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 27-MAR-2024, entry version 229. 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 {ECO:0000312|HGNC:HGNC:9192}; 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 FUNCTION, AND 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 FUNCTION OF POL III. RX PubMed=20413673; DOI=10.1101/gr.101337.109; RA Canella D., Praz V., Reina J.H., Cousin P., Hernandez N.; RT "Defining the RNA polymerase III transcriptome: Genome-wide localization of RT the RNA polymerase III transcription machinery in human cells."; RL Genome Res. 20:710-721(2010). RN [13] 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 [14] 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 [15] 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 [16] 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). RN [17] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION OF POL II, AND RP SUBUNIT. RX PubMed=27193682; DOI=10.1038/nature17970; RA He Y., Yan C., Fang J., Inouye C., Tjian R., Ivanov I., Nogales E.; RT "Near-atomic resolution visualization of human transcription promoter RT opening."; RL Nature 533:359-365(2016). RN [18] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS), FUNCTION OF POL II, AND RP SUBUNIT. RX PubMed=30190596; DOI=10.1038/s41594-018-0118-5; RA Jishage M., Yu X., Shi Y., Ganesan S.J., Chen W.Y., Sali A., Chait B.T., RA Asturias F.J., Roeder R.G.; RT "Architecture of Pol II(G) and molecular mechanism of transcription RT regulation by Gdown1."; RL Nat. Struct. Mol. Biol. 25:859-867(2018). RN [19] RP STRUCTURE BY ELECTRON MICROSCOPY (4.00 ANGSTROMS), SUBUNIT, AND SUBCELLULAR RP LOCATION. RX PubMed=33335104; DOI=10.1038/s41467-020-20262-5; RA Ramsay E.P., Abascal-Palacios G., Daiss J.L., King H., Gouge J., Pilsl M., RA Beuron F., Morris E., Gunkel P., Engel C., Vannini A.; RT "Structure of human RNA polymerase III."; RL Nat. Commun. 11:6409-6421(2020). RN [20] RP STRUCTURE BY ELECTRON MICROSCOPY (2.81 ANGSTROMS), FUNCTION OF POL I, AND RP SUBUNIT. RX PubMed=34671025; DOI=10.1038/s41421-021-00335-5; RA Zhao D., Liu W., Chen K., Wu Z., Yang H., Xu Y.; RT "Structure of the human RNA polymerase I elongation complex."; RL Cell Discov. 7:97-109(2021). RN [21] RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS), AND SUBUNIT. RX PubMed=33674783; DOI=10.1038/s41422-021-00472-2; RA Li L., Yu Z., Zhao D., Ren Y., Hou H., Xu Y.; RT "Structure of human RNA polymerase III elongation complex."; RL Cell Res. 31:791-800(2021). RN [22] RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), AND SUBUNIT. RX PubMed=34675218; DOI=10.1038/s41467-021-26402-9; RA Hou H., Li Y., Wang M., Liu A., Yu Z., Chen K., Zhao D., Xu Y.; RT "Structural insights into RNA polymerase III-mediated transcription RT termination through trapping poly-deoxythymidine."; RL Nat. Commun. 12:6135-6146(2021). RN [23] RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS), AND SUBUNIT. RX PubMed=33558764; DOI=10.1038/s41594-020-00555-5; RA Girbig M., Misiaszek A.D., Vorlander M.K., Lafita A., Grotsch H., RA Baudin F., Bateman A., Muller C.W.; RT "Cryo-EM structures of human RNA polymerase III in its unbound and RT transcribing states."; RL Nat. Struct. Mol. Biol. 28:210-219(2021). RN [24] RP STRUCTURE BY ELECTRON MICROSCOPY (2.70 ANGSTROMS), FUNCTION OF POL I, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=34887565; DOI=10.1038/s41594-021-00693-4; RA Misiaszek A.D., Girbig M., Grotsch H., Baudin F., Murciano B., Lafita A., RA Muller C.W.; RT "Cryo-EM structures of human RNA polymerase I."; RL Nat. Struct. Mol. Biol. 28:997-1008(2021). RN [25] RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS), AND SUBUNIT. RX PubMed=33558766; DOI=10.1038/s41594-021-00557-x; RA Wang Q., Li S., Wan F., Xu Y., Wu Z., Cao M., Lan P., Lei M., Wu J.; RT "Structural insights into transcriptional regulation of human RNA RT polymerase III."; RL Nat. Struct. Mol. Biol. 28:220-227(2021). RN [26] RP STRUCTURE BY ELECTRON MICROSCOPY (4.09 ANGSTROMS), FUNCTION OF POL I, RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=36271492; DOI=10.26508/lsa.202201568; RA Daiss J.L., Pilsl M., Straub K., Bleckmann A., Hocherl M., Heiss F.B., RA Abascal-Palacios G., Ramsay E.P., Tluckova K., Mars J.C., Furtges T., RA Bruckmann A., Rudack T., Bernecky C., Lamour V., Panov K., Vannini A., RA Moss T., Engel C.; RT "The human RNA polymerase I structure reveals an HMG-like docking domain RT specific to metazoans."; RL Life. Sci Alliance 5:1-20(2022). 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/RPABC1 is part of the lower CC jaw surrounding the central large cleft and thought to grab the CC incoming DNA template. {ECO:0000250|UniProtKB:P20434, CC ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:20413673, CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, CC ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34887565, CC ECO:0000269|PubMed:36271492, 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, PubMed:33335104, PubMed:33674783, PubMed:34675218, CC PubMed:33558764, PubMed:33558766). Pol I complex consists of a ten- CC subunit catalytic core composed of POLR1A/RPA1, POLR1B/RPA2, CC POLR1C/RPAC1, POLR1D/RPAC2, POLR1H/RPA12, POLR2E/RPABC1, POLR2F/RPABC2, CC POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile stalk subunit CC POLR1F/RPA43 protruding from the core and additional subunits CC homologous to general transcription factors POLR1E/RPA49 and CC POLR1G/RPA34. Part of Pol I pre-initiation complex (PIC), in which Pol CC I core assembles with RRN3 and promoter-bound UTBF and SL1/TIF-IB CC complex (PubMed:34671025, PubMed:34887565, PubMed:36271492). Pol II CC complex contains a ten-subunit catalytic core composed of POLR2A/RPB1, CC POLR2B/RPB2, POLR2C/RPB3, POLR2I/RPB9, POLR2J/RPB11, POLR2E/RPABC1, CC POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5 and a CC mobile stalk composed of two subunits POLR2D/RPB4 and POLR2G/RPB7. Part CC of Pol II(G) complex, in which Pol II core associates with an CC additional subunit POLR2M; unlike conventional Pol II, Pol II(G) CC functions as a transcriptional repressor. Part of TBP-based Pol II pre- CC initiation complex (PIC), in which Pol II core assembles with general CC transcription factors and other specific initiation factors including CC GTF2E1, GTF2E2, GTF2F1, GTF2F2, TCEA1, ERCC2, ERCC3, GTF2H2, GTF2H3, CC GTF2H4, GTF2H5, GTF2A1, GTF2A2, GTF2B and TBP; this large multi-subunit CC PIC complex mediates DNA unwinding and targets Pol II core to the CC transcription start site where the first phosphodiester bond forms. In CC Pol II complex, this subunit is present in 2-fold molar excess over the CC other subunits (PubMed:9852112, PubMed:27193682, PubMed:30190596). Pol CC III complex consists of a ten-subunit catalytic core composed of CC POLR3A/RPC1, POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10, CC POLR2E/RPABC1, POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and CC POLR2L/RPABC5; a mobile stalk composed of two subunits POLR3H/RPC8 and CC CRCP/RPC9, protruding from the core and functioning primarily in CC transcription initiation; and additional subunits homologous to general CC transcription factors of the RNA polymerase II machinery, POLR3C/RPC3- CC POLR3F/RPC6-POLR3G/RPC7 heterotrimer required for transcription CC initiation and POLR3D/RPC4-POLR3E/RPC5 heterodimer involved in both CC transcription initiation and termination (PubMed:33335104, CC PubMed:33674783, PubMed:34675218, PubMed:33558764, PubMed:33558766). CC Component of the PAQosome complex which is responsible for the CC biogenesis of several protein complexes and which consists of R2TP CC complex members RUVBL1, RUVBL2, RPAP3 and PIH1D1, URI complex members CC PFDN2, PFDN6, PDRG1, UXT and URI1 as well as ASDURF, POLR2E and CC DNAAF10/WDR92 (PubMed:31738558). Interacts with URI1 (PubMed:9819440). CC {ECO:0000269|PubMed:16809778, ECO:0000269|PubMed:27193682, CC ECO:0000269|PubMed:30190596, ECO:0000269|PubMed:31738558, CC ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:33558764, CC ECO:0000269|PubMed:33558766, ECO:0000269|PubMed:33674783, CC ECO:0000269|PubMed:34671025, ECO:0000269|PubMed:34675218, CC ECO:0000269|PubMed:34887565, ECO:0000269|PubMed:36271492, CC ECO:0000269|PubMed:9819440, 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:33335104, CC ECO:0000269|PubMed:9852112}. Nucleus, nucleolus CC {ECO:0000305|PubMed:34887565, ECO:0000305|PubMed:36271492}. CC -!- SIMILARITY: Belongs to the archaeal Rpo5/eukaryotic RPB5 RNA polymerase CC subunit family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 8A43; EM; 4.09 A; E=1-210. DR PDB; 8ITY; EM; 3.90 A; E=1-210. DR PDB; 8IUE; EM; 4.10 A; E=1-210. DR PDB; 8IUH; EM; 3.40 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 PDBsum; 8A43; -. DR PDBsum; 8ITY; -. DR PDBsum; 8IUE; -. DR PDBsum; 8IUH; -. DR AlphaFoldDB; P19388; -. DR EMDB; EMD-11673; -. DR EMDB; EMD-11736; -. DR EMDB; EMD-11738; -. DR EMDB; EMD-11742; -. DR EMDB; EMD-11904; -. DR EMDB; EMD-12795; -. DR EMDB; EMD-12796; -. DR EMDB; EMD-12797; -. DR EMDB; EMD-15135; -. DR EMDB; EMD-22294; -. DR EMDB; EMD-23255; -. DR EMDB; EMD-30577; -. DR EMDB; EMD-30578; -. DR EMDB; EMD-30779; -. DR EMDB; EMD-30865; -. DR EMDB; EMD-31621; -. DR EMDB; EMD-31622; -. DR EMDB; EMD-31876; -. DR EMDB; EMD-31877; -. DR EMDB; EMD-31878; -. DR EMDB; EMD-35712; -. DR EMDB; EMD-35719; -. DR EMDB; EMD-35722; -. DR EMDB; EMD-7997; -. DR EMDB; EMD-8132; -. DR EMDB; EMD-8133; -. DR EMDB; EMD-8134; -. DR EMDB; EMD-8135; -. DR EMDB; EMD-8136; -. DR EMDB; EMD-8137; -. DR EMDB; EMD-8138; -. DR SMR; P19388; -. DR BioGRID; 111430; 281. DR ComplexPortal; CPX-2386; DNA-directed RNA polymerase I complex. DR ComplexPortal; CPX-2387; DNA-directed RNA polymerase II complex, Pol II(G) variant. DR ComplexPortal; CPX-2393; DNA-directed RNA polymerase III complex, POLR3G variant. DR ComplexPortal; CPX-6145; PAQosome co-chaperone complex. DR ComplexPortal; CPX-7481; DNA-directed RNA polymerase II complex. DR ComplexPortal; CPX-7482; DNA-directed RNA polymerase III complex, POLR3GL variant. DR CORUM; P19388; -. DR DIP; DIP-56N; -. DR IntAct; P19388; 162. 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 EPD; P19388; -. DR jPOST; P19388; -. DR MassIVE; P19388; -. DR MaxQB; P19388; -. DR PaxDb; 9606-ENSP00000478303; -. DR PeptideAtlas; P19388; -. DR ProteomicsDB; 53653; -. DR Pumba; P19388; -. DR TopDownProteomics; P19388; -. DR Antibodypedia; 22550; 343 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 AGR; HGNC:9192; -. 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; 101801at2759; -. 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; 834 hits in 1141 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 214 other cell types or tissues. DR ExpressionAtlas; P19388; baseline and differential. 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; IDA:UniProtKB. DR GO; GO:0005665; C:RNA polymerase II, core complex; IDA:UniProtKB. DR GO; GO:0005666; C:RNA polymerase III complex; IDA:UniProtKB. 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; NAS:ComplexPortal. DR GO; GO:0006360; P:transcription by RNA polymerase I; IEA:GOC. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0006383; P:transcription by RNA polymerase III; IEA:GOC. DR Gene3D; 3.40.1340.10; RNA polymerase, Rpb5, N-terminal domain; 1. DR Gene3D; 3.90.940.20; RPB5-like RNA polymerase subunit; 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; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1; 1. DR PANTHER; PTHR10535:SF0; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC1; 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; Eukaryotic RPB5 N-terminal domain; 1. DR SUPFAM; SSF55287; RPB5-like RNA polymerase subunit; 1. DR PROSITE; PS01110; RNA_POL_H_23KD; 1. DR SWISS-2DPAGE; P19388; -. DR Genevisible; P19388; HS. 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 //