Source:http://linkedlifedata.com/resource/entrezgene/hivinteraction/155348-3840
| Predicate | Object |
|---|---|
| rdf:type | |
| entrezgene:pubmed |
pubmed-article:10366569,
pubmed-article:10525473,
pubmed-article:10888652,
pubmed-article:11035935,
pubmed-article:11278458,
pubmed-article:11389849,
pubmed-article:12368302,
pubmed-article:12414950,
pubmed-article:15037073,
pubmed-article:1631159,
pubmed-article:19961612,
pubmed-article:20015032,
pubmed-article:20554775,
pubmed-article:21326825,
pubmed-article:21763491,
pubmed-article:22509482,
pubmed-article:22928108,
pubmed-article:9275210,
pubmed-article:9366553
|
| entrezgene:interactant | |
| entrezgene:geneRifText |
A region encompassing amino acids 251-270 in the C-terminal domain of HIV-1 IN is required for importin alpha3 binding and for nuclear localization,
HIV-1 IN interacts with importin alpha by the BiFC assay and amino acids 161-173 in IN are required for the interaction with importin alpha,
HIV-1 Integrase (IN) double mutant KK215/219AA and RK263/264AA severely impairs its binding to importin 3 alpha. W179A/N183A and W348A/N352A mutations in the major and the minor NLS binding grooves of Impa3 significantly reduce its binding to IN,
HIV-1 Rev disrupts both IN-TNPO3 and IN-importin alpha complexes,
Karyopherin alpha and beta are reported to interact with HIV-1 integrase (IN) to facilitate nuclear import of IN, however a conflicting report indicates nuclear accumulation of IN does not involve karyopherin alpha, beta 1, or beta 2 mediated pathways,
Karyopherin alpha binds to a bipartite nuclear localization signal in HIV-1 integrase (amino acids 186-189 and 211-219),
Some reports indicate a possible role for the interactions between karyopherin alpha and beta with HIV-1 integrase in the nuclear import of HIV-1 preintegration complexes (PIC), while other reports indicate integrase is not involved in PIC nuclear import
|
| entrezgene:keyphrase |
interacts with,
binds,
complexes with,
imported by
|