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Gene Review

HMGB2  -  high mobility group box 2

Homo sapiens

Synonyms: HMG-2, HMG2, High mobility group protein 2, High mobility group protein B2
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Disease relevance of HMGB2


High impact information on HMGB2

  • A GzmA-activated DNase (GAAD) is in an ER associated complex containing pp32 and the GzmA substrates SET, HMG-2, and Ape1 [6].
  • It shares homology with the mating-type protein, Mc, from the fission yeast Schizosaccharomyces pombe and a conserved DNA-binding motif present in the nuclear high-mobility-group proteins HMG1 and HMG2 [7].
  • Yeast Nsgs inhibit degradation of Hmg2p in a highly specific manner, by directly interacting with the sterol-sensing domain (SSD)-containing transmembrane region [8].
  • The C-terminal half of TFIIIB90 contains a high-mobility-group protein 2 (HMG2)-related domain and interacts strongly with TBP [9].
  • Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains [9].

Biological context of HMGB2

  • The phosphorylation sites have been mapped to the acidic C-terminal domains by analysis of tryptic peptides derived from HMGB1 and HMGB2/3 using nanospray ion trap mass spectrometry [10].
  • A detailed analysis of HMGB2 interaction with mitotic chromosomes indicated that two sites encompassing HMG-box A and B are responsible for binding [11].
  • The HMGB1 or HMGB2 expression plasmid, carrying the neo(r) gene as a selection marker, was introduced into HeLa S3 cells to obtain stably-transfected cells [12].
  • Involvement of HMGB1 and HMGB2 proteins in exogenous DNA integration reaction into the genome of HeLa S3 cells [12].
  • Here we have generated recombinant derivatives of the human high-mobility group (HMG) protein HMGB2 and investigated their potential as novel protein-based transfection reagents [1].

Anatomical context of HMGB2


Associations of HMGB2 with chemical compounds

  • HMG-1 and HMG-2 (HMG-1/-2) themselves do not bind to progesterone response elements, but in the presence of PR they were detected as part of an HMG-PR-DNA ternary complex [17].
  • RESULTS: Pauciarticular, but not polyarticular, JRA patient sera were found to recognize a lysine-rich major epitope (KKGKKKDP), which is located in the linker region of the HMG box domains of the HMG-2 nonhistone chromosomal protein [15].
  • We also observed that HMG2 will bind to DNA modified with carboplatin and iproplatin although to a lesser extent than to DNA damaged with CDDP [18].
  • Differential binding of HMG1, HMG2, and a single HMG box to cisplatin-damaged DNA [19].
  • Rice Hmg2 possibly has a housekeeping role involved in the sterol biosynthesis, among the possible roles of plant HMGR genes that have been suggested in other plants [Weissenborn et al. (1995)] [20].
  • HMGB2 knockdown by small interfering RNAs decreased cell proliferation, and overexpression of HMGB2 by expression vectors diminished cisplatin- and etoposide-induced cell death [21].

Physical interactions of HMGB2

  • HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A [13].
  • 2. There are 6.0 amino acids/nucleotide in HMG1-bound DNA and 5.0 in HMGI-bound DNA which suggests that each HMB1 moleculae would cover about 20 base pairs of DNA and each HMG2 molecule would cover about 25 base pairs [22].
  • With this procedure we found that both HMG1 and HMG2 interact with H2A X H2B and also with (H3 X H4)2 [23].

Regulatory relationships of HMGB2


Other interactions of HMGB2

  • HMG2, like SET and APE, is a physiologically relevant granzyme A substrate in targeted cells [13].
  • We examined the effect of the coactivator proteins, HMGB1 and HMGB2, in enhancing ER binding affinity to single and tandem EREs [27].
  • This effect was rescued by transient over-expression of HMGB1, and was partially complemented by HMGB2, but not with the HMGA1 protein [28].
  • A recent study has identified a protein complex bound to D4Z4 that contains YY1 and HMGB2, implicating a role for D4Z4 as a repressor [29].
  • 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 [30].

Analytical, diagnostic and therapeutic context of HMGB2

  • High mobility group protein 1 (HMGB1) quantified by ELISA with a monoclonal antibody that does not cross-react with HMGB2 [31].
  • Our results show that recombinant derivatives of human HMGB2 facilitate efficient nonviral gene delivery and may become useful reagents for applications in gene therapy [1].
  • METHODS: Seventy-seven pauciarticular-onset JRA serum samples from antinuclear antibody (ANA)-positive patients and 42 polyarticular-onset JRA patient sera found to react with HMG-2 by immunoblotting were used in this study [15].
  • CONCLUSIONS: HMG1 and HMG2 are significant target antigens of p-ANCA in AIH [2].
  • Recombinant HMG2-domain A, B, and (A + B) polypeptides were similarly, but non-identically, effective for the stimulation of DSB ligation reaction [32].


  1. Recombinant derivatives of the human high-mobility group protein HMGB2 mediate efficient nonviral gene delivery. Sloots, A., Wels, W.S. FEBS J. (2005) [Pubmed]
  2. High mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2 are significant target antigens of perinuclear anti-neutrophil cytoplasmic antibodies in autoimmune hepatitis. Sobajima, J., Ozaki, S., Uesugi, H., Osakada, F., Inoue, M., Fukuda, Y., Shirakawa, H., Yoshida, M., Rokuhara, A., Imai, H., Kiyosawa, K., Nakao, K. Gut (1999) [Pubmed]
  3. A fragment of the HMGN2 protein homes to the nuclei of tumor cells and tumor endothelial cells in vivo. Porkka, K., Laakkonen, P., Hoffman, J.A., Bernasconi, M., Ruoslahti, E. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  4. Transcription factor Y-box binding protein 1 binds preferentially to cisplatin-modified DNA and interacts with proliferating cell nuclear antigen. Ise, T., Nagatani, G., Imamura, T., Kato, K., Takano, H., Nomoto, M., Izumi, H., Ohmori, H., Okamoto, T., Ohga, T., Uchiumi, T., Kuwano, M., Kohno, K. Cancer Res. (1999) [Pubmed]
  5. Prevalence and characterization of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) directed against HMG1 and HMG2 in ulcerative colitis (UC). Sobajima, J., Ozaki, S., Uesugi, H., Osakada, F., Shirakawa, H., Yoshida, M., Nakao, K. Clin. Exp. Immunol. (1998) [Pubmed]
  6. Tumor suppressor NM23-H1 is a granzyme A-activated DNase during CTL-mediated apoptosis, and the nucleosome assembly protein SET is its inhibitor. Fan, Z., Beresford, P.J., Oh, D.Y., Zhang, D., Lieberman, J. Cell (2003) [Pubmed]
  7. A gene from the human sex-determining region encodes a protein with homology to a conserved DNA-binding motif. Sinclair, A.H., Berta, P., Palmer, M.S., Hawkins, J.R., Griffiths, B.L., Smith, M.J., Foster, J.W., Frischauf, A.M., Lovell-Badge, R., Goodfellow, P.N. Nature (1990) [Pubmed]
  8. INSIG: a broadly conserved transmembrane chaperone for sterol-sensing domain proteins. Flury, I., Garza, R., Shearer, A., Rosen, J., Cronin, S., Hampton, R.Y. EMBO J. (2005) [Pubmed]
  9. Structure and function of a human transcription factor TFIIIB subunit that is evolutionarily conserved and contains both TFIIB- and high-mobility-group protein 2-related domains. Wang, Z., Roeder, R.G. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
  10. Protein kinase CK2 differentially phosphorylates maize chromosomal high mobility group B (HMGB) proteins modulating their stability and DNA interactions. Stemmer, C., Schwander, A., Bauw, G., Fojan, P., Grasser, K.D. J. Biol. Chem. (2002) [Pubmed]
  11. Association of chromatin proteins high mobility group box (HMGB) 1 and HMGB2 with mitotic chromosomes. Pallier, C., Scaffidi, P., Chopineau-Proust, S., Agresti, A., Nordmann, P., Bianchi, M.E., Marechal, V. Mol. Biol. Cell (2003) [Pubmed]
  12. Involvement of HMGB1 and HMGB2 proteins in exogenous DNA integration reaction into the genome of HeLa S3 cells. Ueda, T., Shirakawa, H., Yoshida, M. Biochim. Biophys. Acta (2002) [Pubmed]
  13. HMG2 interacts with the nucleosome assembly protein SET and is a target of the cytotoxic T-lymphocyte protease granzyme A. Fan, Z., Beresford, P.J., Zhang, D., Lieberman, J. Mol. Cell. Biol. (2002) [Pubmed]
  14. Structure of a gene coding for human HMG2 protein. Shirakawa, H., Yoshida, M. J. Biol. Chem. (1992) [Pubmed]
  15. Antibodies against a peptide sequence located in the linker region of the HMG-1/2 box domains in sera from patients with juvenile rheumatoid arthritis. Jung, F., Neuer, G., Bautz, F.A. Arthritis Rheum. (1997) [Pubmed]
  16. Genome scans and gene expression microarrays converge to identify gene regulatory loci relevant in schizophrenia. Vawter, M.P., Atz, M.E., Rollins, B.L., Cooper-Casey, K.M., Shao, L., Byerley, W.F. Hum. Genet. (2006) [Pubmed]
  17. High-mobility group chromatin proteins 1 and 2 functionally interact with steroid hormone receptors to enhance their DNA binding in vitro and transcriptional activity in mammalian cells. Boonyaratanakornkit, V., Melvin, V., Prendergast, P., Altmann, M., Ronfani, L., Bianchi, M.E., Taraseviciene, L., Nordeen, S.K., Allegretto, E.A., Edwards, D.P. Mol. Cell. Biol. (1998) [Pubmed]
  18. Characterization of high mobility group protein binding to cisplatin-damaged DNA. Billings, P.C., Davis, R.J., Engelsberg, B.N., Skov, K.A., Hughes, E.N. Biochem. Biophys. Res. Commun. (1992) [Pubmed]
  19. Differential binding of HMG1, HMG2, and a single HMG box to cisplatin-damaged DNA. Farid, R.S., Bianchi, M.E., Falciola, L., Engelsberg, B.N., Billings, P.C. Toxicol. Appl. Pharmacol. (1996) [Pubmed]
  20. Molecular characterization of Hmg2 gene encoding a 3-hydroxy-methylglutaryl-CoA reductase in rice. Ha, S.H., Lee, S.W., Kim, Y.M., Hwang, Y.S. Mol. Cells (2001) [Pubmed]
  21. Overexpression of high-mobility group box 2 is associated with tumor aggressiveness and prognosis of hepatocellular carcinoma. Kwon, J.H., Kim, J., Park, J.Y., Hong, S.M., Park, C.W., Hong, S.J., Park, S.Y., Choi, Y.J., Do, I.G., Joh, J.W., Kim, D.S., Choi, K.Y. Clin. Cancer Res. (2010) [Pubmed]
  22. Interaction of non-histone chromosomal proteins HMG1 and HMG2 with DNA. Yu, S.S., Li, H.J., Goodwin, G.H., Johns, E.W. Eur. J. Biochem. (1977) [Pubmed]
  23. Identification of the core-histone-binding domains of HMG1 and HMG2. Bernués, J., Espel, E., Querol, E. Biochim. Biophys. Acta (1986) [Pubmed]
  24. HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter. Stros, M., Ozaki, T., Bacikova, A., Kageyama, H., Nakagawara, A. J. Biol. Chem. (2002) [Pubmed]
  25. High-mobility group protein 2 may be involved in the locus control region regulation of the beta-globin gene cluster. Lv, X., Xu, D.D., Liu, D.P., Li, L., Hao, D.L., Liang, C.C. Biochem. Cell Biol. (2002) [Pubmed]
  26. Abundance of mRNAs encoding HMG1/HMG2 class high-mobility-group DNA-binding proteins are differentially regulated in cotyledons of Pharbitis nil. O'Neill, S.D., Zheng, C.C. Plant Mol. Biol. (1998) [Pubmed]
  27. High mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity. Das, D., Peterson, R.C., Scovell, W.M. Mol. Endocrinol. (2004) [Pubmed]
  28. The DNA-bending protein HMGB1 is a cellular cofactor of Sleeping Beauty transposition. Zayed, H., Izsvák, Z., Khare, D., Heinemann, U., Ivics, Z. Nucleic Acids Res. (2003) [Pubmed]
  29. Genomic analysis of facioscapulohumeral muscular dystrophy. Clapp, J., Bolland, D.J., Hewitt, J.E. Briefings in functional genomics & proteomics. (2003) [Pubmed]
  30. 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]
  31. High mobility group protein 1 (HMGB1) quantified by ELISA with a monoclonal antibody that does not cross-react with HMGB2. Yamada, S., Inoue, K., Yakabe, K., Imaizumi, H., Maruyama, I. Clin. Chem. (2003) [Pubmed]
  32. Non-histone chromosomal proteins HMG1 and 2 enhance ligation reaction of DNA double-strand breaks. Nagaki, S., Yamamoto, M., Yumoto, Y., Shirakawa, H., Yoshida, M., Teraoka, H. Biochem. Biophys. Res. Commun. (1998) [Pubmed]
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