BRISC Complex: A Protein Hub for Cellular Signaling and Degradation

Target Name: BRISC complex

NCBI ID: P29118

BRISC complex

Other Name(s): Brcc36-containing isopeptidase complex

BRISC Complex: A Protein Hub for Cellular Signaling and Degradation

The BRISC complex is a protein complex that is highly conserved across various species, including humans. It is composed of a variety of proteins that share a conserved catalytic core, known as the Brrc1p domain, as well as a distinct N-terminal region that is unique to each protein in the complex. The Brrc1p domain is a N-acetyl-D-glutamyl-L-alanine transacetylase, while the N-terminal region varies depending on the specific protein.

The BRISC complex plays a crucial role in various cellular processes, including protein degradation, autophagy, and cellular signaling. It is involved in the degradation of a wide variety of proteins, including intracellular signaling proteins, as well as proteins involved in stress responses and cellular signaling pathways. The BRISC complex is also involved in the formation of multisubunit complexes, which can enhance its catalytic activity and influence the activity of other cellular signaling pathways.

One of the unique features of the BRISC complex is its ability to interact with other protein complexes to regulate their activity. This interaction between the BRISC complex and other protein complexes is critical for the regulation of cellular signaling pathways and for the control of protein function. The BRISC complex can also been used as a drug target or biomarker, as its activity can be modulated by small molecules.

The BRISC complex is also known as the isopeptidase complex because one of its key protein components is isopeptidase, which is a enzyme involved in the degradation of isopreneol, a compound that is involved in various cellular processes, including cell signaling, DNA replication, and inflammation. Isopeptidase is a key component of the BRISC complex and is responsible for the hydrolysis of the isopreneol ring, which leads to the release of the active isopreneol derivative, 2-fold enriching the cellular environment.

The Brcc36-containing isopeptidase complex is a sub-complex of the BRISC complex that is involved in the degradation of various proteins. This sub-complex is composed of the proteins Brcc36, Brcc37, Brcc38, and Brcc39, which share a conserved catalytic core and a similar N-terminal region. The Brcc36-containing isopeptidase complex is able to hydrolyze the isopreneol ring and release the active isopreneol derivative, which can then interact with other cellular signaling pathways and influence protein function.

The Brcc36-containing isopeptidase complex is a critical regulator of cellular signaling pathways and is involved in the regulation of various cellular processes, including cell signaling, DNA replication, and inflammation. It is also involved in the degradation of intracellular signaling proteins and in the formation of multisubunit complexes, which can enhance its catalytic activity and influence the activity of other cellular signaling pathways. The Brcc36-containing isopeptidase complex is a potential drug target or biomarker, and its activity can be modulated by small molecules.

In conclusion, the BRISC complex is a protein complex that is highly conserved across various species and plays a crucial role in various cellular processes, including protein degradation, autophagy, and cellular signaling. The Brrc1p domain and the N-terminal region of each protein in the complex are unique to each protein and are involved in the regulation of cellular signaling pathways. The Brcc36-containing isopeptidase complex is a sub-complex of the BRISC complex that is involved in the degradation of various proteins and is a potential drug target or biomarker. Its activity can be modulated by small molecules and its potential as a drug target is under investigation.

Protein Name: BRISC Complex

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