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Gene Review

KAP104  -  Kap104p

Saccharomyces cerevisiae S288c

Synonyms: Importin subunit beta-2, Importin-104, Karyopherin subunit beta-2, Karyopherin-104, TRN, ...
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High impact information on KAP104

  • Karyopherin-beta2 (transportin) binds a cognate import substrate and targets it to the nuclear pore complex [1].
  • 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 [2].
  • Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins [2].
  • Kap104p is also known to recognize rg-NLSs, and here we show that it compensates for the loss of Kap121p function [3].
  • Kap104 is required for the G(alpha)/phosphatase-mediated effect on Fus3 localization [4].

Biological context of KAP104


Anatomical context of KAP104


Physical interactions of KAP104

  • 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 [7].
  • Truncation of the Kap104 cargo-binding domain blocked the effect of both Gpa1(E364K) and Msg5 on Fus3-GFP localization [4].

Other interactions of KAP104

  • Also, addition of Kap104p to Nab2p and Nab4p/Hrp1p prebound to single-stranded DNA-cellulose stimulated release of both proteins from the resin [6].
  • We also demonstrate that Kap104p, like other known beta-karyopherins (or importins), interacts directly with the small GTPase Ran/Gsp1 [6].
  • Pse1p is predominantly necessary for nuclear uptake of H3 and H4, while Kap104p and Yrb4p also support import [8].


  1. Structure of the nuclear transport complex karyopherin-beta2-Ran x GppNHp. Chook, Y.M., Blobel, G. Nature (1999) [Pubmed]
  2. Kap104p: a karyopherin involved in the nuclear transport of messenger RNA binding proteins. Aitchison, J.D., Blobel, G., Rout, M.P. Science (1996) [Pubmed]
  3. Characterization of karyopherin cargoes reveals unique mechanisms of Kap121p-mediated nuclear import. Leslie, D.M., Zhang, W., Timney, B.L., Chait, B.T., Rout, M.P., Wozniak, R.W., Aitchison, J.D. Mol. Cell. Biol. (2004) [Pubmed]
  4. Effect of the pheromone-responsive G(alpha) and phosphatase proteins of Saccharomyces cerevisiae on the subcellular localization of the Fus3 mitogen-activated protein kinase. Blackwell, E., Halatek, I.M., Kim, H.J., Ellicott, A.T., Obukhov, A.A., Stone, D.E. Mol. Cell. Biol. (2003) [Pubmed]
  5. A defect of Kap104 alleviates the requirement of mitotic exit network gene functions in Saccharomyces cerevisiae. Asakawa, K., Toh-e, A. Genetics (2002) [Pubmed]
  6. 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]
  7. 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]
  8. The histones H2A/H2B and H3/H4 are imported into the yeast nucleus by different mechanisms. Greiner, M., Caesar, S., Schlenstedt, G. Eur. J. Cell Biol. (2004) [Pubmed]
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