The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

NASP  -  nuclear autoantigenic sperm protein...

Homo sapiens

Synonyms: DKFZp547F162, FLB7527, FLJ31599, FLJ35510, MGC19722, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

High impact information on NASP

  • Consequently, we investigated whether NASP is required for normal cell cycle progression and development [1].
  • Nuclear autoantigenic sperm protein (NASP), a linker histone chaperone that is required for cell proliferation [1].
  • Although the null mutation NASP(-/-) caused embryonic lethality, null embryos survive until the blastocyst stage, which may be explained by the presence of stored NASP protein in the cytoplasm of oocytes [1].
  • We conclude from this study that NASP and therefore the linker histones are key players in the assembly of chromatin after DNA replication [1].
  • HSP90 and tNASP are present in both nuclear and cytoplasmic fractions of mouse spermatogenic cells; however, HSP90 bound to NASP only in the cytoplasm [2].

Biological context of NASP

  • Expression of sNASP mRNA is regulated during the cell cycle and, consistent with a role as a histone transport protein, NASP mRNA expression parallels histone mRNA expression [3].
  • Somatic NASP is a shorter version of testicular NASP (tNASP) with two deletions in the coding region arising from alternative splicing and differs from tNASP in its 5' untranslated regions [3].
  • We examined the relationship between NASP mRNA expression and the cell cycle and report that in cultures of synchronized mouse 3T3 cells and HeLa cells sNASP mRNA levels increase during S-phase and decline in G(2), concomitant with histone mRNA levels [3].
  • Multiple sequence alignment (MSA) analysis of the encoded human NASP amino acid sequence with the sequence for the Xenopus histone-binding protein N1/N2 and the rabbit NASP amino acid sequence demonstrates that the human sequence and the Xenopus sequence have extensive amino acid homology upstream of the rabbit initiation codon [4].
  • Putative TATA box-containing transcription initiation sites are present for somatic NASP in human and mouse and for testis hNASP [5].

Anatomical context of NASP

  • When full-length tNASP fused to green fluorescent protein (GFP) is transiently transfected into HeLa cells, it is efficiently transported into the nucleus within 2 h after translation in the cytoplasm, whereas the NASP nuclear localization signal (NLS) deletion mutant (NASP-DeltaNLS-GFP) is retained in the cytoplasm [6].
  • Human spermatozoa contain NASP in the acrosomal region [4].
  • In the human testis, NASP is localized predominantly in primary spermatocytes and round spermatids [4].
  • Following the acrosome reaction, some NASP remains in the equatorial and postacrosomal regions [4].
  • Additionally, we report that human somatic and testis NASP mRNAs are expressed at varying levels in all the transformed cell lines and human tumors tested, further supporting NASP's role in the cell cycle of dividing cells [5].

Associations of NASP with chemical compounds

  • Utilizing a cross-linker, 3,3'-dithiobissulfosuccinimidyl propionate, and mass spectrometry, we have identified HSP90 as a testis/embryo form of NASP (tNASP)-binding partner [2].
  • Purified recombinant polypeptides expressing the full-length hNASP and various deletion constructs covering the entire length of the hNASP sequence were tested by Western blotting and in ELISA for binding to biotin-labeled histones [7].
  • Characterisation of an extracellular serine protease gene (nasp gene) from Dermatophilus congolensis [8].
  • The analogs c-[Phe11-Nasp6-Phe7-D-Trp8-Lys9-Thr10](1), c-[Phe11-Ndab6Phe7-D-Trp8-Lys9-Thr10] (2) and c-[Phen11-Nlys6-Phe7-D-Trp8-Lys9-Thr10](3) where Nasp denotes N-(2-carboxyethyl) glycine, Ndab N-(2-aminoethyl) glycine and Nlys N-(4-aminobutyl) glycine are subject to conformational studies [9].

Other interactions of NASP


Analytical, diagnostic and therapeutic context of NASP

  • Affinity chromatography and histone isolation demonstrate that NASP from myeloma cells is complexed only with H1, linker histones [3].
  • In this study to define the boundaries of antigenic regions and epitope recognition pattern, recombinant deletion mutants spanning the entire protein coding sequence and a human NASP cDNA sublibrary were screened with vasectomy patients' sera [11].
  • Furthermore, using Western blot analysis and enzyme-linked immunosorbent assay, the cross-reaction between the NASP and UreG was verified [12].
  • To further characterize NASP and confirm the structural predictions that NASP was a nuclear protein, specific immunostaining using a specific anti-recombinant protein antibody and in situ hybridization with a cDNA were used [13].
  • The polymerase chain reaction (PCR), using combinations of specific and degenerate oligonucleotide primers, allowed the amplification of a 1738-bp internal fragment of the gene, which was finally characterised by inverse PCR as the first full-length sequenced serine protease gene (nasp) from Dermatophilus congolensis [8].


  1. Nuclear autoantigenic sperm protein (NASP), a linker histone chaperone that is required for cell proliferation. Richardson, R.T., Alekseev, O.M., Grossman, G., Widgren, E.E., Thresher, R., Wagner, E.J., Sullivan, K.D., Marzluff, W.F., O'Rand, M.G. J. Biol. Chem. (2006) [Pubmed]
  2. Association of NASP with HSP90 in mouse spermatogenic cells: stimulation of ATPase activity and transport of linker histones into nuclei. Alekseev, O.M., Widgren, E.E., Richardson, R.T., O'Rand, M.G. J. Biol. Chem. (2005) [Pubmed]
  3. Characterization of the histone H1-binding protein, NASP, as a cell cycle-regulated somatic protein. Richardson, R.T., Batova, I.N., Widgren, E.E., Zheng, L.X., Whitfield, M., Marzluff, W.F., O'Rand, M.G. J. Biol. Chem. (2000) [Pubmed]
  4. Sequence and localization of human NASP: conservation of a Xenopus histone-binding protein. O'Rand, M.G., Richardson, R.T., Zimmerman, L.J., Widgren, E.E. Dev. Biol. (1992) [Pubmed]
  5. Comparison of mouse and human NASP genes and expression in human transformed and tumor cell lines. Richardson, R.T., Bencic, D.C., O'Rand, M.G. Gene (2001) [Pubmed]
  6. Overexpression of the Linker histone-binding protein tNASP affects progression through the cell cycle. Alekseev, O.M., Bencic, D.C., Richardson, R.T., Widgren, E.E., O'Rand, M.G. J. Biol. Chem. (2003) [Pubmed]
  7. Histone-binding domains in a human nuclear autoantigenic sperm protein. Batova, I., O'Rand, M.G. Biol. Reprod. (1996) [Pubmed]
  8. Characterisation of an extracellular serine protease gene (nasp gene) from Dermatophilus congolensis. Garcia-Sanchez, A., Cerrato, R., Larrasa, J., Ambrose, N.C., Parra, A., Alonso, J.M., Hermoso-de-Mendoza, M., Rey, J.M., Mine, M.O., Carnegie, P.R., Ellis, T.M., Masters, A.M., Pemberton, A.D., Hermoso-de-Mendoza, J. FEMS Microbiol. Lett. (2004) [Pubmed]
  9. Conformational analyses by 1H NMR and computer simulations of cyclic hexapeptides related to somatostatin containing acidic and basic peptoid residues. Mattern, R.H., Tran, T.A., Goodman, M. J. Pept. Res. (1999) [Pubmed]
  10. Gene signatures of testicular seminoma with emphasis on expression of ets variant gene 4. Gashaw, I., Grümmer, R., Klein-Hitpass, L., Dushaj, O., Bergmann, M., Brehm, R., Grobholz, R., Kliesch, S., Neuvians, T.P., Schmid, K.W., von Ostau, C., Winterhager, E. Cell. Mol. Life Sci. (2005) [Pubmed]
  11. Analysis of the autoimmune epitopes on human testicular NASP using recombinant and synthetic peptides. Batova, I.N., Richardson, R.T., Widgren, E.E., O'Rand, M.G. Clin. Exp. Immunol. (2000) [Pubmed]
  12. Screening of an Antigen Target for Immunocontraceptives from Cross-Reactive Antigens between Human Sperm and Ureaplasma urealyticum. Shi, J., Yang, Z., Wang, M., Cheng, G., Li, D., Wang, Y., Zhou, Y., Liu, X., Xu, C. Infect. Immun. (2007) [Pubmed]
  13. Characterization of a sperm-specific nuclear autoantigenic protein. II. Expression and localization in the testis. Welch, J.E., O'Rand, M.G. Biol. Reprod. (1990) [Pubmed]
WikiGenes - Universities