Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Tat
|
tat
|
Interaction of HIV-1 Tat with TFIIH stimulates phosphorylation of Ser-5 of the RNA polymerase II C-terminal domain (CTD), which in turn also stimulates co-transcriptional capping of HIV-1 mRNA |
PubMed
|
|
tat
|
TFIIH subunits CDK7 and cyclin H have been identified as two components associated with the Tat-associated CTD kinase (TTK) that binds to HIV-1 Tat |
PubMed
|
|
tat
|
TFIIH interacts with HIV-1 Tat as a component of the HIV-1 transcription preinitiation complex, but is released from the elongation complex which includes P-TEFb |
PubMed
|
|
tat
|
CAK/TFIIH is required for HIV-1 Tat-mediated transactivation of the HIV-1 LTR promoter |
PubMed
|
|
tat
|
Amino acids 1-48 of HIV-1 Tat, which includes the Tat activation domain, mediate the binding of Tat to CAK and the TFIIH complex through a direct interaction with CDK7 and possibly other TFIIH subunits, including p62 and ERCC3 |
PubMed
|
|
tat
|
TFIIH synergizes with HIV-1 Tat to induce transcription elongation from the HIV-1 LTR promoter |
PubMed
|
|
tat
|
HIV-1 Tat interacts with the RNA polymerase II holoenzyme and transcription preinitiation complexes, which include TFIIH, during Tat-mediated transactivation of the HIV-1 LTR |
PubMed
|
Vpr
|
vpr
|
As a component of the TFIIH transcription complex, cyclin H inhibits HIV-1 Vpr cell cycle-arresting function |
PubMed
|
|
vpr
|
As a component of the TFIIH transcription complex, cyclin H enhances the synergistic activation of glucocorticoid receptor by HIV-1 Vpr and p300 |
PubMed
|
Go to the HIV-1, Human Interaction Database