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Gene Review

RANBP9  -  RAN binding protein 9

Homo sapiens

Synonyms: BPM-L, BPM90, RANBPM, Ran-binding protein 9, Ran-binding protein M, ...
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Disease relevance of RANBP9

  • In addition, transient overexpression of RanBPM in prostate cancer cell lines resulted in enhanced AR activity in a ligand-dependent fashion [1].
  • CONCLUSIONS: These findings support the hypothesis that psoriasin may interact with RanBPM and this may influence both epithelial and stromal cells and thus contribute to breast tumor progression [2].
  • RanBPM mRNA is also frequently expressed in invasive breast carcinomas (n = 64) and a higher psoriasin/RanBPM ratio is associated with both ER negative (p < 0.0001) and PR negative status (p < 0.001), and inflammatory cell infiltrates (p < 0.0001) within the tumor [2].
  • Elevated levels of RanBP7 mRNA in colorectal carcinoma are associated with increased proliferation and are similar to the transcription pattern of the proto-oncogene c-myc [3].

High impact information on RANBP9


Biological context of RANBP9


Anatomical context of RANBP9


Associations of RANBP9 with chemical compounds

  • The Mirk-RanBPM association was confirmed by glutathione S-transferase pull-down assays, co-immunoprecipitation studies, and in vivo cross-linking [5].
  • These data demonstrate that RanBPM interacts with steroid receptors to selectively modify their activity [1].
  • Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors [7].
  • In conclusion, we have identified and characterised a novel interaction between RanBPM and the related receptor tyrosine kinases, Axl and Sky. This novel insight into the signalling interactions of Axl and Sky may shed further light on their suspected roles in tumourigenesis, inflammation as well as other cell proliferative diseases [11].
  • Target peptides from Ran-binding protein M and myo-inositol monophosphatase, along with a new target from procaspase-3, are shown to interact with the protein on a surface comprised of alpha5 (EF3), alpha8 (EF4) and the EF2-EF3 and EF4-EF5 loops [12].

Physical interactions of RANBP9


Regulatory relationships of RANBP9


Other interactions of RANBP9


Analytical, diagnostic and therapeutic context of RANBP9


  1. RanBPM, a nuclear protein that interacts with and regulates transcriptional activity of androgen receptor and glucocorticoid receptor. Rao, M.A., Cheng, H., Quayle, A.N., Nishitani, H., Nelson, C.C., Rennie, P.S. J. Biol. Chem. (2002) [Pubmed]
  2. RanBPM interacts with psoriasin in vitro and their expression correlates with specific clinical features in vivo in breast cancer. Emberley, E.D., Gietz, R.D., Campbell, J.D., HayGlass, K.T., Murphy, L.C., Watson, P.H. BMC Cancer (2002) [Pubmed]
  3. Elevated levels of RanBP7 mRNA in colorectal carcinoma are associated with increased proliferation and are similar to the transcription pattern of the proto-oncogene c-myc. Li, S.R., Gyselman, V.G., Dorudi, S., Bustin, S.A. Biochem. Biophys. Res. Commun. (2000) [Pubmed]
  4. When overexpressed, a novel centrosomal protein, RanBPM, causes ectopic microtubule nucleation similar to gamma-tubulin. Nakamura, M., Masuda, H., Horii, J., Kuma, K., Yokoyama, N., Ohba, T., Nishitani, H., Miyata, T., Tanaka, M., Nishimoto, T. J. Cell Biol. (1998) [Pubmed]
  5. Serine/threonine kinase Mirk/Dyrk1B is an inhibitor of epithelial cell migration and is negatively regulated by the Met adaptor Ran-binding protein M. Zou, Y., Lim, S., Lee, K., Deng, X., Friedman, E. J. Biol. Chem. (2003) [Pubmed]
  6. A novel nuclear protein, Twa1, and Muskelin comprise a complex with RanBPM. Umeda, M., Nishitani, H., Nishimoto, T. Gene (2003) [Pubmed]
  7. Identification and characterization of RanBPM, a novel coactivator of thyroid hormone receptors. Poirier, M.B., Laflamme, L., Langlois, M.F. J. Mol. Endocrinol. (2006) [Pubmed]
  8. Protein stability and function of p73 are modulated by a physical interaction with RanBPM in mammalian cultured cells. Kramer, S., Ozaki, T., Miyazaki, K., Kato, C., Hanamoto, T., Nakagawara, A. Oncogene (2005) [Pubmed]
  9. Ran binding protein 9 interacts with Raf kinase but does not contribute to downstream ERK1/2 activation in skeletal myoblasts. Johnson, S.E., Winner, D.G., Wang, X. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  10. RanBPM associates with CD39 and modulates ecto-nucleotidase activity. Wu, Y., Sun, X., Kaczmarek, E., Dwyer, K.M., Bianchi, E., Usheva, A., Robson, S.C. Biochem. J. (2006) [Pubmed]
  11. The Ran binding protein RanBPM interacts with Axl and Sky receptor tyrosine kinases. Hafizi, S., Gustafsson, A., Stenhoff, J., Dahlbäck, B. Int. J. Biochem. Cell Biol. (2005) [Pubmed]
  12. Structure, binding interface and hydrophobic transitions of Ca2+-loaded calbindin-D(28K). Kojetin, D.J., Venters, R.A., Kordys, D.R., Thompson, R.J., Kumar, R., Cavanagh, J. Nat. Struct. Mol. Biol. (2006) [Pubmed]
  13. HIPK2 associates with RanBPM. Wang, Y., Marion Schneider, E., Li, X., Duttenhöfer, I., Debatin, K., Hug, H. Biochem. Biophys. Res. Commun. (2002) [Pubmed]
  14. Calbindin D28K interacts with Ran-binding protein M: identification of interacting domains by NMR spectroscopy. Lutz, W., Frank, E.M., Craig, T.A., Thompson, R., Venters, R.A., Kojetin, D., Cavanagh, J., Kumar, R. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  15. The cyclin-dependent kinase 11(p46) isoform interacts with RanBPM. Mikolajczyk, M., Shi, J., Vaillancourt, R.R., Sachs, N.A., Nelson, M. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
  16. A new role of ran GTPase. Nishimoto, T. Biochem. Biophys. Res. Commun. (1999) [Pubmed]
  17. Identification of RanBMP interacting with Shigella flexneri IpaC invasin by two-hybrid system of yeast. Yao, X., Wang, H.L., Shi, Z.X., Yan, X.Y., Feng, E.L., Yang, B.L., Huang, L.Y. World J. Gastroenterol. (2003) [Pubmed]
  18. Genotyping by mass spectrometric analysis of short DNA fragments. Laken, S.J., Jackson, P.E., Kinzler, K.W., Vogelstein, B., Strickland, P.T., Groopman, J.D., Friesen, M.D. Nat. Biotechnol. (1998) [Pubmed]
  19. Sperm membrane protein (hSMP-1) and RanBPM complex in the microtubule-organizing centre. Tang, X., Zhang, J., Cai, Y., Miao, S., Zong, S., Koide, S.S., Wang, L. J. Mol. Med. (2004) [Pubmed]
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