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ELOC

From Wikipedia, the free encyclopedia

ELOC
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesELOC, SIII, eloC, TCEB1, transcription elongation factor B subunit 1, elongin C
External IDsOMIM: 600788; MGI: 1915173; HomoloGene: 38083; GeneCards: ELOC; OMA:ELOC - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001310470
NM_026456

RefSeq (protein)

NP_001297399
NP_080732

Location (UCSC)Chr 8: 73.94 – 73.97 MbChr 1: 16.71 – 16.73 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Elongin C is a protein that in humans is encoded by the ELOC gene.[5][6]

Function

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Elongin C 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

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TCEB1 has been shown to interact with:

References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000154582Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000079658Ensembl, 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". Science. 269 (5229): 1402–6. Bibcode:1995Sci...269.1402D. doi:10.1126/science.7660122. PMID 7660122. S2CID 22334719.
  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. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  9. ^ 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 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. Bibcode:1995Sci...269.1400K. doi:10.1126/science.7660121. PMID 7660121. S2CID 39758696.
  11. ^ 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.
  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. Bibcode:2002Sci...296.1886M. doi:10.1126/science.1073440. PMID 12004076. S2CID 19641938.
  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. Bibcode:2008PLoSO...3.3801H. 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

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