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Protein TCEB1 PDB 1lm8.png
Available structures
PDB Ortholog search: PDBe RCSB
Aliases ELOC, SIII, eloC, TCEB1, transcription elongation factor B subunit 1
External IDs MGI: 1915173 HomoloGene: 38083 GeneCards: ELOC
RNA expression pattern
PBB GE TCEB1 202824 s at fs.png

PBB GE TCEB1 202823 at fs.png
More reference expression data
Species Human Mouse
RefSeq (mRNA)


RefSeq (protein)


Location (UCSC) Chr 8: 73.94 – 73.97 Mb Chr 1: 16.64 – 16.66 Mb
PubMed search [1] [2]
View/Edit Human View/Edit Mouse

Transcription elongation factor B polypeptide 1 is a protein that in humans is encoded by the TCEB1 gene.[3][4]


This gene encodes the protein elongin C, which is a subunit of the transcription factor B (SIII) complex. The SIII complex is composed of elongins A/A2, B and C. It activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin A functions as the transcriptionally active component of the SIII complex, whereas elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and capable of forming a stable complex with elongins B and C. The von Hippel-Lindau tumor suppressor protein binds to elongins B and C, and thereby inhibits transcription elongation.[5]


TCEB1 has been shown to interact with:


  1. ^ "Human PubMed Reference:". 
  2. ^ "Mouse PubMed Reference:". 
  3. ^ Garrett KP, Haque D, Conaway RC, Conaway JW (Feb 1995). "A human cDNA encoding the small subunit of RNA polymerase II transcription factor SIII". Gene. 150 (2): 413–4. doi:10.1016/0378-1119(94)90467-7. PMID 7821821. 
  4. ^ Duan DR, Pause A, Burgess WH, Aso T, Chen DY, Garrett KP, Conaway RC, Conaway JW, Linehan WM, Klausner RD (Oct 1995). "Inhibition of transcription elongation by the VHL tumor suppressor protein". Science. 269 (5229): 1402–6. doi:10.1126/science.7660122. PMID 7660122. 
  5. ^ "Entrez Gene: TCEB1 transcription elongation factor B (SIII), polypeptide 1 (15kDa, elongin C)". 
  6. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (Oct 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  7. ^ a b Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B, Conaway RC, Conaway JW, Kaelin WG (Dec 1999). "Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein". J. Clin. Invest. 104 (11): 1583–91. doi:10.1172/JCI8161. PMC 481054Freely accessible. PMID 10587522. 
  8. ^ Krumm A, Groudine M (Sep 1995). "Tumor suppression and transcription elongation: the dire consequences of changing partners". Science. 269 (5229): 1400–1. doi:10.1126/science.7660121. PMID 7660121. 
  9. ^ a b Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (Feb 2002). "Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein". J. Biol. Chem. 277 (7): 4656–62. doi:10.1074/jbc.M108269200. PMID 11739384. 
  10. ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D. "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948Freely accessible. PMID 17353931. 
  11. ^ Tsuchiya H, Iseda T, Hino O (Jul 1996). "Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product". Cancer Res. 56 (13): 2881–5. PMID 8674032. 
  12. ^ Min JH, Yang H, Ivan M, Gertler F, Kaelin WG, Pavletich NP (Jun 2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science. 296 (5574): 1886–9. doi:10.1126/science.1073440. PMID 12004076. 
  13. ^ Hacker KE, Lee CM, Rathmell WK. Zhang B, ed. "VHL type 2B mutations retain VBC complex form and function". PLoS ONE. 3 (11): e3801. doi:10.1371/journal.pone.0003801. PMC 2583047Freely accessible. PMID 19030229. 
  14. ^ Kim BY, Kim H, Cho EJ, Youn HD (Feb 2008). "Nur77 upregulates HIF-alpha by inhibiting pVHL-mediated degradation". Exp. Mol. Med. 40 (1): 71–83. doi:10.3858/emm.2008.40.1.71. PMC 2679322Freely accessible. PMID 18305400. 

Further reading[edit]