Exportin-1

Details

Name
Exportin-1
Synonyms
  • Chromosome region maintenance 1 protein homolog
  • CRM1
  • Exp1
Gene Name
XPO1
Organism
Humans
Amino acid sequence
>lcl|BSEQ0052054|Exportin-1
MPAIMTMLADHAARQLLDFSQKLDINLLDNVVNCLYHGEGAQQRMAQEVLTHLKEHPDAW
TRVDTILEFSQNMNTKYYGLQILENVIKTRWKILPRNQCEGIKKYVVGLIIKTSSDPTCV
EKEKVYIGKLNMILVQILKQEWPKHWPTFISDIVGASRTSESLCQNNMVILKLLSEEVFD
FSSGQITQVKSKHLKDSMCNEFSQIFQLCQFVMENSQNAPLVHATLETLLRFLNWIPLGY
IFETKLISTLIYKFLNVPMFRNVSLKCLTEIAGVSVSQYEEQFVTLFTLTMMQLKQMLPL
NTNIRLAYSNGKDDEQNFIQNLSLFLCTFLKEHDQLIEKRLNLRETLMEALHYMLLVSEV
EETEIFKICLEYWNHLAAELYRESPFSTSASPLLSGSQHFDVPPRRQLYLPMLFKVRLLM
VSRMAKPEEVLVVENDQGEVVREFMKDTDSINLYKNMRETLVYLTHLDYVDTERIMTEKL
HNQVNGTEWSWKNLNTLCWAIGSISGAMHEEDEKRFLVTVIKDLLGLCEQKRGKDNKAII
ASNIMYIVGQYPRFLRAHWKFLKTVVNKLFEFMHETHDGVQDMACDTFIKIAQKCRRHFV
QVQVGEVMPFIDEILNNINTIICDLQPQQVHTFYEAVGYMIGAQTDQTVQEHLIEKYMLL
PNQVWDSIIQQATKNVDILKDPETVKQLGSILKTNVRACKAVGHPFVIQLGRIYLDMLNV
YKCLSENISAAIQANGEMVTKQPLIRSMRTVKRETLKLISGWVSRSNDPQMVAENFVPPL
LDAVLIDYQRNVPAAREPEVLSTMAIIVNKLGGHITAEIPQIFDAVFECTLNMINKDFEE
YPEHRTNFFLLLQAVNSHCFPAFLAIPPTQFKLVLDSIIWAFKHTMRNVADTGLQILFTL
LQNVAQEEAAAQSFYQTYFCDILQHIFSVVTDTSHTAGLTMHASILAYMFNLVEEGKIST
SLNPGNPVNNQIFLQEYVANLLKSAFPHLQDAQVKLFVTGLFSLNQDIPAFKEHLRDFLV
QIKEFAGEDTSDLFLEEREIALRQADEEKHKRQMSVPGIFNPHEIPEEMCD
Number of residues
1071
Molecular Weight
123384.98
Theoretical pI
Not Available
GO Classification
Functions
nuclear export signal receptor activity / protein domain specific binding / Ran GTPase binding / RNA binding
Processes
intracellular transport of virus / mRNA transport / negative regulation of transcription by RNA polymerase II / nucleocytoplasmic transport / protein export from nucleus / protein localization to nucleus / regulation of centrosome duplication / regulation of mRNA stability / regulation of protein catabolic process / regulation of protein export from nucleus / response to drug / ribosomal large subunit export from nucleus / ribosomal small subunit export from nucleus / ribosomal subunit export from nucleus / ribosome biogenesis / viral process
Components
annulate lamellae / Cajal body / cytoplasm / cytosol / host cell / intracellular membrane-bounded organelle / kinetochore / membrane / nuclear envelope / nuclear membrane / nucleolus / nucleoplasm / nucleus / protein-containing complex / ribonucleoprotein complex
General 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 a 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.
Specific Function
Nuclear export signal receptor activity
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Cytoplasm
Gene sequence
>lcl|BSEQ0052055|Exportin-1 (XPO1)
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
Chromosome Location
2
Locus
2p15
External Identifiers
ResourceLink
UniProtKB IDO14980
UniProtKB Entry NameXPO1_HUMAN
HGNC IDHGNC:12825
General References
  1. 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. doi: 10.1093/emboj/16.4.807. [Article]
  2. 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. doi: 10.1074/jbc.272.47.29742. [Article]
  3. 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. [Article]
  4. 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. [Article]
  5. 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. [Article]
  6. 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. [Article]
  7. 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. [Article]
  8. 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. doi: 10.1126/science.278.5335.141. [Article]
  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. [Article]
  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. [Article]
  11. 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. [Article]
  12. 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. doi: 10.1073/pnas.96.16.9112. [Article]
  13. 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. doi: 10.1074/jbc.274.24.17309. [Article]
  14. 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. [Article]
  15. 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. doi: 10.1128/JVI.75.1.408-419.2001. [Article]
  16. 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. [Article]
  17. 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. doi: 10.1074/jbc.C100620200. Epub 2002 Apr 3. [Article]
  18. 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. doi: 10.1128/jvi.76.16.8079-8089.2002. [Article]
  19. 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. doi: 10.1242/jcs.00464. Epub 2003 Apr 30. [Article]
  20. 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. [Article]
  21. 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. [Article]
  22. 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. doi: 10.1016/j.cell.2004.09.029. [Article]
  23. 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. doi: 10.1016/j.molcel.2004.11.013. [Article]
  24. 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. doi: 10.1128/MCB.25.2.728-739.2005. [Article]
  25. Bi X, Jones T, Abbasi F, Lee H, Stultz B, Hursh DA, Mortin MA: Drosophila caliban, a nuclear export mediator, can function as a tumor suppressor in human lung cancer cells. Oncogene. 2005 Dec 15;24(56):8229-39. doi: 10.1038/sj.onc.1208962. [Article]
  26. Bartholomeusz G, Wu Y, Ali Seyed M, Xia W, Kwong KY, Hortobagyi G, Hung MC: Nuclear translocation of the pro-apoptotic Bcl-2 family member Bok induces apoptosis. Mol Carcinog. 2006 Feb;45(2):73-83. doi: 10.1002/mc.20156. [Article]
  27. Beausoleil SA, Villen J, Gerber SA, Rush J, Gygi SP: A probability-based approach for high-throughput protein phosphorylation analysis and site localization. Nat Biotechnol. 2006 Oct;24(10):1285-92. Epub 2006 Sep 10. [Article]
  28. Cheong JK, Gunaratnam L, Hsu SI: CRM1-mediated nuclear export is required for 26 S proteasome-dependent degradation of the TRIP-Br2 proto-oncoprotein. J Biol Chem. 2008 Apr 25;283(17):11661-76. doi: 10.1074/jbc.M708365200. Epub 2008 Mar 3. [Article]
  29. 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. [Article]
  30. Dephoure N, Zhou C, Villen J, Beausoleil SA, Bakalarski CE, Elledge SJ, Gygi SP: A quantitative atlas of mitotic phosphorylation. Proc Natl Acad Sci U S A. 2008 Aug 5;105(31):10762-7. doi: 10.1073/pnas.0805139105. Epub 2008 Jul 31. [Article]
  31. 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. [Article]
  32. Wang H, Holloway MP, Ma L, Cooper ZA, Riolo M, Samkari A, Elenitoba-Johnson KS, Chin YE, Altura RA: Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity. J Biol Chem. 2010 Nov 12;285(46):36129-37. doi: 10.1074/jbc.M110.152777. Epub 2010 Sep 8. [Article]
  33. Atasheva S, Fish A, Fornerod M, Frolova EI: Venezuelan equine Encephalitis virus capsid protein forms a tetrameric complex with CRM1 and importin alpha/beta that obstructs nuclear pore complex function. J Virol. 2010 May;84(9):4158-71. doi: 10.1128/JVI.02554-09. Epub 2010 Feb 10. [Article]
  34. Fei E, Ma X, Zhu C, Xue T, Yan J, Xu Y, Zhou J, Wang G: Nucleocytoplasmic shuttling of dysbindin-1, a schizophrenia-related protein, regulates synapsin I expression. J Biol Chem. 2010 Dec 3;285(49):38630-40. doi: 10.1074/jbc.M110.107912. Epub 2010 Oct 4. [Article]
  35. Olsen JV, Vermeulen M, Santamaria A, Kumar C, Miller ML, Jensen LJ, Gnad F, Cox J, Jensen TS, Nigg EA, Brunak S, Mann M: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. Sci Signal. 2010 Jan 12;3(104):ra3. doi: 10.1126/scisignal.2000475. [Article]
  36. Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Burckstummer T, Bennett KL, Superti-Furga G, Colinge J: Initial characterization of the human central proteome. BMC Syst Biol. 2011 Jan 26;5:17. doi: 10.1186/1752-0509-5-17. [Article]
  37. Echeverria PC, Bernthaler A, Dupuis P, Mayer B, Picard D: An interaction network predicted from public data as a discovery tool: application to the Hsp90 molecular chaperone machine. PLoS One. 2011;6(10):e26044. doi: 10.1371/journal.pone.0026044. Epub 2011 Oct 11. [Article]
  38. Wu F, Wang S, Xing J, Li M, Zheng C: Characterization of nuclear import and export signals determining the subcellular localization of WD repeat-containing protein 42A (WDR42A). FEBS Lett. 2012 Apr 24;586(8):1079-85. doi: 10.1016/j.febslet.2012.02.053. Epub 2012 Mar 8. [Article]
  39. Krapivinsky G, Krapivinsky L, Stotz SC, Manasian Y, Clapham DE: POST, partner of stromal interaction molecule 1 (STIM1), targets STIM1 to multiple transporters. Proc Natl Acad Sci U S A. 2011 Nov 29;108(48):19234-9. doi: 10.1073/pnas.1117231108. Epub 2011 Nov 14. [Article]
  40. Hsu CC, Hu CD: Critical role of N-terminal end-localized nuclear export signal in regulation of activating transcription factor 2 (ATF2) subcellular localization and transcriptional activity. J Biol Chem. 2012 Mar 9;287(11):8621-32. doi: 10.1074/jbc.M111.294272. Epub 2012 Jan 24. [Article]
  41. Chao HW, Lai YT, Lu YL, Lin CL, Mai W, Huang YS: NMDAR signaling facilitates the IPO5-mediated nuclear import of CPEB3. Nucleic Acids Res. 2012 Sep 1;40(17):8484-98. doi: 10.1093/nar/gks598. Epub 2012 Jun 22. [Article]
  42. Grzybowska EA, Zayat V, Konopinski R, Trebinska A, Szwarc M, Sarnowska E, Macech E, Korczynski J, Knapp A, Siedlecki JA: HAX-1 is a nucleocytoplasmic shuttling protein with a possible role in mRNA processing. FEBS J. 2013 Jan;280(1):256-72. doi: 10.1111/febs.12066. Epub 2012 Dec 11. [Article]
  43. Zhou H, Di Palma S, Preisinger C, Peng M, Polat AN, Heck AJ, Mohammed S: Toward a comprehensive characterization of a human cancer cell phosphoproteome. J Proteome Res. 2013 Jan 4;12(1):260-71. doi: 10.1021/pr300630k. Epub 2012 Dec 18. [Article]
  44. Bian Y, Song C, Cheng K, Dong M, Wang F, Huang J, Sun D, Wang L, Ye M, Zou H: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. J Proteomics. 2014 Jan 16;96:253-62. doi: 10.1016/j.jprot.2013.11.014. Epub 2013 Nov 22. [Article]
  45. Vaca Jacome AS, Rabilloud T, Schaeffer-Reiss C, Rompais M, Ayoub D, Lane L, Bairoch A, Van Dorsselaer A, Carapito C: N-terminome analysis of the human mitochondrial proteome. Proteomics. 2015 Jul;15(14):2519-24. doi: 10.1002/pmic.201400617. Epub 2015 Jun 8. [Article]
  46. 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. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB11942Selinexorapproved, investigationalyesinhibitorDetails