Home POLR2L
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Regions Overlapping this Feature:
Mouse: 1
Linkage Regions: 1 Available
Linkage Regions: 1 Available
| Locus | Species | Chromosomal Location | Mb | Number of genes | Linkage and Congenic Studies |
|---|---|---|---|---|---|
| Idd13 | Mouse | chr2:114118625..158330390 | 44.21 | 582 | 3 no lod score |
(Human) GRCh37 - chr11:837356..842545 (5.19 kb) View in Genome Browser
(Mouse) NCBIM37 - chr2:126534921..126535293 (372 bp) View in Genome Browser
(Rat) RGSC3.4 - chr4:985235..985438 (203 bp) View in Genome Browser
HaemAtlas Expression Table for POLR2L:|
Expression Legend
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Cell Types Showing Expression: Available
Users should be aware that the scale represents a rank within an experiment rather than a normalized expression signal.
| Human | Mouse | Rat | ||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|
| ductal cells | exocrine pancreas | pancreatic islets | primary beta cells | Pancreatic Islets MPSS | beta cell line | pancreatic islets | whole pancreas | alpha cell | beta cell line | pancreatic islets | primary beta cells | whole pancreas |
| no data | no data | no data | no data | no data | no data | no data | no data | |||||
Expression Legend
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The Beta Cell Gene Atlas is a collection of almost all available public microarray data generated with pancreatic beta cells and related cell lines and types. The expression data comes from 131 array analyses derived from 28 experiments (open details in a new window). The basal (untreated cell) expression signal intensity values in each array were converted to ranks within the experiments; the highest value was used for genes represented by more than one probe. The rank values of genes in a given cell type were averaged with other calculated values from experiments performed with the same cell type. The rank transformation of the expression values enable comparison of gene expression across different organisms and tissues.
A red border around a cell indicates greater certainty in the data; specifically, the gene has >0.95 probability of being expressed in the tissue.
Tissues Showing Expression: Available
| Users should be aware that the scale represents a rank within an experiment rather than a normalized expression signal. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Expression Legend
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| Signal intensity values were converted to ranks within the experiments. For genes represented by more than one probeset, we averaged the intensity signals for each probeset across all tissues and chose the probeset with the highest average value. The rank transformation of the expression values enables comparison of gene expression across different organisms and tissues. | |||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Interactions Table for POLR2L:The POLR2L interactions are shown below. Each row lists the two interactors, the sources which document this as an interaction, a classification of the interaction as empirical or predicted, and Pubmed IDs (if any) for the interaction.
The table of interactions is downloadable as a text file. Please note that the text file will not include data from HPRD due to restrictions imposed by the HPRD funding sources.
| Interactor | Interactor | Sources | Classification | Pubmed IDs |
| POLR2L | CCDC85B | HPRD, MINT, IntAct, BioGRID | empirical | 16189514 |
| POLR2L | POLR3A | Reactome | predicted | |
| POLR2L | CHEK2 | IntAct | empirical | 21988832 |
| POLR2L | MED19 | IntAct, BioGRID | empirical | 15175163 21729782 |
| POLR2L | RPL13A | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | POLR1A | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | INTS6 | BioGRID | empirical | 20133760 |
| POLR2L | MRPL13 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | ZNRD1 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | MVK | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | NFKBIB | HPRD, MINT, IntAct | empirical | 14743216 |
| POLR2L | NOV | HPRD, BioGRID | empirical | 10474687 |
| POLR2L | MEMO1 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | POLR1D | Reactome | predicted | |
| POLR2L | MRPS2 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | SNX7 | IntAct | empirical | 21988832 |
| POLR2L | POLR3K | Reactome | predicted | |
| POLR2L | POLR2A | HPRD, BioGRID, Reactome | empirical | 9201987 |
| POLR2L | POLR2B | HPRD, BioGRID, Reactome | empirical | 9201987 |
| POLR2L | POLR2C | HPRD, BioGRID, Reactome, Sanger Interaction Map | empirical | 10567706 9201987 15345047 |
| POLR2L | POLR2D | HPRD, IntAct, Reactome | empirical | 10567706 21988832 |
| POLR2L | POLR2E | HPRD, BioGRID, Reactome, Sanger Interaction Map | empirical | 9201987 15345047 |
| POLR2L | POLR2F | Reactome, Sanger Interaction Map | predicted | 15345047 |
| POLR2L | POLR2G | BioGRID, Reactome | empirical | 9201987 |
| POLR2L | POLR2H | HPRD, BioGRID, Reactome, Sanger Interaction Map | empirical | 9201987 15345047 |
| POLR2L | POLR2I | Reactome | predicted | |
| POLR2L | POLR2J | Reactome | predicted | |
| POLR2L | POLR2K | Reactome | predicted | |
| POLR2L | IMP3 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | MED29 | IntAct, BioGRID | empirical | 15175163 |
| POLR2L | POLR3B | Reactome | predicted | |
| POLR2L | EXOSC5 | HPRD | empirical | 15231747 |
| POLR2L | RPL18 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | RPS9 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | RPS14 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | RPS16 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | RPS18 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | MRPS9 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | SMARCD1 | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | UBC | BioGRID | empirical | 21139048 21906983 |
| POLR2L | MED28 | IntAct, BioGRID | empirical | 15175163 |
| POLR2L | INTS5 | BioGRID | empirical | 20133760 |
| POLR2L | POLR1B | Sanger Interaction Map | predicted | 15345047 |
| POLR2L | MED10 | IntAct, BioGRID | empirical | 15175163 |
| POLR2L | MED26 | IntAct, BioGRID | empirical | 15175163 21729782 |
| POLR2L | POLR1C | Reactome, Sanger Interaction Map | predicted | 15345047 |
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Publications: 91
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Initial characterization of the human central proteome.
Burkard TR, Planyavsky M, Kaupe I, Breitwieser FP, Bürckstümmer T, Bennett KL, Superti-Furga G, Colinge J
BMC Syst Biol. 2011
PubMed ID: 21269460
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Streamlined analysis schema for high-throughput identification of endogenous protein complexes.
Malovannaya A, Li Y, Bulynko Y, Jung SY, Wang Y, Lanz RB, O'Malley BW, Qin J
Proc Natl Acad Sci U S A. 2010
PubMed ID: 20133760
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Lineage-specific biology revealed by a finished genome assembly of the mouse.
Church DM, Goodstadt L, Hillier LW, Zody MC, Goldstein S, She X, Bult CJ, Agarwala R, Cherry JL, DiCuccio M, Hlavina W, Kapustin Y, Meric P, Maglott D, Birtle Z, Marques AC, Graves T, Zhou S, Teague B, Potamousis K, Churas C, Place M, Herschleb J, Runnheim R, Forrest D, Amos-Landgraf J, Schwartz DC, Cheng Z, Lindblad-Toh K, Eichler EE, Ponting CP, Mouse Genome Sequencing Consortium
PLoS Biol. 2009
PubMed ID: 19468303
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FACT facilitates chromatin transcription by RNA polymerases I and III.
Birch JL, Tan BC, Panov KI, Panova TB, Andersen JS, Owen-Hughes TA, Russell J, Lee SC, Zomerdijk JC
EMBO J. 2009
PubMed ID: 19214185
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Will diverse Tat interactions lead to novel antiretroviral drug targets?
Harrich D, McMillan N, Munoz L, Apolloni A, Meredith L
Curr Drug Targets. 2006
PubMed ID: 17168834
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The regulation of HIV-1 transcription: molecular targets for chemotherapeutic intervention.
Stevens M, De Clercq E, Balzarini J
Med Res Rev. 2006
PubMed ID: 16838299
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RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation of transcription by upstream binding factor.
Panov KI, Panova TB, Gadal O, Nishiyama K, Saito T, Russell J, Zomerdijk JC
Mol Cell Biol. 2006
PubMed ID: 16809778
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Towards a proteome-scale map of the human protein-protein interaction network.
Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M
Nature. 2005
PubMed ID: 16189514
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The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, Klein SL, Old S, Rasooly R, Good P, Guyer M, Peck AM, Derge JG, Lipman D, Collins FS, Jang W, Sherry S, Feolo M, Misquitta L, Lee E, Rotmistrovsky K, Greenhut SF, Schaefer CF, Buetow K, Bonner TI, Haussler D, Kent J, Kiekhaus M, Furey T, Brent M, Prange C, Schreiber K, Shapiro N, Bhat NK, Hopkins RF, Hsie F, Driscoll T, Soares MB, Casavant TL, Scheetz TE, Brown-stein MJ, Usdin TB, Toshiyuki S, Carninci P, Piao Y, Dudekula DB, Ko MS, Kawakami K, Suzuki Y, Sugano S, Gruber CE, Smith MR, Simmons B, Moore T, Waterman R, Johnson SL, Ruan Y, Wei CL, Mathavan S, Gunaratne PH, Wu J, Garcia AM, Hulyk SW, Fuh E, Yuan Y, Sneed A, Kowis C, Hodgson A, Muzny DM, McPherson J, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madari A, Young AC, Wetherby KD, Granite SJ, Kwong PN, Brinkley CP, Pearson RL, Bouffard GG, Blakesly RW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Griffith M, Griffith OL, Krzywinski MI, Liao N, Morin R, Morrin R, Palmquist D, Petrescu AS, Skalska U, Smailus DE, Stott JM, Schnerch A, Schein JE, Jones SJ, Holt RA, Baross A, Marra MA, Clifton S, Makowski KA, Bosak S, Malek J, MGC Project Team
Genome Res. 2004
PubMed ID: 15489334
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A protein interaction framework for human mRNA degradation.
Lehner B, Sanderson CM
Genome Res. 2004
PubMed ID: 15231747
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A set of consensus mammalian mediator subunits identified by multidimensional protein identification technology.
Sato S, Tomomori-Sato C, Parmely TJ, Florens L, Zybailov B, Swanson SK, Banks CA, Jin J, Cai Y, Washburn MP, Conaway JW, Conaway RC
Mol Cell. 2004
PubMed ID: 15175163
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A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway.
Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G
Nat Cell Biol. 2004
PubMed ID: 14743216
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Complete sequencing and characterization of 21,243 full-length human cDNAs.
Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, Wakamatsu A, Hayashi K, Sato H, Nagai K, Kimura K, Makita H, Sekine M, Obayashi M, Nishi T, Shibahara T, Tanaka T, Ishii S, Yamamoto J, Saito K, Kawai Y, Isono Y, Nakamura Y, Nagahari K, Murakami K, Yasuda T, Iwayanagi T, Wagatsuma M, Shiratori A, Sudo H, Hosoiri T, Kaku Y, Kodaira H, Kondo H, Sugawara M, Takahashi M, Kanda K, Yokoi T, Furuya T, Kikkawa E, Omura Y, Abe K, Kamihara K, Katsuta N, Sato K, Tanikawa M, Yamazaki M, Ninomiya K, Ishibashi T, Yamashita H, Murakawa K, Fujimori K, Tanai H, Kimata M, Watanabe M, Hiraoka S, Chiba Y, Ishida S, Ono Y, Takiguchi S, Watanabe S, Yosida M, Hotuta T, Kusano J, Kanehori K, Takahashi-Fujii A, Hara H, Tanase TO, Nomura Y, Togiya S, Komai F, Hara R, Takeuchi K, Arita M, Imose N, Musashino K, Yuuki H, Oshima A, Sasaki N, Aotsuka S, Yoshikawa Y, Matsunawa H, Ichihara T, Shiohata N, Sano S, Moriya S, Momiyama H, Satoh N, Takami S, Terashima Y, Suzuki O, Nakagawa S, Senoh A, Mizoguchi H, Goto Y, Shimizu F, Wakebe H, Hishigaki H, Watanabe T, Sugiyama A, Takemoto M, Kawakami B, Yamazaki M, Watanabe K, Kumagai A, Itakura S, Fukuzumi Y, Fujimori Y, Komiyama M, Tashiro H, Tanigami A, Fujiwara T, Ono T, Yamada K, Fujii Y, Ozaki K, Hirao M, Ohmori Y, Kawabata A, Hikiji T, Kobatake N, Inagaki H, Ikema Y, Okamoto S, Okitani R, Kawakami T, Noguchi S, Itoh T, Shigeta K, Senba T, Matsumura K, Nakajima Y, Mizuno T, Morinaga M, Sasaki M, Togashi T, Oyama M, Hata H, Watanabe M, Komatsu T, Mizushima-Sugano J, Satoh T, Shirai Y, Takahashi Y, Nakagawa K, Okumura K, Nagase T, Nomura N, Kikuchi H, Masuho Y, Yamashita R, Nakai K, Yada T, Nakamura Y, Ohara O, Isogai T, Sugano S
Nat Genet. 2004
PubMed ID: 14702039
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The Tat/TAR-dependent phosphorylation of RNA polymerase II C-terminal domain stimulates cotranscriptional capping of HIV-1 mRNA.
Zhou M, Deng L, Kashanchi F, Brady JN, Shatkin AJ, Kumar A
Proc Natl Acad Sci U S A. 2003
PubMed ID: 14569024
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Acetylation of Tat defines a cyclinT1-independent step in HIV transactivation.
Kaehlcke K, Dorr A, Hetzer-Egger C, Kiermer V, Henklein P, Schnoelzer M, Loret E, Cole PA, Verdin E, Ott M
Mol Cell. 2003
PubMed ID: 12887902
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Differential transcriptional regulation by human immunodeficiency virus type 1 and gp120 in human astrocytes.
Galey D, Becker K, Haughey N, Kalehua A, Taub D, Woodward J, Mattson MP, Nath A
J Neurovirol. 2003
PubMed ID: 12775419
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Human immunodeficiency virus type 1 (HIV-1) Vpr enhances expression from unintegrated HIV-1 DNA.
Poon B, Chen IS
J Virol. 2003
PubMed ID: 12634356
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The RNA polymerase II elongation complex.
Shilatifard A, Conaway RC, Conaway JW
Annu Rev Biochem. 2003
PubMed ID: 12676794
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HIV-1 Vpr binding to HIV-1 LTR C/EBP cis-acting elements and adjacent regions is sequence-specific.
Hogan TH, Nonnemacher MR, Krebs FC, Henderson A, Wigdahl B
Biomed Pharmacother. 2003
PubMed ID: 12642036
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Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences.
Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, Wagner L, Shenmen CM, Schuler GD, Altschul SF, Zeeberg B, Buetow KH, Schaefer CF, Bhat NK, Hopkins RF, Jordan H, Moore T, Max SI, Wang J, Hsieh F, Diatchenko L, Marusina K, Farmer AA, Rubin GM, Hong L, Stapleton M, Soares MB, Bonaldo MF, Casavant TL, Scheetz TE, Brownstein MJ, Usdin TB, Toshiyuki S, Carninci P, Prange C, Raha SS, Loquellano NA, Peters GJ, Abramson RD, Mullahy SJ, Bosak SA, McEwan PJ, McKernan KJ, Malek JA, Gunaratne PH, Richards S, Worley KC, Hale S, Garcia AM, Gay LJ, Hulyk SW, Villalon DK, Muzny DM, Sodergren EJ, Lu X, Gibbs RA, Fahey J, Helton E, Ketteman M, Madan A, Rodrigues S, Sanchez A, Whiting M, Madan A, Young AC, Shevchenko Y, Bouffard GG, Blakesley RW, Touchman JW, Green ED, Dickson MC, Rodriguez AC, Grimwood J, Schmutz J, Myers RM, Butterfield YS, Krzywinski MI, Skalska U, Smailus DE, Schnerch A, Schein JE, Jones SJ, Marra MA, Mammalian Gene Collection Program Team
Proc Natl Acad Sci U S A. 2002
PubMed ID: 12477932
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Transcriptional activators differ in their abilities to control alternative splicing.
Nogues G, Kadener S, Cramer P, Bentley D, Kornblihtt AR
J Biol Chem. 2002
PubMed ID: 12221105
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Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits.
Hu P, Wu S, Sun Y, Yuan CC, Kobayashi R, Myers MP, Hernandez N
Mol Cell Biol. 2002
PubMed ID: 12391170
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Transcription factor TFIIH components enhance the GR coactivator activity but not the cell cycle-arresting activity of the human immunodeficiency virus type-1 protein Vpr.
Kino T, Tsukamoto M, Chrousos G
Biochem Biophys Res Commun. 2002
PubMed ID: 12379213
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HIV-1 Tat interaction with RNA polymerase II C-terminal domain (CTD) and a dynamic association with CDK2 induce CTD phosphorylation and transcription from HIV-1 promoter.
Deng L, Ammosova T, Pumfery A, Kashanchi F, Nekhai S
J Biol Chem. 2002
PubMed ID: 12114499
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Comprehensive proteomic analysis of the human spliceosome.
Zhou Z, Licklider LJ, Gygi SP, Reed R
Nature. 2002
PubMed ID: 12226669
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A bimolecular mechanism of HIV-1 Tat protein interaction with RNA polymerase II transcription elongation complexes.
Zhou C, Rana TM
J Mol Biol. 2002
PubMed ID: 12126615
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HIV envelope induces a cascade of cell signals in non-proliferating target cells that favor virus replication.
Cicala C, Arthos J, Selig SM, Dennis G, Hosack DA, Van Ryk D, Spangler ML, Steenbeke TD, Khazanie P, Gupta N, Yang J, Daucher M, Lempicki RA, Fauci AS
Proc Natl Acad Sci U S A. 2002
PubMed ID: 12089333
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Phosphorylation of the RNA polymerase II carboxyl-terminal domain by CDK9 is directly responsible for human immunodeficiency virus type 1 Tat-activated transcriptional elongation.
Kim YK, Bourgeois CF, Isel C, Churcher MJ, Karn J
Mol Cell Biol. 2002
PubMed ID: 12052871
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HIV-1 Tat-associated RNA polymerase C-terminal domain kinase, CDK2, phosphorylates CDK7 and stimulates Tat-mediated transcription.
Nekhai S, Zhou M, Fernandez A, Lane WS, Lamb NJ, Brady J, Kumar A
Biochem J. 2002
PubMed ID: 12049628
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Spt5 cooperates with human immunodeficiency virus type 1 Tat by preventing premature RNA release at terminator sequences.
Bourgeois CF, Kim YK, Churcher MJ, West MJ, Karn J
Mol Cell Biol. 2002
PubMed ID: 11809800
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DSIF and NELF interact with RNA polymerase II elongation complex and HIV-1 Tat stimulates P-TEFb-mediated phosphorylation of RNA polymerase II and DSIF during transcription elongation.
Ping YH, Rana TM
J Biol Chem. 2001
PubMed ID: 11112772
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Multiple modes of transcriptional regulation by the HIV-1 Tat transactivator.
Marcello A, Zoppé M, Giacca M
IUBMB Life. 2001
PubMed ID: 11547919
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Acetylation of HIV-1 Tat by CBP/P300 increases transcription of integrated HIV-1 genome and enhances binding to core histones.
Deng L, de la Fuente C, Fu P, Wang L, Donnelly R, Wade JD, Lambert P, Li H, Lee CG, Kashanchi F
Virology. 2000
PubMed ID: 11080476
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Cooperative interaction between HIV-1 regulatory proteins Tat and Vpr modulates transcription of the viral genome.
Sawaya BE, Khalili K, Gordon J, Taube R, Amini S
J Biol Chem. 2000
PubMed ID: 10931842
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CDK9 autophosphorylation regulates high-affinity binding of the human immunodeficiency virus type 1 tat-P-TEFb complex to TAR RNA.
Garber ME, Mayall TP, Suess EM, Meisenhelder J, Thompson NE, Jones KA
Mol Cell Biol. 2000
PubMed ID: 10958691
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Tat modifies the activity of CDK9 to phosphorylate serine 5 of the RNA polymerase II carboxyl-terminal domain during human immunodeficiency virus type 1 transcription.
Zhou M, Halanski MA, Radonovich MF, Kashanchi F, Peng J, Price DH, Brady JN
Mol Cell Biol. 2000
PubMed ID: 10866664
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Domains in the SPT5 protein that modulate its transcriptional regulatory properties.
Ivanov D, Kwak YT, Guo J, Gaynor RB
Mol Cell Biol. 2000
PubMed ID: 10757782
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Architecture of RNA polymerase II and implications for the transcription mechanism.
Cramer P, Bushnell DA, Fu J, Gnatt AL, Maier-Davis B, Thompson NE, Burgess RR, Edwards AM, David PR, Kornberg RD
Science. 2000
PubMed ID: 10784442
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BRCA1 interaction with RNA polymerase II reveals a role for hRPB2 and hRPB10alpha in activated transcription.
Schlegel BP, Green VJ, Ladias JA, Parvin JD
Proc Natl Acad Sci U S A. 2000
PubMed ID: 10725406
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Phosphorylation of the RAP74 subunit of TFIIF correlates with Tat-activated transcription of the HIV-1 long terminal repeat.
Zhou M, Kashanchi F, Jiang H, Ge H, Brady JN
Virology. 2000
PubMed ID: 10704353
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TIP30 has an intrinsic kinase activity required for up-regulation of a subset of apoptotic genes.
Xiao H, Palhan V, Yang Y, Roeder RG
EMBO J. 2000
PubMed ID: 10698937
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Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription.
O'Keeffe B, Fong Y, Chen D, Zhou S, Zhou Q
J Biol Chem. 2000
PubMed ID: 10617616
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Regulatory functions of Cdk9 and of cyclin T1 in HIV tat transactivation pathway gene expression.
Romano G, Kasten M, De Falco G, Micheli P, Khalili K, Giordano A
J Cell Biochem. 1999
PubMed ID: 10536359
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Interactions between the full complement of human RNA polymerase II subunits.
Schaller S, Grandemange S, Shpakovski GV, Golemis EA, Kedinger C, Vigneron M
FEBS Lett. 1999
PubMed ID: 10567706
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HIV-1 tat transcriptional activity is regulated by acetylation.
Kiernan RE, Vanhulle C, Schiltz L, Adam E, Xiao H, Maudoux F, Calomme C, Burny A, Nakatani Y, Jeang KT, Benkirane M, Van Lint C
EMBO J. 1999
PubMed ID: 10545121
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Direct evidence that HIV-1 Tat stimulates RNA polymerase II carboxyl-terminal domain hyperphosphorylation during transcriptional elongation.
Isel C, Karn J
J Mol Biol. 1999
PubMed ID: 10438593
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A novel RNA polymerase II-containing complex potentiates Tat-enhanced HIV-1 transcription.
Parada CA, Roeder RG
EMBO J. 1999
PubMed ID: 10393184
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Transcriptional cofactor CA150 regulates RNA polymerase II elongation in a TATA-box-dependent manner.
Suñé C, Garcia-Blanco MA
Mol Cell Biol. 1999
PubMed ID: 10373521
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Human and rodent transcription elongation factor P-TEFb: interactions with human immunodeficiency virus type 1 tat and carboxy-terminal domain substrate.
Ramanathan Y, Reza SM, Young TM, Mathews MB, Pe'ery T
J Virol. 1999
PubMed ID: 10364292
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The HIV-1 Vpr co-activator induces a conformational change in TFIIB.
Agostini I, Navarro JM, Bouhamdan M, Willetts K, Rey F, Spire B, Vigne R, Pomerantz R, Sire J
FEBS Lett. 1999
PubMed ID: 10359081
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Cyclin T1 domains involved in complex formation with Tat and TAR RNA are critical for tat-activation.
Ivanov D, Kwak YT, Nee E, Guo J, García-Martínez LF, Gaynor RB
J Mol Biol. 1999
PubMed ID: 10329125
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Nuclear localisation of NOVH protein: a potential role for NOV in the regulation of gene expression.
Perbal B
Mol Pathol. 1999
PubMed ID: 10474687
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Human immunodeficiency virus type 1 Tat-dependent activation of an arrested RNA polymerase II elongation complex.
Liu Y, Suñé C, Garcia-Blanco MA
Virology. 1999
PubMed ID: 10069959
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Tat-associated kinase (P-TEFb): a component of transcription preinitiation and elongation complexes.
Ping YH, Rana TM
J Biol Chem. 1999
PubMed ID: 10066804
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The HIV-1 virion-associated protein vpr is a coactivator of the human glucocorticoid receptor.
Kino T, Gragerov A, Kopp JB, Stauber RH, Pavlakis GN, Chrousos GP
J Exp Med. 1999
PubMed ID: 9874563
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Immunoaffinity purification and functional characterization of human transcription factor IIH and RNA polymerase II from clonal cell lines that conditionally express epitope-tagged subunits of the multiprotein complexes.
Kershnar E, Wu SY, Chiang CM
J Biol Chem. 1998
PubMed ID: 9852112
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Cloning and characterization of three human cDNAs encoding mRNA (guanine-7-)-methyltransferase, an mRNA cap methylase.
Tsukamoto T, Shibagaki Y, Niikura Y, Mizumoto K
Biochem Biophys Res Commun. 1998
PubMed ID: 9790902
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The HIV-1 Tat cellular coactivator Tat-SF1 is a general transcription elongation factor.
Li XY, Green MR
Genes Dev. 1998
PubMed ID: 9765201
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The ability of positive transcription elongation factor B to transactivate human immunodeficiency virus transcription depends on a functional kinase domain, cyclin T1, and Tat.
Fujinaga K, Cujec TP, Peng J, Garriga J, Price DH, Graña X, Peterlin BM
J Virol. 1998
PubMed ID: 9696809
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Transcriptional control: Tat cofactors and transcriptional elongation.
Yankulov K, Bentley D
Curr Biol. 1998
PubMed ID: 9651670
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Isolation and characterization of a human cDNA for mRNA 5'-capping enzyme.
Yamada-Okabe T, Doi R, Shimmi O, Arisawa M, Yamada-Okabe H
Nucleic Acids Res. 1998
PubMed ID: 9512541
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A novel CDK9-associated C-type cyclin interacts directly with HIV-1 Tat and mediates its high-affinity, loop-specific binding to TAR RNA.
Wei P, Garber ME, Fang SM, Fischer WH, Jones KA
Cell. 1998
PubMed ID: 9491887
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Tat, Tat-associated kinase, and transcription.
Jeang KT
J Biomed Sci. 1998
PubMed ID: 9570510
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Three transitions in the RNA polymerase II transcription complex during initiation.
Holstege FC, Fiedler U, Timmers HT
EMBO J. 1997
PubMed ID: 9405375
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Purification and cDNA cloning of the AdoMet-binding subunit of the human mRNA (N6-adenosine)-methyltransferase.
Bokar JA, Shambaugh ME, Polayes D, Matera AG, Rottman FM
RNA. 1997
PubMed ID: 9409616
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The HIV transactivator TAT binds to the CDK-activating kinase and activates the phosphorylation of the carboxy-terminal domain of RNA polymerase II.
Cujec TP, Okamoto H, Fujinaga K, Meyer J, Chamberlin H, Morgan DO, Peterlin BM
Genes Dev. 1997
PubMed ID: 9334327
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CA150, a nuclear protein associated with the RNA polymerase II holoenzyme, is involved in Tat-activated human immunodeficiency virus type 1 transcription.
Suñé C, Hayashi T, Liu Y, Lane WS, Young RA, Garcia-Blanco MA
Mol Cell Biol. 1997
PubMed ID: 9315662
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A human primary T-lymphocyte-derived human immunodeficiency virus type 1 Tat-associated kinase phosphorylates the C-terminal domain of RNA polymerase II and induces CAK activity.
Nekhai S, Shukla RR, Kumar A
J Virol. 1997
PubMed ID: 9311822
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Interactions between the human RNA polymerase II subunits.
Acker J, de Graaff M, Cheynel I, Khazak V, Kedinger C, Vigneron M
J Biol Chem. 1997
PubMed ID: 9201987
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Purification of a Tat-associated kinase reveals a TFIIH complex that modulates HIV-1 transcription.
García-Martínez LF, Mavankal G, Neveu JM, Lane WS, Ivanov D, Gaynor RB
EMBO J. 1997
PubMed ID: 9184228
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The human immunodeficiency virus transactivator Tat interacts with the RNA polymerase II holoenzyme.
Cujec TP, Cho H, Maldonado E, Meyer J, Reinberg D, Peterlin BM
Mol Cell Biol. 1997
PubMed ID: 9121429
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Association of Tat with purified HIV-1 and HIV-2 transcription preinitiation complexes.
García-Martínez LF, Ivanov D, Gaynor RB
J Biol Chem. 1997
PubMed ID: 9054383
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Enhanced processivity of RNA polymerase II triggered by Tat-induced phosphorylation of its carboxy-terminal domain.
Parada CA, Roeder RG
Nature. 1996
PubMed ID: 8934526
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The general transcription factors of RNA polymerase II.
Orphanides G, Lagrange T, Reinberg D
Genes Dev. 1996
PubMed ID: 8946909
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Requirements for RNA polymerase II carboxyl-terminal domain for activated transcription of human retroviruses human T-cell lymphotropic virus I and HIV-1.
Chun RF, Jeang KT
J Biol Chem. 1996
PubMed ID: 8910388
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Tat-SF1: cofactor for stimulation of transcriptional elongation by HIV-1 Tat.
Zhou Q, Sharp PA
Science. 1996
PubMed ID: 8849451
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Trans-activation by human immunodeficiency virus Tat protein requires the C-terminal domain of RNA polymerase II.
Okamoto H, Sheline CT, Corden JL, Jones KA, Peterlin BM
Proc Natl Acad Sci U S A. 1996
PubMed ID: 8876177
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The human immunodeficiency virus type 1 Vpr transactivator: cooperation with promoter-bound activator domains and binding to TFIIB.
Agostini I, Navarro JM, Rey F, Bouhamdan M, Spire B, Vigne R, Sire J
J Mol Biol. 1996
PubMed ID: 8800208
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Normalization and subtraction: two approaches to facilitate gene discovery.
Bonaldo MF, Lennon G, Soares MB
Genome Res. 1996
PubMed ID: 8889548
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The human immunodeficiency virus Tat proteins specifically associate with TAK in vivo and require the carboxyl-terminal domain of RNA polymerase II for function.
Yang X, Herrmann CH, Rice AP
J Virol. 1996
PubMed ID: 8676484
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Human immunodeficiency virus type-1 Tat is an integral component of the activated transcription-elongation complex.
Keen NJ, Gait MJ, Karn J
Proc Natl Acad Sci U S A. 1996
PubMed ID: 8637904
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The gene (POLR2L) encoding the hRPB7.6 subunit of human RNA polymerase.
Acker J, Murroni O, Mattei MG, Kedinger C, Vigneron M
Genomics. 1996
PubMed ID: 8786124
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Six human RNA polymerase subunits functionally substitute for their yeast counterparts.
McKune K, Moore PA, Hull MW, Woychik NA
Mol Cell Biol. 1995
PubMed ID: 8524256
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Four subunits that are shared by the three classes of RNA polymerase are functionally interchangeable between Homo sapiens and Saccharomyces cerevisiae.
Shpakovski GV, Acker J, Wintzerith M, Lacroix JF, Thuriaux P, Vigneron M
Mol Cell Biol. 1995
PubMed ID: 7651387
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Specific binding of RNA polymerase II to the human immunodeficiency virus trans-activating region RNA is regulated by cellular cofactors and Tat.
Wu-Baer F, Sigman D, Gaynor RB
Proc Natl Acad Sci U S A. 1995
PubMed ID: 7638159
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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.
Herrmann CH, Rice AP
J Virol. 1995
PubMed ID: 7853496
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HIV-1 Tat acts as a processivity factor in vitro in conjunction with cellular elongation factors.
Kato H, Sumimoto H, Pognonec P, Chen CH, Rosen CA, Roeder RG
Genes Dev. 1992
PubMed ID: 1559613
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The human immunodeficiency virus tat protein increases the transcription of human Alu repeated sequences by increasing the activity of the cellular transcription factor TFIIIC.
Jang KL, Collins MK, Latchman DS
J Acquir Immune Defic Syndr. 1992
PubMed ID: 1403646
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Abortive initiation is increased only for the weakest members of a set of down mutants of the adenovirus 2 major late promoter.
Jacob GA, Luse SW, Luse DS
J Biol Chem. 1991
PubMed ID: 1939271
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Activation of transcription by HIV-1 Tat protein tethered to nascent RNA through another protein.
Southgate C, Zapp ML, Green MR
Nature. 1990
PubMed ID: 2190099
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ATP activates transcription initiation from promoters by RNA polymerase II in a reversible step prior to RNA synthesis.
Conaway RC, Conaway JW
J Biol Chem. 1988
PubMed ID: 2449431
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