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YBX3  -  Y box binding protein 3

Homo sapiens

Synonyms: CSDA, CSDA1, Cold shock domain-containing protein A, DBPA, DNA-binding protein A, ...
 
 
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Disease relevance of CSDA

  • Analysis of lambda phage genomic clones revealed that the dbpA gene consists of 10 exons spanning a 24-kb genomic region [1].
  • Independently, the screening of phage expression libraries with depurinated DNA resulted in the isolation of YB-1 and dbpA, a previously isolated cDNA that has homology to YB-1 [2].
  • Canine ZONAB is the homologue of human DbpA, an E2F target gene that is overexpressed in different carcinomas [3].
  • The dbpA was cloned and sequenced from the three pathogenic Borrelia species common in Europe. Sequence analysis revealed high interspecies heterogeneity [4].
 

Psychiatry related information on CSDA

  • The Communication Self-Assessment Scale for Deaf Adults (CSDA) evaluates difficult communication situations, their importance to the respondent, communication strategies, and communication attitudes [5].
 

High impact information on CSDA

  • The amount of the RalA-ZONAB complex increases as epithelial cells become more dense and increase cell contacts [6].
  • Although this regulatory process may also involve regulation of transcription by ZONAB, our data suggest that one mechanism by which ZONAB and ZO-1 influence proliferation is by regulating the nuclear accumulation of CDK4 [7].
  • Previously, we have identified ZO-1-associated nucleic acid binding proteins (ZONAB), a Y-box transcription factor whose nuclear localization and transcriptional activity is regulated by the tight junction-associated candidate tumor suppressor ZO-1 [7].
  • Overexpression of ZONAB resulted in increased cell density in mature monolayers, and depletion of ZONAB or overexpression of ZO-1 reduced cell density [7].
  • Now, we found that reduction of ZONAB expression using an antisense approach or by RNA interference strongly reduced proliferation of MDCK cells [7].
 

Biological context of CSDA

  • UBF belongs to an HMG domain protein family and dbpA belongs to a Y box binding protein family [8].
  • Human DNA-binding protein (dbpA) is a member of a Y-box binding protein family containing a cold shock domain [9].
  • All 16 dbpB (YB-1) clones, isolated from the same genomic library used for dbpA genomic cloning, were processed genes because of their intronless structures and multiple mutations [1].
  • In this study, we analyzed the transcriptional regulatory region of dbpA, and searched for the mutation in this region by a direct sequence method [9].
  • Recently, we isolated a splicing variant of dbpA as a candidate for the cellular recombinogenic protein that leads to genomic instability and inflammation-mediated hepatocarcinogenesis [9].
 

Anatomical context of CSDA

  • To study the in vivo effect of dbpA on hepatocarcinogenesis, we generated the dbpA-transgenic mouse that specifically expressed a transgene in hepatocytes [10].
 

Associations of CSDA with chemical compounds

  • The IMFP and CSDA-range for the biological compounds C5H5N5 (adenine), C5H5N5O (guanine), C4H5N3O (cytosine), C5H6N2O2 (thymine), C20H27N7O13P2 (cytosine-guanine) and C19H26N8O13P2 (thymine-adenine) have been introduced for incident electrons in the energy range 20 eV-1 MeV [11].
  • Positive and negative regulation of the human thymidine kinase promoter mediated by CCAAT binding transcription factors NF-Y/CBF, dbpA, and CDP/cut [12].
  • The resulting fluorogenic Dabcyl- and BODIPY-containing PL analogues, DBPA, DBPC, DBPE, and DBPG, were used in mixed micelle assays to determine PLA 2 kinetics [13].
 

Enzymatic interactions of CSDA

 

Regulatory relationships of CSDA

 

Other interactions of CSDA

  • These results indicate that dbpA and dbpB (YB-1) genes evolved in different fashions after deviation from a common ancestral gene [1].
  • We found that the cold shock domain (Y-box) repressor proteins, dbpA and dbpB/YB-1, bind distinct strands of the human VEGF HRR [14].
  • When dbpA was added, the binding of NF-YA to DNA increased, which could be explained by interaction between these two proteins whose purpose is to increase the binding affinity of NF-YA for DNA [15].
  • In gel shift assays, YY1 binding to the core element is inhibited by either YB-1 or dbpA [16].
  • The interaction between ZONAB/DbpA and symplekin can be reconstituted with recombinant proteins [17].
 

Analytical, diagnostic and therapeutic context of CSDA

References

  1. Characterization of the gene for dbpA, a family member of the nucleic-acid-binding proteins containing a cold-shock domain. Kudo, S., Mattei, M.G., Fukuda, M. Eur. J. Biochem. (1995) [Pubmed]
  2. DNA binding properties of YB-1 and dbpA: binding to double-stranded, single-stranded, and abasic site containing DNAs. Hasegawa, S.L., Doetsch, P.W., Hamilton, K.K., Martin, A.M., Okenquist, S.A., Lenz, J., Boss, J.M. Nucleic Acids Res. (1991) [Pubmed]
  3. Regulation of PCNA and cyclin D1 expression and epithelial morphogenesis by the ZO-1-regulated transcription factor ZONAB/DbpA. Sourisseau, T., Georgiadis, A., Tsapara, A., Ali, R.R., Pestell, R., Matter, K., Balda, M.S. Mol. Cell. Biol. (2006) [Pubmed]
  4. Species-specific serodiagnosis of Lyme arthritis and neuroborreliosis due to Borrelia burgdorferi sensu stricto, B. afzelii, and B. garinii by using decorin binding protein A. Heikkilä, T., Seppälä, I., Saxen, H., Panelius, J., Yrjänäinen, H., Lahdenne, P. J. Clin. Microbiol. (2002) [Pubmed]
  5. Communication Self-Assessment Scale Inventory for Deaf Adults. Kaplan, H., Bally, S.J., Brandt, F. Journal of the American Academy of Audiology. (1991) [Pubmed]
  6. RalA interacts with ZONAB in a cell density-dependent manner and regulates its transcriptional activity. Frankel, P., Aronheim, A., Kavanagh, E., Balda, M.S., Matter, K., Bunney, T.D., Marshall, C.J. EMBO J. (2005) [Pubmed]
  7. The ZO-1-associated Y-box factor ZONAB regulates epithelial cell proliferation and cell density. Balda, M.S., Garrett, M.D., Matter, K. J. Cell Biol. (2003) [Pubmed]
  8. Recombination hot spot of hepatitis B virus genome binds to members of the HMG domain protein family and the Y box binding protein family; implication of these proteins in genomic instability. Kajino, K., Yamamoto, T., Hayashi, J., Umeda, T., Takahara, T., Hino, O. Intervirology (2001) [Pubmed]
  9. Somatic mutation and SNP in the promoter of dbpA and human hepatocarcinogenesis. Hayashi, J., Kajino, K., Umeda, T., Takano, S., Arakawa, Y., Kudo, M., Hino, O. Int. J. Oncol. (2002) [Pubmed]
  10. Gene expression profile of DNA binding protein A transgenic mice. Tobita, H., Kajino, K., Inami, K., Kano, S., Yasen, M., Imamura, O., Kinoshita, Y., Hino, O. Int. J. Oncol. (2006) [Pubmed]
  11. Electron inelastic mean free path formula and CSDA-range calculation in biological compounds for low and intermediate energies. Akar, A., Gümüş, H., Okumuşoğlu, N.T. Applied radiation and isotopes : including data, instrumentation and methods for use in agriculture, industry and medicine. (2006) [Pubmed]
  12. Positive and negative regulation of the human thymidine kinase promoter mediated by CCAAT binding transcription factors NF-Y/CBF, dbpA, and CDP/cut. Kim, E.C., Lau, J.S., Rawlings, S., Lee, A.S. Cell Growth Differ. (1997) [Pubmed]
  13. Fluorogenic phospholipids as head group-selective reporters of phospholipase A activity. Rose, T.M., Prestwich, G.D. ACS chemical biology (2006) [Pubmed]
  14. Phosphorylation of cold shock domain/Y-box proteins by ERK2 and GSK3beta and repression of the human VEGF promoter. Coles, L.S., Lambrusco, L., Burrows, J., Hunter, J., Diamond, P., Bert, A.G., Vadas, M.A., Goodall, G.J. FEBS Lett. (2005) [Pubmed]
  15. Repression of major histocompatibility complex I-A beta gene expression by dbpA and dbpB (mYB-1) proteins. Lloberas, J., Maki, R.A., Celada, A. Mol. Cell. Biol. (1995) [Pubmed]
  16. Suppression of grp78 core promoter element-mediated stress induction by the dbpA and dbpB (YB-1) cold shock domain proteins. Li, W.W., Hsiung, Y., Wong, V., Galvin, K., Zhou, Y., Shi, Y., Lee, A.S. Mol. Cell. Biol. (1997) [Pubmed]
  17. Functional interaction between the ZO-1-interacting transcription factor ZONAB/DbpA and the RNA processing factor symplekin. Kavanagh, E., Buchert, M., Tsapara, A., Choquet, A., Balda, M.S., Hollande, F., Matter, K. J. Cell. Sci. (2006) [Pubmed]
 
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