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Gene Review

PA2G4  -  proliferation-associated 2G4, 38kDa

Homo sapiens

Synonyms: Cell cycle protein p38-2G4 homolog, EBP1, ErbB3-binding protein 1, HG4-1, Proliferation-associated protein 2G4, ...
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Disease relevance of PA2G4


High impact information on PA2G4

  • EBP1 regulates organ size through cell growth and proliferation in plants [4].
  • EBP1 is required for expression of cell cycle genes; CyclinD3;1, ribonucleotide reductase 2 and the cyclin-dependent kinase B1;1 [4].
  • We argue that EBP1 is a conserved, dose-dependent regulator of cell growth that is connected to meristematic competence and cell proliferation via regulation of RBR1 level [4].
  • The regulation of these genes by EBP1 is dose and auxin dependent and might rely on the effect of EBP1 to reduce RBR1 protein level [4].
  • Plant EBP1 levels are tightly regulated; gene expression is highest in developing organs and correlates with genes involved in ribosome biogenesis and function [4].

Biological context of PA2G4


Anatomical context of PA2G4

  • Ectopic expression of ebp1, a member of the PA2G4 family, inhibits the proliferation and induces the differentiation of human breast and prostate cancer cell lines [6].
  • These results strongly suggest that PA2G4 may have an important role on the regulation of DNA replication in eukaryotic cells [8].
  • Here, we show that Ebp1 possesses two different isoforms, p48 and p42, which differentially mediate PC12 cell survival and differentiation [9].
  • Here, we report cloning and characterizing of a novel mitogen-inducible gene from murine macrophages that predicts a cell cycle-specifically modulated nuclear protein of 38 kDa, designated p38-2G4. p38-2G4 displayed a speckled pattern of varying fluorescence intensity confined to the nucleus, but sparing the nucleoli [10].
  • Ebp1 was localized to both the nucleus and the cytoplasm of logarithmically growing AU565 breast cancer cells and HeLa cells as determined by confocal immunofluorescent microscopy [11].

Associations of PA2G4 with chemical compounds

  • Ebp1 expression was reduced in cells that had become androgen-independent [1].
  • EBP1 protein is stabilised by auxin [4].
  • The presence of bases which exhibit increased rates of dimethyl sulfate-induced methylation in the presence of EBP1 indicate that interaction of EBP1 with its recognition site is accompanied by distortion of the DNA double helix [3].
  • Supporting this conclusion is the observation that the polyamine spermidine dramatically increases EBP1 binding to its cognate site on the DNA [3].
  • The TH-induced up-regulation of RcC/EBP-1 mRNAs precedes the up-regulation of liver-specific urea cycle enzyme mRNAs by 6 to 12 hours [12].

Physical interactions of PA2G4


Regulatory relationships of PA2G4


Other interactions of PA2G4


Analytical, diagnostic and therapeutic context of PA2G4


  1. The ErbB3-binding protein Ebp1 suppresses androgen receptor-mediated gene transcription and tumorigenesis of prostate cancer cells. Zhang, Y., Wang, X.W., Jelovac, D., Nakanishi, T., Yu, M.H., Akinmade, D., Goloubeva, O., Ross, D.D., Brodie, A., Hamburger, A.W. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  2. Quantitative profiling of drug-associated proteomic alterations by combined 2-nitrobenzenesulfenyl chloride (NBS) isotope labeling and 2DE/MS identification. Ou, K., Kesuma, D., Ganesan, K., Yu, K., Soon, S.Y., Lee, S.Y., Goh, X.P., Hooi, M., Chen, W., Jikuya, H., Ichikawa, T., Kuyama, H., Matsuo, E., Nishimura, O., Tan, P. J. Proteome Res. (2006) [Pubmed]
  3. Interaction of enhancer-binding protein EBP1 (NF-kappa B) with the human immunodeficiency virus type 1 enhancer. Clark, L., Matthews, J.R., Hay, R.T. J. Virol. (1990) [Pubmed]
  4. EBP1 regulates organ size through cell growth and proliferation in plants. Horv??th, B.M., Magyar, Z., Zhang, Y., Hamburger, A.W., Bak??, L., Visser, R.G., Bachem, C.W., B??gre, L. EMBO J. (2006) [Pubmed]
  5. Molecular cloning and mapping of a human cDNA (PA2G4) that encodes a protein highly homologous to the mouse cell cycle protein p38-2G4. Lamartine, J., Seri, M., Cinti, R., Heitzmann, F., Creaven, M., Radomski, N., Jost, E., Lenoir, G.M., Romeo, G., Sylla, B.S. Cytogenet. Cell Genet. (1997) [Pubmed]
  6. The ErbB3 binding protein Ebp1 interacts with Sin3A to repress E2F1 and AR-mediated transcription. Zhang, Y., Akinmade, D., Hamburger, A.W. Nucleic Acids Res. (2005) [Pubmed]
  7. Specificity and heregulin regulation of Ebp1 (ErbB3 binding protein 1) mediated repression of androgen receptor signalling. Zhang, Y., Hamburger, A.W. Br. J. Cancer (2005) [Pubmed]
  8. Regulation of eukaryotic DNA replication by proliferation associated protein, PA2G4, in vitro. Izuta, S., Kitahara, M., Hamaguchi, T. Nucleic acids symposium series (2004) (2004) [Pubmed]
  9. Ebp1 isoforms distinctively regulate cell survival and differentiation. Liu, Z., Ahn, J.Y., Liu, X., Ye, K. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  10. Molecular cloning of a murine cDNA encoding a novel protein, p38-2G4, which varies with the cell cycle. Radomski, N., Jost, E. Exp. Cell Res. (1995) [Pubmed]
  11. Ebp1, an ErbB-3 binding protein, interacts with Rb and affects Rb transcriptional regulation. Xia, X., Cheng, A., Lessor, T., Zhang, Y., Hamburger, A.W. J. Cell. Physiol. (2001) [Pubmed]
  12. Characterization and expression of C/EPB-like genes in the liver of Rana catesbeiana tadpoles during spontaneous and thyroid hormone-induced metamorphosis. Chen, Y., Hu, H., Atkinson, B.G. Dev. Genet. (1994) [Pubmed]
  13. Interaction of the PA2G4 (EBP1) protein with ErbB-3 and regulation of this binding by heregulin. Yoo, J.Y., Wang, X.W., Rishi, A.K., Lessor, T., Xia, X.M., Gustafson, T.A., Hamburger, A.W. Br. J. Cancer (2000) [Pubmed]
  14. Repression of E2F1-mediated transcription by the ErbB3 binding protein Ebp1 involves histone deacetylases. Zhang, Y., Woodford, N., Xia, X., Hamburger, A.W. Nucleic Acids Res. (2003) [Pubmed]
  15. Ectopic expression of the ErbB-3 binding protein ebp1 inhibits growth and induces differentiation of human breast cancer cell lines. Lessor, T.J., Yoo, J.Y., Xia, X., Woodford, N., Hamburger, A.W. J. Cell. Physiol. (2000) [Pubmed]
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