ELOC

Transcription elongation factor B polypeptide 1 is a protein that in humans is encoded by the TCEB1 gene.[5][6]

ELOC
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 1LM8, 1LQB, 1VCB, 2C9W, 2IZV, 2MA9, 3DCG, 3ZKJ, 3ZNG, 3ZRC, 3ZRF, 3ZTC, 3ZTD, 3ZUN, 4AJY, 4AWJ, 4B95, 4B9K, 4BKS, 4BKT, 4N9F, 4W9C, 4W9D, 4W9E, 4W9F, 4W9G, 4W9H, 4W9I, 4W9J, 4W9K, 4W9L, 4WQO, 5BO4
Identifiers
Aliases	ELOC, SIII, eloC, TCEB1, transcription elongation factor B subunit 1, elongin C
External IDs	OMIM: 600788 MGI: 1915173 HomoloGene: 38083 GeneCards: ELOC
Gene location (Human) Chr. Chromosome 8 (human)[1] Band 8q21.11 Start 73,939,169 bp[1] End 73,972,287 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 A3 Start 16,641,725 bp[2] End 16,657,042 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • GO:0001948 protein binding • ubiquitin-protein transferase activity Cellular component • cytosol • cell nucleus • elongin complex • nucleoplasm Biological process • regulation of transcription from RNA polymerase II promoter • transcription elongation from RNA polymerase II promoter • regulation of transcription, DNA-templated • transcription from RNA polymerase II promoter • ubiquitin-dependent protein catabolic process • transcription, DNA-templated • regulation of transcription from RNA polymerase II promoter in response to hypoxia • GO:0022415 viral process • positive regulation of transcription elongation from RNA polymerase II promoter • post-translational modification • protein ubiquitination Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	6921	67923
Ensembl	ENSG00000154582	ENSMUSG00000079658
UniProt	Q15369	P83940
RefSeq (mRNA)	NM_001204857 NM_001204858 NM_001204859 NM_001204860 NM_001204861 NM_001204862 NM_001204863 NM_001204864 NM_005648	NM_001310470 NM_026456
RefSeq (protein)	NP_001191786 NP_001191787 NP_001191788 NP_001191789 NP_001191790 NP_001191791 NP_001191792 NP_001191793 NP_005639	NP_001297399 NP_080732
Location (UCSC)	Chr 8: 73.94 – 73.97 Mb	Chr 1: 16.64 – 16.66 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

Function

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.[7]

Interactions

TCEB1 has been shown to interact with:

• TCEB2[8][9][10][11] and
• Von Hippel-Lindau tumor suppressor.[9][11][12][13][14][15][16]

References

1. GRCh38: Ensembl release 89: ENSG00000154582 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000079658 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
5. 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.
6. 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" (PDF). Science. 269 (5229): 1402–6. doi:10.1126/science.7660122. PMID 7660122.
7. "Entrez Gene: TCEB1 transcription elongation factor B (SIII), polypeptide 1 (15kDa, elongin C)".
8. 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.
9. 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 481054. PMID 10587522.
10. 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.
11. 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.
12. 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 (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3: 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
13. 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.
14. 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.
15. Hacker KE, Lee CM, Rathmell WK (2008). 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 2583047. PMID 19030229.
16. 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 2679322. PMID 18305400.

Further reading

• Aso T, Lane WS, Conaway JW, Conaway RC (1995). "Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II". Science. 269 (5229): 1439–43. doi:10.1126/science.7660129. PMID 7660129.
• Kibel A, Iliopoulos O, DeCaprio JA, Kaelin WG (1995). "Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B and C". Science. 269 (5229): 1444–6. doi:10.1126/science.7660130. PMID 7660130.
• Bradsher JN, Jackson KW, Conaway RC, Conaway JW (1994). "RNA polymerase II transcription factor SIII. I. Identification, purification, and properties". J. Biol. Chem. 268 (34): 25587–93. PMID 8244996.
• Pause A, Lee S, Worrell RA, Chen DY, Burgess WH, Linehan WM, Klausner RD (1997). "The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins". Proc. Natl. Acad. Sci. U.S.A. 94 (6): 2156–61. doi:10.1073/pnas.94.6.2156. PMC 20057. PMID 9122164.
• Lonergan KM, Iliopoulos O, Ohh M, Kamura T, Conaway RC, Conaway JW, Kaelin WG (1998). "Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes containing elongins B/C and Cul2". Mol. Cell. Biol. 18 (2): 732–41. doi:10.1128/mcb.18.2.732. PMC 108784. PMID 9447969.
• Zhang JG, Farley A, Nicholson SE, Willson TA, Zugaro LM, Simpson RJ, Moritz RL, Cary D, Richardson R, Hausmann G, Kile BJ, Kent SB, Alexander WS, Metcalf D, Hilton DJ, Nicola NA, Baca M (1999). "The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation". Proc. Natl. Acad. Sci. U.S.A. 96 (5): 2071–6. doi:10.1073/pnas.96.5.2071. PMC 26738. PMID 10051596.
• Stebbins CE, Kaelin WG, Pavletich NP (1999). "Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function". Science. 284 (5413): 455–61. doi:10.1126/science.284.5413.455. PMID 10205047.
• Pause A, Peterson B, Schaffar G, Stearman R, Klausner RD (1999). "Studying interactions of four proteins in the yeast two-hybrid system: structural resemblance of the pVHL/elongin BC/hCUL-2 complex with the ubiquitin ligase complex SKP1/cullin/F-box protein". Proc. Natl. Acad. Sci. U.S.A. 96 (17): 9533–8. doi:10.1073/pnas.96.17.9533. PMC 22243. PMID 10449727.
• Iwai K, Yamanaka K, Kamura T, Minato N, Conaway RC, Conaway JW, Klausner RD, Pause A (1999). "Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex". Proc. Natl. Acad. Sci. U.S.A. 96 (22): 12436–41. doi:10.1073/pnas.96.22.12436. PMC 22941. PMID 10535940.
• Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B, Conaway RC, Conaway JW, Kaelin WG (2000). "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 481054. PMID 10587522.
• Aso T, Yamazaki K, Amimoto K, Kuroiwa A, Higashi H, Matsuda Y, Kitajima S, Hatakeyama M (2000). "Identification and characterization of Elongin A2, a new member of the Elongin family of transcription elongation factors, specifically expressed in the testis". J. Biol. Chem. 275 (9): 6546–52. doi:10.1074/jbc.275.9.6546. PMID 10692460.
• Adryan B, Decker HJ, Papas TS, Hsu T (2000). "Tracheal development and the von Hippel-Lindau tumor suppressor homolog in Drosophila". Oncogene. 19 (24): 2803–11. doi:10.1038/sj.onc.1203611. PMID 10851083.
• Kamura T, Sato S, Iwai K, Czyzyk-Krzeska M, Conaway RC, Conaway JW (2000). "Activation of HIF1alpha ubiquitination by a reconstituted von Hippel-Lindau (VHL) tumor suppressor complex". Proc. Natl. Acad. Sci. U.S.A. 97 (19): 10430–5. doi:10.1073/pnas.190332597. PMC 27041. PMID 10973499.
• Aso T, Yamazaki K, Aigaki T, Kitajima S (2000). "Drosophila von Hippel-Lindau tumor suppressor complex possesses E3 ubiquitin ligase activity". Biochem. Biophys. Res. Commun. 276 (1): 355–61. doi:10.1006/bbrc.2000.3451. PMID 11006129.
• Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E, Branton PE, Shilatifard A, Conaway RC, Conaway JW (2001). "Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase". J. Biol. Chem. 276 (32): 29748–53. doi:10.1074/jbc.M103093200. PMID 11384984.
• Li Z, Na X, Wang D, Schoen SR, Messing EM, Wu G (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.
• Yamazaki K, Guo L, Sugahara K, Zhang C, Enzan H, Nakabeppu Y, Kitajima S, Aso T (2002). "Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3". J. Biol. Chem. 277 (29): 26444–51. doi:10.1074/jbc.M202859200. PMID 11994304.
• Porkka K, Saramäki O, Tanner M, Visakorpi T (2002). "Amplification and overexpression of Elongin C gene discovered in prostate cancer by cDNA microarrays". Lab. Invest. 82 (5): 629–37. doi:10.1038/labinvest.3780457. PMID 12004003.