Catenin beta-like protein 1 (CTNNBL1)

Catenin beta-like protein 1 (CTNNBL1) is an evolutionarily conserved nuclear protein distinguished by its armadillo-repeat (ARM) motif-containing central domain, flanked by unique non-ARM structures[1][2][4]. CTNNBL1 functions primarily as a selective nuclear localization signal (NLS)-binding protein that interacts with spliceosomal components (such as CDC5L and Prp31) and with the antibody-diversification enzyme activation-induced cytidine deaminase (AID), thus participating in RNA splicing and immunoglobulin gene diversification[1][2][4][5]. The structure of CTNNBL1 includes a modified ARM domain and additional unique domains, forming a restrictive protein-binding groove. Its interaction with AID is critical for nuclear import and subnuclear localization of AID, thereby influencing somatic hypermutation and class switch recombination in B lymphocytes[1][2][5]. CTNNBL1 is not a classical drug target such as a receptor, enzyme, transporter, or transcription factor, but serves as an important nuclear protein involved in intranuclear transport and nucleic acid processing complexes[1][2][4][5]. There are currently no approved drugs or direct therapeutic modulators targeting CTNNBL1.

Other names

Beta-catenin-like protein 1C20orf33PP8304NAPFLJ21108P14LP14NYD-SP19Nuclear-associated proteinTestis development protein NYD-SP19IMD99dJ633O20.1

Not applicable (no known drugs targeting this protein)