RPAB1_HUMAN
ID RPAB1_HUMAN Reviewed; 210 AA.
AC P19388; B2R6L4; D6W5Y1; O43380; Q6PIH5; Q9BT06;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 4.
DT 03-AUG-2022, entry version 220.
DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC1;
DE Short=RNA polymerases I, II, and III subunit ABC1;
DE AltName: Full=DNA-directed RNA polymerase II 23 kDa polypeptide;
DE AltName: Full=DNA-directed RNA polymerase II subunit E;
DE AltName: Full=RPB5 homolog;
DE AltName: Full=XAP4;
GN Name=POLR2E;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND VARIANT PHE-44.
RX PubMed=2753903; DOI=10.1016/s0021-9258(18)51603-3;
RA Pati U.K., Weissman S.M.;
RT "Isolation and molecular characterization of a cDNA encoding the 23-kDa
RT subunit of human RNA polymerase II.";
RL J. Biol. Chem. 264:13114-13121(1989).
RN [2]
RP ERRATUM OF PUBMED:2753903, AND SEQUENCE REVISION.
RX PubMed=2071613; DOI=10.1016/s0021-9258(18)98863-0;
RA Pati U.K., Weissman S.M.;
RL J. Biol. Chem. 266:13468-13468(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA], VARIANT PHE-44, AND INTERACTION WITH HBV
RP PROTEIN X (MICROBIAL INFECTION).
RX PubMed=7828586; DOI=10.1002/j.1460-2075.1995.tb06984.x;
RA Cheong J.H., Yi M., Lin Y., Murakami S.;
RT "Human RPB5, a subunit shared by eukaryotic nuclear RNA polymerases, binds
RT human hepatitis B virus X protein and may play a role in X
RT transactivation.";
RL EMBO J. 14:143-150(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-44.
RC TISSUE=Heart;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT PHE-44.
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT PHE-44.
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION, IDENTIFICATION IN THE RNA POLYMERASE II CORE-COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9852112; DOI=10.1074/jbc.273.51.34444;
RA Kershnar E., Wu S.-Y., Chiang C.-M.;
RT "Immunoaffinity purification and functional characterization of human
RT transcription factor IIH and RNA polymerase II from clonal cell lines that
RT conditionally express epitope-tagged subunits of the multiprotein
RT complexes.";
RL J. Biol. Chem. 273:34444-34453(1998).
RN [9]
RP INTERACTION WITH URI1.
RX PubMed=9819440; DOI=10.1128/mcb.18.12.7546;
RA Dorjsuren D., Lin Y., Wei W., Yamashita T., Nomura T., Hayashi N.,
RA Murakami S.;
RT "RMP, a novel RNA polymerase II subunit 5-interacting protein, counteracts
RT transactivation by hepatitis B virus X protein.";
RL Mol. Cell. Biol. 18:7546-7555(1998).
RN [10]
RP IDENTIFICATION IN THE RNA POL I COMPLEX.
RX PubMed=16809778; DOI=10.1128/mcb.00230-06;
RA Panov K.I., Panova T.B., Gadal O., Nishiyama K., Saito T., Russell J.,
RA Zomerdijk J.C.B.M.;
RT "RNA polymerase I-specific subunit CAST/hPAF49 has a role in the activation
RT of transcription by upstream binding factor.";
RL Mol. Cell. Biol. 26:5436-5448(2006).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-81, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [15]
RP IDENTIFICATION IN THE PAQOSOME COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=31738558; DOI=10.1021/acs.jproteome.9b00599;
RA Cloutier P., Poitras C., Faubert D., Bouchard A., Blanchette M.,
RA Gauthier M.S., Coulombe B.;
RT "Upstream ORF-Encoded ASDURF Is a Novel Prefoldin-like Subunit of the
RT PAQosome.";
RL J. Proteome Res. 19:18-27(2020).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I, II and III which synthesize
CC ribosomal RNA precursors, mRNA precursors and many functional non-
CC coding RNAs, and small RNAs, such as 5S rRNA and tRNAs, respectively.
CC Pol II is the central component of the basal RNA polymerase II
CC transcription machinery. Pols are composed of mobile elements that move
CC relative to each other. In Pol II, POLR2E/RPB5 is part of the lower jaw
CC surrounding the central large cleft and thought to grab the incoming
CC DNA template. Seems to be the major component in this process (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I), RNA polymerase II
CC (Pol II) and RNA polymerase III (Pol III) complexes consisting of at
CC least 13, 12 and 17 subunits, respectively (PubMed:9852112,
CC PubMed:16809778). In RNA Pol II, this subunit is present in 2-fold
CC molar excess over the other subunits (PubMed:9852112). Component of the
CC PAQosome complex which is responsible for the biogenesis of several
CC protein complexes and which consists of R2TP complex members RUVBL1,
CC RUVBL2, RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT
CC and URI1 as well as ASDURF, POLR2E and DNAAF10/WDR92 (PubMed:31738558).
CC Interacts with URI1 (PubMed:9819440). {ECO:0000269|PubMed:16809778,
CC ECO:0000269|PubMed:31738558, ECO:0000269|PubMed:9819440,
CC ECO:0000269|PubMed:9852112}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HBV protein X.
CC {ECO:0000269|PubMed:7828586}.
CC -!- INTERACTION:
CC P19388; Q86V38: ATN1; NbExp=3; IntAct=EBI-395189, EBI-11954292;
CC P19388; P02489: CRYAA; NbExp=3; IntAct=EBI-395189, EBI-6875961;
CC P19388; Q01658: DR1; NbExp=3; IntAct=EBI-395189, EBI-750300;
CC P19388; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-395189, EBI-356015;
CC P19388; P00488: F13A1; NbExp=3; IntAct=EBI-395189, EBI-2565863;
CC P19388; P22607: FGFR3; NbExp=3; IntAct=EBI-395189, EBI-348399;
CC P19388; Q14957: GRIN2C; NbExp=3; IntAct=EBI-395189, EBI-8285963;
CC P19388; Q00403: GTF2B; NbExp=5; IntAct=EBI-395189, EBI-389564;
CC P19388; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-395189, EBI-1054873;
CC P19388; Q96PC2: IP6K3; NbExp=6; IntAct=EBI-395189, EBI-10990676;
CC P19388; Q92876: KLK6; NbExp=3; IntAct=EBI-395189, EBI-2432309;
CC P19388; Q9Y2X8: UBE2D4; NbExp=3; IntAct=EBI-395189, EBI-745527;
CC P19388; Q9UMX0: UBQLN1; NbExp=3; IntAct=EBI-395189, EBI-741480;
CC P19388; O94763: URI1; NbExp=3; IntAct=EBI-395189, EBI-357067;
CC P19388; Q9Y649; NbExp=3; IntAct=EBI-395189, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9852112}.
CC -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; J04965; AAA62401.1; ALT_SEQ; mRNA.
DR EMBL; S42643; AAB19339.1; -; mRNA.
DR EMBL; D38251; BAA07406.1; -; mRNA.
DR EMBL; AK312625; BAG35511.1; -; mRNA.
DR EMBL; AC004151; AAC03238.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69548.1; -; Genomic_DNA.
DR EMBL; CH471139; EAW69549.1; -; Genomic_DNA.
DR EMBL; BC004441; AAH04441.1; -; mRNA.
DR EMBL; BC034144; AAH34144.1; -; mRNA.
DR CCDS; CCDS12056.1; -.
DR PIR; S52002; A32618.
DR RefSeq; NP_002686.2; NM_002695.3.
DR PDB; 5IY6; EM; 7.20 A; E=1-210.
DR PDB; 5IY7; EM; 8.60 A; E=1-210.
DR PDB; 5IY8; EM; 7.90 A; E=1-210.
DR PDB; 5IY9; EM; 6.30 A; E=1-210.
DR PDB; 5IYA; EM; 5.40 A; E=1-210.
DR PDB; 5IYB; EM; 3.90 A; E=1-210.
DR PDB; 5IYC; EM; 3.90 A; E=1-210.
DR PDB; 5IYD; EM; 3.90 A; E=1-210.
DR PDB; 6DRD; EM; 3.90 A; E=1-210.
DR PDB; 6O9L; EM; 7.20 A; E=1-210.
DR PDB; 6XRE; EM; 4.60 A; E=1-210.
DR PDB; 7A6H; EM; 3.30 A; E=1-210.
DR PDB; 7AE1; EM; 2.80 A; E=1-210.
DR PDB; 7AE3; EM; 3.10 A; E=1-210.
DR PDB; 7AEA; EM; 3.40 A; E=1-210.
DR PDB; 7AST; EM; 4.00 A; F=1-210.
DR PDB; 7D58; EM; 2.90 A; E=1-210.
DR PDB; 7D59; EM; 3.10 A; E=1-210.
DR PDB; 7DN3; EM; 3.50 A; E=1-210.
DR PDB; 7DU2; EM; 3.35 A; E=1-210.
DR PDB; 7FJI; EM; 3.60 A; E=1-210.
DR PDB; 7FJJ; EM; 3.60 A; E=1-210.
DR PDB; 7LBM; EM; 4.80 A; E=1-210.
DR PDB; 7OB9; EM; 2.70 A; E=1-210.
DR PDB; 7OBA; EM; 3.10 A; E=1-210.
DR PDB; 7OBB; EM; 3.30 A; E=1-210.
DR PDB; 7VBA; EM; 2.89 A; E=1-210.
DR PDB; 7VBB; EM; 2.81 A; E=1-210.
DR PDB; 7VBC; EM; 3.01 A; E=1-210.
DR PDBsum; 5IY6; -.
DR PDBsum; 5IY7; -.
DR PDBsum; 5IY8; -.
DR PDBsum; 5IY9; -.
DR PDBsum; 5IYA; -.
DR PDBsum; 5IYB; -.
DR PDBsum; 5IYC; -.
DR PDBsum; 5IYD; -.
DR PDBsum; 6DRD; -.
DR PDBsum; 6O9L; -.
DR PDBsum; 6XRE; -.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; P19388; -.
DR SMR; P19388; -.
DR BioGRID; 111430; 204.
DR ComplexPortal; CPX-6145; PAQosome co-chaperone complex.
DR CORUM; P19388; -.
DR DIP; DIP-56N; -.
DR IntAct; P19388; 159.
DR MINT; P19388; -.
DR STRING; 9606.ENSP00000478303; -.
DR GlyGen; P19388; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P19388; -.
DR MetOSite; P19388; -.
DR PhosphoSitePlus; P19388; -.
DR BioMuta; POLR2E; -.
DR DMDM; 116242767; -.
DR REPRODUCTION-2DPAGE; IPI00291093; -.
DR SWISS-2DPAGE; P19388; -.
DR EPD; P19388; -.
DR jPOST; P19388; -.
DR MassIVE; P19388; -.
DR MaxQB; P19388; -.
DR PaxDb; P19388; -.
DR PeptideAtlas; P19388; -.
DR PRIDE; P19388; -.
DR ProteomicsDB; 53653; -.
DR TopDownProteomics; P19388; -.
DR Antibodypedia; 22550; 316 antibodies from 28 providers.
DR DNASU; 5434; -.
DR Ensembl; ENST00000586746.5; ENSP00000464739.1; ENSG00000099817.12.
DR Ensembl; ENST00000612655.4; ENSP00000485021.1; ENSG00000099817.12.
DR Ensembl; ENST00000615234.5; ENSP00000478303.1; ENSG00000099817.12.
DR GeneID; 5434; -.
DR KEGG; hsa:5434; -.
DR MANE-Select; ENST00000615234.5; ENSP00000478303.1; NM_002695.5; NP_002686.3.
DR UCSC; uc002lre.5; human.
DR CTD; 5434; -.
DR DisGeNET; 5434; -.
DR GeneCards; POLR2E; -.
DR HGNC; HGNC:9192; POLR2E.
DR HPA; ENSG00000099817; Low tissue specificity.
DR MIM; 180664; gene.
DR neXtProt; NX_P19388; -.
DR OpenTargets; ENSG00000099817; -.
DR PharmGKB; PA33512; -.
DR VEuPathDB; HostDB:ENSG00000099817; -.
DR eggNOG; KOG3218; Eukaryota.
DR GeneTree; ENSGT00390000013841; -.
DR HOGENOM; CLU_058320_0_1_1; -.
DR InParanoid; P19388; -.
DR OMA; VRDRGYF; -.
DR OrthoDB; 1255823at2759; -.
DR PhylomeDB; P19388; -.
DR PathwayCommons; P19388; -.
DR Reactome; R-HSA-112382; Formation of RNA Pol II elongation complex.
DR Reactome; R-HSA-113418; Formation of the Early Elongation Complex.
DR Reactome; R-HSA-167152; Formation of HIV elongation complex in the absence of HIV Tat.
DR Reactome; R-HSA-167158; Formation of the HIV-1 Early Elongation Complex.
DR Reactome; R-HSA-167160; RNA Pol II CTD phosphorylation and interaction with CE during HIV infection.
DR Reactome; R-HSA-167161; HIV Transcription Initiation.
DR Reactome; R-HSA-167162; RNA Polymerase II HIV Promoter Escape.
DR Reactome; R-HSA-167172; Transcription of the HIV genome.
DR Reactome; R-HSA-167200; Formation of HIV-1 elongation complex containing HIV-1 Tat.
DR Reactome; R-HSA-167238; Pausing and recovery of Tat-mediated HIV elongation.
DR Reactome; R-HSA-167242; Abortive elongation of HIV-1 transcript in the absence of Tat.
DR Reactome; R-HSA-167243; Tat-mediated HIV elongation arrest and recovery.
DR Reactome; R-HSA-167246; Tat-mediated elongation of the HIV-1 transcript.
DR Reactome; R-HSA-167287; HIV elongation arrest and recovery.
DR Reactome; R-HSA-167290; Pausing and recovery of HIV elongation.
DR Reactome; R-HSA-168325; Viral Messenger RNA Synthesis.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-203927; MicroRNA (miRNA) biogenesis.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-5578749; Transcriptional regulation by small RNAs.
DR Reactome; R-HSA-5601884; PIWI-interacting RNA (piRNA) biogenesis.
DR Reactome; R-HSA-5617472; Activation of anterior HOX genes in hindbrain development during early embryogenesis.
DR Reactome; R-HSA-674695; RNA Polymerase II Pre-transcription Events.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6796648; TP53 Regulates Transcription of DNA Repair Genes.
DR Reactome; R-HSA-6803529; FGFR2 alternative splicing.
DR Reactome; R-HSA-6807505; RNA polymerase II transcribes snRNA genes.
DR Reactome; R-HSA-72086; mRNA Capping.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72165; mRNA Splicing - Minor Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73776; RNA Polymerase II Promoter Escape.
DR Reactome; R-HSA-73779; RNA Polymerase II Transcription Pre-Initiation And Promoter Opening.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-75953; RNA Polymerase II Transcription Initiation.
DR Reactome; R-HSA-75955; RNA Polymerase II Transcription Elongation.
DR Reactome; R-HSA-76042; RNA Polymerase II Transcription Initiation And Promoter Clearance.
DR Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
DR Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
DR Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
DR Reactome; R-HSA-77075; RNA Pol II CTD phosphorylation and interaction with CE.
DR Reactome; R-HSA-8851708; Signaling by FGFR2 IIIa TM.
DR Reactome; R-HSA-9018519; Estrogen-dependent gene expression.
DR Reactome; R-HSA-9670095; Inhibition of DNA recombination at telomere.
DR SignaLink; P19388; -.
DR SIGNOR; P19388; -.
DR BioGRID-ORCS; 5434; 807 hits in 1056 CRISPR screens.
DR ChiTaRS; POLR2E; human.
DR GeneWiki; POLR2E; -.
DR GenomeRNAi; 5434; -.
DR Pharos; P19388; Tbio.
DR PRO; PR:P19388; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P19388; protein.
DR Bgee; ENSG00000099817; Expressed in stromal cell of endometrium and 212 other tissues.
DR ExpressionAtlas; P19388; baseline and differential.
DR Genevisible; P19388; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB.
DR GO; GO:0005666; C:RNA polymerase III complex; IBA:GO_Central.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; IPI:ComplexPortal.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0050821; P:protein stabilization; IC:ComplexPortal.
DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB.
DR Gene3D; 3.40.1340.10; -; 1.
DR Gene3D; 3.90.940.20; -; 1.
DR HAMAP; MF_00025; RNApol_Rpo5_RPB5; 1.
DR InterPro; IPR014381; Arch_Rpo5/euc_Rpb5.
DR InterPro; IPR005571; RNA_pol_Rpb5_N.
DR InterPro; IPR036710; RNA_pol_Rpb5_N_sf.
DR InterPro; IPR000783; RNA_pol_subH/Rpb5_C.
DR InterPro; IPR020608; RNA_pol_subH/Rpb5_CS.
DR InterPro; IPR035913; RPB5-like_sf.
DR PANTHER; PTHR10535; PTHR10535; 1.
DR Pfam; PF01191; RNA_pol_Rpb5_C; 1.
DR Pfam; PF03871; RNA_pol_Rpb5_N; 1.
DR PIRSF; PIRSF000747; RPB5; 1.
DR SUPFAM; SSF53036; SSF53036; 1.
DR SUPFAM; SSF55287; SSF55287; 1.
DR PROSITE; PS01110; RNA_POL_H_23KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Direct protein sequencing;
KW DNA-directed RNA polymerase; Host-virus interaction; Isopeptide bond;
KW Nucleus; Reference proteome; Transcription; Ubl conjugation.
FT CHAIN 1..210
FT /note="DNA-directed RNA polymerases I, II, and III subunit
FT RPABC1"
FT /id="PRO_0000146075"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT CROSSLNK 81
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 44
FT /note="S -> F (in dbSNP:rs12459404)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:2753903,
FT ECO:0000269|PubMed:7828586, ECO:0000269|Ref.6"
FT /id="VAR_028259"
FT CONFLICT 132
FT /note="Q -> E (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 157
FT /note="T -> S (in Ref. 3; BAA07406)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="I -> V (in Ref. 7; AAH34144)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="K -> R (in Ref. 3; BAA07406)"
FT /evidence="ECO:0000305"
FT HELIX 6..23
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 30..33
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 37..43
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 48..51
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 55..58
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 60..66
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 70..75
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 101..108
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 112..120
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 121..124
FT /evidence="ECO:0007829|PDB:7DU2"
FT STRAND 126..132
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 167..169
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 178..183
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 190..196
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 198..210
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 210 AA; 24551 MW; 1E88AFDBCF9C8535 CRC64;
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV
LVAHNDDPTD QMFVFFPEEP KVGIKTIKVY CQRMQEENIT RALIVVQQGM TPSAKQSLVD
MAPKYILEQF LQQELLINIT EHELVPEHVV MTKEEVTELL ARYKLRENQL PRIQAGDPVA
RYFGIKRGQV VKIIRPSETA GRYITYRLVQ
