Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (    ). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition subunit (  ). CUL4B may act within the complex as a scaffold protein, contributing to catalysis through positioning of the substrate and the ubiquitin-conjugating enzyme ( , ). Plays a role as part of the E3 ubiquitin-protein ligase complex in polyubiquitination of CDT1, histone H2A, histone H3 and histone H4 in response to radiation-induced DNA damage ( ). Targeted to UV damaged chromatin by DDB2 and may be important for DNA repair and DNA replication . A number of DCX complexes (containing either TRPC4AP or DCAF12 as substrate-recognition component) are part of the DesCEND (destruction via C-end degrons) pathway, which recognizes a C-degron located at the extreme C terminus of target proteins, leading to their ubiquitination and degradation . The DCX(AMBRA1) complex is a master regulator of the transition from G1 to S cell phase by mediating ubiquitination of phosphorylated cyclin-D (CCND1, CCND2 and CCND3) (, ). The DCX(AMBRA1) complex also acts as a regulator of Cul5-RING (CRL5) E3 ubiquitin-protein ligase complexes by mediating ubiquitination and degradation of Elongin-C (ELOC) component of CRL5 complexes . Required for ubiquitination of cyclin E (CCNE1 or CCNE2), and consequently, normal G1 cell cycle progression (, ). Regulates the mammalian target-of-rapamycin (mTOR) pathway involved in control of cell growth, size and metabolism . Specific CUL4B regulation of the mTORC1-mediated pathway is dependent upon 26S proteasome function and requires interaction between CUL4B and MLST8 . With CUL4A, contributes to ribosome biogenesis .
Subcellular locations: Cytoplasm, Nucleus
More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes.