TCEB3: Difference between revisions
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| | '''Transcription elongation factor B polypeptide 3''' is a [[protein]] that in humans is encoded by the ''TCEB3'' [[gene]].<ref name="pmid8586449">{{cite journal | vauthors = Aso T, Mokady N, Haque D, Conaway RC, Conaway JW | title = Assignment of a human gene encoding the 110-kDa subunit of general transcription factor elongin (SIII) to chromosome 1p36.1 | journal = Genomics | volume = 30 | issue = 2 | pages = 393–4 |date=Mar 1996 | pmid = 8586449 | pmc = | doi = }}</ref><ref name="pmid7660129">{{cite journal | vauthors = Aso T, Lane WS, Conaway JW, Conaway RC | title = Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II | journal = Science | volume = 269 | issue = 5229 | pages = 1439–43 |date=Oct 1995 | pmid = 7660129 | pmc = | doi =10.1126/science.7660129 }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: TCEB3 transcription elongation factor B (SIII), polypeptide 3 (110kDa, elongin A)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6924| accessdate = }}</ref> | ||
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| summary_text = 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.<ref name="entrez" | | summary_text = 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.<ref name="entrez" /> | ||
}} | }} | ||
==References== | ==References== | ||
{{reflist | {{reflist}} | ||
==Further reading== | ==Further reading== | ||
{{refbegin | 2}} | {{refbegin | 2}} | ||
{{PBB_Further_reading | {{PBB_Further_reading | ||
| citations = | | citations = | ||
*{{cite journal | author=Shilatifard A |title=Factors regulating the transcriptional elongation activity of RNA polymerase II | *{{cite journal | author=Shilatifard A |title=Factors regulating the transcriptional elongation activity of RNA polymerase II |journal=FASEB J. |volume=12 |issue= 14 |pages= 1437–46 |year= 1998 |pmid= 9806752 |doi= }} | ||
*{{cite journal | *{{cite journal |vauthors=Kile BT, Schulman BA, Alexander WS, etal |title=The SOCS box: a tale of destruction and degradation |journal=Trends Biochem. Sci. |volume=27 |issue= 5 |pages= 235–41 |year= 2002 |pmid= 12076535 |doi=10.1016/S0968-0004(02)02085-6 }} | ||
*{{cite journal |vauthors=Aso T, Haque D, Fukudome K, etal |title=A human cDNA encoding the 110-kDa A subunit of RNA polymerase II transcription factor elongin |journal=Gene |volume=168 |issue= 2 |pages= 277–8 |year= 1996 |pmid= 8654961 |doi=10.1016/0378-1119(95)00750-4 }} | |||
*{{cite journal | vauthors=Pan G, Aso T, Greenblatt J |title=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 |journal=J. Biol. Chem. |volume=272 |issue= 39 |pages= 24563–71 |year= 1997 |pmid= 9305922 |doi=10.1074/jbc.272.39.24563 }} | |||
*{{cite journal | *{{cite journal |vauthors=Ohh M, Takagi Y, Aso T, etal |title=Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein |journal=J. Clin. Invest. |volume=104 |issue= 11 |pages= 1583–91 |year= 2000 |pmid= 10587522 |doi=10.1172/JCI8161 | pmc=481054 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Kamura T, Burian D, Yan Q, etal |title=Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase |journal=J. Biol. Chem. |volume=276 |issue= 32 |pages= 29748–53 |year= 2001 |pmid= 11384984 |doi= 10.1074/jbc.M103093200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Shaheduzzaman S, Krishnan V, Petrovic A, etal |title=Effects of HIV-1 Nef on cellular gene expression profiles |journal=J. Biomed. Sci. |volume=9 |issue= 1 |pages= 82–96 |year= 2002 |pmid= 11810028 |doi=10.1007/BF02256581 }} | ||
*{{cite journal | *{{cite journal |vauthors=Yamazaki K, Guo L, Sugahara K, etal |title=Identification and biochemical characterization of a novel transcription elongation factor, Elongin A3 |journal=J. Biol. Chem. |volume=277 |issue= 29 |pages= 26444–51 |year= 2002 |pmid= 11994304 |doi= 10.1074/jbc.M202859200 }} | ||
*{{cite journal | *{{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }} | ||
*{{cite journal | *{{cite journal |vauthors=Tamura K, Miyata K, Sugahara K, etal |title=Identification of EloA-BP1, a novel Elongin A binding protein with an exonuclease homology domain |journal=Biochem. Biophys. Res. Commun. |volume=309 |issue= 1 |pages= 189–95 |year= 2003 |pmid= 12943681 |doi=10.1016/S0006-291X(03)01556-0 }} | ||
*{{cite journal | *{{cite journal | vauthors=Stoletov KV, Terman BI |title=Bmx is a downstream Rap1 effector in VEGF-induced endothelial cell activation |journal=Biochem. Biophys. Res. Commun. |volume=320 |issue= 1 |pages= 70–5 |year= 2004 |pmid= 15207703 |doi= 10.1016/j.bbrc.2004.05.134 }} | ||
*{{cite journal | *{{cite journal |vauthors=Beausoleil SA, Jedrychowski M, Schwartz D, etal |title=Large-scale characterization of HeLa cell nuclear phosphoproteins |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=101 |issue= 33 |pages= 12130–5 |year= 2004 |pmid= 15302935 |doi= 10.1073/pnas.0404720101 | pmc=514446 }} | ||
*{{cite journal | | *{{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }} | ||
*{{cite journal | *{{cite journal |vauthors=Andersen JS, Lam YW, Leung AK, etal |title=Nucleolar proteome dynamics |journal=Nature |volume=433 |issue= 7021 |pages= 77–83 |year= 2005 |pmid= 15635413 |doi= 10.1038/nature03207 }} | ||
*{{cite journal | *{{cite journal |vauthors=Rual JF, Venkatesan K, Hao T, etal |title=Towards a proteome-scale map of the human protein-protein interaction network |journal=Nature |volume=437 |issue= 7062 |pages= 1173–8 |year= 2005 |pmid= 16189514 |doi= 10.1038/nature04209 }} | ||
*{{cite journal | *{{cite journal |vauthors=Woo JS, Imm JH, Min CK, etal |title=Structural and functional insights into the B30.2/SPRY domain |journal=EMBO J. |volume=25 |issue= 6 |pages= 1353–63 |year= 2006 |pmid= 16498413 |doi= 10.1038/sj.emboj.7600994 | pmc=1422157 }} | ||
*{{cite journal | |||
*{{cite journal | |||
}} | }} | ||
{{refend}} | {{refend}} | ||
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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
- ↑ 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
- 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.
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