RPC5_HUMAN
ID RPC5_HUMAN Reviewed; 708 AA.
AC Q9NVU0; B4DL24; B4DUP6; H3BT11; Q9BWF7; Q9H8W8; Q9H907; Q9P276;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=DNA-directed RNA polymerase III subunit RPC5;
DE Short=RNA polymerase III subunit C5;
DE AltName: Full=DNA-directed RNA polymerase III 80 kDa polypeptide;
GN Name=POLR3E; Synonyms=KIAA1452;
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] (ISOFORM 1), IDENTIFICATION IN THE RNA POL III
RP COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, AND INTERACTION WITH POLR3D.
RX PubMed=12391170; DOI=10.1128/mcb.22.22.8044-8055.2002;
RA Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.;
RT "Characterization of human RNA polymerase III identifies orthologues for
RT Saccharomyces cerevisiae RNA polymerase III subunits.";
RL Mol. Cell. Biol. 22:8044-8055(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4 AND 5).
RC TISSUE=Teratocarcinoma, and Tongue;
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 GENOMIC DNA].
RX PubMed=15616553; DOI=10.1038/nature03187;
RA Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G.,
RA Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E.,
RA Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J., Buckingham J.M.,
RA Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C.,
RA Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M.,
RA Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M.,
RA Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D.,
RA Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L.,
RA Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E.,
RA Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H.,
RA Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y.,
RA Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J.,
RA Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D.,
RA Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S.,
RA Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A.,
RA Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M.,
RA Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H.,
RA Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A.,
RA Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J.,
RA DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J.,
RA Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M.,
RA Myers R.M., Rubin E.M., Pennacchio L.A.;
RT "The sequence and analysis of duplication-rich human chromosome 16.";
RL Nature 432:988-994(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Eye;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-503 AND SER-522, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [8]
RP FUNCTION.
RX PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
RA Chiu Y.-H., Macmillan J.B., Chen Z.J.;
RT "RNA polymerase III detects cytosolic DNA and induces type I interferons
RT through the RIG-I pathway.";
RL Cell 138:576-591(2009).
RN [9]
RP FUNCTION.
RX PubMed=19609254; DOI=10.1038/ni.1779;
RA Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
RA Hornung V.;
RT "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA
RT polymerase III-transcribed RNA intermediate.";
RL Nat. Immunol. 10:1065-1072(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; TYR-224 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161; SER-162 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192 AND SER-503, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-161 AND SER-162, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498 AND LYS-659, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-498, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-659, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-659, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [20]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-171; LYS-432; LYS-498 AND
RP LYS-659, AND IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Specific peripheric component of RNA polymerase III which synthesizes
CC small RNAs, such as 5S rRNA and tRNAs. Essential for efficient
CC transcription from both the type 2 VAI and type 3 U6 RNA polymerase III
CC promoters. Plays a key role in sensing and limiting infection by
CC intracellular bacteria and DNA viruses. Acts as nuclear and cytosolic
CC DNA sensor involved in innate immune response. Can sense non-self dsDNA
CC that serves as template for transcription into dsRNA. The non-self RNA
CC polymerase III transcripts, such as Epstein-Barr virus-encoded RNAs
CC (EBERs) induce type I interferon and NF- Kappa-B through the RIG-I
CC pathway (By similarity). {ECO:0000250, ECO:0000269|PubMed:19609254,
CC ECO:0000269|PubMed:19631370}.
CC -!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
CC consisting of 17 subunits (By similarity). Interacts with POLR3D/RPC4.
CC {ECO:0000250, ECO:0000269|PubMed:12391170}.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q9NVU0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NVU0-2; Sequence=VSP_007065;
CC Name=3;
CC IsoId=Q9NVU0-3; Sequence=VSP_007064;
CC Name=4;
CC IsoId=Q9NVU0-4; Sequence=VSP_044710;
CC Name=5;
CC IsoId=Q9NVU0-5; Sequence=VSP_046374;
CC -!- MISCELLANEOUS: [Isoform 3]: May result from the retention of an intron
CC in the cDNA. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95976.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAB14481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY092085; AAM18215.1; -; mRNA.
DR EMBL; AB040885; BAA95976.1; ALT_INIT; mRNA.
DR EMBL; AK001371; BAA91655.1; -; mRNA.
DR EMBL; AK023160; BAB14437.1; -; mRNA.
DR EMBL; AK023231; BAB14481.1; ALT_INIT; mRNA.
DR EMBL; AK296813; BAG59386.1; -; mRNA.
DR EMBL; AK300735; BAG62408.1; -; mRNA.
DR EMBL; AC009034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000285; AAH00285.1; -; mRNA.
DR CCDS; CCDS10605.1; -. [Q9NVU0-1]
DR CCDS; CCDS58432.1; -. [Q9NVU0-4]
DR CCDS; CCDS58433.1; -. [Q9NVU0-2]
DR CCDS; CCDS58434.1; -. [Q9NVU0-5]
DR RefSeq; NP_001244962.1; NM_001258033.1. [Q9NVU0-4]
DR RefSeq; NP_001244963.1; NM_001258034.1. [Q9NVU0-5]
DR RefSeq; NP_001244964.1; NM_001258035.1.
DR RefSeq; NP_001244965.1; NM_001258036.1. [Q9NVU0-2]
DR RefSeq; NP_060589.1; NM_018119.3. [Q9NVU0-1]
DR RefSeq; XP_006721126.1; XM_006721063.2.
DR RefSeq; XP_006726676.1; XM_006726613.1.
DR PDB; 7A6H; EM; 3.30 A; M=1-708.
DR PDB; 7AE1; EM; 2.80 A; M=1-708.
DR PDB; 7AE3; EM; 3.10 A; M=1-708.
DR PDB; 7AEA; EM; 3.40 A; M=1-708.
DR PDB; 7AST; EM; 4.00 A; K=1-708.
DR PDB; 7ASU; X-ray; 2.23 A; A=1-708.
DR PDB; 7ASV; X-ray; 1.55 A; A/B=1-708.
DR PDB; 7D58; EM; 2.90 A; M=1-708.
DR PDB; 7D59; EM; 3.10 A; M=1-708.
DR PDB; 7DN3; EM; 3.50 A; M=1-708.
DR PDB; 7DU2; EM; 3.35 A; M=1-708.
DR PDB; 7FJI; EM; 3.60 A; M=1-708.
DR PDB; 7FJJ; EM; 3.60 A; M=1-708.
DR PDBsum; 7A6H; -.
DR PDBsum; 7AE1; -.
DR PDBsum; 7AE3; -.
DR PDBsum; 7AEA; -.
DR PDBsum; 7AST; -.
DR PDBsum; 7ASU; -.
DR PDBsum; 7ASV; -.
DR PDBsum; 7D58; -.
DR PDBsum; 7D59; -.
DR PDBsum; 7DN3; -.
DR PDBsum; 7DU2; -.
DR PDBsum; 7FJI; -.
DR PDBsum; 7FJJ; -.
DR AlphaFoldDB; Q9NVU0; -.
DR SMR; Q9NVU0; -.
DR BioGRID; 120840; 86.
DR BioGRID; 3190820; 9.
DR IntAct; Q9NVU0; 54.
DR MINT; Q9NVU0; -.
DR STRING; 9606.ENSP00000299853; -.
DR GlyGen; Q9NVU0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NVU0; -.
DR PhosphoSitePlus; Q9NVU0; -.
DR BioMuta; POLR3E; -.
DR DMDM; 29428028; -.
DR EPD; Q9NVU0; -.
DR jPOST; Q9NVU0; -.
DR MassIVE; Q9NVU0; -.
DR MaxQB; Q9NVU0; -.
DR PaxDb; Q9NVU0; -.
DR PeptideAtlas; Q9NVU0; -.
DR PRIDE; Q9NVU0; -.
DR ProteomicsDB; 42503; -.
DR ProteomicsDB; 4504; -.
DR ProteomicsDB; 82857; -. [Q9NVU0-1]
DR ProteomicsDB; 82858; -. [Q9NVU0-2]
DR ProteomicsDB; 82859; -. [Q9NVU0-3]
DR Antibodypedia; 25851; 134 antibodies from 23 providers.
DR DNASU; 55718; -.
DR Ensembl; ENST00000299853.10; ENSP00000299853.5; ENSG00000058600.16. [Q9NVU0-1]
DR Ensembl; ENST00000359210.8; ENSP00000352140.4; ENSG00000058600.16. [Q9NVU0-2]
DR Ensembl; ENST00000418581.6; ENSP00000399254.2; ENSG00000058600.16. [Q9NVU0-5]
DR Ensembl; ENST00000564209.5; ENSP00000456967.1; ENSG00000058600.16. [Q9NVU0-4]
DR Ensembl; ENST00000639550.2; ENSP00000492514.2; ENSG00000284282.3. [Q9NVU0-1]
DR Ensembl; ENST00000640588.2; ENSP00000492263.1; ENSG00000284282.3. [Q9NVU0-1]
DR GeneID; 55718; -.
DR KEGG; hsa:55718; -.
DR MANE-Select; ENST00000299853.10; ENSP00000299853.5; NM_018119.4; NP_060589.1.
DR UCSC; uc002dkk.5; human. [Q9NVU0-1]
DR CTD; 55718; -.
DR DisGeNET; 55718; -.
DR GeneCards; POLR3E; -.
DR HGNC; HGNC:30347; POLR3E.
DR HPA; ENSG00000058600; Tissue enhanced (skeletal).
DR MIM; 617815; gene.
DR neXtProt; NX_Q9NVU0; -.
DR OpenTargets; ENSG00000058600; -.
DR PharmGKB; PA134964025; -.
DR VEuPathDB; HostDB:ENSG00000058600; -.
DR eggNOG; KOG2354; Eukaryota.
DR GeneTree; ENSGT00390000016123; -.
DR HOGENOM; CLU_021012_1_0_1; -.
DR InParanoid; Q9NVU0; -.
DR OMA; MDTSACD; -.
DR OrthoDB; 1110776at2759; -.
DR PhylomeDB; Q9NVU0; -.
DR TreeFam; TF103050; -.
DR PathwayCommons; Q9NVU0; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
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-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 SignaLink; Q9NVU0; -.
DR SIGNOR; Q9NVU0; -.
DR BioGRID-ORCS; 55718; 708 hits in 1087 CRISPR screens.
DR ChiTaRS; POLR3E; human.
DR GeneWiki; POLR3E; -.
DR Pharos; Q9NVU0; Tbio.
DR PRO; PR:Q9NVU0; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q9NVU0; protein.
DR Bgee; ENSG00000058600; Expressed in gastrocnemius and 130 other tissues.
DR ExpressionAtlas; Q9NVU0; baseline and differential.
DR Genevisible; Q9NVU0; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
DR InterPro; IPR006886; RNA_pol_III_Rpc5.
DR InterPro; IPR045576; RPC5_C.
DR PANTHER; PTHR12069; PTHR12069; 1.
DR Pfam; PF04801; RPC5; 1.
DR Pfam; PF19725; RPC5_C; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Antiviral defense;
KW DNA-directed RNA polymerase; Immunity; Innate immunity; Isopeptide bond;
KW Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Ubl conjugation.
FT CHAIN 1..708
FT /note="DNA-directed RNA polymerase III subunit RPC5"
FT /id="PRO_0000073970"
FT REGION 146..170
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..518
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 161
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:24275569"
FT MOD_RES 162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 224
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 503
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT CROSSLNK 171
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 432
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 498
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 13..48
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_046374"
FT VAR_SEQ 623..708
FT /note="FPPQTAASPDEQKVFALWESGDMSDQHRQVLLEIFSKNYRVRRNMIQSRLTQ
FT ECGEDLSKQEVDKVLKDCCVSYGGMWYLKGTVQS -> VSRALPARGMGGGGWGEPAVG
FT RPRGDTGGHAW (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10819331"
FT /id="VSP_007064"
FT VAR_SEQ 648..668
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044710"
FT VAR_SEQ 649..690
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007065"
FT VARIANT 46
FT /note="S -> A (in dbSNP:rs2347)"
FT /id="VAR_024623"
FT CONFLICT 14
FT /note="D -> N (in Ref. 2; BAB14437)"
FT /evidence="ECO:0000305"
FT CONFLICT 80
FT /note="N -> D (in Ref. 3; BAG62408)"
FT /evidence="ECO:0000305"
FT CONFLICT 148
FT /note="K -> E (in Ref. 2; BAB14437)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="K -> Q (in Ref. 1; AAM18215)"
FT /evidence="ECO:0000305"
FT HELIX 4..6
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 10..17
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 20..24
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 25..34
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 39..42
FT /evidence="ECO:0007829|PDB:7D58"
FT STRAND 44..49
FT /evidence="ECO:0007829|PDB:7AE1"
FT TURN 51..54
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 57..61
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 64..66
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 71..81
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 93..96
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 99..106
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 114..120
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 123..128
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 130..137
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 140..153
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 193..200
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:7AE3"
FT STRAND 206..211
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:7A6H"
FT HELIX 216..221
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 222..225
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 242..249
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 270..273
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 278..288
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 294..301
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 303..305
FT /evidence="ECO:0007829|PDB:7AEA"
FT HELIX 307..317
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 318..321
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 324..327
FT /evidence="ECO:0007829|PDB:7ASU"
FT HELIX 329..332
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 340..344
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 346..362
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 364..366
FT /evidence="ECO:0007829|PDB:7ASU"
FT HELIX 368..375
FT /evidence="ECO:0007829|PDB:7ASU"
FT HELIX 379..387
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 390..393
FT /evidence="ECO:0007829|PDB:7ASU"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:7ASU"
FT STRAND 397..402
FT /evidence="ECO:0007829|PDB:7ASU"
FT HELIX 406..411
FT /evidence="ECO:0007829|PDB:7ASU"
FT HELIX 413..433
FT /evidence="ECO:0007829|PDB:7ASU"
FT HELIX 559..573
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 574..577
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 578..591
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 597..599
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 604..613
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 616..619
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 631..634
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 636..639
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 646..657
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 661..663
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 665..676
FT /evidence="ECO:0007829|PDB:7ASV"
FT HELIX 682..692
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 699..702
FT /evidence="ECO:0007829|PDB:7ASV"
FT STRAND 706..708
FT /evidence="ECO:0007829|PDB:7D59"
SQ SEQUENCE 708 AA; 79898 MW; E9DB71615CC367A5 CRC64;
MANEEDDPVV QEIDVYLAKS LAEKLYLFQY PVRPASMTYD DIPHLSAKIK PKQQKVELEM
AIDTLNPNYC RSKGEQIALN VDGACADETS TYSSKLMDKQ TFCSSQTTSN TSRYAAALYR
QGELHLTPLH GILQLRPSFS YLDKADAKHR EREAANEAGD SSQDEAEDDV KQITVRFSRP
ESEQARQRRV QSYEFLQKKH AEEPWVHLHY YGLRDSRSEH ERQYLLCPGS SGVENTELVK
SPSEYLMMLM PPSQEEEKDK PVAPSNVLSM AQLRTLPLAD QIKILMKNVK VMPFANLMSL
LGPSIDSVAV LRGIQKVAML VQGNWVVKSD ILYPKDSSSP HSGVPAEVLC RGRDFVMWKF
TQSRWVVRKE VATVTKLCAE DVKDFLEHMA VVRINKGWEF ILPYDGEFIK KHPDVVQRQH
MLWTGIQAKL EKVYNLVKET MPKKPDAQSG PAGLVCGDQR IQVAKTKAQQ NHALLERELQ
RRKEQLRVPA VPPGVRIKEE PVSEEGEEDE EQEAEEEPMD TSPSGLHSKL ANGLPLGRAA
GTDSFNGHPP QGCASTPVAR ELKAFVEATF QRQFVLTLSE LKRLFNLHLA SLPPGHTLFS
GISDRMLQDT VLAAGCKQIL VPFPPQTAAS PDEQKVFALW ESGDMSDQHR QVLLEIFSKN
YRVRRNMIQS RLTQECGEDL SKQEVDKVLK DCCVSYGGMW YLKGTVQS
