The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)



Gene Review

TBPL2  -  TATA box binding protein like 2

Homo sapiens

Synonyms: TATA box-binding protein-like protein 2, TATA box-binding protein-related factor 3, TBP-like protein 2, TBP-related factor 3, TBP2, ...
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of TBPL2

  • In the TBP-2-overexpressing cells, a G1 arrest was observed in association with an increase of p16 expression and reduction of retinoblastoma phosphorylation [1].
  • We found that TBP-2 ectopically expressed in the breast cancer cell line MCF-7 was localized predominantly in the nucleus exhibiting growth suppressive activity [2].
  • Molecular characterization of hybrid Tbp2 proteins from Neisseria meningitidis [3].
  • Here, we analysed the mechanism of loss of TBP-2 expression and the role of TBP-2 in IL-2-dependent growth in the in vitro model to investigate multistep transformation of HTLV-I [4].
  • Mice were inoculated with purified outer membrane vesicles (blebs) from 5 selected N. meningitidis strains, and the five serum samples obtained were analyzed for anti-TBP2 antibodies by using the homologous strain and for cross-reactivity with the TBP2 of the 4 other selected strains and another 35 heterologous N. meningitidis strains [5].

High impact information on TBPL2

  • TRF3 is a nuclear protein that is present in all human and mouse tissues and cell lines examined [6].
  • The TRF3 gene is present and expressed in vertebrates, from fish through humans, but absent from the genomes of the urochordate Ciona intestinalis and the lower eukaryotes D. melanogaster and Caenorhabditis elegans [6].
  • As the expression of TBP-2 mRNA is increased, the expression of a second gene, thioredoxin, is decreased [7].
  • In this study we show that SAHA induces the expression of vitamin D-up-regulated protein 1/thioredoxin-binding protein-2 (TBP-2) in transformed cells [7].
  • These results support a model in which the expression of a subset of genes (i.e., including TBP-2) is repressed in transformed cells, leading to a block in differentiation, and culture of transformed cells with SAHA causes re-expression of these genes, leading to induction of growth arrest, differentiation, and/or apoptosis [7].

Biological context of TBPL2

  • Regulated expression of TATA-binding protein-related factor 3 (TRF3) during early embryogenesis [8].
  • In transient transfection assays, HDAC inhibitors induce TBP-2 promoter constructs, and this induction requires an NF-Y binding site [7].
  • Knockdown of zebrafish TBP2 results in specific reduction of the protein level, leading to a phenotype, which indicates the requirement of TBP2 for embryonic patterning [9].
  • Treatment of HL-60 cells with 1alpha, 25-dihydroxyvitamin D(3) caused an increase of TBP-2/VDUP1 expression and down-regulation of the expression and the reducing activity of TRX [10].
  • The analysis of tbp2 clones isolated from various bacterial strains revealed extensive divergences throughout the open reading frame (ORF), with predicted amino acid (aa) sequences displaying 47% to 83% identity [3].

Anatomical context of TBPL2

  • We examined the expression of TRF3 in maturing oocytes and early embryos and found that TRF3 was co-expressed with TBP in the meiotic oocytes and early embryos from the late one-cell stage onward [8].
  • Ectopic overexpression of TBP-2 in HTLV-I-positive T cells resulted in growth suppression [1].
  • However, TBP2 shows contrasting expression patterns in the gonads and during embryonic development in comparison to TBP, suggesting differential function [9].
  • In gene array analysis, we found that TBP-2 expression was reduced during human osteoclast differentiation compared with macrophage differentiation [11].
  • This suggests that the TBP2 epitopes of different strains differ in nature or in their accessibility to the immune system [5].

Associations of TBPL2 with chemical compounds

  • The physical interaction between TBP-2 and Rch1 was confirmed with a glutathione S-transferase pull-down assay [2].
  • Two mAbs reacting with TNF-R55 (H398 and TBP2) induced O2 release in a similar manner but to a lesser extent than TNF [12].
  • Sequential treatment with 5-aza-2'-deoxycytidine and a histone deacetylase inhibitor augmented histone acetylation and TBP-2 expression, suggesting that loss of TBP-2 expression is due to DNA methylation and histone deacetylation [4].
  • There are three highly homologous genes of TBP-2/vitamin D3 up-regulated protein 1 in humans, but their functions remain unclear [13].
  • Isogenic mutants deficient in expression of Tbp1 or Tbp2 or both proteins were prepared by insertion of the Tn903 kanamycin resistance cassette into cloned sequences and reintroduction of the interrupted sequences into the wild-type chromosome [14].

Physical interactions of TBPL2

  • To investigate the mechanism underlying the nuclear localization, we performed a yeast two-hybrid screening and identified importin alpha(1) (Rch1) as a protein interacting with TBP-2 [2].

Regulatory relationships of TBPL2


Other interactions of TBPL2

  • Collectively, our results strongly suggest that an interaction with importin system is required for TBP-2 nuclear translocation and growth control tightly associated with TRX-dependent redox regulation of transcription factors [2].
  • One of the candidates, designated as thioredoxin-binding protein-2 (TBP-2), was identical to vitamin D(3) up-regulated protein 1 (VDUP1) [10].
  • CONCLUSIONS: These data support significant roles for TBP-2 and the Trx system in osteoclast differentiation that are mediated by redox regulation of AP-1 transcription [11].
  • Our aim was to determine the roles of TBP-2 and Trx-1 in human osteoclastogenesis and RANKL signaling [11].
  • This antiserum also cross-reacted with the TBP 2 of several strains of H. influenzae type b, thus showing the presence of common antigenic domains among these functionally equivalent proteins in different pathogens; no cross-reaction was detected with a purified sample of the human transferrin receptor [16].

Analytical, diagnostic and therapeutic context of TBPL2

  • Chromatin immunoprecipitation (ChIP) assay revealed that different gene promoters in mouse embryonic stem (ES) cells recruited TRF3 and TBP selectively [8].
  • Expression of TBP-2 and Trx-1 was quantified by real-time PCR and Western analysis [11].
  • Human convalescent-phase sera obtained from five patients infected with meningococci of different serogroups and serotypes contained fully cross-reactive antibodies to TBP2 but no anti-TBP1 antibodies, when examined on Western blots [17].
  • Here, we report that antiserum against purified TBP 2 from one strain of N. meningitidis cross-reacts on immunoblotting with the TBP 2 of all meningococcal isolates examined, as well as with the TBP 2 of N. gonorrhoeae [16].
  • Mixtures of TBP1 and TBP2 (TBP1 + 2) from three meningococcal strains were purified using affinity chromatography and used to determine anti-TBP antibodies in human sera by ELISA [18].


  1. Loss of thioredoxin-binding protein-2/vitamin D3 up-regulated protein 1 in human T-cell leukemia virus type I-dependent T-cell transformation: implications for adult T-cell leukemia leukemogenesis. Nishinaka, Y., Nishiyama, A., Masutani, H., Oka, S., Ahsan, K.M., Nakayama, Y., Ishii, Y., Nakamura, H., Maeda, M., Yodoi, J. Cancer Res. (2004) [Pubmed]
  2. Importin alpha1 (Rch1) mediates nuclear translocation of thioredoxin-binding protein-2/vitamin D(3)-up-regulated protein 1. Nishinaka, Y., Masutani, H., Oka, S., Matsuo, Y., Yamaguchi, Y., Nishio, K., Ishii, Y., Yodoi, J. J. Biol. Chem. (2004) [Pubmed]
  3. Molecular characterization of hybrid Tbp2 proteins from Neisseria meningitidis. Legrain, M., Findeli, A., Villeval, D., Quentin-Millet, M.J., Jacobs, E. Mol. Microbiol. (1996) [Pubmed]
  4. Loss of interleukin-2-dependency in HTLV-I-infected T cells on gene silencing of thioredoxin-binding protein-2. Ahsan, M.K., Masutani, H., Yamaguchi, Y., Kim, Y.C., Nosaka, K., Matsuoka, M., Nishinaka, Y., Maeda, M., Yodoi, J. Oncogene (2006) [Pubmed]
  5. Immunogenicity and antigenic heterogeneity of a human transferrin-binding protein in Neisseria meningitidis. Ferron, L., Ferreiros, C.M., Criado, M.T., Pintor, M. Infect. Immun. (1992) [Pubmed]
  6. TRF3, a TATA-box-binding protein-related factor, is vertebrate-specific and widely expressed. Persengiev, S.P., Zhu, X., Dixit, B.L., Maston, G.A., Kittler, E.L., Green, M.R. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  7. The histone deacetylase inhibitor SAHA arrests cancer cell growth, up-regulates thioredoxin-binding protein-2, and down-regulates thioredoxin. Butler, L.M., Zhou, X., Xu, W.S., Scher, H.I., Rifkind, R.A., Marks, P.A., Richon, V.M. Proc. Natl. Acad. Sci. U.S.A. (2002) [Pubmed]
  8. Regulated expression of TATA-binding protein-related factor 3 (TRF3) during early embryogenesis. Yang, Y., Cao, J., Huang, L., Fang, H.Y., Sheng, H.Z. Cell Res. (2006) [Pubmed]
  9. TBP2, a vertebrate-specific member of the TBP family, is required in embryonic development of zebrafish. Bártfai, R., Balduf, C., Hilton, T., Rathmann, Y., Hadzhiev, Y., Tora, L., Orbán, L., Müller, F. Curr. Biol. (2004) [Pubmed]
  10. Identification of thioredoxin-binding protein-2/vitamin D(3) up-regulated protein 1 as a negative regulator of thioredoxin function and expression. Nishiyama, A., Matsui, M., Iwata, S., Hirota, K., Masutani, H., Nakamura, H., Takagi, Y., Sono, H., Gon, Y., Yodoi, J. J. Biol. Chem. (1999) [Pubmed]
  11. Regulation of human osteoclast differentiation by thioredoxin binding protein-2 and redox-sensitive signaling. Aitken, C.J., Hodge, J.M., Nishinaka, Y., Vaughan, T., Yodoi, J., Day, C.J., Morrison, N.A., Nicholson, G.C. J. Bone Miner. Res. (2004) [Pubmed]
  12. TNF-induced superoxide anion production in adherent human neutrophils involves both the p55 and p75 TNF receptor. Richter, J., Gullberg, U., Lantz, M. J. Immunol. (1995) [Pubmed]
  13. Thioredoxin-binding protein-2-like inducible membrane protein is a novel vitamin D3 and peroxisome proliferator-activated receptor (PPAR)gamma ligand target protein that regulates PPARgamma signaling. Oka, S., Masutani, H., Liu, W., Horita, H., Wang, D., Kizaka-Kondoh, S., Yodoi, J. Endocrinology (2006) [Pubmed]
  14. Identification and characterization of genes encoding the human transferrin-binding proteins from Haemophilus influenzae. Gray-Owen, S.D., Loosmore, S., Schryvers, A.B. Infect. Immun. (1995) [Pubmed]
  15. The role of receptors for tumour necrosis factor-alpha in the induction of human polymorphonuclear neutrophil chemiluminescence. Zeman, K., Kantorski, J., Paleolog, E.M., Feldmann, M., Tchórzewski, H. Immunol. Lett. (1996) [Pubmed]
  16. Common antigenic domains in transferrin-binding protein 2 of Neisseria meningitidis, Neisseria gonorrhoeae, and Haemophilus influenzae type b. Stevenson, P., Williams, P., Griffiths, E. Infect. Immun. (1992) [Pubmed]
  17. Immune responses in humans and animals to meningococcal transferrin-binding proteins: implications for vaccine design. Ala'Aldeen, D.A., Stevenson, P., Griffiths, E., Gorringe, A.R., Irons, L.I., Robinson, A., Hyde, S., Borriello, S.P. Infect. Immun. (1994) [Pubmed]
  18. Human antibody response to meningococcal transferrin binding proteins: evidence for vaccine potential. Gorringe, A.R., Borrow, R., Fox, A.J., Robinson, A. Vaccine (1995) [Pubmed]
WikiGenes - Universities