The nuclear import of karyophilic proteins is directed by short amino acid sequences termed nuclear localization signals (NLSs). Karyopherins, or importins, are cytoplasmic proteins that recognize NLSs and dock NLS-containing proteins to the nuclear pore complex. The protein encoded by this gene shares the sequence similarity with Xenopus importin-alpha and Saccharomyces cerevisiae Srp1. This protein is found to interact with the NLSs of DNA helicase Q1 and SV40 T antigen.[3]
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↑Köhler M, Ansieau S, Prehn S, Leutz A, Haller H, Hartmann E (Nov 1997). "Cloning of two novel human importin-alpha subunits and analysis of the expression pattern of the importin-alpha protein family". FEBS Letters. 417 (1): 104–8. doi:10.1016/S0014-5793(97)01265-9. PMID9395085.
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Gallay P, Swingler S, Song J, Bushman F, Trono D (Nov 1995). "HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase". Cell. 83 (4): 569–76. doi:10.1016/0092-8674(95)90097-7. PMID7585960.
Gallay P, Swingler S, Aiken C, Trono D (Feb 1995). "HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator". Cell. 80 (3): 379–88. doi:10.1016/0092-8674(95)90488-3. PMID7859280.
Bukrinsky MI, Haggerty S, Dempsey MP, Sharova N, Adzhubel A, Spitz L, Lewis P, Goldfarb D, Emerman M, Stevenson M (Oct 1993). "A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells". Nature. 365 (6447): 666–9. doi:10.1038/365666a0. PMID8105392.
Sato A, Yoshimoto J, Isaka Y, Miki S, Suyama A, Adachi A, Hayami M, Fujiwara T, Yoshie O (Jun 1996). "Evidence for direct association of Vpr and matrix protein p17 within the HIV-1 virion". Virology. 220 (1): 208–12. doi:10.1006/viro.1996.0302. PMID8659115.
Freed EO, Englund G, Maldarelli F, Martin MA (Jan 1997). "Phosphorylation of residue 131 of HIV-1 matrix is not required for macrophage infection". Cell. 88 (2): 171–3, discussion 173–4. doi:10.1016/S0092-8674(00)81836-X. PMID9008157.