Protein interactions
Protein |
Gene |
Interaction |
Pubs |
Envelope surface glycoprotein gp120
|
env
|
Tandem affinity purification and mass spectrometry analysis identify cytoplasmic unit 1 of polyA binding protein (PABPC1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
Gag-Pol
|
gag-pol
|
Tandem affinity purification and mass spectrometry analysis identify cytoplasmic unit 1 of polyA binding protein (PABPC1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
Nef
|
nef
|
Tandem affinity purification and mass spectrometry analysis identify cytoplasmic unit 1 of polyA binding protein (PABPC1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
Pr55(Gag)
|
gag
|
Tandem affinity purification and mass spectrometry analysis identify cytoplasmic unit 1 of polyA binding protein (PABPC1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells |
PubMed
|
Rev
|
rev
|
HIV-1 Rev interacting protein, poly(A) binding protein 1 (PABPC1), is identified by the in-vitro binding experiments involving cytosolic or nuclear extracts from HeLa cells. The interaction of Rev with PABPC1 is increased by RRE |
PubMed
|
|
rev
|
binding of PAB1 to HIV-1 mRNA requires the presence of Rev and results in polyadenylation of the mRNA which is necessary for the Rev-dependent nucleocytoplasmic transport of HIV-1 mRNA |
PubMed
|
Tat
|
tat
|
Poly(A) binding protein, cytoplasmic 1 (PABPC1) is identified to interact with HIV-1 Tat mutant Nullbasic in HeLa cells by LC MS/MS |
PubMed
|
retropepsin
|
gag-pol
|
HIV-1 PR-induced PABP cleavage is involved in the inhibition of poly(A)-dependent translation. However, PABP cleavage has little impact on the translation of polyadenylated encephalomyocarditis virus internal ribosome entry site-containing mRNAs |
PubMed
|
|
gag-pol
|
Purified HIV-1 protease cleaves poly(A)-binding protein 1 (PABP1) directly at positions 237 and 477, separating the two first RNA-recognition motifs from the C-terminal domain of PABP |
PubMed
|
Go to the HIV-1, Human Interaction Database