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Gene Review

NAB2  -  Nab2p

Saccharomyces cerevisiae S288c

Synonyms: Nuclear polyadenylated RNA-binding protein NAB2, YGL122C
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High impact information on NAB2

  • Depletion of Kap104p resulted in a rapid shift of Nab2p from the nucleus to the cytoplasm without affecting the localization of other nuclear proteins tested [1].
  • The protein bound directly to repeat-containing nucleoporins and to a cytosolic pool of two nuclear messenger RNA (mRNA) binding proteins, Nab2p and Nab4p [1].
  • We propose that Nab2p and Yra1p are required for proper mRNP docking to the Mlp platform [2].
  • Here, we identify Nab2p as a nuclear poly(A)-binding protein required for both poly(A) tail length control and nuclear export of mRNA [3].
  • Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export [3].

Biological context of NAB2


Anatomical context of NAB2


Associations of NAB2 with chemical compounds

  • Our experiments demonstrate that arginine methylation is required for the export of Nab2p from the nucleus and therefore establish an in vivo effect of this modification [7].
  • The Nab2 protein consists of the following four domains: a unique N-terminal domain, a glutamine-rich domain, an arginine-glycine (RGG) domain, and a zinc finger domain [8].

Physical interactions of NAB2

  • Here, we define a Nab2p sequence that binds to Kap104p and that functions as an NLS in both human and yeast cells despite lacking any evident similarity to basic or M9 NLSs [5].
  • This N-terminal Nab2 domain is distinct from its RNA binding domains suggesting Nab2 could bind Gfd1 and RNA simultaneously [9].

Regulatory relationships of NAB2


Other interactions of NAB2

  • Nab1p, Nab2p, and Nab3p were isolated by a method which uses UV light to cross-link proteins directly bound to poly(A)+ RNA in vivo [10].
  • Also, addition of Kap104p to Nab2p and Nab4p/Hrp1p prebound to single-stranded DNA-cellulose stimulated release of both proteins from the resin [11].
  • Supporting the hypothesis that these proteins display transcript specificity, we identified a unique 7-nucleotide sequence overrepresented in the transcripts highly associated with Nab2 and Nab4/Hrp1 using the REDUCE algorithm [12].
  • In addition, our experiments reveal that the C-terminal domain of Mlp1p is both necessary and sufficient to cause accumulation of poly(A) RNA and Nab2p in the nucleus [13].
  • A Nab2-Gfd1 complex was also identified by coimmunoprecipitation from yeast lysates [9].

Analytical, diagnostic and therapeutic context of NAB2

  • Cellular immunofluorescence, using both monoclonal and polyclonal antibodies, demonstrates that the NAB2 protein is localized within the nucleus [4].


  1. Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Aitchison, J.D., Blobel, G., Rout, M.P. Science (1996) [Pubmed]
  2. Perinuclear Mlp proteins downregulate gene expression in response to a defect in mRNA export. Vinciguerra, P., Iglesias, N., Camblong, J., Zenklusen, D., Stutz, F. EMBO J. (2005) [Pubmed]
  3. Dual requirement for yeast hnRNP Nab2p in mRNA poly(A) tail length control and nuclear export. Hector, R.E., Nykamp, K.R., Dheur, S., Anderson, J.T., Non, P.J., Urbinati, C.R., Wilson, S.M., Minvielle-Sebastia, L., Swanson, M.S. EMBO J. (2002) [Pubmed]
  4. NAB2: a yeast nuclear polyadenylated RNA-binding protein essential for cell viability. Anderson, J.T., Wilson, S.M., Datar, K.V., Swanson, M.S. Mol. Cell. Biol. (1993) [Pubmed]
  5. Identification and functional characterization of a novel nuclear localization signal present in the yeast Nab2 poly(A)+ RNA binding protein. Truant, R., Fridell, R.A., Benson, R.E., Bogerd, H., Cullen, B.R. Mol. Cell. Biol. (1998) [Pubmed]
  6. Functional conservation of the transportin nuclear import pathway in divergent organisms. Siomi, M.C., Fromont, M., Rain, J.C., Wan, L., Wang, F., Legrain, P., Dreyfuss, G. Mol. Cell. Biol. (1998) [Pubmed]
  7. Nab2p is required for poly(A) RNA export in Saccharomyces cerevisiae and is regulated by arginine methylation via Hmt1p. Green, D.M., Marfatia, K.A., Crafton, E.B., Zhang, X., Cheng, X., Corbett, A.H. J. Biol. Chem. (2002) [Pubmed]
  8. Domain analysis of the Saccharomyces cerevisiae heterogeneous nuclear ribonucleoprotein, Nab2p. Dissecting the requirements for Nab2p-facilitated poly(A) RNA export. Marfatia, K.A., Crafton, E.B., Green, D.M., Corbett, A.H. J. Biol. Chem. (2003) [Pubmed]
  9. Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a direct interaction with Gfd1 and to Gle1 function. Suntharalingam, M., Alcázar-Román, A.R., Wente, S.R. J. Biol. Chem. (2004) [Pubmed]
  10. Characterization of nuclear polyadenylated RNA-binding proteins in Saccharomyces cerevisiae. Wilson, S.M., Datar, K.V., Paddy, M.R., Swedlow, J.R., Swanson, M.S. J. Cell Biol. (1994) [Pubmed]
  11. Kap104p-mediated nuclear import. Nuclear localization signals in mRNA-binding proteins and the role of Ran and Rna. Lee, D.C., Aitchison, J.D. J. Biol. Chem. (1999) [Pubmed]
  12. Functional specificity of shuttling hnRNPs revealed by genome-wide analysis of their RNA binding profiles. Kim Guisbert, K., Duncan, K., Li, H., Guthrie, C. RNA (2005) [Pubmed]
  13. The C-terminal domain of myosin-like protein 1 (Mlp1p) is a docking site for heterogeneous nuclear ribonucleoproteins that are required for mRNA export. Green, D.M., Johnson, C.P., Hagan, H., Corbett, A.H. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
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