Anti-VPRBP / DCAF1

0.5mg/ml if reconstituted with 0.2ml sterile DI water. VprBP was first identified as a protein that can interact with HIV-1 viral protein R. It is a component of the CUL4A-RBX1-DDB1-VprBP/DCAF1 E3 ubiquitin-protein ligase complex that could interact with HIV-1 virus Vpr protein and HIV-2 virus Vpx protein. VprBP is a 1,507-amino acid protein that contains conserved domains, including YXXY repeats, the Lis homology motif, and WD40 repeats. Through binding to Vpr, VprBP allows Vpr to modulate the catalytic activity of the CUL4-DDB1 complex, which in turn leads to the induction of G2 phase arrest in the virus-infected cells. Recently it has been reported that VprBP is able to regulate the p53-induced transcription and apoptotic pathway. Protein function: 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. Probable substrate-specific adapter of a DCX (DDB1-CUL4-X-box) E3 ubiquitin- protein ligase complex, named CUL4A-RBX1-DDB1-DCAF1/VPRBP complex, which mediates ubiquitination and proteasome-dependent degradation of proteins such as NF2. Involved in the turnover of methylated proteins: recognizes and binds methylated proteins via its chromo domain, leading to ubiquitination of target proteins by the RBX1-DDB1-DCAF1/VPRBP complex (PubMed:23063525). The CUL4A-RBX1-DDB1-DCAF1/VPRBP complex is also involved in B-cell development: DCAF1 is recruited by RAG1 to ubiquitinate proteins, leading to limit error-prone repair during V(D)J recombination. Also part of the EDVP complex, an E3 ligase complex that mediates ubiquitination of proteins such as TERT, leading to TERT degradation and telomerase inhibition (PubMed:23362280). Also acts as an atypical serine/threonine-protein kinase that specifically mediates phosphorylation of 'Thr-120' of histone H2A (H2AT120ph) in a nucleosomal context, thereby repressing transcription. H2AT120ph is present in the regulatory region of many tumor suppresor genes, down- regulates their transcription and is present at high level in a number of tumors (PubMed:24140421). Involved in JNK-mediated apoptosis during cell competition process via its interaction with LLGL1 and LLGL2 (PubMed:20644714). [The UniProt Consortium]