ID RPC4_HUMAN Reviewed; 398 AA. AC P05423; Q6FI28; Q9BPV7; Q9BPZ1; Q9BXB3; DT 01-NOV-1988, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2003, sequence version 2. DT 27-MAR-2024, entry version 201. DE RecName: Full=DNA-directed RNA polymerase III subunit RPC4; DE Short=RNA polymerase III subunit C4; DE AltName: Full=DNA-directed RNA polymerase III subunit D; DE AltName: Full=Protein BN51; DE AltName: Full=RNA polymerase III 47 kDa subunit; DE AltName: Full=RPC53 homolog; GN Name=POLR3D {ECO:0000312|HGNC:HGNC:1080}; Synonyms=BN51, BN51T; 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=3683386; DOI=10.1128/mcb.7.10.3386-3393.1987; RA Ittmann M., Greco A., Basilico C.; RT "Isolation of the human gene that complements a temperature-sensitive cell RT cycle mutation in BHK cells."; RL Mol. Cell. Biol. 7:3386-3393(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN THE RNA POL III COMPLEX, RP IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH POLR3E, AND FUNCTION. 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 [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Lymph; 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 [MRNA] OF 1-50. RX PubMed=11279001; DOI=10.1074/jbc.m100088200; RA Chong S.S., Hu P., Hernandez N.; RT "Reconstitution of transcription from the human U6 small nuclear RNA RT promoter with eight recombinant polypeptides and a partially purified RNA RT polymerase III complex."; RL J. Biol. Chem. 276:20727-20734(2001). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. RA Ittmann M.; RT "Promoter structure and cell cycle control of the BN51 cell cycle gene, RT which encodes a subunit of RNA polymerase III."; RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases. RN [7] 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 [8] 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 [9] 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 [10] 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 [11] RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY RP 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 [13] RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-95; ARG-97 AND ARG-99, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Colon carcinoma; RX PubMed=24129315; DOI=10.1074/mcp.o113.027870; RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M., RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V., RA Bedford M.T., Comb M.J.; RT "Immunoaffinity enrichment and mass spectrometry analysis of protein RT methylation."; RL Mol. Cell. Proteomics 13:372-387(2014). RN [14] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-141; LYS-206; LYS-220 AND RP LYS-302, AND 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 [15] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-141; LYS-220; LYS-285 AND RP LYS-302, AND IDENTIFICATION BY MASS 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 [16] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-78; LYS-141; LYS-220; LYS-302 AND RP LYS-396, AND IDENTIFICATION BY MASS 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 [17] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-68; LYS-78; LYS-141; LYS-152; RP LYS-160; LYS-190; LYS-199; LYS-206; LYS-220; LYS-285; LYS-302; LYS-310 AND RP LYS-396, 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). RN [18] RP FUNCTION OF POL III, AND SUBUNIT. RX PubMed=35637192; DOI=10.1038/s41467-022-30323-6; RA Van Bortle K., Marciano D.P., Liu Q., Chou T., Lipchik A.M., Gollapudi S., RA Geller B.S., Monte E., Kamakaka R.T., Snyder M.P.; RT "A cancer-associated RNA polymerase III identity drives robust RT transcription and expression of snaR-A non-coding RNA."; RL Nat. Commun. 13:3007-3007(2022). 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 (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 [21] RP STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS), FUNCTION, 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 [22] RP STRUCTURE BY ELECTRON MICROSCOPY (2.80 ANGSTROMS), FUNCTION, SUBUNIT, AND RP SUMOYLATION AT LYS-141. 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 [23] 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). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of CC DNA into RNA using the four ribonucleoside triphosphates as substrates CC (PubMed:20413673, PubMed:12391170, PubMed:35637192, PubMed:34675218, CC PubMed:33558764). Specific peripheric component of RNA polymerase III CC (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, CC snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. CC Assembles with POLR3E/RPC5 forming a subcomplex that binds the Pol III CC core. Enables recruitment of Pol III at transcription initiation site CC and drives transcription initiation from both type 2 and type 3 DNA CC promoters. Required for efficient transcription termination and CC reinitiation (PubMed:20413673, PubMed:12391170, PubMed:35637192) (By CC similarity). Pol III plays a key role in sensing and limiting infection CC by intracellular bacteria and DNA viruses. Acts as nuclear and CC cytosolic DNA sensor involved in innate immune response. Can sense non- CC self dsDNA that serves as template for transcription into dsRNA. The CC non-self RNA polymerase III transcripts, such as Epstein-Barr virus- CC encoded RNAs (EBERs) induce type I interferon and NF-kappa-B through CC the RIG-I pathway (PubMed:19609254, PubMed:19631370). CC {ECO:0000250|UniProtKB:P25441, ECO:0000269|PubMed:12391170, CC ECO:0000269|PubMed:19609254, ECO:0000269|PubMed:19631370, CC ECO:0000269|PubMed:20413673, ECO:0000269|PubMed:33558764, CC ECO:0000269|PubMed:34675218, ECO:0000269|PubMed:35637192}. CC -!- SUBUNIT: Component of the RNA polymerase III complex consisting of 17 CC subunits: a ten-subunit horseshoe-shaped 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:12391170, CC PubMed:33335104, PubMed:33674783, PubMed:34675218). CC {ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:33335104, CC ECO:0000269|PubMed:33674783, ECO:0000269|PubMed:34675218}. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}. CC -!- PTM: Sumoylation on Lys-141 can serve as a signal to mark misfolded Pol CC III for proteasomal degradation. {ECO:0000269|PubMed:33558764}. CC -!- SIMILARITY: Belongs to the eukaryotic RPC4/POLR3D RNA polymerase CC subunit family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BC000516; Type=Frameshift; Evidence={ECO:0000305}; CC Sequence=BC003039; Type=Frameshift; Evidence={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; M17754; AAA51838.1; -; mRNA. DR EMBL; AY092086; AAM18216.1; -; mRNA. DR EMBL; CR536509; CAG38747.1; -; mRNA. DR EMBL; CR541803; CAG46602.1; -; mRNA. DR EMBL; BC000516; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC003039; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; BC002603; AAH02603.1; -; mRNA. DR EMBL; BC004484; AAH04484.1; -; mRNA. DR EMBL; AF346574; AAK15371.1; -; mRNA. DR EMBL; L15301; AAA72377.1; -; Genomic_DNA. DR CCDS; CCDS34858.1; -. DR PIR; A43700; A43700. DR RefSeq; NP_001713.2; NM_001722.2. DR PDB; 7A6H; EM; 3.30 A; N=1-398. DR PDB; 7AE1; EM; 2.80 A; N=1-398. DR PDB; 7AE3; EM; 3.10 A; N=1-398. DR PDB; 7AEA; EM; 3.40 A; N=1-398. DR PDB; 7AST; EM; 4.00 A; L=1-398. DR PDB; 7D58; EM; 2.90 A; N=1-398. DR PDB; 7D59; EM; 3.10 A; N=1-398. DR PDB; 7DN3; EM; 3.50 A; N=1-398. DR PDB; 7DU2; EM; 3.35 A; N=1-398. DR PDB; 7FJI; EM; 3.60 A; N=1-398. DR PDB; 7FJJ; EM; 3.60 A; N=1-398. DR PDB; 8ITY; EM; 3.90 A; N=1-398. DR PDB; 8IUE; EM; 4.10 A; N=1-398. DR PDB; 8IUH; EM; 3.40 A; N=1-398. 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; 8ITY; -. DR PDBsum; 8IUE; -. DR PDBsum; 8IUH; -. DR AlphaFoldDB; P05423; -. DR EMDB; EMD-11673; -. DR EMDB; EMD-11736; -. DR EMDB; EMD-11738; -. DR EMDB; EMD-11742; -. DR EMDB; EMD-11904; -. 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-35712; -. DR EMDB; EMD-35719; -. DR EMDB; EMD-35722; -. DR SMR; P05423; -. DR BioGRID; 107129; 86. DR ComplexPortal; CPX-2393; DNA-directed RNA polymerase III complex, POLR3G variant. DR ComplexPortal; CPX-7482; DNA-directed RNA polymerase III complex, POLR3GL variant. DR DIP; DIP-56155N; -. DR IntAct; P05423; 38. DR MINT; P05423; -. DR STRING; 9606.ENSP00000380904; -. DR GlyGen; P05423; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P05423; -. DR PhosphoSitePlus; P05423; -. DR SwissPalm; P05423; -. DR BioMuta; POLR3D; -. DR DMDM; 29429159; -. DR EPD; P05423; -. DR jPOST; P05423; -. DR MassIVE; P05423; -. DR MaxQB; P05423; -. DR PaxDb; 9606-ENSP00000380904; -. DR PeptideAtlas; P05423; -. DR ProteomicsDB; 51838; -. DR Pumba; P05423; -. DR Antibodypedia; 22571; 205 antibodies from 28 providers. DR DNASU; 661; -. DR Ensembl; ENST00000306433.9; ENSP00000303088.4; ENSG00000168495.13. DR Ensembl; ENST00000397802.8; ENSP00000380904.3; ENSG00000168495.13. DR GeneID; 661; -. DR KEGG; hsa:661; -. DR MANE-Select; ENST00000306433.9; ENSP00000303088.4; NM_001722.3; NP_001713.2. DR UCSC; uc003xbl.4; human. DR AGR; HGNC:1080; -. DR CTD; 661; -. DR DisGeNET; 661; -. DR GeneCards; POLR3D; -. DR HGNC; HGNC:1080; POLR3D. DR HPA; ENSG00000168495; Low tissue specificity. DR MIM; 187280; gene. DR neXtProt; NX_P05423; -. DR OpenTargets; ENSG00000168495; -. DR PharmGKB; PA25390; -. DR VEuPathDB; HostDB:ENSG00000168495; -. DR eggNOG; KOG3122; Eukaryota. DR GeneTree; ENSGT00390000013948; -. DR HOGENOM; CLU_042288_0_0_1; -. DR InParanoid; P05423; -. DR OMA; QAENTCT; -. DR OrthoDB; 11394at2759; -. DR PhylomeDB; P05423; -. DR PathwayCommons; P05423; -. 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; P05423; -. DR SIGNOR; P05423; -. DR BioGRID-ORCS; 661; 429 hits in 1161 CRISPR screens. DR ChiTaRS; POLR3D; human. DR GeneWiki; POLR3D; -. DR GenomeRNAi; 661; -. DR Pharos; P05423; Tbio. DR PRO; PR:P05423; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; P05423; Protein. DR Bgee; ENSG00000168495; Expressed in sural nerve and 137 other cell types or tissues. DR ExpressionAtlas; P05423; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005666; C:RNA polymerase III complex; IDA:UniProtKB. DR GO; GO:0003682; F:chromatin binding; IDA:MGI. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. 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:0045089; P:positive regulation of innate immune response; IDA:UniProtKB. DR GO; GO:0032728; P:positive regulation of interferon-beta production; IDA:UniProtKB. DR GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IBA:GO_Central. DR InterPro; IPR007811; RPC4. DR PANTHER; PTHR13408; DNA-DIRECTED RNA POLYMERASE III; 1. DR PANTHER; PTHR13408:SF0; DNA-DIRECTED RNA POLYMERASE III SUBUNIT RPC4; 1. DR Pfam; PF05132; RNA_pol_Rpc4; 1. DR Genevisible; P05423; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Antiviral defense; DNA-directed RNA polymerase; KW Immunity; Innate immunity; Isopeptide bond; Methylation; Nucleus; KW Phosphoprotein; Reference proteome; Transcription; Ubl conjugation. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:22814378" FT CHAIN 2..398 FT /note="DNA-directed RNA polymerase III subunit RPC4" FT /id="PRO_0000073967" FT REGION 1..114 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 220..244 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 62..100 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 220..236 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylserine" FT /evidence="ECO:0007744|PubMed:22814378" FT MOD_RES 42 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 95 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 97 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT MOD_RES 99 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0007744|PubMed:24129315" FT CROSSLNK 68 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 78 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 141 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0000269|PubMed:33558764, FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733" FT CROSSLNK 152 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 160 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 190 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 199 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 206 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25218447, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 220 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 CROSSLNK 285 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25772364, FT ECO:0007744|PubMed:28112733" FT CROSSLNK 302 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 CROSSLNK 310 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT CROSSLNK 396 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:25755297, FT ECO:0007744|PubMed:28112733" FT CONFLICT 9..18 FT /note="EPSTPGGPRP -> RPARQGPDL (in Ref. 1; AAA51838)" FT /evidence="ECO:0000305" FT CONFLICT 9..12 FT /note="EPST -> RPAR (in Ref. 6; AAA72377)" FT /evidence="ECO:0000305" FT CONFLICT 26..40 FT /note="LIGRRPAPPLTPGRL -> SSGGGGLPSPPAV (in Ref. 1)" FT /evidence="ECO:0000305" FT CONFLICT 98 FT /note="G -> R (in Ref. 1; AAA51838)" FT /evidence="ECO:0000305" FT CONFLICT 233 FT /note="K -> R (in Ref. 2; AAM18216)" FT /evidence="ECO:0000305" FT CONFLICT 286 FT /note="P -> L (in Ref. 2; AAM18216)" FT /evidence="ECO:0000305" FT TURN 37..41 FT /evidence="ECO:0007829|PDB:7D58" FT HELIX 112..123 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 133..135 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 144..147 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 148..150 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 250..256 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 257..260 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 265..270 FT /evidence="ECO:0007829|PDB:7AE1" FT TURN 318..320 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 323..331 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 333..335 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 337..340 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 342..350 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 356..364 FT /evidence="ECO:0007829|PDB:7AE1" FT STRAND 367..387 FT /evidence="ECO:0007829|PDB:7AE1" FT HELIX 389..395 FT /evidence="ECO:0007829|PDB:7AE1" SQ SEQUENCE 398 AA; 44396 MW; CD8AFF3257B78410 CRC64; MSEGNAAGEP STPGGPRPLL TGARGLIGRR PAPPLTPGRL PSIRSRDLTL GGVKKKTFTP NIISRKIKEE PKEEVTVKKE KRERDRDRQR EGHGRGRGRP EVIQSHSIFE QGPAEMMKKK GNWDKTVDVS DMGPSHIINI KKEKRETDEE TKQILRMLEK DDFLDDPGLR NDTRNMPVQL PLAHSGWLFK EENDEPDVKP WLAGPKEEDM EVDIPAVKVK EEPRDEEEEA KMKAPPKAAR KTPGLPKDVS VAELLRELSL TKEEELLFLQ LPDTLPGQPP TQDIKPIKTE VQGEDGQVVL IKQEKDREAK LAENACTLAD LTEGQVGKLL IRKSGRVQLL LGKVTLDVTM GTACSFLQEL VSVGLGDSRT GEMTVLGHVK HKLVCSPDFE SLLDHKHR //