Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Tat
|
tat
|
HIV-1 Tat peptides bind core histones H2A, H2B, H3 and H4, and Tat protein recruits histone acetyltransferases to the HIV-1 LTR promoter leading to acetylation of histones H3 and H4, derepressing chromatin structure and increasing NFkappaB responsiveness |
PubMed
|
Vpr
|
vpr
|
Soluble HIV-1 Vpr induces a DNA damage response by forming H2AX- and 53BP1-containing DNA repair foci |
PubMed
|
|
vpr
|
HIV-1 Vpr expression in HeLa cells and human primary CD4+ lymphocytes induces phosphorylation of H2AFX and formation of nuclear foci containing H2AFX and BRCA1 |
PubMed
|
|
vpr
|
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 |
PubMed
|
|
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 |
PubMed
|
integrase
|
gag-pol
|
HIV-1 IN-mediated proviral DNA integration triggers cell death during HIV-1 infection. The mechanism of killing during viral integration involves activation of DNA-PK, which causes phosphorylation of p53 and histone gammaH2AX |
PubMed
|
Go to the HIV-1, Human Interaction Database