From Wikipedia, the free encyclopedia
Jump to: navigation, search
Exportin 1
Exportin1, CRM1, free form.jpg
PDB rendering based on 4FGV.
Available structures
PDB Ortholog search: PDBe, RCSB
Symbols XPO1 ; CRM1; emb; exp1
External IDs OMIM602559 MGI2144013 HomoloGene2554 ChEMBL: 5661 GeneCards: XPO1 Gene
RNA expression pattern
PBB GE XPO1 208775 at tn.png
More reference expression data
Species Human Mouse
Entrez 7514 103573
Ensembl ENSG00000082898 ENSMUSG00000020290
UniProt O14980 Q6P5F9
RefSeq (mRNA) NM_003400 NM_001035226
RefSeq (protein) NP_003391 NP_001030303
Location (UCSC) Chr 2:
61.7 – 61.77 Mb
Chr 11:
23.26 – 23.3 Mb
PubMed search [1] [2]

Exportin-1 is a protein that in humans is encoded by the XPO1 gene.[1][2]


The protein encoded by this gene mediates leucine-rich nuclear export signal (NES)-dependent protein transport. Exportin 1 specifically inhibits the nuclear export of Rev and U snRNAs. It is involved in the control of several cellular processes by controlling the localization of cyclin B, MPAK, and MAPKAP kinase 2. This protein also regulates NFAT and AP-1.[3]


XPO1 has been shown to interact with:

See also[edit]


  1. ^ Fornerod M, van Baal S, Valentine V, Shapiro D, Grosveld G (September 1997). "Chromosomal localization of genes encoding CAN/Nup214-interacting proteins--human CRM1 localizes to 2p16, whereas Nup88 localizes to 17p13 and is physically linked to SF2p32". Genomics 42 (3): 538–40. doi:10.1006/geno.1997.4767. PMID 9205132. 
  2. ^ Kudo N, Khochbin S, Nishi K, Kitano K, Yanagida M, Yoshida M et al. (Dec 1997). "Molecular cloning and cell cycle-dependent expression of mammalian CRM1, a protein involved in nuclear export of proteins". J Biol Chem 272 (47): 29742–51. doi:10.1074/jbc.272.47.29742. PMID 9368044. 
  3. ^ "Entrez Gene: XPO1 exportin 1 (CRM1 homolog, yeast)". 
  4. ^ a b Tickenbrock L, Cramer J, Vetter I, Muller O (August 2002). "The coiled coil region (amino acids 129-250) of the tumor suppressor protein adenomatous polyposis coli (APC). Its structure and its interaction with chromosome maintenance region 1 (Crm-1)". J. Biol. Chem. 277 (35): 32332–8. doi:10.1074/jbc.M203990200. PMID 12070164. 
  5. ^ Ishida N, Hara T, Kamura T, Yoshida M, Nakayama K, Nakayama K (April 2002). "Phosphorylation of p27Kip1 on serine 10 is required for its binding to CRM1 and nuclear export". J. Biol. Chem. 277 (17): 14355–8. doi:10.1074/jbc.C100762200. PMID 11889117. 
  6. ^ Connor M, Kotchetkov R, Cariou S, Resch A, Lupetti R, Beniston R et al. (January 2003). "CRM1/Ran-mediated nuclear export of p27(Kip1) involves a nuclear export signal and links p27 export and proteolysis". Mol. Biol. Cell 14 (1): 201–13. doi:10.1091/mbc.E02-06-0319. PMC 140238. PMID 12529437. 
  7. ^ Raval A, Weissman J, Howcroft T, Singer D (January 2003). "The GTP-binding domain of class II transactivator regulates its nuclear export". J. Immunol. 170 (2): 922–30. PMID 12517958. 
  8. ^ Voong L, Slater A, Kratovac S, Cressman D (April 2008). "Mitogen-activated protein kinase ERK1/2 regulates the class II transactivator". J. Biol. Chem. 283 (14): 9031–9. doi:10.1074/jbc.M706487200. PMC 2431044. PMID 18245089. 
  9. ^ Thomas F, Kutay U (June 2003). "Biogenesis and nuclear export of ribosomal subunits in higher eukaryotes depend on the CRM1 export pathway". J. Cell. Sci. 116 (Pt 12): 2409–19. doi:10.1242/jcs.00464. PMID 12724356. 
  10. ^ a b Lindsay M, Holaska J, Welch K, Paschal B, Macara I (June 2001). "Ran-binding protein 3 is a cofactor for Crm1-mediated nuclear protein export". J. Cell Biol. 153 (7): 1391–402. PMC 2150735. PMID 11425870. 
  11. ^ Kehlenbach R, Dickmanns A, Kehlenbach A, Guan T, Gerace L (May 1999). "A role for RanBP1 in the release of CRM1 from the nuclear pore complex in a terminal step of nuclear export". J. Cell Biol. 145 (4): 645–57. PMC 2133185. PMID 10330396. 
  12. ^ a b Plafker K, Macara I (May 2000). "Facilitated nucleocytoplasmic shuttling of the Ran binding protein RanBP1". Mol. Cell. Biol. 20 (10): 3510–21. PMC 85643. PMID 10779340. 
  13. ^ Singh B, Patel H, Roepman R, Schick D, Ferreira P (Dec 1999). "The zinc finger cluster domain of RanBP2 is a specific docking site for the nuclear export factor, exportin-1". J. Biol. Chem. 274 (52): 37370–8. PMID 10601307. 
  14. ^ Lindsay M, Plafker K, Smith A, Clurman B, Macara I (August 2002). "Npap60/Nup50 is a tri-stable switch that stimulates importin-alpha:beta-mediated nuclear protein import". Cell 110 (3): 349–60. PMID 12176322. 
  15. ^ Fornerod M, Ohno M, Yoshida M, Mattaj I (September 1997). "CRM1 is an export receptor for leucine-rich nuclear export signals". Cell 90 (6): 1051–60. PMID 9323133. 
  16. ^ Craig E, Zhang Z, Davies K, Kalpana G (January 2002). "A masked NES in INI1/hSNF5 mediates hCRM1-dependent nuclear export: implications for tumorigenesis". EMBO J. 21 (1-2): 31–42. doi:10.1093/emboj/21.1.31. PMC 125819. PMID 11782423. 
  17. ^ Kanai M, Hanashiro K, Kim S, Hanai S, Boulares A, Miwa M et al. (September 2007). "Inhibition of Crm1-p53 interaction and nuclear export of p53 by poly(ADP-ribosyl)ation". Nat. Cell Biol. 9 (10): 1175–83. doi:10.1038/ncb1638. PMID 17891139. 
  18. ^ Shao C, Lu C, Chen L, Koty P, Cobos E, Gao W (August 2010). "p53-Dependent anticancer effects of leptomycin B on lung adenocarcinoma". Cancer Chemother. Pharmacol. 67 (6): 1369–80. doi:10.1007/s00280-010-1434-6. PMID 20803015. 

Further reading[edit]

External links[edit]