Linked Life Data

155807-1642

Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/155807-1642

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
entrezgene:pubmed
entrezgene:interactant
entrezgene:geneRifText
DCAF1 interacts with DDB1 as well as the Vpr-UNG2 complex, which leads to polyubiquitination of UNG2 via Vpr, DDB1 overexpression enables G2 cell cycle arrest by both HIV-1 Vpr and its carboxy-terminally truncated form C81, 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 binds the Cul4A-DDB1-VprBP complex and increases the levels of neddylated Cul4A in that complex only, HIV-1 Vpr interacts with damage-specific DNA-binding protein 1 (DDB1) in cells. L64P mutation in DDB1 fails to interact efficiently with Vpr, HIV-1 Vpr interferes with the interaction of DDB1 and DDB2 in cells, 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, which is defective in Cul4A-DDB1 (DCAF1) binding, undergoes proteasome-mediated degradation at a higher rate than wild-type Vpr. DCAF1 overexpression stabilizes wild-type Vpr and leads to its cytoplasmic accumulation, The interaction between Vpr and the Cul4A-DDB1-VprBP complex is required for the induction of G2 arrest, The interaction of Vpr with DDB1 facilitates the formation of complexes containing Cul4A-Roc1 E3 ubiquitin ligase. The association of Vpr with DDB1-containing E3 ligase mediates the degradation of UNG2 and SMUG1, 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
entrezgene:keyphrase
inhibits, interacts with, cooperates with, binds, stabilized by, induces complex with