DDB1- and CUL4-associated factor 16 (DCAF16)

DDB1- and CUL4-associated factor 16 (DCAF16) is a member of the DCAF family, which serves as substrate receptors for the CUL4-DDB1 E3 ubiquitin ligase complex in the ubiquitin-proteasome pathway[1][3]. DCAF16 is an atypical DCAF factor lacking canonical WD40 domains, and it helps recruit protein substrates for polyubiquitination and proteasomal degradation[3]. DCAF16 is primarily localized in the nucleus and can be covalently engaged by electrophilic ligands, making it a valuable E3 ligase component for ligand-induced protein degradation technologies such as PROTACs and molecular glues[1][2]. This property allows degradation of nuclear proteins by covalent recruitment, even when only a minority of DCAF16 is modified[2]. DCAF16 is expressed in various normal epithelial tissues at low levels and is upregulated in several human carcinomas, correlating with degree of tumor differentiation and possible roles in carcinogenesis[3]. Current pharmacological targeting remains experimental, with no approved drugs, and possible effects on normal physiology remain to be elucidated.

Other names

DCAF16C4orf30FLJ20280

Recruiter for targeted protein degradation (PROTACs or 'molecular glue' linkers covalently engage DCAF16, forming a ternary complex with target proteins to induce ubiquitination and subsequent proteasomal degradation) Efficient even at low target occupancy due to catalytic action of E3 ligase complexes