DDB1- and CUL4-associated factor 13 (DCAF13)

DDB1- and CUL4-associated factor 13 (DCAF13) is a highly conserved WD repeat and SOF1 domain-containing protein serving as a substrate recognition adaptor in the CRL4 (Cullin-RING Ligase 4) E3 ubiquitin-protein ligase complex. It mediates the protein polyubiquitination and subsequent degradation of specific substrates—including PERP, SUV39H1, PTEN, PMP22—regulating cell cycle progression, chromatin organization, epigenetic modifications, and ribosome biogenesis. DCAF13 is both an RNA-binding protein and a critical factor in the processing of 18S rRNA and chromatin regulation during oocyte development and early embryogenesis. In multiple cancers (notably breast and liver), DCAF13 expression is frequently upregulated, correlating with poor prognosis and increased proliferation, migration, and invasion of cancer cells. Its expression level is a potential diagnostic and prognostic biomarker for cancer, and it is considered a promising but challenging therapeutic target due to its essential roles in cell division and developmental processes. No approved drugs are known to target DCAF13 directly as of September 2025.

Other names

WDSOF1HSPC064DKFZP564O0463Gm83Sof1WD repeat and SOF domain-containing protein 1GM83WD repeats and SOF1 domain containingDCA13

As part of CRL4 E3 ubiquitin ligase, DCAF13 acts as a substrate recognition adaptor, promoting ubiquitination and proteasomal degradation of target proteins such as PERP, SUV39H1, PTEN, PMP22