 | epididymis secretory sperm binding protein Li 125m | TRA1

HSP90B1: Key Regulator of ECM and Potential Drug Target

HSP90B1 (HEL-S-125m) is a protein that is expressed in various tissues of the body, including the brain, heart, and kidneys. It is a key regulator of the extracellular matrix (ECM), which is a complex matrix of cytoskeletal components that provides structural support to cells and plays a crucial role in cell-cell and cell-tissue interactions.

HSP90B1 functions as a chaperone, which means it helps to transport and facilitate the movement of other proteins into specific areas of the body. It does this by forming a cation-liquid (CL) complex with other proteins, allowing them to interact and form complex structures.

One of the unique features of HSP90B1 is its ability to form long-term stable CL bonds with other proteins. This stability is important for the regulation of cellular processes such as cell division, migration, and invasion, as well as for the formation of tissues and organs during development.

HSP90B1 is also involved in the regulation of inflammation and immune responses. It has been shown to play a key role in the regulation of neuroimmune interactions, which are critical for the immune system's regulation of the central nervous system.

Due to its involvement in so many cellular processes, HSP90B1 has been identified as a potential drug target. The high prevalence of HSP90B1 expression in various tissues makes it an attractive target for small molecule inhibitors, which can be used to modulate its activity and improve therapeutic outcomes.

One of the most promising small molecules for targeting HSP90B1 is a peptide called S63845. This peptide is derived from the N-terminus of HSP90B1 and has been shown to inhibit the activity of HSP90B1 in cell culture models of various diseases, including cancer, neurodegenerative diseases, and autoimmune disorders.

Another small molecule that is being investigated for its ability to target HSP90B1 is a compound called BHV-3500. This compound is a peptide that is similar in sequence to the N-terminus of HSP90B1 and has been shown to inhibit the activity of HSP90B1 in cell culture models of cancer.

In addition to its potential as a drug target, HSP90B1 is also being investigated as a biomarker for various diseases. Its expression has been shown to be elevated in a variety of diseases, including cancer, neurodegenerative diseases, and autoimmune disorders. This suggests that HSP90B1 may be a useful biomarker for the diagnosis and treatment of these diseases.

Overall, HSP90B1 is a protein that is involved in a wide range of cellular processes and has been identified as a potential drug target and biomarker for various diseases. Further research is needed to fully understand its role in these processes and to develop effective therapies that can modulate its activity.

Protein Name: Heat Shock Protein 90 Beta Family Member 1

Functions: Molecular chaperone that functions in the processing and transport of secreted proteins (By similarity). When associated with CNPY3, required for proper folding of Toll-like receptors (By similarity). Functions in endoplasmic reticulum associated degradation (ERAD) (PubMed:18264092). Has ATPase activity (By similarity). May participate in the unfolding of cytosolic leaderless cargos (lacking the secretion signal sequence) such as the interleukin 1/IL-1 to facilitate their translocation into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and secretion; the translocation process is mediated by the cargo receptor TMED10 (PubMed:32272059)

More Common Targets

HSP90B2P | HSP90B3P | HSPA12A | HSPA12B | HSPA13 | HSPA14 | HSPA1A | HSPA1B | HSPA1L | HSPA2 | HSPA2-AS1 | HSPA4 | HSPA4L | HSPA5 | HSPA5-DT | HSPA5P1 | HSPA6 | HSPA7 | HSPA8 | HSPA8P1 | HSPA8P19 | HSPA9 | HSPA9P1 | HSPB1 | HSPB11 | HSPB2 | HSPB2-C11orf52 | HSPB3 | HSPB6 | HSPB7 | HSPB8 | HSPB9 | HSPBAP1 | HSPBP1 | HSPC102 | HSPC324 | HSPD1 | HSPD1P11 | HSPD1P2 | HSPD1P3 | HSPD1P5 | HSPD1P8 | HSPD1P9 | HSPE1 | HSPE1-MOB4 | HSPE1P8 | HSPG2 | HSPH1 | HTATIP2 | HTATSF1 | HTATSF1P2 | HTD2 | HTN1 | HTN3 | HTR1A | HTR1D | HTR1E | HTR1F | HTR2A | HTR2A-AS1 | HTR2B | HTR2C | HTR3A | HTR3B | HTR3C | HTR3D | HTR3E | HTR3E-AS1 | HTR4 | HTR5A | HTR5A-AS1 | HTR5BP | HTR6 | HTR7 | HTR7P1 | HTRA1 | HTRA2 | HTRA3 | HTRA4 | HTT | HTT-AS | HULC | Human chorionic gonadotropin | HUNK | HUS1 | HUS1B | HUWE1 | HVCN1 | HYAL1 | HYAL2 | HYAL3 | HYAL4 | HYAL6P | Hyaluronidase | HYCC1 | HYCC2 | HYDIN | HYI | HYKK | HYLS1