Nuclear autoantigenic sperm protein is a protein that in humans is encoded by the NASPgene.[1][2] Multiple isoforms are encoded by transcript variants of this gene.
Function
This gene encodes a histone H1 binding protein that is involved in transporting histones into the nucleus of dividing cells.[3] The somatic form is expressed in all mitotic cells, is localized to the nucleus, and is coupled to the cell cycle. The testicular form is expressed in embryonic tissues, tumor cells, and the testis. In male germ cells, this protein is localized to the cytoplasm of primary spermatocytes, the nucleus of spermatids, and the periacrosomal region of mature spermatozoa.[2]
References
↑O'Rand MG, Richardson RT, Zimmerman LJ, Widgren EE (Dec 1992). "Sequence and localization of human NASP: conservation of a Xenopus histone-binding protein". Dev Biol. 154 (1): 37–44. doi:10.1016/0012-1606(92)90045-I. PMID1426632.
↑Alekseev OM, Widgren EE, Richardson RT, O'Rand MG (January 2005). "Association of NASP with HSP90 in mouse spermatogenic cells: stimulation of ATPase activity and transport of linker histones into nuclei". J. Biol. Chem. 280 (4): 2904–11. doi:10.1074/jbc.M410397200. PMID15533935.
Further reading
Welch JE, Zimmerman LJ, Joseph DR, O'Rand MG (1991). "Characterization of a sperm-specific nuclear autoantigenic protein. I. Complete sequence and homology with the Xenopus protein, N1/N2". Biol. Reprod. 43 (4): 559–68. doi:10.1095/biolreprod43.4.559. PMID2289010.
Welch JE, O'Rand MG (1991). "Characterization of a sperm-specific nuclear autoantigenic protein. II. Expression and localization in the testis". Biol. Reprod. 43 (4): 569–78. doi:10.1095/biolreprod43.4.569. PMID2289011.
Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID8125298.
Lee YH, O'Rand MG (1993). "Ultrastructural localization of a nuclear autoantigenic sperm protein in spermatogenic cells and spermatozoa". Anat. Rec. 236 (3): 442–8. doi:10.1002/ar.1092360304. PMID8363049.
Batova I, O'Rand MG (1996). "Histone-binding domains in a human nuclear autoantigenic sperm protein". Biol. Reprod. 54 (6): 1238–44. doi:10.1095/biolreprod54.6.1238. PMID8724350.
Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID9373149.
Richardson RT, Batova IN, Widgren EE, et al. (2000). "Characterization of the histone H1-binding protein, NASP, as a cell cycle-regulated somatic protein". J. Biol. Chem. 275 (39): 30378–86. doi:10.1074/jbc.M003781200. PMID10893414.
Minami N, Sasaki K, Aizawa A, et al. (2001). "Analysis of gene expression in mouse 2-cell embryos using fluorescein differential display: comparison of culture environments". Biol. Reprod. 64 (1): 30–5. doi:10.1095/biolreprod64.1.30. PMID11133655.
Richardson RT, Bencic DC, O'Rand MG (2001). "Comparison of mouse and human NASP genes and expression in human transformed and tumor cell lines". Gene. 274 (1–2): 67–75. doi:10.1016/S0378-1119(01)00605-9. PMID11674998.
Alekseev OM, Bencic DC, Richardson RT, et al. (2003). "Overexpression of the Linker histone-binding protein tNASP affects progression through the cell cycle". J. Biol. Chem. 278 (10): 8846–52. doi:10.1074/jbc.M210352200. PMID12509435.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.
Groth A, Ray-Gallet D, Quivy JP, et al. (2005). "Human Asf1 regulates the flow of S phase histones during replicational stress". Mol. Cell. 17 (2): 301–11. doi:10.1016/j.molcel.2004.12.018. PMID15664198.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.
