Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Rev
|
rev
|
Downregulation of HIV-1 Rev activity by HIC is dependent on the I-mfa domain in a cell-specific manner |
PubMed
|
|
rev
|
HIV-1 Rev nuclear import mediated by importin beta is selectively inhibited by competitive excess of HIC in a cell-specific fashion |
PubMed
|
|
rev
|
HIV-1 Rev and HIC interact directly and form a complex through the I-mfa domain (residues 144-246) of HIC |
PubMed
|
Tat
|
tat
|
I-mfa (inhibitor of MyoD family a) and HIC (human I-mfa-domain-containing) proteins serve as substrates for P-TEFb. Their I-mfa domains bind the activation domain of HIV-1 Tat and inhibit Tat- and P-TEFb-dependent HIV-1 transcription |
PubMed
|
|
tat
|
HIC binds both HIV-1 Tat and cyclin T1 through its I-mfa domain (amino acids 165-246) and modulates Tat transactivation of the HIV-1 LTR promoter |
PubMed
|
|
tat
|
HIC binds the NLS domain of HIV-1 Tat located between amino acid residues 48 and 60 of Tat |
PubMed
|
Go to the HIV-1, Human Interaction Database