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Identification
HMDB Protein ID HMDBP08617
Secondary Accession Numbers
  • 14332
Name Exportin-1
Synonyms
  1. Chromosome region maintenance 1 protein homolog
  2. Exp1
Gene Name XPO1
Protein Type Unknown
Biological Properties
General Function Involved in binding
Specific Function Mediates the nuclear export of cellular proteins (cargos) bearing a leucine-rich nuclear export signal (NES) and of RNAs. In the nucleus, in association with RANBP3, binds cooperatively to the NES on its target protein and to the GTPase RAN in its active GTP-bound form (Ran-GTP). Docking of this complex to the nuclear pore complex (NPC) is mediated through binding to nucleoporins. Upon transit of an nuclear export complex into the cytoplasm, disassembling of the complex and hydrolysis of Ran-GTP to Ran-GDP (induced by RANBP1 and RANGAP1, respectively) cause release of the cargo from the export receptor. The directionality of nuclear export is thought to be conferred by an asymmetric distribution of the GTP- and GDP-bound forms of Ran between the cytoplasm and nucleus. Involved in U3 snoRNA transport from Cajal bodies to nucleoli. Binds to late precursor U3 snoRNA bearing a TMG cap. Several viruses, among them HIV-1, HTLV-1 and influenza A use it to export their unspliced or incompletely spliced RNAs out of the nucleus. Interacts with, and mediates the nuclear export of HIV-1 Rev and HTLV-1 Rex proteins. Involved in HTLV-1 Rex multimerization
Pathways Not Available
Reactions Not Available
GO Classification
Function
binding
protein transporter activity
transporter activity
substrate-specific transporter activity
Process
establishment of localization
transport
protein transport
intracellular protein transport
Cellular Location
  1. Nucleus
  2. Nucleus
  3. Nucleus
  4. Cytoplasm
  5. nucleolus
  6. nucleoplasm
  7. Cajal body
Gene Properties
Chromosome Location Chromosome:2
Locus 2p16
SNPs XPO1
Gene Sequence
>3216 bp
ATGCCAGCAATTATGACAATGTTAGCAGACCATGCAGCTCGTCAGCTGCTTGATTTCAGC
CAAAAACTGGATATCAACTTATTAGATAATGTGGTGAATTGCTTATACCATGGAGAAGGA
GCCCAGCAAAGAATGGCTCAAGAAGTACTGACACATTTAAAGGAGCATCCTGATGCTTGG
ACAAGAGTCGACACAATTTTGGAATTTTCTCAGAATATGAATACGAAATACTATGGACTA
CAAATTTTGGAAAATGTGATAAAAACAAGGTGGAAGATTCTTCCAAGGAACCAGTGCGAA
GGAATAAAAAAATACGTTGTTGGCCTCATTATCAAGACGTCATCTGACCCAACTTGTGTA
GAGAAAGAAAAGGTGTATATCGGAAAATTAAATATGATCCTTGTTCAGATACTGAAACAA
GAATGGCCCAAACATTGGCCAACTTTTATCAGTGATATTGTTGGAGCAAGTAGGACCAGC
GAAAGTCTCTGTCAAAATAATATGGTGATTCTTAAACTCTTGAGTGAAGAAGTATTTGAT
TTCTCTAGTGGACAGATAACCCAAGTCAAATCTAAGCATTTAAAAGACAGCATGTGCAAT
GAATTCTCACAGATATTTCAACTGTGTCAGTTTGTAATGGAAAATTCTCAAAATGCTCCA
CTTGTACATGCAACCTTGGAAACATTGCTCAGATTTCTGAACTGGATTCCCCTGGGATAT
ATTTTTGAGACCAAATTAATCAGCACATTGATTTATAAGTTCCTGAATGTTCCAATGTTT
CGAAATGTCTCTCTGAAGTGCCTCACTGAGATTGCTGGTGTGAGTGTAAGCCAATATGAA
GAACAATTTGTAACACTATTTACTCTGACAATGATGCAACTAAAGCAGATGCTTCCTTTA
AATACCAATATTCGACTTGCGTACTCAAATGGAAAAGATGATGAACAGAACTTCATTCAA
AATCTCAGTTTGTTTCTCTGCACCTTTCTTAAGGAACATGATCAACTTATAGAAAAAAGA
TTAAATCTCAGGGAAACTCTTATGGAGGCCCTTCATTATATGTTGTTGGTATCTGAAGTA
GAAGAAACTGAAATCTTTAAAATTTGTCTTGAATACTGGAATCATTTGGCTGCTGAACTC
TATAGAGAGAGTCCATTCTCTACATCTGCCTCTCCGTTGCTTTCTGGAAGTCAACATTTT
GATGTTCCTCCCAGGAGACAGCTATATTTGCCCATGTTATTCAAGGTCCGTTTATTAATG
GTTAGTCGAATGGCTAAACCAGAGGAAGTATTGGTTGTAGAGAATGATCAAGGAGAAGTT
GTGAGAGAATTCATGAAGGATACAGATTCCATAAATTTGTATAAGAATATGAGGGAAACA
TTGGTTTATCTTACTCATCTGGATTATGTAGATACAGAAAGAATAATGACAGAGAAGCTT
CACAATCAAGTGAATGGTACAGAGTGGTCATGGAAAAATTTGAATACATTGTGTTGGGCA
ATAGGCTCCATTAGTGGAGCAATGCATGAAGAGGACGAAAAACGATTTCTTGTTACTGTT
ATAAAGGATCTATTAGGATTATGTGAACAGAAAAGAGGCAAAGATAATAAAGCTATTATT
GCATCAAATATCATGTACATAGTAGGTCAATACCCACGTTTTTTGAGAGCTCACTGGAAA
TTTCTGAAGACTGTAGTTAACAAGCTGTTCGAATTCATGCATGAGACCCATGATGGAGTC
CAGGATATGGCTTGTGATACTTTCATTAAAATAGCCCAAAAATGCCGCAGGCATTTCGTT
CAGGTTCAGGTTGGAGAAGTGATGCCATTTATTGATGAAATTTTGAACAACATTAACACT
ATTATTTGTGATCTTCAGCCTCAACAGGTTCATACGTTTTATGAAGCTGTGGGGTACATG
ATTGGTGCACAAACAGATCAAACAGTACAAGAACACTTGATAGAAAAGTACATGTTACTC
CCTAATCAAGTGTGGGATAGTATAATCCAGCAGGCAACCAAAAATGTGGATATACTGAAA
GATCCTGAAACAGTCAAGCAGCTTGGTAGCATTTTGAAAACAAATGTGAGAGCCTGCAAA
GCTGTTGGACACCCCTTTGTAATTCAGCTTGGAAGAATTTATTTAGATATGCTTAATGTA
TACAAGTGCCTCAGTGAAAATATTTCTGCAGCTATCCAAGCTAATGGTGAAATGGTTACA
AAGCAACCATTGATTAGAAGTATGCGAACTGTAAAAAGGGAAACTTTAAAGTTAATATCT
GGTTGGGTGAGCCGATCCAATGATCCACAGATGGTCGCTGAAAATTTTGTTCCCCCTCTG
TTGGATGCAGTTCTCATTGATTATCAGAGAAATGTCCCAGCTGCTAGAGAACCAGAAGTG
CTTAGTACTATGGCCATAATTGTCAACAAGTTAGGGGGACATATAACAGCTGAAATACCT
CAAATATTTGATGCTGTTTTTGAATGCACATTGAATATGATAAATAAGGACTTTGAAGAA
TATCCTGAACATAGAACGAACTTTTTCTTACTACTTCAGGCTGTCAATTCTCATTGTTTC
CCAGCATTCCTTGCTATTCCACCTACACAGTTTAAACTTGTTTTGGATTCCATCATTTGG
GCTTTCAAACATACTATGAGGAATGTCGCAGATACGGGCTTACAGATACTTTTTACACTC
TTACAAAATGTTGCACAAGAAGAAGCTGCAGCTCAGAGTTTTTATCAAACTTATTTTTGT
GATATTCTCCAGCATATCTTTTCTGTTGTGACAGACACTTCACATACTGCTGGTTTAACA
ATGCATGCATCAATTCTTGCATATATGTTTAATTTGGTTGAAGAAGGAAAAATAAGTACA
TCATTAAATCCTGGAAATCCAGTTAACAACCAAATCTTTCTTCAGGAATATGTGGCTAAT
CTCCTTAAGTCGGCCTTCCCTCACCTACAAGATGCTCAAGTAAAGCTCTTTGTGACAGGG
CTTTTCAGCTTAAATCAAGATATTCCTGCTTTCAAGGAACATTTAAGAGATTTCCTAGTT
CAAATAAAGGAATTTGCAGGTGAAGACACTTCTGATTTGTTTTTGGAAGAGAGAGAAATA
GCCCTACGGCAGGCTGATGAAGAGAAACATAAACGTCAAATGTCTGTCCCTGGCATCTTT
AATCCACATGAGATTCCAGAAGAAATGTGTGATTAA
Protein Properties
Number of Residues 1071
Molecular Weight 123385.0
Theoretical pI 5.98
Pfam Domain Function
Signals
  • None
Transmembrane Regions
  • None
Protein Sequence
>Exportin-1
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAW
TRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCV
EKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFD
FSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGY
IFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPL
NTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEV
EETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLM
VSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKL
HNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAII
ASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFV
QVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLL
PNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNV
YKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPL
LDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEE
YPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTL
LQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKIST
SLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLV
QIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
GenBank ID Protein 62822401
UniProtKB/Swiss-Prot ID O14980
UniProtKB/Swiss-Prot Entry Name XPO1_HUMAN
PDB IDs
GenBank Gene ID AC016727
GeneCard ID XPO1
GenAtlas ID XPO1
HGNC ID HGNC:12825
References
General References
  1. Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S: Complete sequencing and characterization of 21,243 full-length human cDNAs. Nat Genet. 2004 Jan;36(1):40-5. Epub 2003 Dec 21. [PubMed:14702039 ]
  2. Hillier LW, Graves TA, Fulton RS, Fulton LA, Pepin KH, Minx P, Wagner-McPherson C, Layman D, Wylie K, Sekhon M, Becker MC, Fewell GA, Delehaunty KD, Miner TL, Nash WE, Kremitzki C, Oddy L, Du H, Sun H, Bradshaw-Cordum H, Ali J, Carter J, Cordes M, Harris A, Isak A, van Brunt A, Nguyen C, Du F, Courtney L, Kalicki J, Ozersky P, Abbott S, Armstrong J, Belter EA, Caruso L, Cedroni M, Cotton M, Davidson T, Desai A, Elliott G, Erb T, Fronick C, Gaige T, Haakenson W, Haglund K, Holmes A, Harkins R, Kim K, Kruchowski SS, Strong CM, Grewal N, Goyea E, Hou S, Levy A, Martinka S, Mead K, McLellan MD, Meyer R, Randall-Maher J, Tomlinson C, Dauphin-Kohlberg S, Kozlowicz-Reilly A, Shah N, Swearengen-Shahid S, Snider J, Strong JT, Thompson J, Yoakum M, Leonard S, Pearman C, Trani L, Radionenko M, Waligorski JE, Wang C, Rock SM, Tin-Wollam AM, Maupin R, Latreille P, Wendl MC, Yang SP, Pohl C, Wallis JW, Spieth J, Bieri TA, Berkowicz N, Nelson JO, Osborne J, Ding L, Meyer R, Sabo A, Shotland Y, Sinha P, Wohldmann PE, Cook LL, Hickenbotham MT, Eldred J, Williams D, Jones TA, She X, Ciccarelli FD, Izaurralde E, Taylor J, Schmutz J, Myers RM, Cox DR, Huang X, McPherson JD, Mardis ER, Clifton SW, Warren WC, Chinwalla AT, Eddy SR, Marra MA, Ovcharenko I, Furey TS, Miller W, Eichler EE, Bork P, Suyama M, Torrents D, Waterston RH, Wilson RK: Generation and annotation of the DNA sequences of human chromosomes 2 and 4. Nature. 2005 Apr 7;434(7034):724-31. [PubMed:15815621 ]
  3. Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). Genome Res. 2004 Oct;14(10B):2121-7. [PubMed:15489334 ]
  4. Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M: Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science. 2009 Aug 14;325(5942):834-40. doi: 10.1126/science.1175371. Epub 2009 Jul 16. [PubMed:19608861 ]
  5. Daub H, Olsen JV, Bairlein M, Gnad F, Oppermann FS, Korner R, Greff Z, Keri G, Stemmann O, Mann M: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. Mol Cell. 2008 Aug 8;31(3):438-48. doi: 10.1016/j.molcel.2008.07.007. [PubMed:18691976 ]
  6. Matsuoka S, Ballif BA, Smogorzewska A, McDonald ER 3rd, Hurov KE, Luo J, Bakalarski CE, Zhao Z, Solimini N, Lerenthal Y, Shiloh Y, Gygi SP, Elledge SJ: ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage. Science. 2007 May 25;316(5828):1160-6. [PubMed:17525332 ]
  7. Bechtel S, Rosenfelder H, Duda A, Schmidt CP, Ernst U, Wellenreuther R, Mehrle A, Schuster C, Bahr A, Blocker H, Heubner D, Hoerlein A, Michel G, Wedler H, Kohrer K, Ottenwalder B, Poustka A, Wiemann S, Schupp I: The full-ORF clone resource of the German cDNA Consortium. BMC Genomics. 2007 Oct 31;8:399. [PubMed:17974005 ]
  8. Fornerod M, Ohno M, Yoshida M, Mattaj IW: CRM1 is an export receptor for leucine-rich nuclear export signals. Cell. 1997 Sep 19;90(6):1051-60. [PubMed:9323133 ]
  9. Askjaer P, Jensen TH, Nilsson J, Englmeier L, Kjems J: The specificity of the CRM1-Rev nuclear export signal interaction is mediated by RanGTP. J Biol Chem. 1998 Dec 11;273(50):33414-22. [PubMed:9837918 ]
  10. Paraskeva E, Izaurralde E, Bischoff FR, Huber J, Kutay U, Hartmann E, Luhrmann R, Gorlich D: CRM1-mediated recycling of snurportin 1 to the cytoplasm. J Cell Biol. 1999 Apr 19;145(2):255-64. [PubMed:10209022 ]
  11. Englmeier L, Fornerod M, Bischoff FR, Petosa C, Mattaj IW, Kutay U: RanBP3 influences interactions between CRM1 and its nuclear protein export substrates. EMBO Rep. 2001 Oct;2(10):926-32. Epub 2001 Sep 24. [PubMed:11571268 ]
  12. Lindsay ME, Holaska JM, Welch K, Paschal BM, Macara IG: Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export. J Cell Biol. 2001 Jun 25;153(7):1391-402. [PubMed:11425870 ]
  13. Haendeler J, Hoffmann J, Brandes RP, Zeiher AM, Dimmeler S: Hydrogen peroxide triggers nuclear export of telomerase reverse transcriptase via Src kinase family-dependent phosphorylation of tyrosine 707. Mol Cell Biol. 2003 Jul;23(13):4598-610. [PubMed:12808100 ]
  14. Hakata Y, Yamada M, Shida H: A multifunctional domain in human CRM1 (exportin 1) mediates RanBP3 binding and multimerization of human T-cell leukemia virus type 1 Rex protein. Mol Cell Biol. 2003 Dec;23(23):8751-61. [PubMed:14612415 ]
  15. Petosa C, Schoehn G, Askjaer P, Bauer U, Moulin M, Steuerwald U, Soler-Lopez M, Baudin F, Mattaj IW, Muller CW: Architecture of CRM1/Exportin1 suggests how cooperativity is achieved during formation of a nuclear export complex. Mol Cell. 2004 Dec 3;16(5):761-75. [PubMed:15574331 ]
  16. Nemergut ME, Lindsay ME, Brownawell AM, Macara IG: Ran-binding protein 3 links Crm1 to the Ran guanine nucleotide exchange factor. J Biol Chem. 2002 May 17;277(20):17385-8. Epub 2002 Apr 3. [PubMed:11932251 ]
  17. Boulon S, Verheggen C, Jady BE, Girard C, Pescia C, Paul C, Ospina JK, Kiss T, Matera AG, Bordonne R, Bertrand E: PHAX and CRM1 are required sequentially to transport U3 snoRNA to nucleoli. Mol Cell. 2004 Dec 3;16(5):777-87. [PubMed:15574332 ]
  18. Fornerod M, van Deursen J, van Baal S, Reynolds A, Davis D, Murti KG, Fransen J, Grosveld G: The human homologue of yeast CRM1 is in a dynamic subcomplex with CAN/Nup214 and a novel nuclear pore component Nup88. EMBO J. 1997 Feb 17;16(4):807-16. [PubMed:9049309 ]
  19. Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, Yoshida M, Horinouchi S: Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins. J Biol Chem. 1997 Nov 21;272(47):29742-51. [PubMed:9368044 ]
  20. Ossareh-Nazari B, Bachelerie F, Dargemont C: Evidence for a role of CRM1 in signal-mediated nuclear protein export. Science. 1997 Oct 3;278(5335):141-4. [PubMed:9311922 ]
  21. Boyle SM, Ruvolo V, Gupta AK, Swaminathan S: Association with the cellular export receptor CRM 1 mediates function and intracellular localization of Epstein-Barr virus SM protein, a regulator of gene expression. J Virol. 1999 Aug;73(8):6872-81. [PubMed:10400785 ]
  22. Kudo N, Matsumori N, Taoka H, Fujiwara D, Schreiner EP, Wolff B, Yoshida M, Horinouchi S: Leptomycin B inactivates CRM1/exportin 1 by covalent modification at a cysteine residue in the central conserved region. Proc Natl Acad Sci U S A. 1999 Aug 3;96(16):9112-7. [PubMed:10430904 ]
  23. Farjot G, Sergeant A, Mikaelian I: A new nucleoporin-like protein interacts with both HIV-1 Rev nuclear export signal and CRM-1. J Biol Chem. 1999 Jun 11;274(24):17309-17. [PubMed:10358091 ]
  24. Elton D, Simpson-Holley M, Archer K, Medcalf L, Hallam R, McCauley J, Digard P: Interaction of the influenza virus nucleoprotein with the cellular CRM1-mediated nuclear export pathway. J Virol. 2001 Jan;75(1):408-19. [PubMed:11119609 ]
  25. Hakata Y, Yamada M, Mabuchi N, Shida H: The carboxy-terminal region of the human immunodeficiency virus type 1 protein Rev has multiple roles in mediating CRM1-related Rev functions. J Virol. 2002 Aug;76(16):8079-89. [PubMed:12134013 ]
  26. Thomas F, Kutay U: Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway. J Cell Sci. 2003 Jun 15;116(Pt 12):2409-19. Epub 2003 Apr 30. [PubMed:12724356 ]
  27. Yedavalli VS, Neuveut C, Chi YH, Kleiman L, Jeang KT: Requirement of DDX3 DEAD box RNA helicase for HIV-1 Rev-RRE export function. Cell. 2004 Oct 29;119(3):381-92. [PubMed:15507209 ]
  28. Daelemans D, Costes SV, Lockett S, Pavlakis GN: Kinetic and molecular analysis of nuclear export factor CRM1 association with its cargo in vivo. Mol Cell Biol. 2005 Jan;25(2):728-39. [PubMed:15632073 ]