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Gene Review

TCEB2  -  transcription elongation factor B (SIII),...

Homo sapiens

Synonyms: ELOB, EloB, Elongin 18 kDa subunit, Elongin-B, RNA polymerase II transcription factor SIII subunit B, ...
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Disease relevance of TCEB2

  • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function [1].
  • Germline mutations in VHL patients, as well as somatic mutations in different tumors, including hemangioblastomas, have been identified, its ability to act as a tumor suppressor in vivo has been confirmed, and interaction with transcription factors Elongin B and C leading to inhibition of transcriptional elongation has been demonstrated [2].

High impact information on TCEB2

  • These results suggest that the tumor suppression function of pVHL may be linked to its ability to bind to Elongin B and C [3].
  • A peptide replica of this region inhibited binding of pVHL to Elongin B and C whereas a point-mutant derivative, corresponding to a naturally occurring VHL missense mutation, had no effect [3].
  • Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein [4].
  • Thus, CCT likely functions, at least in part, by retaining VHL chains pending the availability of elongin B/C for final folding and/or assembly [5].
  • The von Hippel-Lindau (VHL) tumour suppressorgene product is believed to be involved in the down-regulation of transcriptional elongation by preventing the association of elongin B and C with the catalytic subunit elongin A [6].

Biological context of TCEB2


Associations of TCEB2 with chemical compounds

  • O2 -dependent degradation of the HIF-1alpha subunit is mediated by prolyl hydroxylase (PHD), the von Hippel-Lindau (VHL)/Elongin-C/Elongin-B E3 ubiquitin ligase, and the proteasome [8].

Physical interactions of TCEB2

  • In this report, we identify Elongin C mutants that fall into multiple functional classes based on their abilities to bind Elongin B and to bind and activate Elongin A under our assay conditions [9].

Regulatory relationships of TCEB2

  • The VHL protein was shown to bind tightly and specifically to the Elongin B and C subunits and to inhibit Elongin (SIII) transcriptional activity in vitro [10].

Other interactions of TCEB2


Analytical, diagnostic and therapeutic context of TCEB2

  • Here we report molecular cloning and biochemical characterization of the SIII p18 subunit, which is found to be a member of the ubiquitin homology (UbH) gene family and functions as a positive regulatory subunit of SIII. p18 is a 118-amino acid protein composed of an 84-residue N-terminal UbH domain fused to a 34-residue C-terminal tail [11].


  1. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. Kobayashi, M., Takaori-Kondo, A., Miyauchi, Y., Iwai, K., Uchiyama, T. J. Biol. Chem. (2005) [Pubmed]
  2. Pathology, genetics and cell biology of hemangioblastomas. Wizigmann-Voos, S., Plate, K.H. Histol. Histopathol. (1996) [Pubmed]
  3. Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C. Kibel, A., Iliopoulos, O., DeCaprio, J.A., Kaelin, W.G. Science (1995) [Pubmed]
  4. Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein. Ohh, M., Takagi, Y., Aso, T., Stebbins, C.E., Pavletich, N.P., Zbar, B., Conaway, R.C., Conaway, J.W., Kaelin, W.G. J. Clin. Invest. (1999) [Pubmed]
  5. Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity. Hansen, W.J., Ohh, M., Moslehi, J., Kondo, K., Kaelin, W.G., Welch, W.J. Mol. Cell. Biol. (2002) [Pubmed]
  6. Expression of the von Hippel-Lindau-binding protein-1 (Vbp1) in fetal and adult mouse tissues. Hemberger, M., Himmelbauer, H., Neumann, H.P., Plate, K.H., Schwarzkopf, G., Fundele, R. Hum. Mol. Genet. (1999) [Pubmed]
  7. Contrasting effects on HIF-1alpha regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease. Clifford, S.C., Cockman, M.E., Smallwood, A.C., Mole, D.R., Woodward, E.R., Maxwell, P.H., Ratcliffe, P.J., Maher, E.R. Hum. Mol. Genet. (2001) [Pubmed]
  8. RACK1 vs. HSP90: competition for HIF-1alpha degradation vs. stabilization. Liu, Y.V., Semenza, G.L. Cell Cycle (2007) [Pubmed]
  9. Characterization of elongin C functional domains required for interaction with elongin B and activation of elongin A. Takagi, Y., Conaway, R.C., Conaway, J.W. J. Biol. Chem. (1996) [Pubmed]
  10. Inhibition of transcription elongation by the VHL tumor suppressor protein. Duan, D.R., Pause, A., Burgess, W.H., Aso, T., Chen, D.Y., Garrett, K.P., Conaway, R.C., Conaway, J.W., Linehan, W.M., Klausner, R.D. Science (1995) [Pubmed]
  11. Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog. Garrett, K.P., Aso, T., Bradsher, J.N., Foundling, S.I., Lane, W.S., Conaway, R.C., Conaway, J.W. Proc. Natl. Acad. Sci. U.S.A. (1995) [Pubmed]
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