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Gene Review

UBP1  -  upstream binding protein 1 (LBP-1a)

Homo sapiens

Synonyms: LBP-1B, LBP-1a, LBP1, LBP1A, LBP1B, ...
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Disease relevance of UBP1


High impact information on UBP1


Biological context of UBP1

  • Comparison of the amino acid sequence of LBP-1 with entries in the available protein data bases revealed the identity of LBP-1c to alpha-CP2, an alpha-globin transcription factor [1].
  • Severe mutations of the high affinity LBP-1 binding sites between -4 and +21 did not relieve the LBP-1-dependent block [9].
  • In particular, YY1 and LBP-1 have been shown to cooperate in repressing HIV-1-long terminal repeat reporter gene expression by in vitro cotransfection experiments [10].
  • Consistent with a role in pre-mRNA processing, overexpression of UBP1 in N. plumabaginifolia protoplasts enhances the splicing of suboptimal introns and increases the steady-state levels of reporter mRNAs, even intronless ones [8].
  • Several studies have demonstrated that TAR DNA can bind cellular proteins, such as UBP-1/LBP-1, which repress HIV-1 gene expression and other factors which are involved in the generation of short, nonprocessive transcripts [11].

Anatomical context of UBP1

  • Nicotiana plumbaginifolia UBP1 is an hnRNP-like protein associated with the poly(A)(+) RNA in the cell nucleus [8].
  • The low-affinity site for LBP-1 (UBP-1) functioned as a negative regulator of LTR activity in undifferentiated macrophages, but this influence was lost upon differentiation [12].
  • Transiently expressed LBP-1 proteins in COS-7 cells formed speckles in the nucleus [13].
  • Investigation of subcellular localization of LBP-1 proteins fused to YFP revealed that the LBP-1b was localized in the nucleus, whereas LBP-1a and LBP-1c were exclusively localized in the cytosol [13].

Physical interactions of UBP1


Other interactions of UBP1

  • The cellular factor, LBP-1, can repress HIV-1 transcription by preventing the binding of TFIID to the promoter [9].
  • However, addition of LBP-1 after RNA polymerase was stalled at +13 strongly inhibited further elongation ("chase") by reducing RNA polymerase processivity [9].
  • Transcription factor NF2d9 (LBP-1a) interacts with the positive regulatory element for the xenobiotic responsive element [15].
  • Moreover, we show that c-Myc can interact with the initiator binding proteins YY-1 and LBP-1 and can cooperate with these factors to synergistically repress HIV-1 LTR transcription [16].
  • The maximum turnover number for LBP was approximately 150 molecules of LPS min-1 LBP-1 [17].

Analytical, diagnostic and therapeutic context of UBP1

  • Gel-shift analysis shows that protein binds specifically to this region, but competition studies suggest that it is unlikely to be LBP-1 [18].
  • Antiserum specific for either the M. catarrhalis Tbp1+2 molecules, the M. catarrhalis Lbp1 molecule, or for a commercial preparation of human lactoferrin did not react on western blots with the same organisms' affinity purified Lbp2 [2].


  1. Characterization of a family of related cellular transcription factors which can modulate human immunodeficiency virus type 1 transcription in vitro. Yoon, J.B., Li, G., Roeder, R.G. Mol. Cell. Biol. (1994) [Pubmed]
  2. Biochemical analysis of lactoferrin receptors in the Neisseriaceae: identification of a second bacterial lactoferrin receptor protein. Bonnah, R.A., Yu, R., Schryvers, A.B. Microb. Pathog. (1995) [Pubmed]
  3. Herpes simplex virus-mediated activation of human immunodeficiency virus is inhibited by oligonucleoside methylphosphonates that target immediate-early mRNAs 1 and 3. Feng, C.P., Kulka, M., Smith, C., Aurelian, L. Antisense Nucleic Acid Drug Dev. (1996) [Pubmed]
  4. Bacterial lactoferrin receptors. Schryvers, A.B., Bonnah, R., Yu, R.H., Wong, H., Retzer, M. Adv. Exp. Med. Biol. (1998) [Pubmed]
  5. Repression of HIV-1 transcription by a cellular protein. Kato, H., Horikoshi, M., Roeder, R.G. Science (1991) [Pubmed]
  6. Purification of the human immunodeficiency virus type 1 enhancer and TAR binding proteins EBP-1 and UBP-1. Wu, F.K., Garcia, J.A., Harrich, D., Gaynor, R.B. EMBO J. (1988) [Pubmed]
  7. A Family of MicroRNAs Present in Plants and Animals. Arteaga-Vázquez, M., Caballero-Pérez, J., Vielle-Calzada, J.P. Plant Cell (2006) [Pubmed]
  8. UBA1 and UBA2, two proteins that interact with UBP1, a multifunctional effector of pre-mRNA maturation in plants. Lambermon, M.H., Fu, Y., Wieczorek Kirk, D.A., Dupasquier, M., Filipowicz, W., Lorković, Z.J. Mol. Cell. Biol. (2002) [Pubmed]
  9. A novel LBP-1-mediated restriction of HIV-1 transcription at the level of elongation in vitro. Parada, C.A., Yoon, J.B., Roeder, R.G. J. Biol. Chem. (1995) [Pubmed]
  10. In vivo administration of recombinant IL-2 to individuals infected by HIV down-modulates the binding and expression of the transcription factors ying-yang-1 and leader binding protein-1/late simian virus 40 factor. Bovolenta, C., Camorali, L., Lorini, A.L., Vallanti, G., Ghezzi, S., Tambussi, G., Lazzarin, A., Poli, G. J. Immunol. (1999) [Pubmed]
  11. Cloning and characterization of a novel cellular protein, TDP-43, that binds to human immunodeficiency virus type 1 TAR DNA sequence motifs. Ou, S.H., Wu, F., Harrich, D., García-Martínez, L.F., Gaynor, R.B. J. Virol. (1995) [Pubmed]
  12. Differential role of long terminal repeat control elements for the regulation of basal and Tat-mediated transcription of the human immunodeficiency virus in stimulated and unstimulated primary human macrophages. Moses, A.V., Ibanez, C., Gaynor, R., Ghazal, P., Nelson, J.A. J. Virol. (1994) [Pubmed]
  13. Heterodimerization with LBP-1b is necessary for nuclear localization of LBP-1a and LBP-1c. Sato, F., Yasumoto, K., Kimura, K., Numayama-Tsuruta, K., Sogawa, K. Genes Cells (2005) [Pubmed]
  14. Herpes simplex virus type 1-mediated induction of human immunodeficiency virus type 1 provirus correlates with binding of nuclear proteins to the NF-kappa B enhancer and leader sequence. Vlach, J., Pitha, P.M. J. Virol. (1992) [Pubmed]
  15. Transcription factor NF2d9 (LBP-1a) interacts with the positive regulatory element for the xenobiotic responsive element. Kurose, K., Tohkin, M., Hasegawa, R. Biochim. Biophys. Acta (2005) [Pubmed]
  16. Repression of the human immunodeficiency virus type-1 long terminal repeat by the c-Myc oncoprotein. Stojanova, A., Caro, C., Jarjour, R.J., Oster, S.K., Penn, L.Z., Germinario, R.J. J. Cell. Biochem. (2004) [Pubmed]
  17. Catalytic properties of lipopolysaccharide (LPS) binding protein. Transfer of LPS to soluble CD14. Yu, B., Wright, S.D. J. Biol. Chem. (1996) [Pubmed]
  18. Transcriptional activity of the human tissue inhibitor of metalloproteinases 1 (TIMP-1) gene in fibroblasts involves elements in the promoter, exon 1 and intron 1. Clark, I.M., Rowan, A.D., Edwards, D.R., Bech-Hansen, T., Mann, D.A., Bahr, M.J., Cawston, T.E. Biochem. J. (1997) [Pubmed]
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