TCEB2

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Transcription elongation factor B (SIII), polypeptide 2 (18kDa, elongin B)
Protein TCEB2 PDB 1lm8.png
PDB rendering based on 1lm8.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols TCEB2 ; ELOB; SIII
External IDs OMIM600787 MGI1914923 HomoloGene38275 GeneCards: TCEB2 Gene
Orthologs
Species Human Mouse
Entrez 6923 67673
Ensembl ENSG00000103363 ENSMUSG00000055839
UniProt Q15370 P62869
RefSeq (mRNA) NM_007108 NM_026305
RefSeq (protein) NP_009039 NP_080581
Location (UCSC) Chr 16:
2.82 – 2.83 Mb
Chr 17:
23.82 – 23.83 Mb
PubMed search [1] [2]

Transcription elongation factor B polypeptide 2 is a protein that in humans is encoded by the TCEB2 gene.[1]

This gene encodes the protein elongin B, 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. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene.[2]

Interactions[edit]

TCEB2 has been shown to interact with TCEB1,[3][4][5][6] Von Hippel-Lindau tumor suppressor[4][7][8][9][10] and CUL2.[10][11]

References[edit]

  1. ^ Garrett KP, Aso T, Bradsher JN, Foundling SI, Lane WS, Conaway RC, Conaway JW (September 1995). "Positive regulation of general transcription factor SIII by a tailed ubiquitin homolog". Proc Natl Acad Sci U S A 92 (16): 7172–6. doi:10.1073/pnas.92.16.7172. PMC 41301. PMID 7638163. 
  2. ^ "Entrez Gene: TCEB2 transcription elongation factor B (SIII), polypeptide 2 (18kDa, elongin B)". 
  3. ^ Rual, Jean-François; Venkatesan Kavitha, Hao Tong, Hirozane-Kishikawa Tomoko, Dricot Amélie, Li Ning, Berriz Gabriel F, Gibbons Francis D, Dreze Matija, Ayivi-Guedehoussou Nono, Klitgord Niels, Simon Christophe, Boxem Mike, Milstein Stuart, Rosenberg Jennifer, Goldberg Debra S, Zhang Lan V, Wong Sharyl L, Franklin Giovanni, Li Siming, Albala Joanna S, Lim Janghoo, Fraughton Carlene, Llamosas Estelle, Cevik Sebiha, Bex Camille, Lamesch Philippe, Sikorski Robert S, Vandenhaute Jean, Zoghbi Huda Y, Smolyar Alex, Bosak Stephanie, Sequerra Reynaldo, Doucette-Stamm Lynn, Cusick Michael E, Hill David E, Roth Frederick P, Vidal Marc (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature (England) 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514. 
  4. ^ a b Ohh, M; Takagi Y, Aso T, Stebbins C E, Pavletich N P, Zbar B, Conaway R C, Conaway J W, Kaelin W G (Dec 1999). "Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein". J. Clin. Invest. (UNITED STATES) 104 (11): 1583–91. doi:10.1172/JCI8161. ISSN 0021-9738. PMC 481054. PMID 10587522. 
  5. ^ Aso, T; Lane W S, Conaway J W, Conaway R C (September 1995). "Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II". Science (UNITED STATES) 269 (5229): 1439–43. doi:10.1126/science.7660129. ISSN 0036-8075. PMID 7660121. 
  6. ^ Li, Zaibo; Na Xi, Wang Dakun, Schoen Susan R, Messing Edward M, Wu Guan (February 2002). "Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein". J. Biol. Chem. (United States) 277 (7): 4656–62. doi:10.1074/jbc.M108269200. ISSN 0021-9258. PMID 11739384. 
  7. ^ Ewing, Rob M; Chu Peter, Elisma Fred, Li Hongyan, Taylor Paul, Climie Shane, McBroom-Cerajewski Linda, Robinson Mark D, O'Connor Liam, Li Michael, Taylor Rod, Dharsee Moyez, Ho Yuen, Heilbut Adrian, Moore Lynda, Zhang Shudong, Ornatsky Olga, Bukhman Yury V, Ethier Martin, Sheng Yinglun, Vasilescu Julian, Abu-Farha Mohamed, Lambert Jean-Philippe, Duewel Henry S, Stewart Ian I, Kuehl Bonnie, Hogue Kelly, Colwill Karen, Gladwish Katharine, Muskat Brenda, Kinach Robert, Adams Sally-Lin, Moran Michael F, Morin Gregg B, Topaloglou Thodoros, Figeys Daniel (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. (England) 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931. 
  8. ^ Min, Jung-Hyun; Yang Haifeng, Ivan Mircea, Gertler Frank, Kaelin William G, Pavletich Nikola P (June 2002). "Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling". Science (United States) 296 (5574): 1886–9. doi:10.1126/science.1073440. PMID 12004076. 
  9. ^ Hacker, Kathryn E; Lee Caroline Martz, Rathmell W Kimryn (2008). "VHL type 2B mutations retain VBC complex form and function". In Zhang, Baohong. PLoS ONE (United States) 3 (11): e3801. doi:10.1371/journal.pone.0003801. PMC 2583047. PMID 19030229. 
  10. ^ a b Menon, Suchithra; Tsuge Tomohiko, Dohmae Naoshi, Takio Koji, Wei Ning (2008). "Association of SAP130/SF3b-3 with Cullin-RING ubiquitin ligase complexes and its regulation by the COP9 signalosome". BMC Biochem. (England) 9: 1. doi:10.1186/1471-2091-9-1. PMC 2265268. PMID 18173839. 
  11. ^ Kamura, T; Burian D, Yan Q, Schmidt S L, Lane W S, Querido E, Branton P E, Shilatifard A, Conaway R C, Conaway J W (August 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. (United States) 276 (32): 29748–53. doi:10.1074/jbc.M103093200. ISSN 0021-9258. PMID 11384984. 

Further reading[edit]