ID RPAB5_HUMAN Reviewed; 67 AA. AC P62875; P52436; Q6FHX3; DT 16-AUG-2004, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 1. DT 27-MAR-2024, entry version 179. DE RecName: Full=DNA-directed RNA polymerases I, II, and III subunit RPABC5; DE Short=RNA polymerases I, II, and III subunit ABC5; DE AltName: Full=DNA-directed RNA polymerase III subunit L; DE AltName: Full=RNA polymerase II 7.6 kDa subunit; DE Short=RPB7.6; DE AltName: Full=RPB10 homolog; GN Name=POLR2L {ECO:0000312|HGNC:HGNC:9199}; 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]. RX PubMed=8524256; DOI=10.1128/mcb.15.12.6895; RA McKune K., Moore P.A., Hull M.W., Woychik N.A.; RT "Six human RNA polymerase subunits functionally substitute for their yeast RT counterparts."; RL Mol. Cell. Biol. 15:6895-6900(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Cerebellum; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone marrow, and Kidney; 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 [5] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-32. RX PubMed=7651387; DOI=10.1128/mcb.15.9.4702; RA Shpakovski G.V., Acker J., Wintzerith M., Lacroix J.F., Thuriaux P., RA Vigneron M.; RT "Four subunits that are shared by the three classes of RNA polymerase are RT functionally interchangeable between Homo sapiens and Saccharomyces RT cerevisiae."; RL Mol. Cell. Biol. 15:4702-4710(1995). RN [6] 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 [7] RP IDENTIFICATION IN THE RNA POL I COMPLEX, FUNCTION, AND SUBCELLULAR RP LOCATION. 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 [8] 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 [9] 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 [10] RP STRUCTURE BY ELECTRON MICROSCOPY (3.90 ANGSTROMS) IN COMPLEX WITH ZN(2+), RP FUNCTION OF POL II, AND 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 [11] 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 [12] 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 [13] 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 [14] RP STRUCTURE BY ELECTRON MICROSCOPY (3.35 ANGSTROMS) IN COMPLEX WITH ZN(2+), RP 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 [15] 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 [16] RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS) IN COMPLEX WITH ZN(2+), RP 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 [17] 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 [18] RP STRUCTURE BY ELECTRON MICROSCOPY (2.90 ANGSTROMS) IN COMPLEX WITH ZN(2+), RP 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 [19] 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 a small RNAs, such as 5S rRNA and tRNAs, respectively. CC {ECO:0000250, ECO:0000250|UniProtKB:P22139, 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:27193682, CC PubMed:30190596, PubMed:33335104, PubMed:33558764, PubMed:33558766, CC PubMed:33674783, PubMed:34675218). 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 CC (PubMed:9852112, PubMed:27193682, PubMed:30190596). Pol III complex CC consists of a ten-subunit catalytic core composed of POLR3A/RPC1, CC POLR3B/RPC2, POLR1C/RPAC1, POLR1D/RPAC2, POLR3K/RPC10, POLR2E/RPABC1, CC POLR2F/RPABC2, POLR2H/RPABC3, POLR2K/RPABC4 and POLR2L/RPABC5; a mobile CC stalk composed of two subunits POLR3H/RPC8 and CRCP/RPC9, protruding CC from the core and functioning primarily in transcription initiation; CC and additional subunits homologous to general transcription factors of CC the RNA polymerase II machinery, POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 CC heterotrimer required for transcription initiation and POLR3D/RPC4- CC POLR3E/RPC5 heterodimer involved in both transcription initiation and CC termination (PubMed:33335104, PubMed:33674783, PubMed:34675218, CC PubMed:33558764, PubMed:33558766). {ECO:0000250|UniProtKB:P22139, CC ECO:0000269|PubMed:27193682, ECO:0000269|PubMed:30190596, 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:9852112}. CC -!- INTERACTION: CC P62875; O95994: AGR2; NbExp=3; IntAct=EBI-359527, EBI-712648; CC P62875; Q8N9N5: BANP; NbExp=3; IntAct=EBI-359527, EBI-744695; CC P62875; P38432: COIL; NbExp=3; IntAct=EBI-359527, EBI-945751; CC P62875; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-359527, EBI-19153639; CC P62875; Q96JM7: L3MBTL3; NbExp=3; IntAct=EBI-359527, EBI-2686809; CC P62875; Q96RE7: NACC1; NbExp=3; IntAct=EBI-359527, EBI-7950997; CC P62875; Q8IXK0: PHC2; NbExp=3; IntAct=EBI-359527, EBI-713786; CC P62875; O15514: POLR2D; NbExp=3; IntAct=EBI-359527, EBI-394737; CC P62875; P60900: PSMA6; NbExp=3; IntAct=EBI-359527, EBI-357793; CC P62875; Q04864: REL; NbExp=3; IntAct=EBI-359527, EBI-307352; CC P62875; Q04864-2: REL; NbExp=3; IntAct=EBI-359527, EBI-10829018; CC P62875; Q9BWH6: RPAP1; NbExp=3; IntAct=EBI-359527, EBI-1048085; CC P62875; Q96R06: SPAG5; NbExp=3; IntAct=EBI-359527, EBI-413317; CC P62875; Q9NVV9: THAP1; NbExp=3; IntAct=EBI-359527, EBI-741515; CC P62875; Q13625-3: TP53BP2; NbExp=3; IntAct=EBI-359527, EBI-10175039; CC P62875; Q15645: TRIP13; NbExp=3; IntAct=EBI-359527, EBI-358993; CC P62875; O43829: ZBTB14; NbExp=3; IntAct=EBI-359527, EBI-10176632; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16809778, CC ECO:0000269|PubMed:33335104, ECO:0000269|PubMed:9852112}. Nucleus, CC nucleolus {ECO:0000305|PubMed:34887565, ECO:0000305|PubMed:36271492}. CC -!- SIMILARITY: Belongs to the archaeal Rpo10/eukaryotic RPB10 RNA CC polymerase 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; U37690; AAA91459.1; -; mRNA. DR EMBL; CR536565; CAG38802.1; -; mRNA. DR EMBL; AK311997; BAG34935.1; -; mRNA. DR EMBL; BC005903; AAH05903.1; -; mRNA. DR EMBL; BC018649; AAH18649.1; -; mRNA. DR EMBL; Z47729; CAA87658.1; -; Genomic_DNA. DR EMBL; Z47728; CAA87657.1; -; Genomic_DNA. DR CCDS; CCDS7720.1; -. DR PIR; S53015; S53015. DR RefSeq; NP_066951.1; NM_021128.4. DR PDB; 5IY6; EM; 7.20 A; J=1-67. DR PDB; 5IY7; EM; 8.60 A; J=1-67. DR PDB; 5IY8; EM; 7.90 A; J=1-67. DR PDB; 5IY9; EM; 6.30 A; J=1-67. DR PDB; 5IYA; EM; 5.40 A; J=1-67. DR PDB; 5IYB; EM; 3.90 A; J=1-67. DR PDB; 5IYC; EM; 3.90 A; J=1-67. DR PDB; 5IYD; EM; 3.90 A; J=1-67. DR PDB; 6DRD; EM; 3.90 A; J=1-67. DR PDB; 6O9L; EM; 7.20 A; J=1-67. DR PDB; 6XRE; EM; 4.60 A; J=1-67. DR PDB; 7A6H; EM; 3.30 A; J=1-67. DR PDB; 7AE1; EM; 2.80 A; J=1-67. DR PDB; 7AE3; EM; 3.10 A; J=1-67. DR PDB; 7AEA; EM; 3.40 A; J=1-67. DR PDB; 7AST; EM; 4.00 A; B=1-67. DR PDB; 7D58; EM; 2.90 A; J=1-67. DR PDB; 7D59; EM; 3.10 A; J=1-67. DR PDB; 7DN3; EM; 3.50 A; J=1-67. DR PDB; 7DU2; EM; 3.35 A; J=1-67. DR PDB; 7FJI; EM; 3.60 A; J=1-67. DR PDB; 7FJJ; EM; 3.60 A; J=1-67. DR PDB; 7LBM; EM; 4.80 A; J=1-67. DR PDB; 7OB9; EM; 2.70 A; J=1-67. DR PDB; 7OBA; EM; 3.10 A; J=1-67. DR PDB; 7OBB; EM; 3.30 A; J=1-67. DR PDB; 7VBA; EM; 2.89 A; J=1-67. DR PDB; 7VBB; EM; 2.81 A; J=1-67. DR PDB; 7VBC; EM; 3.01 A; J=1-67. DR PDB; 8A43; EM; 4.09 A; J=1-67. DR PDB; 8ITY; EM; 3.90 A; J=1-67. DR PDB; 8IUE; EM; 4.10 A; J=1-67. DR PDB; 8IUH; EM; 3.40 A; J=1-67. 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; P62875; -. 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-16828; -. DR EMDB; EMD-16832; -. DR EMDB; EMD-16833; -. 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; P62875; -. DR BioGRID; 111437; 174. 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-7481; DNA-directed RNA polymerase II complex. DR ComplexPortal; CPX-7482; DNA-directed RNA polymerase III complex, POLR3GL variant. DR CORUM; P62875; -. DR DIP; DIP-32960N; -. DR IntAct; P62875; 55. DR MINT; P62875; -. DR STRING; 9606.ENSP00000324124; -. DR iPTMnet; P62875; -. DR PhosphoSitePlus; P62875; -. DR SwissPalm; P62875; -. DR BioMuta; POLR2L; -. DR DMDM; 51338657; -. DR EPD; P62875; -. DR jPOST; P62875; -. DR MassIVE; P62875; -. DR MaxQB; P62875; -. DR PaxDb; 9606-ENSP00000324124; -. DR PeptideAtlas; P62875; -. DR ProteomicsDB; 57442; -. DR Pumba; P62875; -. DR TopDownProteomics; P62875; -. DR Antibodypedia; 22712; 120 antibodies from 21 providers. DR DNASU; 5441; -. DR Ensembl; ENST00000322028.5; ENSP00000324124.4; ENSG00000177700.6. DR Ensembl; ENST00000534030.1; ENSP00000432807.1; ENSG00000177700.6. DR GeneID; 5441; -. DR KEGG; hsa:5441; -. DR MANE-Select; ENST00000322028.5; ENSP00000324124.4; NM_021128.5; NP_066951.1. DR UCSC; uc001lsc.4; human. DR AGR; HGNC:9199; -. DR CTD; 5441; -. DR DisGeNET; 5441; -. DR GeneCards; POLR2L; -. DR HGNC; HGNC:9199; POLR2L. DR HPA; ENSG00000177700; Low tissue specificity. DR MIM; 601189; gene. DR neXtProt; NX_P62875; -. DR OpenTargets; ENSG00000177700; -. DR PharmGKB; PA33519; -. DR VEuPathDB; HostDB:ENSG00000177700; -. DR eggNOG; KOG3497; Eukaryota. DR GeneTree; ENSGT00390000007087; -. DR HOGENOM; CLU_143122_1_1_1; -. DR InParanoid; P62875; -. DR OMA; KYCCRRM; -. DR OrthoDB; 257at2759; -. DR PhylomeDB; P62875; -. DR TreeFam; TF103046; -. DR PathwayCommons; P62875; -. 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; P62875; -. DR SIGNOR; P62875; -. DR BioGRID-ORCS; 5441; 847 hits in 1154 CRISPR screens. DR ChiTaRS; POLR2L; human. DR GeneWiki; POLR2L; -. DR GenomeRNAi; 5441; -. DR Pharos; P62875; Tbio. DR PRO; PR:P62875; -. DR Proteomes; UP000005640; Chromosome 11. DR RNAct; P62875; Protein. DR Bgee; ENSG00000177700; Expressed in apex of heart and 213 other cell types or tissues. 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:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc. DR GO; GO:0008270; F:zinc ion binding; IDA:UniProtKB. DR GO; GO:0006356; P:regulation of transcription by RNA polymerase I; TAS:ProtInc. DR GO; GO:0006360; P:transcription by RNA polymerase I; IBA:GO_Central. DR GO; GO:0006366; P:transcription by RNA polymerase II; IDA:UniProtKB. DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IBA:GO_Central. DR Gene3D; 1.10.10.60; Homeodomain-like; 1. DR HAMAP; MF_00250; RNApol_arch_Rpo10; 1. DR InterPro; IPR023580; RNA_pol_su_RPB10. DR InterPro; IPR020789; RNA_pol_suN_Zn-BS. DR InterPro; IPR000268; RPABC5/Rpb10. DR PANTHER; PTHR23431:SF10; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5; 1. DR PANTHER; PTHR23431; DNA-DIRECTED RNA POLYMERASES I, II, AND III SUBUNIT RPABC5 FAMILY MEMBER; 1. DR Pfam; PF01194; RNA_pol_N; 1. DR PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1. DR SUPFAM; SSF46924; RNA polymerase subunit RPB10; 1. DR PROSITE; PS01112; RNA_POL_N_8KD; 1. DR Genevisible; P62875; HS. PE 1: Evidence at protein level; KW 3D-structure; DNA-directed RNA polymerase; Metal-binding; Nucleus; KW Reference proteome; Transcription; Zinc. FT CHAIN 1..67 FT /note="DNA-directed RNA polymerases I, II, and III subunit FT RPABC5" FT /id="PRO_0000121333" FT BINDING 7 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, FT ECO:0000269|PubMed:33674783, ECO:0007744|PDB:5IY6, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7DN3" FT BINDING 10 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, FT ECO:0000269|PubMed:33674783, ECO:0007744|PDB:5IY6, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7DN3" FT BINDING 44 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33558766, FT ECO:0000269|PubMed:33674783, ECO:0007744|PDB:5IY6, FT ECO:0007744|PDB:7AE1, ECO:0007744|PDB:7D58, FT ECO:0007744|PDB:7DN3" FT BINDING 45 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000269|PubMed:27193682, FT ECO:0000269|PubMed:33558764, ECO:0000269|PubMed:33674783, FT ECO:0007744|PDB:5IY6, ECO:0007744|PDB:7AE1, FT ECO:0007744|PDB:7DN3" FT STRAND 8..10 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 15..17 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 18..26 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 31..36 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 37..39 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 43..50 FT /evidence="ECO:0007829|PDB:7OB9" FT HELIX 55..59 FT /evidence="ECO:0007829|PDB:7OB9" FT TURN 60..62 FT /evidence="ECO:0007829|PDB:7OB9" SQ SEQUENCE 67 AA; 7645 MW; 9E8A72F667FE7EC5 CRC64; MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK //