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Gene Review

HMGN1  -  high mobility group nucleosome binding...

Homo sapiens

Synonyms: FLJ27265, FLJ31471, HMG14, High mobility group nucleosome-binding domain-containing protein 1, MGC104230, ...
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Disease relevance of HMGN1


High impact information on HMGN1


Chemical compound and disease context of HMGN1

  • HMG 14 and 17, but not HMB 1 and 2, were phosphorylated in the nuclei of all cell lines with a serine being the site of modification for both proteins in Ehrlich ascites cells [10].

Biological context of HMGN1


Anatomical context of HMGN1

  • To examine the posttranslational modifications of HMG-14 and -17 in vivo, HMG proteins were prepared from nuclear vs. cytosolic fractions of human K562 cells treated with 12-O-tetradecanoylphorbol 13-acetate (TPA) or okadaic acid (OA) and examined by electrospray mass spectrometry [14].
  • Transformed Hmgn1-/- fibroblasts grow in soft agar and produce tumors in nude mice with a significantly higher efficiency than Hmgn1+/+ fibroblasts, suggesting that loss of HMGN1 protein disrupts cellular events controlling proliferation and growth [5].
  • Using human-rodent somatic cell hybrids, the HMG-14 gene was localized to human chromosome 21 [15].
  • Revertant colonies, which lost the ability to express human HMG-14, regained the ability to differentiate into myotubes [3].
  • Recently, it was suggested that subgroups of HMG-14, HMG-14a and 14b, but not HMG-17, were phosphorylated in situ in HeLa cells [16].

Associations of HMGN1 with chemical compounds

  • To our knowledge, this is the first demonstration that each of the three serine residues in the acidic C-terminal region of human HMGN1 can be phosphorylated [1].
  • Induction of human HMG-14 expression by dexamethasone inhibited the myogenic process [3].
  • However, even in this 30-residue long peptide there are significant differences between the proteins as the proline content of HMG-17 (8 residues) is twice that of HMG-14 [17].
  • Chromosomal proteins HMG-14 and HMG-17. Distinct multigene families coding for similar types of transcripts [17].
  • Subsequent perchloric acid extraction of the nuclei, followed by selective acetone precipitation, CM-Sephadex ion exchange chromatography, and gel filtration yielded radioactively labeled high mobility group (HMG) proteins HMG-14 and HMG-17 in pure form [18].

Physical interactions of HMGN1

  • Third, by comparing the full-length protein with different domains, we demonstrate that the acidic carboxyl-terminal domain is absolutely required for nucleosome spacing, neither the nucleosome binding domain of HMG 14 or HMG 17 nor the amino-terminal domain plus the nucleosome binding domain of HMG 14 could space nucleosomes [19].

Enzymatic interactions of HMGN1

  • In order to definitively determine whether HMG-17 is indeed phosphorylated or whether the protein previously identified as [32P]HMG-17 was a subgroup of HMG-14, we have used the technique of electroblotting in conjunction with an immunochemical procedure utilizing anti-HMG-17 IgG [16].
  • Surprisingly, in the course of these studies we found that in vivo radiolabeling experiments revealed that only two minor HMG-14 subspecies (and/or possibly a minor HMG-I subspecies) are phosphorylated whereas HMG-1, -2, -17, and the major HMG-14 are not heavily phosphorylated [20].
  • In vitro only casein kinase II specifically catalyzed phosphorylation of hHMG 14 alpha 1 and alpha 2 among a mixture of hHMG proteins; phosphorylation occurred at the site which was phosphorylated in vivo [21].

Other interactions of HMGN1

  • The pattern of tissue-specific expression differs considerably from those of HMGN1 and HMGN2 at both the mRNA and the protein level [22].
  • To examine the function of ZNF219 in the modulation of transcription, we constructed Gal4 DNA binding domain (DBD)/ZNF219 fusion proteins and demonstrated that ZNF219 functioned as a transcriptional repressor for the HMGN1 promoter [13].
  • The in vitro reconstitution of nucleosome and its binding patterns with HMG1/2 and HMG14/17 proteins [23].
  • Here we show that the histone acetyltransferase p300 specifically acetylates HMG-14, a nonhistone structural protein that binds to nucleosomes and reduces the compactness of the chromatin fiber [24].
  • Strikingly, transcriptional and structural activities of HMG-14 are maintained upon replacement of the C-terminal fragment by acidic regions from either GAL4 or HMG-2 [4].

Analytical, diagnostic and therapeutic context of HMGN1


  1. Identification of novel in vivo phosphorylation sites in high mobility group N1 protein from the MCF-7 human breast cancer cells. Zou, Y., Jiang, X., Wang, Y. Biochemistry (2004) [Pubmed]
  2. Chromosomal protein HMG-14 gene maps to the Down syndrome region of human chromosome 21 and is overexpressed in mouse trisomy 16. Pash, J., Popescu, N., Matocha, M., Rapoport, S., Bustin, M. Proc. Natl. Acad. Sci. U.S.A. (1990) [Pubmed]
  3. Aberrant expression of high mobility group chromosomal protein 14 affects cellular differentiation. Pash, J.M., Alfonso, P.J., Bustin, M. J. Biol. Chem. (1993) [Pubmed]
  4. Alleviation of histone H1-mediated transcriptional repression and chromatin compaction by the acidic activation region in chromosomal protein HMG-14. Ding, H.F., Bustin, M., Hansen, U. Mol. Cell. Biol. (1997) [Pubmed]
  5. Increased tumorigenicity and sensitivity to ionizing radiation upon loss of chromosomal protein HMGN1. Birger, Y., Catez, F., Furusawa, T., Lim, J.H., Prymakowska-Bosak, M., West, K.L., Postnikov, Y.V., Haines, D.C., Bustin, M. Cancer Res. (2005) [Pubmed]
  6. Stimulation of RNA polymerase II elongation by chromosomal protein HMG-14. Ding, H.F., Rimsky, S., Batson, S.C., Bustin, M., Hansen, U. Science (1994) [Pubmed]
  7. Chromatin unfolding and activation by HMGN(*) chromosomal proteins. Bustin, M. Trends Biochem. Sci. (2001) [Pubmed]
  8. MSK2 and MSK1 mediate the mitogen- and stress-induced phosphorylation of histone H3 and HMG-14. Soloaga, A., Thomson, S., Wiggin, G.R., Rampersaud, N., Dyson, M.H., Hazzalin, C.A., Mahadevan, L.C., Arthur, J.S. EMBO J. (2003) [Pubmed]
  9. Chromosomal proteins HMG-14 and HMG-17 are released from mitotic chromosomes and imported into the nucleus by active transport. Hock, R., Scheer, U., Bustin, M. J. Cell Biol. (1998) [Pubmed]
  10. The phosphorylation of high mobility group proteins 14 and 17 and their distribution in chromatin. Saffer, J.D., Glazer, R.I. J. Biol. Chem. (1982) [Pubmed]
  11. Mitotic phosphorylation of chromosomal protein HMGN1 inhibits nuclear import and promotes interaction with 14.3.3 proteins. Prymakowska-Bosak, M., Hock, R., Catez, F., Lim, J.H., Birger, Y., Shirakawa, H., Lee, K., Bustin, M. Mol. Cell. Biol. (2002) [Pubmed]
  12. Effects of HMGN1 on chromatin structure and SWI/SNF-mediated chromatin remodeling. Hill, D.A., Peterson, C.L., Imbalzano, A.N. J. Biol. Chem. (2005) [Pubmed]
  13. Identification of the DNA binding specificity of the human ZNF219 protein and its function as a transcriptional repressor. Sakai, T., Hino, K., Wada, S., Maeda, H. DNA Res. (2003) [Pubmed]
  14. Phosphorylation and subcellular redistribution of high mobility group proteins 14 and 17, analyzed by mass spectrometry. Louie, D.F., Gloor, K.K., Galasinski, S.C., Resing, K.A., Ahn, N.G. Protein Sci. (2000) [Pubmed]
  15. Chromosomal protein HMG-14. Identification, characterization, and chromosome localization of a functional gene from the large human multigene family. Landsman, D., McBride, O.W., Soares, N., Crippa, M.P., Srikantha, T., Bustin, M. J. Biol. Chem. (1989) [Pubmed]
  16. Evidence that high mobility group protein 17 is not phosphorylated in human colon carcinoma cells. Chapekar, M.S., Bustin, M., Glazer, R.I. Biochim. Biophys. Acta (1985) [Pubmed]
  17. Chromosomal proteins HMG-14 and HMG-17. Distinct multigene families coding for similar types of transcripts. Landsman, D., Bustin, M. J. Biol. Chem. (1986) [Pubmed]
  18. Studies of acetylation and deacetylation in high mobility group proteins. Identification of the sites of acetylation in high mobility group proteins 14 and 17. Sterner, R., Vidali, G., Allfrey, V.G. J. Biol. Chem. (1981) [Pubmed]
  19. High mobility group protein 14 and 17 can prevent the close packing of nucleosomes by increasing the strength of protein contacts in the linker DNA. Tremethick, D.J., Hyman, L. J. Biol. Chem. (1996) [Pubmed]
  20. Purification and postsynthetic modifications of Friend erythroleukemic cell high mobility group protein HMG-I. Elton, T.S., Reeves, R. Anal. Biochem. (1986) [Pubmed]
  21. Identity of the in vivo phosphorylation site in high mobility group 14 protein in HeLa cells with the site phosphorylated by casein kinase II in vitro. Walton, G.M., Gill, G.N. J. Biol. Chem. (1983) [Pubmed]
  22. HMGN3a and HMGN3b, two protein isoforms with a tissue-specific expression pattern, expand the cellular repertoire of nucleosome-binding proteins. West, K.L., Ito, Y., Birger, Y., Postnikov, Y., Shirakawa, H., Bustin, M. J. Biol. Chem. (2001) [Pubmed]
  23. The in vitro reconstitution of nucleosome and its binding patterns with HMG1/2 and HMG14/17 proteins. Zhang, S.B., Huang, J., Zhao, H., Zhang, Y., Hou, C.H., Cheng, X.D., Jiang, C., Li, M.Q., Hu, J., Qian, R.L. Cell Res. (2003) [Pubmed]
  24. Acetylation of novel sites in the nucleosomal binding domain of chromosomal protein HMG-14 by p300 alters its interaction with nucleosomes. Bergel, M., Herrera, J.E., Thatcher, B.J., Prymakowska-Bosak, M., Vassilev, A., Nakatani, Y., Martin, B., Bustin, M. J. Biol. Chem. (2000) [Pubmed]
  25. The cooperative binding of chromosomal protein HMG-14 to nucleosome cores is reduced by single point mutations in the nucleosomal binding domain. Postnikov, Y.V., Lehn, D.A., Robinson, R.C., Friedman, F.K., Shiloach, J., Bustin, M. Nucleic Acids Res. (1994) [Pubmed]
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