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Gene Review

BASP1  -  brain abundant, membrane attached signal...

Homo sapiens

Synonyms: 22 kDa neuronal tissue-enriched acidic protein, Brain acid soluble protein 1, CAP-23, CAP23, NAP-22, ...
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Disease relevance of BASP1


High impact information on BASP1

  • Taken together, our results show that BASP1 is a WT1-associated factor that can regulate WT1 transcriptional activity [1].
  • In addition, the expression of growth-associated proteins such as GAP-43 and CAP-23 in neurons lowers the threshold for nerve sprouting and potentiates its vigour [4].
  • Furthermore, phosphorylation of CAP-23/NAP-22 by protein kinase C was also found myristoylation-dependent, suggesting the importance of myristoylation in protein-protein interactions [5].
  • In light of these facts, we consider GAP-43, MARCKS, and BASP1 both separately and in conjunction [6].
  • Our results demonstrated that the NAP-22 peptide interacts with membranes in a concentration-dependent manner, preferentially inserting into DOPC (l(d)) domains [7].

Chemical compound and disease context of BASP1


Biological context of BASP1


Anatomical context of BASP1

  • BASP1 is present in the developing nephron structures of the embryonic kidney and, coincident with that of WT1, its expression is restricted to the highly specialized podocyte cells of the adult kidney [1].
  • Proteins BASP1 and GAP-43/B-50, which are abundant in nerve endings, show a number of similar physico-chemical properties [8].
  • Unlike GAP-43/B-50, BASP1 is present in high amounts also in some non-nervous tissues: testis, kidney and lymphoid organs (spleen, thymus) [8].
  • They also share 45% and 41% amino acid sequence identities with chicken CAP-23 (23 kDa cytoskeleton associated protein) [11].
  • A protein, NAP-22, present in high abundance in the synaptic cell membrane and synaptic vesicle, promotes the formation of cholesterol crystallites in lipid mixtures in which cholesterol would be completely dissolved in the membrane in the absence of protein [12].

Associations of BASP1 with chemical compounds


Other interactions of BASP1


Analytical, diagnostic and therapeutic context of BASP1

  • Tracking peptide-membrane interactions: Insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly [7].
  • We have applied in situ correlated atomic force and confocal microscopies to characterize the interaction of the NAP-22 peptide with model membranes prepared as supported planar bilayers containing both liquid-ordered and liquid-disordered domains [7].
  • No obvious morphological changes in mitochondria were observed by electron microscopy of thin sections of CAP-23 cells [13].


  1. BASP1 is a transcriptional cosuppressor for the Wilms' tumor suppressor protein WT1. Carpenter, B., Hill, K.J., Charalambous, M., Wagner, K.J., Lahiri, D., James, D.I., Andersen, J.S., Schumacher, V., Royer-Pokora, B., Mann, M., Ward, A., Roberts, S.G. Mol. Cell. Biol. (2004) [Pubmed]
  2. Nef of HIV-1 interacts directly with calcium-bound calmodulin. Hayashi, N., Matsubara, M., Jinbo, Y., Titani, K., Izumi, Y., Matsushima, N. Protein Sci. (2002) [Pubmed]
  3. Expression and myristoylation of NAP-22 using a baculovirus transfer vector system. Maekawa, S., Matsuura, Y., Nakamura, S. Biochim. Biophys. Acta (1994) [Pubmed]
  4. Intrinsic neuronal determinants that promote axonal sprouting and elongation. Caroni, P. Bioessays (1997) [Pubmed]
  5. Identification of the calmodulin-binding domain of neuron-specific protein kinase C substrate protein CAP-22/NAP-22. Direct involvement of protein myristoylation in calmodulin-target protein interaction. Takasaki, A., Hayashi, N., Matsubara, M., Yamauchi, E., Taniguchi, H. J. Biol. Chem. (1999) [Pubmed]
  6. Nerve ending "signal" proteins GAP-43, MARCKS, and BASP1. Mosevitsky, M.I. Int. Rev. Cytol. (2005) [Pubmed]
  7. Tracking peptide-membrane interactions: Insights from in situ coupled confocal-atomic force microscopy imaging of NAP-22 peptide insertion and assembly. Shaw, J.E., Epand, R.F., Sinnathamby, K., Li, Z., Bittman, R., Epand, R.M., Yip, C.M. J. Struct. Biol. (2006) [Pubmed]
  8. The BASP1 family of myristoylated proteins abundant in axonal termini. Primary structure analysis and physico-chemical properties. Mosevitsky, M.I., Capony, J.P., Skladchikova GYu, n.u.l.l., Novitskaya, V.A., Plekhanov AYu, n.u.l.l., Zakharov, V.V. Biochimie (1997) [Pubmed]
  9. Proteomic analysis of apical microvillous membranes of syncytiotrophoblast cells reveals a high degree of similarity with lipid rafts. Paradela, A., Bravo, S.B., Henríquez, M., Riquelme, G., Gavilanes, F., González-Ros, J.M., Albar, J.P. J. Proteome Res. (2005) [Pubmed]
  10. Assignment of brain acid-soluble protein 1 (BASP1) to human chromosome 5p15.1-->p14, differential expression in human cancer cell lines as a result of alterations in gene dosage. Fitzgibbon, J., Neat, M.J., Foot, N., Hill, A.S., Lister, T.A., Gupta, R.K. Cytogenet. Cell Genet. (2000) [Pubmed]
  11. Characterization of bovine and human cDNAs encoding NAP-22 (22 kDa neuronal tissue-enriched acidic protein) homologs. Park, S., Kim, Y.I., Kim, B., Seong, C., Oh, Y., Baek, K., Yoon, J. Mol. Cells (1998) [Pubmed]
  12. The arrangement of cholesterol in membranes and binding of NAP-22. Epand, R.M., Epand, R.F., Maekawa, S. Chem. Phys. Lipids (2003) [Pubmed]
  13. Isolation of chloramphenicol-resistant variants from a human cell line. Mitchell, C.H., England, J.M., Attardi, G. Somatic Cell Genet. (1975) [Pubmed]
  14. Cholesterol-dependent partitioning of PtdIns(4,5)P2 into membrane domains by the N-terminal fragment of NAP-22 (neuronal axonal myristoylated membrane protein of 22 kDa). Epand, R.M., Vuong, P., Yip, C.M., Maekawa, S., Epand, R.F. Biochem. J. (2004) [Pubmed]
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