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Gene Review

NAP1L1  -  nucleosome assembly protein 1-like 1

Homo sapiens

Synonyms: MGC23410, MGC8688, NAP-1-related protein, NAP1, NAP1L, ...
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Disease relevance of NAP1L1

  • CONCLUSIONS: These data demonstrate that malignant APCs and goblet cell adenocarcinoids have elevated expression of NAP1L1, MAGE-D2, and MTA1 compared with appendiceal carcinoids identified at surgery for appendicitis [1].
  • When expressed as a fusion protein in Escherichia coli, hNRP reacted specifically with a monoclonal antibody raised against human NAP-I [2].
  • By QRT-PCR, NAP1L1 was significantly (P < .03) overexpressed in SIC compared with colorectal carcinomas and healthy tissue [3].
  • NRP/B expression was upregulated during the differentiation of murine Neuro 2A and human SH-SY5Y neuroblastoma cells [4].

High impact information on NAP1L1

  • Glycerol gradient sedimentation and immunoprecipitation assays demonstrate that the acetylation of histones by p300 facilitates the transfer of H2A-H2B from nucleosomes to NAP-1 [5].
  • We have used a purified recombinant chromatin assembly system, including ACF (Acf-1 + ISWI) and NAP-1, to examine the role of histone acetylation in ATP-dependent chromatin remodeling [5].
  • NAP-1-IgG did not compete with 125I-NAP-1 for binding to neutrophils, which suggests that IgG anti-NAP-1 is a molecular trap that prevents binding of NAP-1 to neutrophils after it diffuses from production sites into the circulation [6].
  • However, at pH 2.0 in 9 M urea approximately 15% of the total NAP-1 could be dissociated from the complex [6].
  • We have discovered a novel nuclear matrix protein, NRP/B (nuclear restricted protein/brain), which contains two major structural elements: a BTB domain-like structure in the predicted NH2 terminus, and a "kelch motif" in the predicted COOH-terminal domain [4].

Chemical compound and disease context of NAP1L1

  • Both in vivo and in vitro experiments demonstrate that NRP/B can be phosphorylated and can bind to the functionally active hypophosphorylated form of the p110(RB) during neuronal differentiation of SH-SY5Y neuroblastoma cells induced by retinoic acid [4].

Biological context of NAP1L1

  • Formation of NAP-1-p300 complexes was found to increase during S phase, suggesting a potential role for p300 in chromatin assembly [7].
  • Interacting proteins and differences in nuclear transport reveal specific functions for the NAP1 family proteins in plants [8].
  • Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation [2].
  • The deduced amino acid sequence for this newly identified cDNA, designated hNRP (human NAP-related protein), contains a potential seven-residue nuclear localization motif, three clusters of highly acidic residues and other structural features found in various proteins implicated in chromatin formation [2].
  • These results demonstrate a correlation between induction of hNRP expression and mitogenesis and taken together with the structural similarities between hNRP and yeast NAP-I suggest that the hNRP gene product participates in DNA replication and thereby plays an important role in the process of cell proliferation [2].

Anatomical context of NAP1L1

  • NAP1L1 was elevated (> 10-fold, P < 0.03) in both malignant and goblet cell adenocarcinoids compared with normal and incidental lesions (P < 0.006) [1].
  • Here we report that CENP-A, highly purified from HeLa cells, can indeed replace histone H3 in a nucleosome reconstitution system mediated by nucleosome assembly protein-1 (NAP-1) [9].
  • Moreover, levels of both hNRP mRNA and protein increased rapidly in cultured T-lymphocytes induced to proliferate by incubation with phorbol ester and ionomycin [2].
  • The hNRP transcript was detected in all tissues and cell lines studied, but levels were somewhat increased in rapidly proliferating cells [2].
  • Neutrophil attractant protein-1-immunoglobulin G immune complexes and free anti-NAP-1 antibody in normal human serum [6].

Associations of NAP1L1 with chemical compounds

  • CONCLUSIONS: SICs overexpress the neoplasia-related genes NAP1L1 (mitotic regulation), MAGE-D2 (adhesion), and MTA1 (estrogen antagonism) [3].
  • In this study, the potential of COM domains was exploited in vivo by establishing a system for the true biocombinatorial synthesis of lipopeptides via directed reprogramming of a natural NRP biosynthetic assembly line (i.e., surfactin) [10].
  • Neutrophil attractant/activation protein-1 (NAP-1) causes human basophil histamine release [11].
  • NR was estimated by active posterior rhinometry at both a 0.5 L/s flow (NRF) and a 1 cm H2O pressure (NRP), under four conditions: in the basal state, with Respir+, with Nozovent, and after treatment with Pernazène [12].

Other interactions of NAP1L1

  • These observations underscore the importance of a high affinity between H2A-H2B and NAP-1 for ordered transfer of core histones onto DNA [13].
  • In the assembly reaction with a supercoiled template, ACF need not be added simultaneously with NAP-1 [13].
  • Among a small set of proteins that bind specifically to VP22, we identified TAF-I (template-activating factor I), a chromatin remodelling protein and close homologue of the histone chaperone protein NAP-1 [14].

Analytical, diagnostic and therapeutic context of NAP1L1


  1. Genetic differentiation of appendiceal tumor malignancy: a guide for the perplexed. Modlin, I.M., Kidd, M., Latich, I., Zikusoka, M.N., Eick, G.N., Mane, S.M., Camp, R.L. Ann. Surg. (2006) [Pubmed]
  2. Molecular characterization of hNRP, a cDNA encoding a human nucleosome-assembly-protein-I-related gene product involved in the induction of cell proliferation. Simon, H.U., Mills, G.B., Kozlowski, M., Hogg, D., Branch, D., Ishimi, Y., Siminovitch, K.A. Biochem. J. (1994) [Pubmed]
  3. The role of genetic markers--NAP1L1, MAGE-D2, and MTA1--in defining small-intestinal carcinoid neoplasia. Kidd, M., Modlin, I.M., Mane, S.M., Camp, R.L., Eick, G., Latich, I. Ann. Surg. Oncol. (2006) [Pubmed]
  4. NRP/B, a novel nuclear matrix protein, associates with p110(RB) and is involved in neuronal differentiation. Kim, T.A., Lim, J., Ota, S., Raja, S., Rogers, R., Rivnay, B., Avraham, H., Avraham, S. J. Cell Biol. (1998) [Pubmed]
  5. p300-mediated acetylation facilitates the transfer of histone H2A-H2B dimers from nucleosomes to a histone chaperone. Ito, T., Ikehara, T., Nakagawa, T., Kraus, W.L., Muramatsu, M. Genes Dev. (2000) [Pubmed]
  6. Neutrophil attractant protein-1-immunoglobulin G immune complexes and free anti-NAP-1 antibody in normal human serum. Sylvester, I., Yoshimura, T., Sticherling, M., Schröder, J.M., Ceska, M., Peichl, P., Leonard, E.J. J. Clin. Invest. (1992) [Pubmed]
  7. Dual roles of p300 in chromatin assembly and transcriptional activation in cooperation with nucleosome assembly protein 1 in vitro. Asahara, H., Tartare-Deckert, S., Nakagawa, T., Ikehara, T., Hirose, F., Hunter, T., Ito, T., Montminy, M. Mol. Cell. Biol. (2002) [Pubmed]
  8. Interacting proteins and differences in nuclear transport reveal specific functions for the NAP1 family proteins in plants. Dong, A., Liu, Z., Zhu, Y., Yu, F., Li, Z., Cao, K., Shen, W.H. Plant Physiol. (2005) [Pubmed]
  9. Human centromere protein A (CENP-A) can replace histone H3 in nucleosome reconstitution in vitro. Yoda, K., Ando, S., Morishita, S., Houmura, K., Hashimoto, K., Takeyasu, K., Okazaki, T. Proc. Natl. Acad. Sci. U.S.A. (2000) [Pubmed]
  10. In vivo biocombinatorial synthesis of lipopeptides by COM domain-mediated reprogramming of the surfactin biosynthetic complex. Chiocchini, C., Linne, U., Stachelhaus, T. Chem. Biol. (2006) [Pubmed]
  11. Neutrophil attractant/activation protein-1 (NAP-1) causes human basophil histamine release. White, M.V., Yoshimura, T., Hook, W., Kaliner, M.A., Leonard, E.J. Immunol. Lett. (1989) [Pubmed]
  12. Effects of different mechanical treatments on nasal resistance assessed by rhinometry. Lorino, A.M., Lofaso, F., Drogou, I., Abi-Nader, F., Dahan, E., Coste, A., Lorino, H. Chest (1998) [Pubmed]
  13. Multistep chromatin assembly on supercoiled plasmid DNA by nucleosome assembly protein-1 and ATP-utilizing chromatin assembly and remodeling factor. Nakagawa, T., Bulger, M., Muramatsu, M., Ito, T. J. Biol. Chem. (2001) [Pubmed]
  14. Herpes simplex virus type 1 tegument protein VP22 interacts with TAF-I proteins and inhibits nucleosome assembly but not regulation of histone acetylation by INHAT. van Leeuwen, H., Okuwaki, M., Hong, R., Chakravarti, D., Nagata, K., O'Hare, P. J. Gen. Virol. (2003) [Pubmed]
  15. Molecular cloning and functional characterization of a cDNA encoding nucleosome assembly protein 1 (NAP-1) from soybean. Yoon, H.W., Kim, M.C., Lee, S.Y., Hwang, I., Bahk, J.D., Hong, J.C., Ishimi, Y., Cho, M.J. Mol. Gen. Genet. (1995) [Pubmed]
  16. NAP1 modulates binding of linker histone H1 to chromatin and induces an extended chromatin fiber conformation. Kepert, J.F., Mazurkiewicz, J., Heuvelman, G.L., Tóth, K.F., Rippe, K. J. Biol. Chem. (2005) [Pubmed]
  17. Leukocyte specificity and binding of human neutrophil attractant/activation protein-1. Leonard, E.J., Skeel, A., Yoshimura, T., Noer, K., Kutvirt, S., Van Epps, D. J. Immunol. (1990) [Pubmed]
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