Health Dictionary
Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.
TCEB3
Introduction
Transcription elongation factor B polypeptide 3 is a protein that in humans is encoded by the TCEB3 gene.[1][2][3]
This gene encodes the protein elongin A, 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.[3]
References
References
- ↑ Aso T, Mokady N, Haque D, Conaway RC, Conaway JW (Mar 1996). “Assignment of a human gene encoding the 110-kDa subunit of general transcription factor elongin (SIII) to chromosome 1p36.1”. Genomics. 30 (2): 393–4. PMID 8586449.
- ↑ Aso T, Lane WS, Conaway JW, Conaway RC (Oct 1995). “Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II”. Science. 269 (5229): 1439–43. doi:10.1126/science.7660129. PMID 7660129.
- ↑ 3.0 3.1 “Entrez Gene: TCEB3 transcription elongation factor B (SIII), polypeptide 3 (110kDa, elongin A)”.
Further reading
Further reading
- Shilatifard A (1998). “Factors regulating the transcriptional elongation activity of RNA polymerase II”. FASEB J. 12 (14): 1437–46. PMID 9806752.
- Kile BT, Schulman BA, Alexander WS, et al. (2002). “The SOCS box: a tale of destruction and degradation”. Trends Biochem. Sci. 27 (5): 235–41. doi:10.1016/S0968-0004(02)02085-6. PMID 12076535.
- Aso T, Haque D, Fukudome K, et al. (1996). “A human cDNA encoding the 110-kDa A subunit of RNA polymerase II transcription factor elongin”. Gene. 168 (2): 277–8. doi:10.1016/0378-1119(95)00750-4. PMID 8654961.
- Pan G, Aso T, Greenblatt J (1997). “Interaction of elongation factors TFIIS and elongin A with a human RNA polymerase II holoenzyme capable of promoter-specific initiation and responsive to transcriptional activators”. J. Biol. Chem. 272 (39): 24563–71. doi:10.1074/jbc.272.39.24563. PMID 9305922.
- Ohh M, Takagi Y, Aso T, et al. (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.
- Kamura T, Burian D, Yan Q, et al. (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.
- Shaheduzzaman S, Krishnan V, Petrovic A, et al. (2002). “Effects of HIV-1 Nef on cellular gene expression profiles”. J. Biomed. Sci. 9 (1): 82–96. doi:10.1007/BF02256581. PMID 11810028.
- Yamazaki K, Guo L, Sugahara K, et al. (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.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2003). “Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences”. Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Tamura K, Miyata K, Sugahara K, et al. (2003). “Identification of EloA-BP1, a novel Elongin A binding protein with an exonuclease homology domain”. Biochem. Biophys. Res. Commun. 309 (1): 189–95. doi:10.1016/S0006-291X(03)01556-0. PMID 12943681.
- Stoletov KV, Terman BI (2004). “Bmx is a downstream Rap1 effector in VEGF-induced endothelial cell activation”. Biochem. Biophys. Res. Commun. 320 (1): 70–5. doi:10.1016/j.bbrc.2004.05.134. PMID 15207703.
- Beausoleil SA, Jedrychowski M, Schwartz D, et al. (2004). “Large-scale characterization of HeLa cell nuclear phosphoproteins”. Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130–5. doi:10.1073/pnas.0404720101. PMC 514446. PMID 15302935.
- Gerhard DS, Wagner L, Feingold EA, et al. (2004). “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)”. Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Andersen JS, Lam YW, Leung AK, et al. (2005). “Nucleolar proteome dynamics”. Nature. 433 (7021): 77–83. doi:10.1038/nature03207. PMID 15635413.
- Rual JF, Venkatesan K, Hao T, et al. (2005). “Towards a proteome-scale map of the human protein-protein interaction network”. Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID 16189514.
- Woo JS, Imm JH, Min CK, et al. (2006). “Structural and functional insights into the B30.2/SPRY domain”. EMBO J. 25 (6): 1353–63. doi:10.1038/sj.emboj.7600994. PMC 1422157. PMID 16498413.