KPNA2
From Wikipedia, the free encyclopedia
Karyopherin alpha 2 (RAG cohort 1, importin alpha 1)
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PDB rendering based on 1ejl. | ||||||||||||||
Available structures: 1ejl, 1ejy, 1ial, 1iq1, 1pjm, 1pjn, 1q1s, 1q1t, 1qgk, 1y2a, 2c1m | ||||||||||||||
Identifiers | ||||||||||||||
Symbol(s) | KPNA2; IPOA1; QIP2; RCH1; SRP1alpha | |||||||||||||
External IDs | OMIM: 600685 MGI: 103561 HomoloGene: 1708 | |||||||||||||
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Orthologs | ||||||||||||||
Human | Mouse | |||||||||||||
Entrez | 3838 | 16647
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Refseq | XM_001133253 (mRNA) XP_001133253 (protein) |
XM_987865 (mRNA) XP_992959 (protein) |
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Pubmed search | [1] | [2] |
Karyopherin alpha 2 (RAG cohort 1, importin alpha 1), also known as KPNA2, is a human gene.
The import of proteins into the nucleus is a process that involves at least 2 steps. The first is an energy-independent docking of the protein to the nuclear envelope and the second is an energy-dependent translocation through the nuclear pore complex. Imported proteins require a nuclear localization sequence (NLS) which generally consists of a short region of basic amino acids or 2 such regions spaced about 10 amino acids apart. Proteins involved in the first step of nuclear import have been identified in different systems. These include the Xenopus protein importin and its yeast homolog, SRP1 (a suppressor of certain temperature-sensitive mutations of RNA polymerase I in Saccharomyces cerevisiae), which bind to the NLS. KPNA2 protein interacts with the NLSs of DNA helicase Q1 and SV40 T antigen and may be involved in the nuclear transport of proteins. KPNA2 also may play a role in V(D)J recombination[1]
[edit] References
[edit] Further reading
- Bukrinsky MI, Haffar OK (2004). "HIV-1 nuclear import: in search of a leader.". Front. Biosci. 2: d578–87. PMID 9366553.
- Bukrinsky MI, Haffar OK (1998). "HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr.". Mol. Med. 4 (3): 138–43. PMID 9562972.
- Kino T, Pavlakis GN (2004). "Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1.". DNA Cell Biol. 23 (4): 193–205. doi: . PMID 15142377.
- Teng SC, Wu KJ, Tseng SF, et al. (2007). "Importin KPNA2, NBS1, DNA repair and tumorigenesis.". J. Mol. Histol. 37 (5-7): 293–9. doi: . PMID 16752129.
- Bukrinsky MI, Sharova N, Dempsey MP, et al. (1992). "Active nuclear import of human immunodeficiency virus type 1 preintegration complexes.". Proc. Natl. Acad. Sci. U.S.A. 89 (14): 6580–4. PMID 1631159.
- Sharova N, Bukrinskaya A (1991). "p17 and p17-containing gag precursors of input human immunodeficiency virus are transported into the nuclei of infected cells.". AIDS Res. Hum. Retroviruses 7 (3): 303–6. PMID 2064827.
- Di Marzio P, Choe S, Ebright M, et al. (1996). "Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr.". J. Virol. 69 (12): 7909–16. PMID 7494303.
- Küssel P, Frasch M (1995). "Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis.". Mol. Gen. Genet. 248 (3): 351–63. PMID 7565597.
- Gallay P, Swingler S, Song J, et al. (1995). "HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase.". Cell 83 (4): 569–76. PMID 7585960.
- Moroianu J, Hijikata M, Blobel G, Radu A (1995). "Mammalian karyopherin alpha 1 beta and alpha 2 beta heterodimers: alpha 1 or alpha 2 subunit binds nuclear localization signal and beta subunit interacts with peptide repeat-containing nucleoporins.". Proc. Natl. Acad. Sci. U.S.A. 92 (14): 6532–6. PMID 7604027.
- Freed EO, Englund G, Martin MA (1995). "Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection.". J. Virol. 69 (6): 3949–54. PMID 7745752.
- Weis K, Mattaj IW, Lamond AI (1995). "Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences.". Science 268 (5213): 1049–53. PMID 7754385.
- Gallay P, Swingler S, Aiken C, Trono D (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. PMID 7859280.
- Cuomo CA, Kirch SA, Gyuris J, et al. (1994). "Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein.". Proc. Natl. Acad. Sci. U.S.A. 91 (13): 6156–60. PMID 8016130.
- von Schwedler U, Kornbluth RS, Trono D (1994). "The nuclear localization signal of the matrix protein of human immunodeficiency virus type 1 allows the establishment of infection in macrophages and quiescent T lymphocytes.". Proc. Natl. Acad. Sci. U.S.A. 91 (15): 6992–6. PMID 8041734.
- Heinzinger NK, Bukinsky MI, Haggerty SA, et al. (1994). "The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells.". Proc. Natl. Acad. Sci. U.S.A. 91 (15): 7311–5. PMID 8041786.
- Bukrinsky MI, Haggerty S, Dempsey MP, et al. (1993). "A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells.". Nature 365 (6447): 666–9. doi: . PMID 8105392.
- Dubrovsky L, Ulrich P, Nuovo GJ, et al. (1996). "Nuclear localization signal of HIV-1 as a novel target for therapeutic intervention.". Mol. Med. 1 (2): 217–30. PMID 8529100.
- Gallay P, Stitt V, Mundy C, et al. (1996). "Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import.". J. Virol. 70 (2): 1027–32. PMID 8551560.
- Bukrinskaya AG, Ghorpade A, Heinzinger NK, et al. (1996). "Phosphorylation-dependent human immunodeficiency virus type 1 infection and nuclear targeting of viral DNA.". Proc. Natl. Acad. Sci. U.S.A. 93 (1): 367–71. PMID 8552640.