Statements in which the resource exists as a subject.
PredicateObject
rdf:type
entrezgene:pubmed
pubmed-article:11223251, pubmed-article:17314515, pubmed-article:17559673, pubmed-article:17609381, pubmed-article:17626091, pubmed-article:17630831, pubmed-article:17855541, pubmed-article:18187620, pubmed-article:18514189, pubmed-article:18541215, pubmed-article:18606781, pubmed-article:19275579, pubmed-article:19275585, pubmed-article:19275588, pubmed-article:19458171, pubmed-article:19657269, pubmed-article:19667756, pubmed-article:19798433, pubmed-article:19838296, pubmed-article:20008788, pubmed-article:20012529, pubmed-article:20018238, pubmed-article:20069611, pubmed-article:20089662, pubmed-article:20347598, pubmed-article:20380700, pubmed-article:20824083, pubmed-article:20870715, pubmed-article:21318276, pubmed-article:21489275, pubmed-article:21526938, pubmed-article:21566118, pubmed-article:21918813, pubmed-article:21994772, pubmed-article:22190034, pubmed-article:22292079, pubmed-article:22422068, pubmed-article:22438978, pubmed-article:22776683, pubmed-article:8195203
entrezgene:interactant
entrezgene:geneRifText
A highly conserved 18WxxxxFxxFxxxAFxH33 motif of the HIV-1 Vpr binds to DCAF1, leading to Vpr-induced G2 arrest. Vpr mutants L22S/L23S and V30S/V31S impair the ability to induce G2 arrest, DCAF1 interacts with DDB1 as well as the Vpr-UNG2 complex, which leads to polyubiquitination of UNG2 via Vpr, HIV-1 Vpr binds DCAF1 and activates the DNA damage response in renal tubule epithelial cells, in which gamma H2AX-positive nuclei are abundant compared to the control, HIV-1 Vpr binds a ternary complex composed of DDB1, DDA1, and VprBP, and modulates the interaction between the DDB1-DDA1-VprBP complex and other factors, HIV-1 Vpr forms nuclear foci containing VPRBP and partially co-localizes with DNA repair foci components 53BP1 and phosphorylated RPA32, HIV-1 Vpr significantly downregulates expression level of MFN2 in the mitochondria via VprBP-DDB1-CUL4A ubiquitin ligase in a proteasome-dependent manner, HIV-1 Vpr(Q65R) mutant fails to bind DDB1 and VprBP, and also fails to induce G2 arrest, Recruitment of a catalytically active CRL4A (VPRBP) complex is required to observe HIV-1 Vpr-interacting unknown cellular ubiquitinated proteins. Phosphorylation of H2AX requires Vpr-induced K48 residue polyubiquitination, The interaction between Vpr and the Cul4A-DDB1-VprBP complex is required for the induction of G2 arrest, The leucine/isoleucine-rich domain of HIV-1 Vpr (amino acids 60-81) mediates binding of Vpr to the C-terminal half of VprBP (amino acids 636-1507), resulting in the cytoplasmic retention of Vpr, Upregulation of NKG2D ligands is dependent on HIV-1 Vpr-mediated activation of the TAR DNA damage/stress pathway, which requires the recruitment of the Cul4/DDB1/DCAF1 E3 ubiquitin ligase complex, W54R/S79A Vpr mutant impairs to interact with UNG2, but is still able to recruit DCAF1. Three G2 arrest-defective Vpr mutants, Q65R, K27M, and S79A, can interact with DCAF1
entrezgene:keyphrase
interacts with, cooperates with, co-localizes with, binds