DCAF1 Protein, Human (sf9, His, Strep)

DCAF1 is a multifunctional protein that acts both as a substrate recognition component of E3 ubiquitin-protein ligase complexes and as an atypical serine/threonine-protein kinase, playing key roles in various processes such as cell cycle, telomerase regulation, and histone modification. It serves as a probable substrate-specific adapter of the DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex (e.g., CUL4A-RBX1-DDB1-DCAF1/VPRBP complex), mediating ubiquitination and proteasome-dependent degradation of proteins like NF2. DCAF1 recognizes and binds methylated proteins via its chromo domain, promoting ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex. This complex is also involved in B-cell development (by similar), where DCAF1 is recruited by RAG1 to ubiquitinate proteins, limiting error-prone repair during V(D)J recombination. Additionally, DCAF1 is part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition, as well as ubiquitination and degradation of CCP110. As an atypical kinase, DCAF1 specifically phosphorylates 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, repressing transcription, with H2AT120ph being highly expressed in various tumors. It also participates in JNK-mediated apoptosis during cell competition via interaction with LLGL1 and LLGL2 and is essential for oocyte maintenance at the primordial follicle stage by acting on TET dioxygenases (by similar).