View source for POLR2E

{{Infobox_gene}}
'''DNA-directed RNA polymerases I, II, and III subunit RPABC1''' is a [[protein]] that in humans is encoded by the ''POLR2E'' [[gene]].<ref name="pmid8034326">{{cite journal |vauthors=Acker J, Mattei MG, Wintzerith M, Roeckel N, Depetris D, Vigneron M, Kedinger C | title = Chromosomal localization of human RNA polymerase II subunit genes | journal = Genomics | volume = 20 | issue = 3 | pages = 496–9 |date=Aug 1994 | pmid = 8034326 | pmc =  | doi = 10.1006/geno.1994.1208 }}</ref>

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{{PBB_Summary
| section_title = 
| summary_text = This gene encodes the fifth largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. This subunit is shared by the other two DNA-directed RNA polymerases and is present in two-fold molar excess over the other polymerase subunits. An interaction between this subunit and a hepatitis virus transactivating protein has been demonstrated, suggesting that interaction between transcriptional activators and the polymerase can occur through this subunit. A pseudogene is located on chromosome 11.<ref>{{cite web | title = Entrez Gene: POLR2E polymerase (RNA) II (DNA directed) polypeptide E, 25kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5434| accessdate = }}</ref>
}}

==Interactions==
POLR2E has been shown to [[Protein-protein interaction|interact]] with [[TAF15]],<ref name=pmid9488465>{{cite journal |last=Bertolotti |first=A |authorlink= |author2=Melot T |author3=Acker J |author4=Vigneron M |author5=Delattre O |author6=Tora L  |date=Mar 1998 |title=EWS, but not EWS-FLI-1, is associated with both TFIID and RNA polymerase II: interactions between two members of the TET family, EWS and hTAFII68, and subunits of TFIID and RNA polymerase II complexes |journal=Mol. Cell. Biol. |volume=18 |issue=3 |pages=1489–97 |publisher= |location = UNITED STATES| issn = 0270-7306| pmid = 9488465 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = |pmc=108863 | doi=10.1128/mcb.18.3.1489}}</ref> [[POLR2C]],<ref name=pmid9201987>{{cite journal |doi=10.1074/jbc.272.27.16815 |last=Acker |first=J |authorlink= |author2=de Graaff M |author3=Cheynel I |author4=Khazak V |author5=Kedinger C |author6=Vigneron M  |date=Jul 1997 |title=Interactions between the human RNA polymerase II subunits |journal=J. Biol. Chem. |volume=272 |issue=27 |pages=16815–21 |publisher= |location = UNITED STATES| issn = 0021-9258| pmid = 9201987 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref> [[POLR2G]],<ref name=pmid9201987/> [[POLR2H]],<ref name=pmid9201987/> [[POLR2A]],<ref name=pmid9201987/> [[POLR2B]],<ref name=pmid9201987/> [[POLR2L]]<ref name=pmid9201987/> and [[GTF2F2]].<ref name=pmid11278533>{{cite journal |last=Wei |first=W |authorlink= |author2=Dorjsuren D |author3=Lin Y |author4=Qin W |author5=Nomura T |author6=Hayashi N |author7=Murakami S  |date=Apr 2001 |title=Direct interaction between the subunit RAP30 of transcription factor IIF (TFIIF) and RNA polymerase subunit 5, which contributes to the association between TFIIF and RNA polymerase II |journal=J. Biol. Chem. |volume=276 |issue=15 |pages=12266–73 |publisher= |location = United States| issn = 0021-9258| pmid = 11278533 |doi = 10.1074/jbc.M009634200 | bibcode = | oclc =| id = | url = | language = | format = | accessdate = | laysummary = | laysource = | laydate = | quote = }}</ref>

==References==
{{reflist}}

==Further reading==
{{refbegin | 2}}
{{PBB_Further_reading 
| citations = 
*{{cite journal  | author=Jeang KT |title=Tat, Tat-associated kinase, and transcription. |journal=J. Biomed. Sci. |volume=5 |issue= 1 |pages= 24–7 |year= 1998 |pmid= 9570510 |doi=10.1007/BF02253352  }}
*{{cite journal  |vauthors=Yankulov K, Bentley D |title=Transcriptional control: Tat cofactors and transcriptional elongation. |journal=Curr. Biol. |volume=8 |issue= 13 |pages= R447–9 |year= 1998 |pmid= 9651670 |doi=10.1016/S0960-9822(98)70289-1  }}
*{{cite journal   |vauthors=Romano G, Kasten M, De Falco G, etal |title=Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression. |journal=J. Cell. Biochem. |volume=75 |issue= 3 |pages= 357–68 |year= 2000 |pmid= 10536359 |doi=10.1002/(SICI)1097-4644(19991201)75:3<357::AID-JCB1>3.0.CO;2-K  }}
*{{cite journal  |vauthors=Marcello A, Zoppé M, Giacca M |title=Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator. |journal=IUBMB Life |volume=51 |issue= 3 |pages= 175–81 |year= 2002 |pmid= 11547919 |doi=10.1080/152165401753544241  }}
*{{cite journal  |vauthors=Stevens M, De Clercq E, Balzarini J |title=The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention. |journal=Med Res Rev |volume=26 |issue= 5 |pages= 595–625 |year= 2007 |pmid= 16838299 |doi= 10.1002/med.20081 }}
*{{cite journal   |vauthors=Harrich D, McMillan N, Munoz L, etal |title=Will diverse Tat interactions lead to novel antiretroviral drug targets? |journal=Current drug targets |volume=7 |issue= 12 |pages= 1595–606 |year= 2007 |pmid= 17168834 |doi=10.2174/138945006779025338  }}
*{{cite journal   |vauthors=Kato H, Sumimoto H, Pognonec P, etal |title=HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors. |journal=Genes Dev. |volume=6 |issue= 4 |pages= 655–66 |year= 1992 |pmid= 1559613 |doi=10.1101/gad.6.4.655  }}
*{{cite journal  |vauthors=Pati UK, Weissman SM |title=Isolation and molecular characterization of a cDNA encoding the 23-kDa subunit of human RNA polymerase II. |journal=J. Biol. Chem. |volume=266 |issue= 20 |pages= 13468 |year= 1991 |pmid= 2071613 |doi=  }}
*{{cite journal  |vauthors=Southgate C, Zapp ML, Green MR |title=Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein. |journal=Nature |volume=345 |issue= 6276 |pages= 640–2 |year= 1990 |pmid= 2190099 |doi= 10.1038/345640a0 |bibcode=1990Natur.345..640S }}
*{{cite journal  |vauthors=Pati UK, Weissman SM |title=Isolation and molecular characterization of a cDNA encoding the 23-kDa subunit of human RNA polymerase II. |journal=J. Biol. Chem. |volume=264 |issue= 22 |pages= 13114–21 |year= 1989 |pmid= 2753903 |doi=  }}
*{{cite journal  |vauthors=Wu-Baer F, Sigman D, Gaynor RB |title=Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=92 |issue= 16 |pages= 7153–7 |year= 1995 |pmid= 7638159 |doi=10.1073/pnas.92.16.7153  | pmc=41297  |bibcode=1995PNAS...92.7153W }}
*{{cite journal  |vauthors=Cheong JH, Yi M, Lin Y, Murakami S |title=Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds human hepatitis B virus X protein and may play a role in X transactivation. |journal=EMBO J. |volume=14 |issue= 1 |pages= 143–50 |year= 1995 |pmid= 7828586 |doi=  | pmc=398061  }}
*{{cite journal  |vauthors=Herrmann CH, Rice AP |title=Lentivirus Tat proteins specifically associate with a cellular protein kinase, TAK, that hyperphosphorylates the carboxyl-terminal domain of the large subunit of RNA polymerase II: candidate for a Tat cofactor. |journal=J. Virol. |volume=69 |issue= 3 |pages= 1612–20 |year= 1995 |pmid= 7853496 |doi=  | pmc=188757  }}
*{{cite journal  |vauthors=Keen NJ, Gait MJ, Karn J |title=Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 6 |pages= 2505–10 |year= 1996 |pmid= 8637904 |doi=10.1073/pnas.93.6.2505  | pmc=39827  |bibcode=1996PNAS...93.2505K }}
*{{cite journal  |vauthors=Yang X, Herrmann CH, Rice AP |title=The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function. |journal=J. Virol. |volume=70 |issue= 7 |pages= 4576–84 |year= 1996 |pmid= 8676484 |doi=  | pmc=190394  }}
*{{cite journal   |vauthors=Agostini I, Navarro JM, Rey F, etal |title=The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB. |journal=J. Mol. Biol. |volume=261 |issue= 5 |pages= 599–606 |year= 1996 |pmid= 8800208 |doi= 10.1006/jmbi.1996.0485 }}
*{{cite journal  |vauthors=Zhou Q, Sharp PA |title=Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat. |journal=Science |volume=274 |issue= 5287 |pages= 605–10 |year= 1996 |pmid= 8849451 |doi=10.1126/science.274.5287.605  |bibcode=1996Sci...274..605Z }}
*{{cite journal   |vauthors=Okamoto H, Sheline CT, Corden JL, etal |title=Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=93 |issue= 21 |pages= 11575–9 |year= 1996 |pmid= 8876177 |doi=10.1073/pnas.93.21.11575  | pmc=38099  |bibcode=1996PNAS...9311575O }}
*{{cite journal  |vauthors=Chun RF, Jeang KT |title=Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1. |journal=J. Biol. Chem. |volume=271 |issue= 44 |pages= 27888–94 |year= 1996 |pmid= 8910388 |doi=10.1074/jbc.271.44.27888  }}
}}
{{refend}}

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