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<!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. -->
{{Infobox_gene}}
{{PBB_Controls
'''DNA-directed RNA polymerase II subunit RPB3''' is an [[enzyme]] that in humans is encoded by the ''POLR2C'' [[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>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image =
| image_source =
| PDB =
| Name = Polymerase (RNA) II (DNA directed) polypeptide C, 33kDa
| HGNCid = 9189
| Symbol = POLR2C
| AltSymbols =; RPB3; RPB31; hRPB33; hsRPB3
| OMIM = 180663
| ECnumber = 
| Homologene = 2017
| MGIid = 109299
| GeneAtlas_image1 = PBB_GE_POLR2C_208996_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_POLR2C_214263_x_at_tn.png
| GeneAtlas_image3 = PBB_GE_POLR2C_216282_x_at_tn.png
| Function = {{GNF_GO|id=GO:0003677 |text = DNA binding}} {{GNF_GO|id=GO:0003899 |text = DNA-directed RNA polymerase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0046983 |text = protein dimerization activity}}
| Component = {{GNF_GO|id=GO:0005634 |text = nucleus}} {{GNF_GO|id=GO:0005665 |text = DNA-directed RNA polymerase II, core complex}} {{GNF_GO|id=GO:0005737 |text = cytoplasm}}
| Process = {{GNF_GO|id=GO:0006350 |text = transcription}} {{GNF_GO|id=GO:0006366 |text = transcription from RNA polymerase II promoter}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 5432
    | Hs_Ensembl = ENSG00000102978
    | Hs_RefseqProtein = NP_116558
    | Hs_RefseqmRNA = NM_032940
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 16
    | Hs_GenLoc_start = 56054080
    | Hs_GenLoc_end = 56063422
    | Hs_Uniprot = P19387
    | Mm_EntrezGene = 20021
    | Mm_Ensembl = 
    | Mm_RefseqmRNA = XM_977880
    | Mm_RefseqProtein = XP_982974
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 
    | Mm_GenLoc_start = 
    | Mm_GenLoc_end = 
    | Mm_Uniprot =
  }}
}}
'''Polymerase (RNA) II (DNA directed) polypeptide C, 33kDa''', also known as '''POLR2C''', is a human [[gene]].


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
This gene encodes the third largest subunit of [[RNA polymerase II]], the polymerase responsible for synthesizing messenger [[RNA]] in eukaryotes. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, [[POLR2J]]. These two subunits form a core subassembly unit of the polymerase. A [[pseudogene]] has been identified on chromosome 21.<ref>{{cite web | title = Entrez Gene: POLR2C polymerase (RNA) II (DNA directed) polypeptide C, 33kDa| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5432| accessdate = }}</ref>
{{PBB_Summary
| section_title =
| summary_text = This gene encodes the third largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J. These two subunits form a core subassembly unit of the polymerase. A pseudogene has been identified on chromosome 21.<ref>{{cite web | title = Entrez Gene: POLR2C polymerase (RNA) II (DNA directed) polypeptide C, 33kDa| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5432| accessdate = }}</ref>
}}


==References==
== Interactions ==
{{reflist|2}}
POLR2C has been shown to [[Protein-protein interaction|interact]] with:
==Further reading==
{{div col|colwidth=20em}}
* [[ATF4]],<ref name = pmid12860379>{{cite journal | vauthors = De Angelis R, Iezzi S, Bruno T, Corbi N, Di Padova M, Floridi A, Fanciulli M, Passananti C | title = Functional interaction of the subunit 3 of RNA polymerase II (RPB3) with transcription factor-4 (ATF4) | journal = FEBS Lett. | volume = 547 | issue = 1–3 | pages = 15–9 | date = Jul 2003 | pmid = 12860379 | doi =  10.1016/s0014-5793(03)00659-8}}</ref>
* [[CCHCR1]],<ref name = pmid16141233>{{cite journal | vauthors = Corbi N, Bruno T, De Angelis R, Di Padova M, Libri V, Di Certo MG, Spinardi L, Floridi A, Fanciulli M, Passananti C | title = RNA polymerase II subunit 3 is retained in the cytoplasm by its interaction with HCR, the psoriasis vulgaris candidate gene product | journal = J. Cell Sci. | volume = 118 | issue = Pt 18 | pages = 4253–60 | date = Sep 2005 | pmid = 16141233 | doi = 10.1242/jcs.02545 }}</ref>
* [[Myogenin]],<ref name = pmid12207009/>
* [[POLR2A]],<ref name = pmid9201987/>
* [[POLR2B]],<ref name = pmid9201987/>
* [[POLR2E]]<ref name = pmid9201987/> and
* [[POLR2F]],<ref name = pmid9201987>{{cite journal | vauthors = Acker J, de Graaff M, Cheynel I, Khazak V, Kedinger C, Vigneron M | title = Interactions between the human RNA polymerase II subunits | journal = J. Biol. Chem. | volume = 272 | issue = 27 | pages = 16815–21 | date = Jul 1997 | pmid = 9201987 | doi =  10.1074/jbc.272.27.16815}}</ref>
* [[POLR2G]],<ref name = pmid9201987/>
* [[POLR2H]],<ref name = pmid9201987/>
* [[POLR2J]],<ref name = pmid12207009>{{cite journal | vauthors = Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C | title = The alpha-like RNA polymerase II core subunit 3 (RPB3) is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor myogenin | journal = FASEB J. | volume = 16 | issue = 12 | pages = 1639–41 | date = Oct 2002 | pmid = 12207009 | doi = 10.1096/fj.02-0123fje }}</ref><ref name = pmid9201987/>
* [[POLR2K]],<ref name = pmid9201987/>
* [[POLR2L]],<ref name = pmid9201987/>  and
* [[TAF15]].<ref name = pmid9488465>{{cite journal | vauthors = Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L | 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 | date = Mar 1998 | pmid = 9488465 | pmc = 108863 | doi =  10.1128/mcb.18.3.1489}}</ref>
{{Div col end}}
 
== References ==
{{reflist}}
 
== Further reading ==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading
* {{cite journal | vauthors = 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 }}
| citations =
* {{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 | 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= }}
* {{cite journal | vauthors = Romano G, Kasten M, De Falco G, Micheli P, Khalili K, Giordano A | 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 | author=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= }}
* {{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 | author=Romano G, Kasten M, De Falco G, ''et al.'' |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= }}
* {{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 | author=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= }}
* {{cite journal | vauthors = Harrich D, McMillan N, Munoz L, Apolloni A, Meredith L | 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 | author=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 = Kato H, Sumimoto H, Pognonec P, Chen CH, Rosen CA, Roeder RG | 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 | author=Harrich D, McMillan N, Munoz L, ''et al.'' |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= }}
* {{cite journal | vauthors = Pati UK, Weissman SM | title = The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB 33 is highly conserved among eukaryotes. | journal = J. Biol. Chem. | volume = 265 | issue = 15 | pages = 8400–3 | year = 1990 | pmid = 2187864 | doi =  }}
*{{cite journal | author=Kato H, Sumimoto H, Pognonec P, ''et al.'' |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= }}
* {{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 }}
*{{cite journal | author=Pati UK, Weissman SM |title=The amino acid sequence of the human RNA polymerase II 33-kDa subunit hRPB 33 is highly conserved among eukaryotes. |journal=J. Biol. Chem. |volume=265 |issue= 15 |pages= 8400-3 |year= 1990 |pmid= 2187864 |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 | pmc = 41297 | doi = 10.1073/pnas.92.16.7153 }}
*{{cite journal | author=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 }}
* {{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 | pmc = 188757 | doi =  }}
*{{cite journal | author=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= }}
* {{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 | pmc = 39827 | doi = 10.1073/pnas.93.6.2505 }}
*{{cite journal | author=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=  }}
* {{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 | pmc = 190394 | doi =  }}
*{{cite journal | author=Acker J, Mattei MG, Wintzerith M, ''et al.'' |title=Chromosomal localization of human RNA polymerase II subunit genes. |journal=Genomics |volume=20 |issue= 3 |pages= 496-9 |year= 1994 |pmid= 8034326 |doi= 10.1006/geno.1994.1208 }}
* {{cite journal | vauthors = Agostini I, Navarro JM, Rey F, Bouhamdan M, Spire B, Vigne R, Sire J | 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 | author=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=  }}
* {{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 }}
*{{cite journal | author=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= }}
* {{cite journal | vauthors = Okamoto H, Sheline CT, Corden JL, Jones KA, Peterlin BM | 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 | pmc = 38099 | doi = 10.1073/pnas.93.21.11575 }}
*{{cite journal | author=Agostini I, Navarro JM, Rey F, ''et al.'' |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 = 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 }}
*{{cite journal | author=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= }}
* {{cite journal | vauthors = Parada CA, Roeder RG | title = Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. | journal = Nature | volume = 384 | issue = 6607 | pages = 375–8 | year = 1996 | pmid = 8934526 | doi = 10.1038/384375a0 }}
*{{cite journal | author=Okamoto H, Sheline CT, Corden JL, ''et al.'' |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= }}
* {{cite journal | vauthors = García-Martínez LF, Ivanov D, Gaynor RB | title = Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. | journal = J. Biol. Chem. | volume = 272 | issue = 11 | pages = 6951–8 | year = 1997 | pmid = 9054383 | doi = 10.1074/jbc.272.11.6951 }}
*{{cite journal | author=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= }}
*{{cite journal | author=Parada CA, Roeder RG |title=Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain. |journal=Nature |volume=384 |issue= 6607 |pages= 375-8 |year= 1996 |pmid= 8934526 |doi= 10.1038/384375a0 }}
*{{cite journal  | author=García-Martínez LF, Ivanov D, Gaynor RB |title=Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes. |journal=J. Biol. Chem. |volume=272 |issue= 11 |pages= 6951-8 |year= 1997 |pmid= 9054383 |doi=  }}
}}
{{refend}}
{{refend}}


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Latest revision as of 09:14, 10 January 2019

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

DNA-directed RNA polymerase II subunit RPB3 is an enzyme that in humans is encoded by the POLR2C gene.[1]

Function

This gene encodes the third largest subunit of RNA polymerase II, the polymerase responsible for synthesizing messenger RNA in eukaryotes. The product of this gene contains a cysteine rich region and exists as a heterodimer with another polymerase subunit, POLR2J. These two subunits form a core subassembly unit of the polymerase. A pseudogene has been identified on chromosome 21.[2]

Interactions

POLR2C has been shown to interact with:

References

  1. ↑ Acker J, Mattei MG, Wintzerith M, Roeckel N, Depetris D, Vigneron M, Kedinger C (Aug 1994). "Chromosomal localization of human RNA polymerase II subunit genes". Genomics. 20 (3): 496–9. doi:10.1006/geno.1994.1208. PMID 8034326.
  2. ↑ "Entrez Gene: POLR2C polymerase (RNA) II (DNA directed) polypeptide C, 33kDa".
  3. ↑ De Angelis R, Iezzi S, Bruno T, Corbi N, Di Padova M, Floridi A, Fanciulli M, Passananti C (Jul 2003). "Functional interaction of the subunit 3 of RNA polymerase II (RPB3) with transcription factor-4 (ATF4)". FEBS Lett. 547 (1–3): 15–9. doi:10.1016/s0014-5793(03)00659-8. PMID 12860379.
  4. ↑ Corbi N, Bruno T, De Angelis R, Di Padova M, Libri V, Di Certo MG, Spinardi L, Floridi A, Fanciulli M, Passananti C (Sep 2005). "RNA polymerase II subunit 3 is retained in the cytoplasm by its interaction with HCR, the psoriasis vulgaris candidate gene product". J. Cell Sci. 118 (Pt 18): 4253–60. doi:10.1242/jcs.02545. PMID 16141233.
  5. ↑ 5.0 5.1 Corbi N, Di Padova M, De Angelis R, Bruno T, Libri V, Iezzi S, Floridi A, Fanciulli M, Passananti C (Oct 2002). "The alpha-like RNA polymerase II core subunit 3 (RPB3) is involved in tissue-specific transcription and muscle differentiation via interaction with the myogenic factor myogenin". FASEB J. 16 (12): 1639–41. doi:10.1096/fj.02-0123fje. PMID 12207009.
  6. ↑ 6.0 6.1 6.2 6.3 6.4 6.5 6.6 6.7 6.8 Acker J, de Graaff M, Cheynel I, Khazak V, Kedinger C, Vigneron M (Jul 1997). "Interactions between the human RNA polymerase II subunits". J. Biol. Chem. 272 (27): 16815–21. doi:10.1074/jbc.272.27.16815. PMID 9201987.
  7. ↑ Bertolotti A, Melot T, Acker J, Vigneron M, Delattre O, Tora L (Mar 1998). "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". Mol. Cell. Biol. 18 (3): 1489–97. doi:10.1128/mcb.18.3.1489. PMC 108863. PMID 9488465.

Further reading


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