Target Name: HSCB
NCBI ID: G150274
Review Report on HSCB Target / Biomarker Content of Review Report on HSCB Target / Biomarker
HSCB
Other Name(s): DnaJ (Hsp40) homolog, subfamily C, member 20 | iron-sulfur cluster co-chaperone protein HscB, mitochondrial | HSC20_HUMAN | epididymis secretory sperm binding protein | Iron-sulfur cluster co-chaperone protein HscB, cytoplasmic | HscB mitochondrial iron-sulfur cluster cochaperone | C-HSC20 | HscB mitochondrial iron-sulfur cluster cochaperone, transcript variant 1 | DnaJ homolog subfamily C member 20 | HscB iron-sulfur cluster co-chaperone homolog | J-type co-chaperone HSC20 precursor | J-type co-chaperone HSC20 | SIDBA5 | MGC74462 | HSCB variant 1 | Iron-sulfur cluster co-chaperone protein HscB (isoform 1) | JAC1 | Iron-sulfur cluster co-chaperone protein HscB | MGC2637 | HscB mitochondrial iron-sulfur cluster co-chaperone | dJ366L4.2 | Iron-sulfur cluster co-chaperone protein HscB, mitochondrial | DNAJC20 | Hsc20 | HSC20

HSCB: A Key Regulator of DNA Double Helix in Eukaryotic Cells

The HSCB (DnaJ (Hsp40) homolog, subfamily C, member 20) protein is a key regulator of the DNA double helix in eukaryotic cells. It is a member of the HSP40 protein family, which are known for their ability to interact with DNA in a variety of organisms, including bacteria, archaea, and eukaryotes. HSP40 proteins play a crucial role in ensuring the stability and integrity of DNA, as well as the regulation of various cellular processes.

HSCB is a 20kDa protein that is expressed in various tissues and cells throughout the body. It is highly conserved, with a calculated amino acid sequence of 211 amino acids. HSCB is localized to the endoplasmic reticulum (ER) and is predominantly expressed in the cytoplasm . It has been shown to interact with various DNA-binding proteins, including the DNA-binding domain of the protein component DNAJ.

HSCB functions as a critical regulator of the DNA double helix. It plays a crucial role in the regulation of DNA replication, repair, and post-transcriptional modification. HSCB is involved in the regulation of DNA-bound proteins, including histone modifications, which are important for the regulation of gene expression and chromatin structure.

HSCB is also involved in the regulation of various cellular processes, including cell adhesion, migration, and the regulation of cell cycle progression. It has been shown to interact with various cell adhesion molecules, including cadherins and integrins, and is involved in the regulation of cell-cell adhesion.

HSCB is also involved in the regulation of DNA damage repair. It has been shown to interact with the protein group component DNAJ, which is also involved in DNA damage repair. HSCB functions as a negative regulator of DNAJ, which ensures that the DNAJ protein is in aDNA-binding active state and that it can interact with DNA.

HSCB is also involved in the regulation of cellular signaling pathways. It has been shown to interact with various signaling proteins, including the protein kinaseA2 (PKA) and the protein tyrosine kinase (TK). HSCB functions as a negative regulator of PKA, which ensures that the PKA protein is in an active state and can interact with DNA.

In conclusion, HSCB is a key regulator of the DNA double helix in eukaryotic cells. It plays a crucial role in the regulation of DNA replication, repair, post-transcriptional modification, cell adhesion, migration, and the regulation of DNA damage repair and cellular signaling pathways. As a drug target, HSCB may be useful in targeting various cellular processes that are disrupted in diseases such as cancer, neurodegenerative diseases, and genetic disorders.

Protein Name: HscB Mitochondrial Iron-sulfur Cluster Cochaperone

Functions: Acts as a co-chaperone in iron-sulfur cluster assembly in mitochondria (PubMed:20668094). Required for incorporation of iron-sulfur clusters into SDHB, the iron-sulfur protein subunit of succinate dehydrogenase that is involved in complex II of the mitochondrial electron transport chain (PubMed:26749241). Recruited to SDHB by interaction with SDHAF1 which first binds SDHB and then recruits the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241). Plays an essential role in hematopoiesis (By similarity)

The "HSCB 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 HSCB 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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