BCR E3 Ubiquitin Ligase Complex: A Potential Drug Target Or Biomarker

Target Name: BCR(BACURD3) E3 ubiquitin ligase complex

NCBI ID: P21073

Other Name(s): BCR (BTB-CUL3-RBX1) E3 ubiquitin-protein ligase complex

BCR E3 Ubiquitin Ligase Complex: A Potential Drug Target Or Biomarker

The BCR (BACURD3) E3 ubiquitin ligase complex is a protein complex that plays a critical role in the regulation of gene expression and cell signaling. The BCR E3 ubiquitin ligase complex is composed of the protein BCR (BACURD3), E3 ubiquitin, and RBX1.

The BCR E3 ubiquitin ligase complex is responsible for the covalent binding of E3 ubiquitin to target proteins, which leads to the ubiquitination of these proteins and subsequent degradation or modification. This process is critical for the regulation of gene expression, as the levels of ubiquitinated proteins can affect protein stability, localization, and interactions with other cellular components.

The BCR E3 ubiquitin ligase complex is a complex that has been identified as a potential drug target or biomarker in various diseases, including cancer, neurodegenerative diseases, and autoimmune diseases.

One of the key advantages of the BCR E3 ubiquitin ligase complex is its modularity. The complex is composed of three distinct subunits: BCR, E3 ubiquitin, and RBX1. Each subunit has a distinct function, and the interactions between these subunits are highly regulated to ensure the proper function of the complex.

The BCR subunit of the BCR E3 ubiquitin ligase complex is a 24 kDa protein that contains a nucleotide-binding oligomerization domain (NBD) and a catalytic domain. The NBD domain is responsible for the binding of the E3 ubiquitin protein, while the catalytic domain is responsible for the catalytic activity of the complex.

The E3 ubiquitin subunit is a 26 kDa protein that contains an amino-terminal domain, a catalytic domain, and a carboxy-terminal domain. The amino-terminal domain is responsible for the binding of the E3 ubiquitin protein, while the catalytic domain is responsible for the catalytic activity of the complex.

The RBX1 subunit is a 19 kDa protein that contains an amino-terminal domain, a catalytic domain, and a carboxy-terminal domain. The amino-terminal domain is responsible for the binding of the RBX1 protein, while the catalytic domain is responsible for the catalytic activity of the complex.

The BCR E3 ubiquitin ligase complex plays a critical role in the regulation of gene expression and cell signaling by covalently binding to E3 ubiquitin and ubiquitinated proteins. The complex's modularity and specific functions make it a potential drug target or biomarker in various diseases.

Protein Name: BCR(BACURD3) E3 Ubiquitin Ligase Complex

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