內輸蛋白亞基α-2

內輸蛋白亞基α-2
已知的結構
PDB	直系同源搜索: PDBe RCSB
PDBID列表
	1EFX、1QGK、1QGR、3FEX、3FEY、3WPT、4E4V、4WV6
識別號
別名	KPNA2；, IPOA1, QIP2, RCH1, SRP1alpha, Karyopherin alpha 2, SRP1-alpha, karyopherin subunit alpha 2, PTAC58
外部ID	OMIM：600685 MGI：103561 HomoloGene：1708 GeneCards：KPNA2
基因位置（人類）
染色體	17號染色體
終止	68,047,364 bp
基因位置（小鼠）
染色體	小鼠11號染色體
終止	106,890,367 bp
基因本體
分子功能	• histone deacetylase binding; • 血漿蛋白結合; • nuclear localization sequence binding; • RNA binding; • nuclear import signal receptor activity;
細胞組分	• 膜; • 核孔; • 核質; • 細胞核; • 細胞質; • 細胞質基質; • host cell; • extrinsic component of postsynaptic specialization membrane; • glutamatergic synapse;
生物學過程	• regulation of DNA recombination; • protein import into nucleus; • DNA代謝過程; • protein transport; • viral process; • NLS-bearing protein import into nucleus; • modulation by virus of host cellular process; • intracellular transport of virus; • transport; • postsynapse to nucleus signaling pathway; • entry of viral genome into host nucleus through nuclear pore complex via importin; • positive regulation of viral life cycle;
	Sources:Amigo / QuickGO
直系同源
	3838
	16647
	ENSG00000182481
	ENSMUSG00000018362
	P52292
	P52293
	NM_002266; NM_001320611
	NM_010655
	NP_001307540; NP_002257
	NP_034785
	維基數據
檢視/編輯人類	檢視/編輯小鼠

內輸蛋白亞基α-2（英語：Importin subunit alpha-2）是人體內的一種蛋白質，為內輸蛋白α（英語：Importin α）的一種，由17號染色體上的KPNA2基因編碼。^[5]^[6]

功能

內輸蛋白亞基α-2參與了蛋白質由細胞質轉運進細胞核的過程，細胞質中，內輸蛋白α可結合具有核定位序列的蛋白質^[7]，接著再與內輸蛋白β結合而形成二聚體，後者可與核孔複合物互動，使二聚體和蛋白質一起進入細胞核中。入核後，內輸蛋白二聚體與Ran-GTP結合而將原本結合的蛋白質釋出，再回到細胞質中。此過程與Ran循環（英語：Ran (protein)）偶連，並需消耗能量^[8]。

除了協助蛋白質進入細胞核外，KPNA2可能也參與V(D)J重組（英語：V(D)J recombination）^[9]。

交互作用

核轉運蛋白α-2會與以下的蛋白質產生交互作用：

參考文獻

^ ^1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000182481 - Ensembl, May 2017
^ ^2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000018362 - Ensembl, May 2017
^ Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Cuomo CA, Kirch SA, Gyuris J, Brent R, Oettinger MA. Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein. Proceedings of the National Academy of Sciences of the United States of America. Jun 1994, 91 (13): 6156–60. PMC 44157  . PMID 8016130. doi:10.1073/pnas.91.13.6156.
^ Weis K, Mattaj IW, Lamond AI. Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science. May 1995, 268 (5213): 1049–53. PMID 7754385. doi:10.1126/science.7754385.
^ Moroianu, J; Blobel, G; Radu, A. Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes.. Proceedings of the National Academy of Sciences of the United States of America. 1995-03-14, 92 (6): 2008–2011. ISSN 0027-8424. PMC 42412  . PMID 7892216. doi:10.1073/pnas.92.6.2008.
^ Goldfarb, David S.; Corbett, Anita H.; Mason, D. Adam; Harreman, Michelle T.; Adam, Stephen A. Importin α: a multipurpose nuclear-transport receptor. Trends in Cell Biology. 2004, 14 (9): 505–514. PMID 15350979. doi:10.1016/j.tcb.2004.07.016.
^ Entrez Gene: KPNA2 karyopherin alpha 2 (RAG cohort 1, importin alpha 1). （原始內容存檔於2010-12-05）.
^ Lin CY, Huang PH, Liao WL, Cheng HJ, Huang CF, Kuo JC, Patton WA, Massenburg D, Moss J, Lee FJ. ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli. The Journal of Biological Chemistry. Dec 2000, 275 (48): 37815–23. PMID 10980193. doi:10.1074/jbc.M002470200.
^ Perez-Villar JJ, O'Day K, Hewgill DH, Nadler SG, Kanner SB. Nuclear localization of the tyrosine kinase Itk and interaction of its SH3 domain with karyopherin alpha (Rch1alpha). International Immunology. Oct 2001, 13 (10): 1265–74. PMID 11581171. doi:10.1093/intimm/13.10.1265.
^ Nagoshi E, Yoneda Y. Dimerization of sterol regulatory element-binding protein 2 via the helix-loop-helix-leucine zipper domain is a prerequisite for its nuclear localization mediated by importin beta. Molecular and Cellular Biology. Apr 2001, 21 (8): 2779–89. PMC 86908  . PMID 11283257. doi:10.1128/MCB.21.8.2779-2789.2001.
^ Köhler M, Speck C, Christiansen M, Bischoff FR, Prehn S, Haller H, Görlich D, Hartmann E. Evidence for distinct substrate specificities of importin alpha family members in nuclear protein import. Molecular and Cellular Biology. Nov 1999, 19 (11): 7782–91. PMC 84838  . PMID 10523667. doi:10.1128/mcb.19.11.7782.
^ Kutay U, Bischoff FR, Kostka S, Kraft R, Görlich D. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell. Sep 1997, 90 (6): 1061–71. PMID 9323134. doi:10.1016/s0092-8674(00)80372-4.
^ Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML. Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal. The Journal of Biological Chemistry. May 2002, 277 (22): 19673–8. PMID 11882654. doi:10.1074/jbc.M112112200.
^ Seki T, Tada S, Katada T, Enomoto T. Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase Q1/RecQL. Biochemical and Biophysical Research Communications. May 1997, 234 (1): 48–53. PMID 9168958. doi:10.1006/bbrc.1997.6535.
^ Maiyar AC, Leong ML, Firestone GL. Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain. Molecular Biology of the Cell. Mar 2003, 14 (3): 1221–39. PMC 151592  . PMID 12631736. doi:10.1091/mbc.E02-03-0170.

延伸閱讀

Bukrinsky MI, Haffar OK. HIV-1 nuclear import: in search of a leader. Frontiers in Bioscience. Dec 1997, 2 (4): d578–87. PMID 9366553. doi:10.2741/A213.
Bukrinsky MI, Haffar OK. HIV-1 nuclear import: matrix protein is back on center stage, this time together with Vpr. Molecular Medicine. Mar 1998, 4 (3): 138–43. PMC 2230352  . PMID 9562972. doi:10.1007/BF03401911.
Kino T, Pavlakis GN. Partner molecules of accessory protein Vpr of the human immunodeficiency virus type 1. DNA and Cell Biology. Apr 2004, 23 (4): 193–205 [2019-07-18]. PMID 15142377. doi:10.1089/104454904773819789. （原始內容存檔於2020-11-07）.
Teng SC, Wu KJ, Tseng SF, Wong CW, Kao L. Importin KPNA2, NBS1, DNA repair and tumorigenesis. Journal of Molecular Histology. Sep 2006, 37 (5–7): 293–9. PMID 16752129. doi:10.1007/s10735-006-9032-y.
Bukrinsky MI, Sharova N, Dempsey MP, Stanwick TL, Bukrinskaya AG, Haggerty S, Stevenson M. Active nuclear import of human immunodeficiency virus type 1 preintegration complexes. Proceedings of the National Academy of Sciences of the United States of America. Jul 1992, 89 (14): 6580–4. PMC 49545  . PMID 1631159. doi:10.1073/pnas.89.14.6580.
Sharova N, Bukrinskaya A. p17 and p17-containing gag precursors of input human immunodeficiency virus are transported into the nuclei of infected cells. AIDS Research and Human Retroviruses. Mar 1991, 7 (3): 303–6. PMID 2064827. doi:10.1089/aid.1991.7.303.
Di Marzio P, Choe S, Ebright M, Knoblauch R, Landau NR. Mutational analysis of cell cycle arrest, nuclear localization and virion packaging of human immunodeficiency virus type 1 Vpr. Journal of Virology. Dec 1995, 69 (12): 7909–16. PMC 189735  . PMID 7494303.
Küssel P, Frasch M. Yeast Srp1, a nuclear protein related to Drosophila and mouse pendulin, is required for normal migration, division, and integrity of nuclei during mitosis. Molecular & General Genetics. Aug 1995, 248 (3): 351–63. PMID 7565597. doi:10.1007/BF02191602.
Gallay P, Swingler S, Song J, Bushman F, Trono D. HIV nuclear import is governed by the phosphotyrosine-mediated binding of matrix to the core domain of integrase. Cell. Nov 1995, 83 (4): 569–76. PMID 7585960. doi:10.1016/0092-8674(95)90097-7.
Moroianu J, Hijikata M, Blobel G, Radu A. 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. Proceedings of the National Academy of Sciences of the United States of America. Jul 1995, 92 (14): 6532–6. PMC 41552  . PMID 7604027. doi:10.1073/pnas.92.14.6532.
Freed EO, Englund G, Martin MA. Role of the basic domain of human immunodeficiency virus type 1 matrix in macrophage infection. Journal of Virology. Jun 1995, 69 (6): 3949–54. PMC 189124  . PMID 7745752.
Gallay P, Swingler S, Aiken C, Trono D. HIV-1 infection of nondividing cells: C-terminal tyrosine phosphorylation of the viral matrix protein is a key regulator. Cell. Feb 1995, 80 (3): 379–88. PMID 7859280. doi:10.1016/0092-8674(95)90488-3.
von Schwedler U, Kornbluth RS, Trono D. 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. Proceedings of the National Academy of Sciences of the United States of America. Jul 1994, 91 (15): 6992–6. PMC 44324  . PMID 8041734. doi:10.1073/pnas.91.15.6992.
Heinzinger NK, Bukrinsky MI, Haggerty SA, Ragland AM, Kewalramani V, Lee MA, Gendelman HE, Ratner L, Stevenson M, Emerman M. The Vpr protein of human immunodeficiency virus type 1 influences nuclear localization of viral nucleic acids in nondividing host cells. Proceedings of the National Academy of Sciences of the United States of America. Jul 1994, 91 (15): 7311–5. PMC 44389  . PMID 8041786. doi:10.1073/pnas.91.15.7311.
Bukrinsky MI, Haggerty S, Dempsey MP, Sharova N, Adzhubel A, Spitz L, Lewis P, Goldfarb D, Emerman M, Stevenson M. A nuclear localization signal within HIV-1 matrix protein that governs infection of non-dividing cells. Nature. Oct 1993, 365 (6447): 666–9. PMID 8105392. doi:10.1038/365666a0.
Dubrovsky L, Ulrich P, Nuovo GJ, Manogue KR, Cerami A, Bukrinsky M. Nuclear localization signal of HIV-1 as a novel target for therapeutic intervention. Molecular Medicine. Jan 1995, 1 (2): 217–30. PMC 2229944  . PMID 8529100. doi:10.1007/BF03401569.
Gallay P, Stitt V, Mundy C, Oettinger M, Trono D. Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. Journal of Virology. Feb 1996, 70 (2): 1027–32. PMC 189908  . PMID 8551560.
Bukrinskaya AG, Ghorpade A, Heinzinger NK, Smithgall TE, Lewis RE, Stevenson M. Phosphorylation-dependent human immunodeficiency virus type 1 infection and nuclear targeting of viral DNA. Proceedings of the National Academy of Sciences of the United States of America. Jan 1996, 93 (1): 367–71. PMC 40239  . PMID 8552640. doi:10.1073/pnas.93.1.367.

[refGRCh38Ensembl-1] 1.0 ^1.1 ^1.2 GRCh38: Ensembl release 89: ENSG00000182481 - Ensembl, May 2017

[refGRCm38Ensembl-2] 2.0 ^2.1 ^2.2 GRCm38: Ensembl release 89: ENSMUSG00000018362 - Ensembl, May 2017

[3] Human PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] Mouse PubMed Reference:. National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid8016130-5] Cuomo CA, Kirch SA, Gyuris J, Brent R, Oettinger MA. Rch1, a protein that specifically interacts with the RAG-1 recombination-activating protein. Proceedings of the National Academy of Sciences of the United States of America. Jun 1994, 91 (13): 6156–60. PMC 44157  . PMID 8016130. doi:10.1073/pnas.91.13.6156.

[pmid7754385-6] Weis K, Mattaj IW, Lamond AI. Identification of hSRP1 alpha as a functional receptor for nuclear localization sequences. Science. May 1995, 268 (5213): 1049–53. PMID 7754385. doi:10.1126/science.7754385.

[7] Moroianu, J; Blobel, G; Radu, A. Previously identified protein of uncertain function is karyopherin alpha and together with karyopherin beta docks import substrate at nuclear pore complexes.. Proceedings of the National Academy of Sciences of the United States of America. 1995-03-14, 92 (6): 2008–2011. ISSN 0027-8424. PMC 42412  . PMID 7892216. doi:10.1073/pnas.92.6.2008.

[8] Goldfarb, David S.; Corbett, Anita H.; Mason, D. Adam; Harreman, Michelle T.; Adam, Stephen A. Importin α: a multipurpose nuclear-transport receptor. Trends in Cell Biology. 2004, 14 (9): 505–514. PMID 15350979. doi:10.1016/j.tcb.2004.07.016.

[entrez-9] Entrez Gene: KPNA2 karyopherin alpha 2 (RAG cohort 1, importin alpha 1). （原始內容存檔於2010-12-05）.

[pmid10980193-10] Lin CY, Huang PH, Liao WL, Cheng HJ, Huang CF, Kuo JC, Patton WA, Massenburg D, Moss J, Lee FJ. ARL4, an ARF-like protein that is developmentally regulated and localized to nuclei and nucleoli. The Journal of Biological Chemistry. Dec 2000, 275 (48): 37815–23. PMID 10980193. doi:10.1074/jbc.M002470200.

[pmid11581171-11] Perez-Villar JJ, O'Day K, Hewgill DH, Nadler SG, Kanner SB. Nuclear localization of the tyrosine kinase Itk and interaction of its SH3 domain with karyopherin alpha (Rch1alpha). International Immunology. Oct 2001, 13 (10): 1265–74. PMID 11581171. doi:10.1093/intimm/13.10.1265.

[pmid11283257-12] Nagoshi E, Yoneda Y. Dimerization of sterol regulatory element-binding protein 2 via the helix-loop-helix-leucine zipper domain is a prerequisite for its nuclear localization mediated by importin beta. Molecular and Cellular Biology. Apr 2001, 21 (8): 2779–89. PMC 86908  . PMID 11283257. doi:10.1128/MCB.21.8.2779-2789.2001.

[pmid10523667-13] Köhler M, Speck C, Christiansen M, Bischoff FR, Prehn S, Haller H, Görlich D, Hartmann E. Evidence for distinct substrate specificities of importin alpha family members in nuclear protein import. Molecular and Cellular Biology. Nov 1999, 19 (11): 7782–91. PMC 84838  . PMID 10523667. doi:10.1128/mcb.19.11.7782.

[pmid9323134-14] Kutay U, Bischoff FR, Kostka S, Kraft R, Görlich D. Export of importin alpha from the nucleus is mediated by a specific nuclear transport factor. Cell. Sep 1997, 90 (6): 1061–71. PMID 9323134. doi:10.1016/s0092-8674(00)80372-4.

[pmid11882654-15] Braem CV, Kas K, Meyen E, Debiec-Rychter M, Van De Ven WJ, Voz ML. Identification of a karyopherin alpha 2 recognition site in PLAG1, which functions as a nuclear localization signal. The Journal of Biological Chemistry. May 2002, 277 (22): 19673–8. PMID 11882654. doi:10.1074/jbc.M112112200.

[pmid9168958-16] Seki T, Tada S, Katada T, Enomoto T. Cloning of a cDNA encoding a novel importin-alpha homologue, Qip1: discrimination of Qip1 and Rch1 from hSrp1 by their ability to interact with DNA helicase Q1/RecQL. Biochemical and Biophysical Research Communications. May 1997, 234 (1): 48–53. PMID 9168958. doi:10.1006/bbrc.1997.6535.

[pmid12631736-17] Maiyar AC, Leong ML, Firestone GL. Importin-alpha mediates the regulated nuclear targeting of serum- and glucocorticoid-inducible protein kinase (Sgk) by recognition of a nuclear localization signal in the kinase central domain. Molecular Biology of the Cell. Mar 2003, 14 (3): 1221–39. PMC 151592  . PMID 12631736. doi:10.1091/mbc.E02-03-0170.

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