Target intelligence / Profile preview

BRISC complex subunit Abraxas 2 (ABRAXAS2)

Target
ABRAXAS2
Molecular classification
Other, Deubiquitination complex scaffold protein
01

Overview

BRISC complex subunit Abraxas 2 (ABRAXAS2) is a scaffolding protein within the BRISC (BRCC36 isopeptidase complex), a cytoplasmic multiprotein complex specializing in the selective cleavage of Lys-63-linked polyubiquitin chains from substrate proteins[1][5]. ABRAXAS2 serves to assemble and stabilize the BRISC complex, orchestrating deubiquitination activities crucial for the regulation of apoptotic signaling, spindle assembly during mitosis, attachment of microtubules to kinetochores, interferon receptor signaling (via deubiquitination and stabilization of IFNAR1 at the cell surface), and negative regulation of inflammatory responses to bacterial LPS[1][3][4][5]. It also plays a role in facilitating proper induction of p53-dependent transcription and apoptosis after DNA damage. ABRAXAS2 is evolutionarily related to ABRAXAS1 but has distinct roles, and dysfunction is associated with disorders like Fanconi anemia and may contribute to aberrant immune or cell division signals relevant in cancer[1][3]. There are no documented small-molecule drugs or clinical inhibitors that directly target ABRAXAS2; it is not considered a typical therapeutic target such as an enzyme, receptor, or transporter, but rather functions as a regulatory scaffolding component essential for normal cellular homeostasis[1][5].

Other names
ABRO1FAM175BKIAA0157Abraxas brother protein 1Abraxas brotherProtein FAM175BAbraxas brother 1family with sequence similarity 175 member B
02

Biological functions

Protein scaffolding in BRISC complexRegulation of K63-linked deubiquitinationRegulation of apoptosisMitotic spindle assembly and microtubule attachment to kinetochoresRegulation of interferon signaling via IFNAR1 deubiquitinationNegative regulation of response to bacterial LPSRegulation of p53 induction following DNA damage
03

Disease associations

Myocardial infarctionFanconi anemia (complementation group I)Potential links to cancer (via regulation of p53 and DNA damage pathways)Immune dysregulation (interferon signaling modulation)

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