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DNA-directed RNA polymerase II subunit RPB1 (RNA polymerase II subunit B1) (EC 2.7.7.6) (DNA-directed RNA polymerase II subunit A) (DNA-directed RNA polymerase III largest subunit) (RNA-directed RNA polymerase II subunit RPB1) (EC 2.7.7.48)

 RPB1_HUMAN              Reviewed;        1970 AA.
P24928; A6NN93; B9EH88; Q6NX41;
01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
15-DEC-2009, sequence version 2.
30-AUG-2017, entry version 194.
RecName: Full=DNA-directed RNA polymerase II subunit RPB1;
Short=RNA polymerase II subunit B1;
EC=2.7.7.6;
AltName: Full=DNA-directed RNA polymerase II subunit A;
AltName: Full=DNA-directed RNA polymerase III largest subunit;
AltName: Full=RNA-directed RNA polymerase II subunit RPB1;
EC=2.7.7.48;
Name=POLR2A; Synonyms=POLR2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1542581; DOI=10.1093/nar/20.4.910;
Wintzerith M., Acker J., Vicaire S., Vigneron M., Kedinger C.;
"Complete sequence of the human RNA polymerase II largest subunit.";
Nucleic Acids Res. 20:910-910(1992).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=7622068; DOI=10.1016/0378-1119(95)00081-G;
Mita K., Tsuji H., Morimyo M., Takahashi E., Nenoi M., Ichimura S.,
Yamauchi M., Hongo E., Hayashi A.;
"The human gene encoding the largest subunit of RNA polymerase II.";
Gene 159:285-286(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain, and Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
SUBCELLULAR LOCATION.
PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
Kershnar E., Wu S.-Y., Chiang C.-M.;
"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.";
J. Biol. Chem. 273:34444-34453(1998).
[7]
INTERACTION WITH SAFB.
PubMed=9671816; DOI=10.1093/nar/26.15.3542;
Nayler O., Straetling W., Bourquin J.-P., Stagljar I., Lindemann L.,
Jasper H., Hartmann A.M., Fackelmeyer F.O., Ullrich A., Stamm S.;
"SAF-B couples transcription and pre-mRNA splicing to SAR/MAR
elements.";
Nucleic Acids Res. 26:3542-3549(1998).
[8]
IDENTIFICATION IN A COMPLEX WITH HTATSF1; CCNT1; NCL; SUPT5H AND CDK9.
PubMed=10393184; DOI=10.1093/emboj/18.13.3688;
Parada C.A., Roeder R.G.;
"A novel RNA polymerase II-containing complex potentiates Tat-enhanced
HIV-1 transcription.";
EMBO J. 18:3688-3701(1999).
[9]
INTERACTION WITH HTATSF1.
PubMed=10454543; DOI=10.1128/MCB.19.9.5960;
Kim J.B., Yamaguchi Y., Wada T., Handa H., Sharp P.A.;
"Tat-SF1 protein associates with RAP30 and human SPT5 proteins.";
Mol. Cell. Biol. 19:5960-5968(1999).
[10]
INTERACTION WITH FNBP3.
PubMed=12381297; DOI=10.1016/S0022-2836(02)00968-3;
Allen M., Friedler A., Schon O., Bycroft M.;
"The structure of an FF domain from human HYPA/FBP11.";
J. Mol. Biol. 323:411-416(2002).
[11]
INTERACTION WITH SYNCRIP.
PubMed=12376575; DOI=10.1074/mcp.M200029-MCP200;
Carty S.M., Greenleaf A.L.;
"Hyperphosphorylated C-terminal repeat domain-associating proteins in
the nuclear proteome link transcription to DNA/chromatin modification
and RNA processing.";
Mol. Cell. Proteomics 1:598-610(2002).
[12]
INTERACTION WITH DDX5.
PubMed=12527917; DOI=10.1038/sj.onc.1206067;
Rossow K.L., Janknecht R.;
"Synergism between p68 RNA helicase and the transcriptional
coactivators CBP and p300.";
Oncogene 22:151-156(2003).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[14]
INTERACTION WITH CCNT2.
PubMed=15563843; DOI=10.1016/j.gene.2004.08.027;
Kurosu T., Zhang F., Peterlin B.M.;
"Transcriptional activity and substrate recognition of cyclin T2 from
P-TEFb.";
Gene 343:173-179(2004).
[15]
INTERACTION WITH CCNL2.
PubMed=14684736; DOI=10.1074/jbc.M312895200;
Yang L., Li N., Wang C., Yu Y., Yuan L., Zhang M., Cao X.;
"Cyclin L2, a novel RNA polymerase II-associated cyclin, is involved
in pre-mRNA splicing and induces apoptosis of human hepatocellular
carcinoma cells.";
J. Biol. Chem. 279:11639-11648(2004).
[16]
INTERACTION WITH MEN1.
PubMed=14992727; DOI=10.1016/S1097-2765(04)00081-4;
Hughes C.M., Rozenblatt-Rosen O., Milne T.A., Copeland T.D.,
Levine S.S., Lee J.C., Hayes D.N., Shanmugam K.S., Bhattacharjee A.,
Biondi C.A., Kay G.F., Hayward N.K., Hess J.L., Meyerson M.;
"Menin associates with a trithorax family histone methyltransferase
complex and with the hoxc8 locus.";
Mol. Cell 13:587-597(2004).
[17]
INTERACTION WITH SFRS19.
PubMed=15992770; DOI=10.1016/j.bbrc.2005.06.053;
Katsarou M.E., Papakyriakou A., Katsaros N., Scorilas A.;
"Expression of the C-terminal domain of novel human SR-A1 protein:
interaction with the CTD domain of RNA polymerase II.";
Biochem. Biophys. Res. Commun. 334:61-68(2005).
[18]
INTERACTION WITH SETD2.
PubMed=16118227; DOI=10.1074/jbc.M504012200;
Sun X.-J., Wei J., Wu X.-Y., Hu M., Wang L., Wang H.-H., Zhang Q.-H.,
Chen S.-J., Huang Q.-H., Chen Z.;
"Identification and characterization of a novel human histone H3
lysine 36 specific methyltransferase.";
J. Biol. Chem. 280:35261-35271(2005).
[19]
INTERACTION WITH SETD2.
PubMed=16314571; DOI=10.1073/pnas.0506350102;
Li M., Phatnani H.P., Guan Z., Sage H., Greenleaf A.L., Zhou P.;
"Solution structure of the Set2-Rpb1 interacting domain of human Set2
and its interaction with the hyperphosphorylated C-terminal domain of
Rpb1.";
Proc. Natl. Acad. Sci. U.S.A. 102:17636-17641(2005).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1909 AND TYR-1923, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[21]
INTERACTION WITH PAF1 IN PAF1/RNA POLYMERASE II.
TISSUE=Fetal pancreas;
PubMed=16491129; DOI=10.1038/sj.onc.1209353;
Moniaux N., Nemos C., Schmied B.M., Chauhan S.C., Deb S., Morikane K.,
Choudhury A., Vanlith M., Sutherlin M., Sikela J.M.,
Hollingsworth M.A., Batra S.K.;
"The human homologue of the RNA polymerase II-associated factor 1
(hPaf1), localized on the 19q13 amplicon, is associated with
tumorigenesis.";
Oncogene 25:3247-3257(2006).
[22]
INTERACTION WITH SUPT6H, AND PHOSPHORYLATION.
PubMed=17234882; DOI=10.1101/gad.1503107;
Yoh S.M., Cho H., Pickle L., Evans R.M., Jones K.A.;
"The Spt6 SH2 domain binds Ser2-P RNAPII to direct Iws1-dependent mRNA
splicing and export.";
Genes Dev. 21:160-174(2007).
[23]
INTERACTION WITH CMTR1.
PubMed=18533109; DOI=10.1016/j.bbrc.2008.05.137;
Haline-Vaz T., Silva T.C.L., Zanchin N.I.T.;
"The human interferon-regulated ISG95 protein interacts with RNA
polymerase II and shows methyltransferase activity.";
Biochem. Biophys. Res. Commun. 372:719-724(2008).
[24]
INTERACTION WITH SCAF8.
PubMed=18550522; DOI=10.1074/jbc.M803540200;
Becker R., Loll B., Meinhart A.;
"Snapshots of the RNA processing factor SCAF8 bound to different
phosphorylated forms of the carboxyl-terminal domain of RNA polymerase
II.";
J. Biol. Chem. 283:22659-22669(2008).
[25]
FUNCTION AS RNA-DIRECTED RNA POLYMERASE.
PubMed=18032511; DOI=10.1128/JVI.01758-07;
Chang J., Nie X., Chang H.E., Han Z., Taylor J.;
"Transcription of hepatitis delta virus RNA by RNA polymerase II.";
J. Virol. 82:1118-1127(2008).
[26]
INTERACTION WITH SETD1A; SETD1B AND WDR82.
PubMed=17998332; DOI=10.1128/MCB.01356-07;
Lee J.H., Skalnik D.G.;
"Wdr82 is a C-terminal domain-binding protein that recruits the Setd1A
Histone H3-Lys4 methyltransferase complex to transcription start sites
of transcribed human genes.";
Mol. Cell. Biol. 28:609-618(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1849; TYR-1874;
SER-1896; TYR-1909; SER-1913; SER-1920; TYR-1923; SER-1927 AND
SER-1934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[28]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[29]
INTERACTION WITH ATF7IP.
PubMed=19106100; DOI=10.1074/jbc.M807098200;
Liu L., Ishihara K., Ichimura T., Fujita N., Hino S., Tomita S.,
Watanabe S., Saitoh N., Ito T., Nakao M.;
"MCAF1/AM is involved in Sp1-mediated maintenance of cancer-associated
telomerase activity.";
J. Biol. Chem. 284:5165-5174(2009).
[30]
PHOSPHORYLATION BY CDK7.
PubMed=19450536; DOI=10.1016/j.molcel.2009.04.016;
Akhtar M.S., Heidemann M., Tietjen J.R., Zhang D.W., Chapman R.D.,
Eick D., Ansari A.Z.;
"TFIIH kinase places bivalent marks on the carboxy-terminal domain of
RNA polymerase II.";
Mol. Cell 34:387-393(2009).
[31]
PHOSPHORYLATION BY CDK7 AND CDK9.
PubMed=19667075; DOI=10.1128/MCB.00637-09;
Glover-Cutter K., Larochelle S., Erickson B., Zhang C., Shokat K.,
Fisher R.P., Bentley D.L.;
"TFIIH-associated Cdk7 kinase functions in phosphorylation of C-
terminal domain Ser7 residues, promoter-proximal pausing, and
termination by RNA polymerase II.";
Mol. Cell. Biol. 29:5455-5464(2009).
[32]
PHOSPHORYLATION BY CDK7.
PubMed=19136461; DOI=10.1093/nar/gkn1061;
Lolli G.;
"Binding to DNA of the RNA-polymerase II C-terminal domain allows
discrimination between Cdk7 and Cdk9 phosphorylation.";
Nucleic Acids Res. 37:1260-1268(2009).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1843; THR-1854;
SER-1878; SER-1882; SER-1899; SER-1913; SER-1917; SER-1920; SER-1927;
SER-1931 AND SER-1934, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[34]
INTERACTION WITH RECQL5, AND FUNCTION.
PubMed=20231364; DOI=10.1128/MCB.01583-09;
Islam M.N., Fox D. III, Guo R., Enomoto T., Wang W.;
"RecQL5 promotes genome stabilization through two parallel
mechanisms--interacting with RNA polymerase II and acting as a
helicase.";
Mol. Cell. Biol. 30:2460-2472(2010).
[35]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[36]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[37]
INTERACTION WITH U2AF2.
PubMed=21536736; DOI=10.1101/gad.2038011;
David C.J., Boyne A.R., Millhouse S.R., Manley J.L.;
"The RNA polymerase II C-terminal domain promotes splicing activation
through recruitment of a U2AF65-Prp19 complex.";
Genes Dev. 25:972-983(2011).
[38]
PHOSPHORYLATION BY CDK9.
PubMed=21127351; DOI=10.1074/jbc.M110.176628;
Cojocaru M., Bouchard A., Cloutier P., Cooper J.J., Varzavand K.,
Price D.H., Coulombe B.;
"Transcription factor IIS cooperates with the E3 ligase UBR5 to
ubiquitinate the CDK9 subunit of the positive transcription elongation
factor B.";
J. Biol. Chem. 286:5012-5022(2011).
[39]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1917 AND SER-1931, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[40]
METHYLATION AT ARG-1810 BY CARM1, AND MUTAGENESIS OF ARG-1810.
PubMed=21454787; DOI=10.1126/science.1202663;
Sims R.J. III, Rojas L.A., Beck D., Bonasio R., Schuller R.,
Drury W.J. III, Eick D., Reinberg D.;
"The C-terminal domain of RNA polymerase II is modified by site-
specific methylation.";
Science 332:99-103(2011).
[41]
PHOSPHORYLATION, AND DOMAIN.
PubMed=22137580; DOI=10.1016/j.molcel.2011.11.006;
Egloff S., Zaborowska J., Laitem C., Kiss T., Murphy S.;
"Ser7 phosphorylation of the CTD recruits the RPAP2 Ser5 phosphatase
to snRNA genes.";
Mol. Cell 45:111-122(2012).
[42]
UBIQUITINATION.
PubMed=22466610; DOI=10.1038/ng.2229;
Nakazawa Y., Sasaki K., Mitsutake N., Matsuse M., Shimada M.,
Nardo T., Takahashi Y., Ohyama K., Ito K., Mishima H., Nomura M.,
Kinoshita A., Ono S., Takenaka K., Masuyama R., Kudo T., Slor H.,
Utani A., Tateishi S., Yamashita S., Stefanini M., Lehmann A.R.,
Yoshiura K.I., Ogi T.;
"Mutations in UVSSA cause UV-sensitive syndrome and impair RNA
polymerase IIo processing in transcription-coupled nucleotide-excision
repair.";
Nat. Genet. 44:586-592(2012).
[43]
INTERACTION WITH HERPES SIMPLEX VIRUS 1 PROTEIN ICP22 (MICROBIAL
INFECTION).
PubMed=23029222; DOI=10.1371/journal.pone.0045749;
Guo L., Wu W.J., Liu L.D., Wang L.C., Zhang Y., Wu L.Q., Guan Y.,
Li Q.H.;
"Herpes simplex virus 1 ICP22 inhibits the transcription of viral gene
promoters by binding to and blocking the recruitment of P-TEFb.";
PLoS ONE 7:E45749-E45749(2012).
[44]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-217; SER-1850;
SER-1864; SER-1868; SER-1878; SER-1882; THR-1885; SER-1899; SER-1913;
SER-1920; SER-1927 AND SER-1934, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[45]
ACETYLATION BY EP300, AND FUNCTION.
PubMed=24207025; DOI=10.1016/j.molcel.2013.10.009;
Schroeder S., Herker E., Itzen F., He D., Thomas S., Gilchrist D.A.,
Kaehlcke K., Cho S., Pollard K.S., Capra J.A., Schnoelzer M.,
Cole P.A., Geyer M., Bruneau B.G., Adelman K., Ott M.;
"Acetylation of RNA polymerase II regulates growth-factor-induced gene
transcription in mammalian cells.";
Mol. Cell 52:314-324(2013).
[46]
INTERACTION WITH SETX.
PubMed=23149945; DOI=10.1128/MCB.01195-12;
Yuce O., West S.C.;
"Senataxin, defective in the neurodegenerative disorder ataxia with
oculomotor apraxia 2, lies at the interface of transcription and the
DNA damage response.";
Mol. Cell. Biol. 33:406-417(2013).
[47]
INTERACTION WITH PIH1D1.
PubMed=24656813; DOI=10.1016/j.celrep.2014.03.013;
Horejsi Z., Stach L., Flower T.G., Joshi D., Flynn H., Skehel J.M.,
O'Reilly N.J., Ogrodowicz R.W., Smerdon S.J., Boulton S.J.;
"Phosphorylation-dependent PIH1D1 interactions define substrate
specificity of the R2TP cochaperone complex.";
Cell Rep. 7:19-26(2014).
[48]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-1874; SER-1906; TYR-1909
AND TYR-1923, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[49]
METHYLATION, AND ACETYLATION.
PubMed=26687004; DOI=10.7554/eLife.11215;
Dias J.D., Rito T., Torlai Triglia E., Kukalev A., Ferrai C.,
Chotalia M., Brookes E., Kimura H., Pombo A.;
"Methylation of RNA polymerase II non-consensus Lysine residues marks
early transcription in mammalian cells.";
Elife 4:0-0(2015).
[50]
SUBCELLULAR LOCATION, ACETYLATION AT LYS-1866; LYS-1887; LYS-1922 AND
LYS-1936, METHYLATION AT LYS-1859; LYS-1866; LYS-1873; LYS-1887;
LYS-1922 AND LYS-1936, AND PHOSPHORYLATION AT THR-1840; SER-1843;
SER-1845; SER-1849; SER-1850; SER-1857; TYR-1860; SER-1861; THR-1863;
SER-1864; TYR-1867; THR-1870; TYR-1874; SER-1875; THR-1877; SER-1878;
TYR-1881; SER-1882; TYR-1909; THR-1912; SER-1913; THR-1915; TYR-1916;
SER-1917; THR-1919; SER-1920; TYR-1923; THR-1926; SER-1927; THR-1929;
TYR-1930; SER-1931; THR-1933 AND SER-1934.
PubMed=26566685; DOI=10.1080/21541264.2015.1114983;
Voss K., Forne I., Descostes N., Hintermair C., Schueller R.,
Maqbool M.A., Heidemann M., Flatley A., Imhof A., Gut M., Gut I.,
Kremmer E., Andrau J.C., Eick D.;
"Site-specific methylation and acetylation of lysine residues in the
C-terminal domain (CTD) of RNA polymerase II.";
Transcription 6:91-101(2015).
[51]
INTERACTION WITH TDRD3; PRMT5; SETX; SMN1 AND XRN2, METHYLATION AT
ARG-1603 AND ARG-1810, AND MUTAGENESIS OF ARG-1810.
PubMed=26700805; DOI=10.1038/nature16469;
Yanling Zhao D., Gish G., Braunschweig U., Li Y., Ni Z.,
Schmitges F.W., Zhong G., Liu K., Li W., Moffat J., Vedadi M., Min J.,
Pawson T.J., Blencowe B.J., Greenblatt J.F.;
"SMN and symmetric arginine dimethylation of RNA polymerase II C-
terminal domain control termination.";
Nature 529:48-53(2016).
[52]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 1796-1803 IN COMPLEX WITH
CTDSP1, AND DEPHOSPHORYLATION.
PubMed=17157258; DOI=10.1016/j.molcel.2006.10.027;
Zhang Y., Kim Y., Genoud N., Gao J., Kelly J.W., Pfaff S.L.,
Gill G.N., Dixon J.E., Noel J.P.;
"Determinants for dephosphorylation of the RNA polymerase II C-
terminal domain by Scp1.";
Mol. Cell 24:759-770(2006).
[53]
STRUCTURE BY ELECTRON MICROSCOPY IN COMPLEX WITH RECQL5, INTERACTION
WITH RECQL5 AND TCEA1, SUBUNIT, AND FUNCTION.
PubMed=23748380; DOI=10.1038/nsmb.2596;
Kassube S.A., Jinek M., Fang J., Tsutakawa S., Nogales E.;
"Structural mimicry in transcription regulation of human RNA
polymerase II by the DNA helicase RECQL5.";
Nat. Struct. Mol. Biol. 20:892-899(2013).
-!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
of DNA into RNA using the four ribonucleoside triphosphates as
substrates. Largest and catalytic component of RNA polymerase II
which synthesizes mRNA precursors and many functional non-coding
RNAs. Forms the polymerase active center together with the second
largest subunit. Pol II is the central component of the basal RNA
polymerase II transcription machinery. It is composed of mobile
elements that move relative to each other. RPB1 is part of the
core element with the central large cleft, the clamp element that
moves to open and close the cleft and the jaws that are thought to
grab the incoming DNA template. At the start of transcription, a
single-stranded DNA template strand of the promoter is positioned
within the central active site cleft of Pol II. A bridging helix
emanates from RPB1 and crosses the cleft near the catalytic site
and is thought to promote translocation of Pol II by acting as a
ratchet that moves the RNA-DNA hybrid through the active site by
switching from straight to bent conformations at each step of
nucleotide addition. During transcription elongation, Pol II moves
on the template as the transcript elongates. Elongation is
influenced by the phosphorylation status of the C-terminal domain
(CTD) of Pol II largest subunit (RPB1), which serves as a platform
for assembly of factors that regulate transcription initiation,
elongation, termination and mRNA processing. Regulation of gene
expression levels depends on the balance between methylation and
acetylation levels of tha CTD-lysines (By similarity). Initiation
or early elongation steps of transcription of growth-factors-
induced immediate early genes are regulated by the acetylation
status of the CTD (PubMed:24207025). Methylation and dimethylation
have a repressive effect on target genes expression (By
similarity). {ECO:0000250|UniProtKB:P08775,
ECO:0000269|PubMed:20231364, ECO:0000269|PubMed:23748380,
ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:9852112}.
-!- FUNCTION: (Microbial infection) Acts as an RNA-dependent RNA
polymerase when associated with small delta antigen of Hepatitis
delta virus, acting both as a replicate and transcriptase for the
viral RNA circular genome. {ECO:0000269|PubMed:18032511}.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1).
-!- SUBUNIT: Component of the RNA polymerase II (Pol II) complex
consisting of 12 subunits. Component of a complex which is at
least composed of HTATSF1/Tat-SF1, the P-TEFb complex components
CDK9 and CCNT1, RNA polymerase II, SUPT5H, and NCL/nucleolin. The
large PER complex involved in the repression of transcriptional
termination is composed of at least PER2, CDK9, DDX5, DHX9, NCBP1
and POLR2A (active). Interacts (via the C-terminal domain (CTD))
with U2AF2; recruits PRPF19 and the Prp19 complex to the pre-mRNA
and may couple transcription to pre-mRNA splicing. Interacts (via
the C-terminal domain (CTD)) with SMN1/SMN2; recruits SMN1/SMN2 to
RNA Pol II elongation complexes. Interacts via the phosphorylated
C-terminal domain with WDR82 and with SETD1A and SETD1B only in
the presence of WDR82. When phosphorylated at 'Ser-5', interacts
with MEN1; the unphosphorylated form, or phosphorylated at 'Ser-2'
does not interact. When phosphorylated at 'Ser-2', interacts with
SUPT6H (via SH2 domain). Interacts with RECQL5 and TCEA1; binding
of RECQL5 prevents TCEA1 binding. The phosphorylated C-terminal
domain interacts with FNBP3 and SYNCRIP. Interacts with ATF7IP.
Interacts with DDX5. Interacts with WWP2. Interacts with SETX.
Interacts (phosphorylated) with PIH1D1. Interacts (via the C-
terminal domain (CTD)) with TDRD3. Interacts with PRMT5. Interacts
with XRN2. Interacts with SAFB/SAFB1. Interacts with CCNL1.
Interacts with CCNL2, MYO1C, PAF1 and SFRS19. Interacts (via C-
terminus) with CMTR1, CTDSP1 and SCAF8. Interacts (via the C-
terminal domain (CTD)) with CCNT2 (PubMed:15563843).
{ECO:0000250|UniProtKB:P08775, ECO:0000269|PubMed:10393184,
ECO:0000269|PubMed:10454543, ECO:0000269|PubMed:12376575,
ECO:0000269|PubMed:12381297, ECO:0000269|PubMed:12527917,
ECO:0000269|PubMed:14684736, ECO:0000269|PubMed:14992727,
ECO:0000269|PubMed:15563843, ECO:0000269|PubMed:15992770,
ECO:0000269|PubMed:16118227, ECO:0000269|PubMed:16314571,
ECO:0000269|PubMed:16491129, ECO:0000269|PubMed:17157258,
ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:17998332,
ECO:0000269|PubMed:18533109, ECO:0000269|PubMed:18550522,
ECO:0000269|PubMed:19106100, ECO:0000269|PubMed:20231364,
ECO:0000269|PubMed:21536736, ECO:0000269|PubMed:23149945,
ECO:0000269|PubMed:23748380, ECO:0000269|PubMed:24656813,
ECO:0000269|PubMed:26700805, ECO:0000269|PubMed:9671816,
ECO:0000269|PubMed:9852112}.
-!- SUBUNIT: (Microbial infection) Interacts with herpes simplex virus
1 protein ICP22; this interaction causes loss of CTD 'Ser-2'
phosphorylation from pol II engaged in transcription
(PubMed:23029222). {ECO:0000269|PubMed:23029222}.
-!- INTERACTION:
Q6P1J9:CDC73; NbExp=5; IntAct=EBI-295301, EBI-930143;
P17844:DDX5; NbExp=3; IntAct=EBI-295301, EBI-351962;
Q98140:ORF24 (xeno); NbExp=2; IntAct=EBI-295301, EBI-14033488;
L8B1Q7:ORF6 (xeno); NbExp=3; IntAct=EBI-295301, EBI-11712334;
Q67020:PA (xeno); NbExp=2; IntAct=EBI-295301, EBI-11514477;
Q8N7H5:PAF1; NbExp=5; IntAct=EBI-295301, EBI-2607770;
Q9NQG5:RPRD1B; NbExp=5; IntAct=EBI-295301, EBI-747925;
Q96H20:SNF8; NbExp=2; IntAct=EBI-295301, EBI-747719;
O00267:SUPT5H; NbExp=4; IntAct=EBI-295301, EBI-710464;
Q9HCS7:XAB2; NbExp=2; IntAct=EBI-295301, EBI-295232;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26566685,
ECO:0000269|PubMed:9852112}. Cytoplasm
{ECO:0000269|PubMed:26566685}. Note=Hypophosphorylated form is
mainly found in the cytoplasm, while the hyperphosphorylated and
active form is nuclear. {ECO:0000269|PubMed:26566685}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P24928-1; Sequence=Displayed;
Name=2;
IsoId=P24928-2; Sequence=VSP_056184, VSP_056185;
Note=No experimental confirmation available.;
-!- DOMAIN: The C-terminal domain (CTD) serves as a platform for
assembly of factors that regulate transcription initiation,
elongation, termination and mRNA processing.
{ECO:0000303|PubMed:22137580}.
-!- PTM: The tandem heptapeptide repeats in the C-terminal domain
(CTD) can be highly phosphorylated. The phosphorylation activates
Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and
'Ser-5' of the heptapeptide repeat and is mediated, at least, by
CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA
promotes transcription initiation by triggering dissociation from
DNA. Phosphorylation also takes place at 'Ser-7' of the
heptapeptide repeat, which is required for efficient transcription
of snRNA genes and processing of the transcripts. The
phosphorylation state is believed to result from the balanced
action of site-specific CTD kinases and phosphatases, and a 'CTD
code' that specifies the position of Pol II within the
transcription cycle has been proposed. Dephosphorylated by the
protein phosphatase CTDSP1. {ECO:0000269|PubMed:17157258,
ECO:0000269|PubMed:17234882, ECO:0000269|PubMed:19136461,
ECO:0000269|PubMed:19450536, ECO:0000269|PubMed:19667075,
ECO:0000269|PubMed:21127351, ECO:0000269|PubMed:22137580,
ECO:0000269|PubMed:26566685}.
-!- PTM: Among tandem heptapeptide repeats of the C-terminal domain
(CTD) some do not match the Y-S-P-T-S-P-S consensus, the seventh
serine residue 'Ser-7' being replaced by a lysine. 'Lys-7' in
these non-consensus heptapeptide repeats can be alternatively
acetylated, methylated and dimethylated. EP300 is one of the
enzyme able to acetylate 'Lys-7'. Acetylation at 'Lys-7' of non-
consensus heptapeptide repeats is associated with 'Ser-2'
phosphorylation and active transcription. Regulates initiation or
early elongation steps of transcription specially for inducible
genes. {ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26566685,
ECO:0000269|PubMed:26687004}.
-!- PTM: Methylated at Arg-1810 prior to transcription initiation when
the CTD is hypophosphorylated, phosphorylation at Ser-1805 and
Ser-1808 preventing this methylation. Symmetrically or
asymmetrically dimethylated at Arg-1810 by PRMT5 and CARM1
respectively. Symmetric or asymmetric dimethylation modulates
interactions with CTD-binding proteins like SMN1/SMN2 and TDRD3.
SMN1/SMN2 interacts preferentially with the symmetrically
dimethylated form while TDRD3 interacts with the asymmetric form.
Through the recruitment of SMN1/SMN2, symmetric dimethylation is
required for resolving RNA-DNA hybrids created by RNA polymerase
II, that form R-loop in transcription terminal regions, an
important step in proper transcription termination. CTD
dimethylation may also facilitate the expression of select RNAs.
Among tandem heptapeptide repeats of the C-terminal domain (CTD)
some do not match the Y-S-P-T-S-P-S consensus, the seventh serine
residue 'Ser-7' being replaced by a lysine. 'Lys-7' in these non-
consensus heptapeptide repeats can be alternatively acetylated,
methylated, dimethylated and trimethylated. Methylation occurs in
the earliest transcription stages and precedes or is concomitant
to 'Ser-5' and 'Ser-7' phosphorylation. Dimethylation and
trimehtylation at 'Lys-7' of non-consensus heptapeptide repeats
are exclusively associated with phosphorylated CTD.
{ECO:0000250|UniProtKB:P08775, ECO:0000269|PubMed:26566685,
ECO:0000269|PubMed:26687004, ECO:0000269|PubMed:26700805}.
-!- PTM: Ubiquitinated by WWP2 leading to proteasomal degradation (By
similarity). Following UV treatment, the elongating form of RNA
polymerase II (RNA pol IIo) is ubiquitinated on UV damage sites
without leading to degradation: ubiquitination is facilitated by
KIAA1530/UVSSA and promotes RNA pol IIo backtracking to allow
access to the nucleotide excision repair machinery.
{ECO:0000250|UniProtKB:P08775, ECO:0000269|PubMed:22466610}.
-!- MISCELLANEOUS: The binding of ribonucleoside triphosphate to the
RNA polymerase II transcribing complex probably involves a two-
step mechanism. The initial binding seems to occur at the entry
(E) site and involves a magnesium ion temporarily coordinated by
three conserved aspartate residues of the two largest RNA Pol II
subunits. The ribonucleoside triphosphate is transferred by a
rotation to the nucleotide addition (A) site for pairing with the
template DNA. The catalytic A site involves three conserved
aspartate residues of the RNA Pol II largest subunit which
permanently coordinate a second magnesium ion.
-!- SIMILARITY: Belongs to the RNA polymerase beta' chain family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X63564; CAA45125.1; -; mRNA.
EMBL; X74874; CAA52862.1; -; Genomic_DNA.
EMBL; X74873; CAA52862.1; JOINED; Genomic_DNA.
EMBL; X74872; CAA52862.1; JOINED; Genomic_DNA.
EMBL; X74871; CAA52862.1; JOINED; Genomic_DNA.
EMBL; X74870; CAA52862.1; JOINED; Genomic_DNA.
EMBL; AC113189; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471108; EAW90181.1; -; Genomic_DNA.
EMBL; BC067295; AAH67295.1; -; mRNA.
EMBL; BC137231; AAI37232.1; -; mRNA.
PIR; I38186; I38186.
PIR; S21054; S21054.
RefSeq; NP_000928.1; NM_000937.4.
UniGene; Hs.270017; -.
PDB; 2GHQ; X-ray; 2.05 A; C/D=1795-1803.
PDB; 2GHT; X-ray; 1.80 A; C/D=1796-1803.
PDB; 2LTO; NMR; -; B=1804-1816.
PDB; 3D9K; X-ray; 2.20 A; Y/Z=1790-1803.
PDB; 3D9L; X-ray; 2.20 A; Y/Z=1790-1803.
PDB; 3D9M; X-ray; 1.75 A; Y/Z=1790-1803.
PDB; 3D9N; X-ray; 1.60 A; Y/Z=1790-1803.
PDB; 3D9O; X-ray; 2.00 A; Z=1790-1803.
PDB; 3D9P; X-ray; 2.10 A; Y/Z=1790-1803.
PDB; 4JXT; X-ray; 1.90 A; B=1787-1805.
PDB; 5IY6; EM; 7.20 A; A=1-1970.
PDB; 5IY7; EM; 8.60 A; A=1-1970.
PDB; 5IY8; EM; 7.90 A; A=1-1970.
PDB; 5IY9; EM; 6.30 A; A=1-1970.
PDB; 5IYA; EM; 5.40 A; A=1-1970.
PDB; 5IYB; EM; 3.90 A; A=1-1970.
PDB; 5IYC; EM; 3.90 A; A=1-1970.
PDB; 5IYD; EM; 3.90 A; A=1-1970.
PDB; 5M3H; X-ray; 2.50 A; X/Y=1713-1740.
PDB; 5M3J; X-ray; 3.50 A; X=1713-1740.
PDBsum; 2GHQ; -.
PDBsum; 2GHT; -.
PDBsum; 2LTO; -.
PDBsum; 3D9K; -.
PDBsum; 3D9L; -.
PDBsum; 3D9M; -.
PDBsum; 3D9N; -.
PDBsum; 3D9O; -.
PDBsum; 3D9P; -.
PDBsum; 4JXT; -.
PDBsum; 5IY6; -.
PDBsum; 5IY7; -.
PDBsum; 5IY8; -.
PDBsum; 5IY9; -.
PDBsum; 5IYA; -.
PDBsum; 5IYB; -.
PDBsum; 5IYC; -.
PDBsum; 5IYD; -.
PDBsum; 5M3H; -.
PDBsum; 5M3J; -.
ProteinModelPortal; P24928; -.
SMR; P24928; -.
BioGrid; 111426; 287.
DIP; DIP-29011N; -.
IntAct; P24928; 69.
MINT; MINT-156582; -.
STRING; 9606.ENSP00000314949; -.
BindingDB; P24928; -.
ChEMBL; CHEMBL1641353; -.
iPTMnet; P24928; -.
PhosphoSitePlus; P24928; -.
BioMuta; POLR2A; -.
DMDM; 281185484; -.
EPD; P24928; -.
MaxQB; P24928; -.
PaxDb; P24928; -.
PeptideAtlas; P24928; -.
PRIDE; P24928; -.
Ensembl; ENST00000572844; ENSP00000461879; ENSG00000181222. [P24928-2]
GeneID; 5430; -.
KEGG; hsa:5430; -.
UCSC; uc002ghe.4; human. [P24928-1]
CTD; 5430; -.
DisGeNET; 5430; -.
GeneCards; POLR2A; -.
H-InvDB; HIX0173727; -.
HGNC; HGNC:9187; POLR2A.
HPA; CAB012226; -.
HPA; CAB016388; -.
HPA; CAB022311; -.
HPA; HPA021563; -.
HPA; HPA053012; -.
MIM; 180660; gene+phenotype.
neXtProt; NX_P24928; -.
OpenTargets; ENSG00000181222; -.
PharmGKB; PA33507; -.
eggNOG; KOG0260; Eukaryota.
eggNOG; COG0086; LUCA.
GeneTree; ENSGT00870000136522; -.
HOGENOM; HOG000222975; -.
HOVERGEN; HBG004339; -.
InParanoid; P24928; -.
KO; K03006; -.
PhylomeDB; P24928; -.
TreeFam; TF103036; -.
Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
Reactome; R-HSA-112387; Elongation arrest and recovery.
Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
Reactome; R-HSA-167161; HIV Transcription Initiation.
Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
Reactome; R-HSA-167172; Transcription of the HIV genome.
Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
Reactome; R-HSA-167287; HIV elongation arrest and recovery.
Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
Reactome; R-HSA-452723; Transcriptional regulation of pluripotent stem cells.
Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
Reactome; R-HSA-6782135; Dual incision in TC-NER.
Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
Reactome; R-HSA-6803529; FGFR2 alternative splicing.
Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
Reactome; R-HSA-72086; mRNA Capping.
Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
SIGNOR; P24928; -.
ChiTaRS; POLR2A; human.
EvolutionaryTrace; P24928; -.
GeneWiki; POLR2A; -.
GenomeRNAi; 5430; -.
PRO; PR:P24928; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000181222; -.
CleanEx; HS_POLR2A; -.
ExpressionAtlas; P24928; baseline and differential.
Genevisible; P24928; HS.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005665; C:DNA-directed RNA polymerase II, core complex; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003677; F:DNA binding; TAS:ProtInc.
GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:BHF-UCL.
GO; GO:0006370; P:7-methylguanosine mRNA capping; TAS:Reactome.
GO; GO:0006353; P:DNA-templated transcription, termination; IMP:UniProtKB.
GO; GO:0008543; P:fibroblast growth factor receptor signaling pathway; TAS:Reactome.
GO; GO:0000398; P:mRNA splicing, via spliceosome; TAS:Reactome.
GO; GO:0033120; P:positive regulation of RNA splicing; IDA:UniProtKB.
GO; GO:0050434; P:positive regulation of viral transcription; TAS:Reactome.
GO; GO:0060964; P:regulation of gene silencing by miRNA; TAS:Reactome.
GO; GO:0006355; P:regulation of transcription, DNA-templated; NAS:UniProtKB.
GO; GO:0016070; P:RNA metabolic process; TAS:Reactome.
GO; GO:0042795; P:snRNA transcription from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0035019; P:somatic stem cell population maintenance; TAS:Reactome.
GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006366; P:transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; TAS:Reactome.
GO; GO:0006351; P:transcription, DNA-templated; TAS:Reactome.
GO; GO:0006283; P:transcription-coupled nucleotide-excision repair; TAS:Reactome.
InterPro; IPR000722; RNA_pol_asu.
InterPro; IPR000684; RNA_pol_II_repeat_euk.
InterPro; IPR006592; RNA_pol_N.
InterPro; IPR007080; RNA_pol_Rpb1_1.
InterPro; IPR007066; RNA_pol_Rpb1_3.
InterPro; IPR007083; RNA_pol_Rpb1_4.
InterPro; IPR007081; RNA_pol_Rpb1_5.
InterPro; IPR007075; RNA_pol_Rpb1_6.
InterPro; IPR007073; RNA_pol_Rpb1_7.
Pfam; PF04997; RNA_pol_Rpb1_1; 1.
Pfam; PF00623; RNA_pol_Rpb1_2; 1.
Pfam; PF04983; RNA_pol_Rpb1_3; 1.
Pfam; PF05000; RNA_pol_Rpb1_4; 1.
Pfam; PF04998; RNA_pol_Rpb1_5; 1.
Pfam; PF04992; RNA_pol_Rpb1_6; 1.
Pfam; PF04990; RNA_pol_Rpb1_7; 1.
Pfam; PF05001; RNA_pol_Rpb1_R; 40.
SMART; SM00663; RPOLA_N; 1.
PROSITE; PS00115; RNA_POL_II_REPEAT; 42.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Complete proteome;
Cytoplasm; DNA-binding; DNA-directed RNA polymerase; Magnesium;
Metal-binding; Methylation; Nucleotidyltransferase; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat;
RNA-directed RNA polymerase; Transcription; Transferase;
Ubl conjugation; Zinc.
CHAIN 1 1970 DNA-directed RNA polymerase II subunit
RPB1.
/FTId=PRO_0000073940.
REPEAT 1593 1599 1.
REPEAT 1600 1606 2; approximate.
REPEAT 1608 1614 3.
REPEAT 1615 1621 4.
REPEAT 1622 1628 5.
REPEAT 1629 1635 6.
REPEAT 1636 1642 7.
REPEAT 1643 1649 8.
REPEAT 1650 1656 9.
REPEAT 1657 1663 10.
REPEAT 1664 1670 11.
REPEAT 1671 1677 12.
REPEAT 1678 1684 13.
REPEAT 1685 1691 14.
REPEAT 1692 1698 15.
REPEAT 1699 1705 16.
REPEAT 1706 1712 17.
REPEAT 1713 1719 18.
REPEAT 1720 1726 19.
REPEAT 1727 1733 20.
REPEAT 1734 1740 21.
REPEAT 1741 1747 22.
REPEAT 1748 1754 23.
REPEAT 1755 1761 24.
REPEAT 1762 1768 25.
REPEAT 1769 1775 26.
REPEAT 1776 1782 27.
REPEAT 1783 1789 28.
REPEAT 1790 1796 29.
REPEAT 1797 1803 30.
REPEAT 1804 1810 31.
REPEAT 1811 1817 32.
REPEAT 1818 1824 33.
REPEAT 1825 1831 34.
REPEAT 1832 1838 35.
REPEAT 1839 1845 36.
REPEAT 1846 1852 37.
REPEAT 1853 1859 38.
REPEAT 1860 1866 39.
REPEAT 1867 1873 40.
REPEAT 1874 1880 41.
REPEAT 1881 1887 42.
REPEAT 1888 1894 43.
REPEAT 1895 1901 44.
REPEAT 1902 1908 45.
REPEAT 1909 1915 46.
REPEAT 1916 1922 47.
REPEAT 1923 1929 48.
REPEAT 1930 1936 49.
REPEAT 1940 1946 50.
REPEAT 1947 1953 51; approximate.
REPEAT 1954 1960 52; approximate.
REGION 833 845 Bridging helix.
REGION 1593 1960 C-terminal domain (CTD); 52 X 7 AA
approximate tandem repeats of Y-[ST]-P-
[STQ]-[ST]-P-[SRTEVKGN].
METAL 71 71 Zinc 1. {ECO:0000250}.
METAL 74 74 Zinc 1. {ECO:0000250}.
METAL 81 81 Zinc 1. {ECO:0000250}.
METAL 84 84 Zinc 1. {ECO:0000250}.
METAL 111 111 Zinc 2. {ECO:0000250}.
METAL 114 114 Zinc 2. {ECO:0000250}.
METAL 154 154 Zinc 2. {ECO:0000250}.
METAL 184 184 Zinc 2. {ECO:0000250}.
METAL 495 495 Magnesium 1; catalytic. {ECO:0000250}.
METAL 495 495 Magnesium 2; shared with RPB2.
{ECO:0000250}.
METAL 497 497 Magnesium 1; catalytic. {ECO:0000250}.
METAL 497 497 Magnesium 2; shared with RPB2.
{ECO:0000250}.
METAL 499 499 Magnesium 1; catalytic. {ECO:0000250}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 27 27 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 217 217 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1603 1603 Omega-N-methylated arginine; by CARM1; in
vitro. {ECO:0000269|PubMed:26700805}.
MOD_RES 1810 1810 Asymmetric dimethylarginine; alternate;
by CARM1. {ECO:0000269|PubMed:21454787,
ECO:0000269|PubMed:26700805}.
MOD_RES 1810 1810 Symmetric dimethylarginine; alternate; by
PRMT5. {ECO:0000269|PubMed:26700805}.
MOD_RES 1840 1840 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1843 1843 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:26566685}.
MOD_RES 1845 1845 Phosphoserine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1847 1847 Phosphoserine.
{ECO:0000250|UniProtKB:P08775}.
MOD_RES 1849 1849 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:26566685}.
MOD_RES 1850 1850 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1854 1854 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 1857 1857 Phosphoserine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1859 1859 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1859 1859 N6-methyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1860 1860 Phosphotyrosine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1861 1861 Phosphoserine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1863 1863 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1864 1864 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1866 1866 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1866 1866 N6,N6-dimethyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1866 1866 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1866 1866 N6-methyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1867 1867 Phosphotyrosine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1868 1868 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1870 1870 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1873 1873 N6,N6,N6-trimethyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1873 1873 N6-methyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1874 1874 Phosphotyrosine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26566685}.
MOD_RES 1875 1875 Phosphoserine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1877 1877 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1878 1878 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1881 1881 Phosphotyrosine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1882 1882 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1885 1885 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1887 1887 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1887 1887 N6-methyllysine; alternate.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1894 1894 Phosphothreonine.
{ECO:0000250|UniProtKB:P08775}.
MOD_RES 1896 1896 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1899 1899 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1906 1906 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1909 1909 Phosphotyrosine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26566685}.
MOD_RES 1912 1912 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1913 1913 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1915 1915 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1916 1916 Phosphotyrosine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1917 1917 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:26566685}.
MOD_RES 1919 1919 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1920 1920 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1922 1922 N6-acetyllysine; alternate.
{ECO:0000305|PubMed:26566685}.
MOD_RES 1922 1922 N6-methyllysine; alternate.
{ECO:0000305|PubMed:26566685}.
MOD_RES 1923 1923 Phosphotyrosine.
{ECO:0000244|PubMed:16964243,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:26566685}.
MOD_RES 1926 1926 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1927 1927 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:26566685}.
MOD_RES 1929 1929 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1930 1930 Phosphotyrosine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1931 1931 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:26566685}.
MOD_RES 1933 1933 Phosphothreonine.
{ECO:0000269|PubMed:26566685}.
MOD_RES 1934 1934 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 1936 1936 N6-acetyllysine; alternate.
{ECO:0000305|PubMed:26566685}.
MOD_RES 1936 1936 N6-methyllysine; alternate.
{ECO:0000305|PubMed:26566685}.
VAR_SEQ 558 566 GEVMNLLMF -> VCGPNGNLA (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056184.
VAR_SEQ 567 1970 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_056185.
VARIANT 292 292 R -> C (in dbSNP:rs2229198).
/FTId=VAR_051872.
MUTAGEN 1810 1810 R->A: Misexpression of a variety of small
nuclear RNAs and small nucleolar RNAs.
Loss of interaction with TDRD3 and
SMN1/SMN2. {ECO:0000269|PubMed:21454787,
ECO:0000269|PubMed:26700805}.
MUTAGEN 1838 1838 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1859;
R-1866; R-1873; R-1887; R-1908; R-1922
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1859 1859 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1838;
R-1866; R-1873; R-1887; R-1908; R-1922
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1866 1866 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1859;
R-1859; R-1873; R-1887; R-1908; R-1922
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1873 1873 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1838;
R-1859; R-1866; R-1887; R-1908; R-1922
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1887 1887 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1838;
R-1859; R-1866; R-1873; R-1908; R-1922
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1908 1908 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R.1838;
R-1859; R-1866; R-1873; R-1887; R-1922
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1922 1922 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1838;
R-1859; R-1866; R-1873; R-1887; R-1908
and R-1936.
{ECO:0000269|PubMed:24207025}.
MUTAGEN 1936 1936 K->R: Loss of acetylation and loss of
regulation of growth-factor-induced gene
expression; when associated with R-1838;
R-1859; R-1866; R-1873; R-1887; R-1908
and R-1922.
{ECO:0000269|PubMed:24207025}.
CONFLICT 1067 1067 W -> L (in Ref. 2; CAA52862).
{ECO:0000305}.
CONFLICT 1449 1449 D -> Y (in Ref. 2; CAA52862).
{ECO:0000305}.
CONFLICT 1835 1835 A -> T (in Ref. 1; CAA45125 and 2;
CAA52862). {ECO:0000305}.
STRAND 1722 1724 {ECO:0000244|PDB:5M3H}.
STRAND 1808 1811 {ECO:0000244|PDB:2LTO}.
SEQUENCE 1970 AA; 217176 MW; 28D6FD25693A6472 CRC64;
MHGGGPPSGD SACPLRTIKR VQFGVLSPDE LKRMSVTEGG IKYPETTEGG RPKLGGLMDP
RQGVIERTGR CQTCAGNMTE CPGHFGHIEL AKPVFHVGFL VKTMKVLRCV CFFCSKLLVD
SNNPKIKDIL AKSKGQPKKR LTHVYDLCKG KNICEGGEEM DNKFGVEQPE GDEDLTKEKG
HGGCGRYQPR IRRSGLELYA EWKHVNEDSQ EKKILLSPER VHEIFKRISD EECFVLGMEP
RYARPEWMIV TVLPVPPLSV RPAVVMQGSA RNQDDLTHKL ADIVKINNQL RRNEQNGAAA
HVIAEDVKLL QFHVATMVDN ELPGLPRAMQ KSGRPLKSLK QRLKGKEGRV RGNLMGKRVD
FSARTVITPD PNLSIDQVGV PRSIAANMTF AEIVTPFNID RLQELVRRGN SQYPGAKYII
RDNGDRIDLR FHPKPSDLHL QTGYKVERHM CDGDIVIFNR QPTLHKMSMM GHRVRILPWS
TFRLNLSVTT PYNADFDGDE MNLHLPQSLE TRAEIQELAM VPRMIVTPQS NRPVMGIVQD
TLTAVRKFTK RDVFLERGEV MNLLMFLSTW DGKVPQPAIL KPRPLWTGKQ IFSLIIPGHI
NCIRTHSTHP DDEDSGPYKH ISPGDTKVVV ENGELIMGIL CKKSLGTSAG SLVHISYLEM
GHDITRLFYS NIQTVINNWL LIEGHTIGIG DSIADSKTYQ DIQNTIKKAK QDVIEVIEKA
HNNELEPTPG NTLRQTFENQ VNRILNDARD KTGSSAQKSL SEYNNFKSMV VSGAKGSKIN
ISQVIAVVGQ QNVEGKRIPF GFKHRTLPHF IKDDYGPESR GFVENSYLAG LTPTEFFFHA
MGGREGLIDT AVKTAETGYI QRRLIKSMES VMVKYDATVR NSINQVVQLR YGEDGLAGES
VEFQNLATLK PSNKAFEKKF RFDYTNERAL RRTLQEDLVK DVLSNAHIQN ELEREFERMR
EDREVLRVIF PTGDSKVVLP CNLLRMIWNA QKIFHINPRL PSDLHPIKVV EGVKELSKKL
VIVNGDDPLS RQAQENATLL FNIHLRSTLC SRRMAEEFRL SGEAFDWLLG EIESKFNQAI
AHPGEMVGAL AAQSLGEPAT QMTLNTFHYA GVSAKNVTLG VPRLKELINI SKKPKTPSLT
VFLLGQSARD AERAKDILCR LEHTTLRKVT ANTAIYYDPN PQSTVVAEDQ EWVNVYYEMP
DFDVARISPW LLRVELDRKH MTDRKLTMEQ IAEKINAGFG DDLNCIFNDD NAEKLVLRIR
IMNSDENKMQ EEEEVVDKMD DDVFLRCIES NMLTDMTLQG IEQISKVYMH LPQTDNKKKI
IITEDGEFKA LQEWILETDG VSLMRVLSEK DVDPVRTTSN DIVEIFTVLG IEAVRKALER
ELYHVISFDG SYVNYRHLAL LCDTMTCRGH LMAITRHGVN RQDTGPLMKC SFEETVDVLM
EAAAHGESDP MKGVSENIML GQLAPAGTGC FDLLLDAEKC KYGMEIPTNI PGLGAAGPTG
MFFGSAPSPM GGISPAMTPW NQGATPAYGA WSPSVGSGMT PGAAGFSPSA ASDASGFSPG
YSPAWSPTPG SPGSPGPSSP YIPSPGGAMS PSYSPTSPAY EPRSPGGYTP QSPSYSPTSP
SYSPTSPSYS PTSPNYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS YSPTSPSYSP
TSPSYSPTSP SYSPTSPSYS PTSPSYSPTS PSYSPTSPSY SPTSPSYSPT SPSYSPTSPS
YSPTSPNYSP TSPNYTPTSP SYSPTSPSYS PTSPNYTPTS PNYSPTSPSY SPTSPSYSPT
SPSYSPSSPR YTPQSPTYTP SSPSYSPSSP SYSPASPKYT PTSPSYSPSS PEYTPTSPKY
SPTSPKYSPT SPKYSPTSPT YSPTTPKYSP TSPTYSPTSP VYTPTSPKYS PTSPTYSPTS
PKYSPTSPTY SPTSPKGSTY SPTSPGYSPT SPTYSLTSPA ISPDDSDEEN


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