ID   TF3C1_HUMAN             Reviewed;        2109 AA.
AC   Q12789; B2RP21; Q12838; Q6DKN9; Q9Y4W9;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 4.
DT   27-NOV-2024, entry version 195.
DE   RecName: Full=General transcription factor 3C polypeptide 1;
DE   AltName: Full=TF3C-alpha;
DE   AltName: Full=TFIIIC box B-binding subunit;
DE   AltName: Full=Transcription factor IIIC 220 kDa subunit;
DE            Short=TFIIIC 220 kDa subunit;
DE            Short=TFIIIC220;
DE   AltName: Full=Transcription factor IIIC subunit alpha;
GN   Name=GTF3C1;
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), AND PROTEIN SEQUENCE OF 1103-1121.
RX   PubMed=8127861; DOI=10.1073/pnas.91.5.1652;
RA   L'Etoile N.D., Fahnestock M.L., Shen Y., Aebersold R., Berk A.J.;
RT   "Human transcription factor IIIC box B binding subunit.";
RL   Proc. Natl. Acad. Sci. U.S.A. 91:1652-1656(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=10493829; DOI=10.1006/geno.1999.5927;
RA   Loftus B.J., Kim U.-J., Sneddon V.P., Kalush F., Brandon R., Fuhrmann J.,
RA   Mason T., Crosby M.L., Barnstead M., Cronin L., Mays A.D., Cao Y., Xu R.X.,
RA   Kang H.-L., Mitchell S., Eichler E.E., Harris P.C., Venter J.C.,
RA   Adams M.D.;
RT   "Genome duplications and other features in 12 Mb of DNA sequence from human
RT   chromosome 16p and 16q.";
RL   Genomics 60:295-308(1999).
RN   [3]
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP   [LARGE SCALE MRNA] OF 1107-2109 (ISOFORM 2).
RC   TISSUE=Brain, and Cervix;
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 71-728 (ISOFORM 1).
RX   PubMed=8164661; DOI=10.1128/mcb.14.5.3053-3064.1994;
RA   Lagna G., Kovelman R., Sukegawa J., Roeder R.G.;
RT   "Cloning and characterization of an evolutionarily divergent DNA-binding
RT   subunit of mammalian TFIIIC.";
RL   Mol. Cell. Biol. 14:3053-3064(1994).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA   Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT   "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT   networks.";
RL   Cell 127:635-648(2006).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1653, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=16964243; DOI=10.1038/nbt1240;
RA   Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT   "A probability-based approach for high-throughput protein phosphorylation
RT   analysis and site localization.";
RL   Nat. Biotechnol. 24:1285-1292(2006).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1969, AND IDENTIFICATION BY
RP   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   [9]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-1062; SER-1632;
RP   SER-1653; SER-1856; SER-1865 AND SER-1868, AND IDENTIFICATION BY MASS
RP   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   [11]
RP   INTERACTION WITH MAF1.
RX   PubMed=18377933; DOI=10.1016/j.jmb.2008.02.060;
RA   Goodfellow S.J., Graham E.L., Kantidakis T., Marshall L., Coppins B.A.,
RA   Oficjalska-Pham D., Gerard M., Lefebvre O., White R.J.;
RT   "Regulation of RNA polymerase III transcription by Maf1 in mammalian
RT   cells.";
RL   J. Mol. Biol. 378:481-491(2008).
RN   [12]
RP   IDENTIFICATION BY MASS 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   [13]
RP   INTERACTION WITH IGHMBP2.
RX   PubMed=19299493; DOI=10.1093/hmg/ddp134;
RA   de Planell-Saguer M., Schroeder D.G., Rodicio M.C., Cox G.A.,
RA   Mourelatos Z.;
RT   "Biochemical and genetic evidence for a role of IGHMBP2 in the
RT   translational machinery.";
RL   Hum. Mol. Genet. 18:2115-2126(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1068; SER-1865 AND SER-1868,
RP   AND 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1062; SER-1068; SER-1632;
RP   SER-1653; SER-1865 AND SER-1868, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [16]
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   [17]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-667; SER-739; SER-1062 AND
RP   SER-1068, AND 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   [18]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-739; SER-1068; SER-1253;
RP   SER-1611; SER-1632; SER-1653; SER-1865 AND SER-1868, 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   [19]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1911, AND IDENTIFICATION BY
RP   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   [20]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-833 AND LYS-1142, AND
RP   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   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-529; LYS-770; LYS-833 AND
RP   LYS-1142, 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: Required for RNA polymerase III-mediated transcription.
CC       Component of TFIIIC that initiates transcription complex assembly on
CC       tRNA and is required for transcription of 5S rRNA and other stable
CC       nuclear and cytoplasmic RNAs. Binds to the box B promoter element.
CC   -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC       subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6
CC       (PubMed:19299493). Interacts with IGHMBP2. Interacts with MAF1
CC       (PubMed:18377933). {ECO:0000269|PubMed:18377933,
CC       ECO:0000269|PubMed:19299493}.
CC   -!- INTERACTION:
CC       Q12789; Q6RW13: AGTRAP; NbExp=3; IntAct=EBI-357956, EBI-741181;
CC       Q12789; Q96DZ9: CMTM5; NbExp=3; IntAct=EBI-357956, EBI-2548702;
CC       Q12789; Q8WUA4: GTF3C2; NbExp=3; IntAct=EBI-357956, EBI-1237062;
CC       Q12789; Q1RN33: MAGEA4; NbExp=3; IntAct=EBI-357956, EBI-10194128;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q12789-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q12789-3; Sequence=VSP_021819;
CC   -!- SIMILARITY: Belongs to the TFIIIC subunit 1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA17985.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAA85638.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential vector sequence at the N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; U02619; AAA17985.1; ALT_FRAME; mRNA.
DR   EMBL; AC002303; AAB67637.1; -; Genomic_DNA.
DR   EMBL; AC025275; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC002551; AAC05811.1; -; Genomic_DNA.
DR   EMBL; BC044857; AAH44857.1; -; mRNA.
DR   EMBL; BC137229; AAI37230.1; -; mRNA.
DR   EMBL; U06485; AAA85638.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS32414.1; -. [Q12789-2]
DR   CCDS; CCDS66988.1; -. [Q12789-3]
DR   PIR; B56011; B56011.
DR   PIR; I38414; I38414.
DR   RefSeq; NP_001273171.1; NM_001286242.1. [Q12789-3]
DR   RefSeq; NP_001511.2; NM_001520.3. [Q12789-2]
DR   PDB; 8CLI; EM; 3.20 A; A=1-2109.
DR   PDB; 8CLJ; EM; 3.20 A; A/F=1-2109.
DR   PDB; 8CLK; EM; 3.50 A; A=1-2109.
DR   PDB; 8CLL; EM; 3.40 A; A/F=1-2109.
DR   PDBsum; 8CLI; -.
DR   PDBsum; 8CLJ; -.
DR   PDBsum; 8CLK; -.
DR   PDBsum; 8CLL; -.
DR   AlphaFoldDB; Q12789; -.
DR   EMDB; EMD-16713; -.
DR   EMDB; EMD-16714; -.
DR   EMDB; EMD-16715; -.
DR   EMDB; EMD-16717; -.
DR   SMR; Q12789; -.
DR   BioGRID; 109230; 273.
DR   ComplexPortal; CPX-2373; General transcription factor TFIIIC complex.
DR   CORUM; Q12789; -.
DR   DIP; DIP-38212N; -.
DR   IntAct; Q12789; 123.
DR   MINT; Q12789; -.
DR   STRING; 9606.ENSP00000348510; -.
DR   GlyCosmos; Q12789; 1 site, 1 glycan.
DR   GlyGen; Q12789; 4 sites, 1 O-linked glycan (4 sites).
DR   iPTMnet; Q12789; -.
DR   MetOSite; Q12789; -.
DR   PhosphoSitePlus; Q12789; -.
DR   SwissPalm; Q12789; -.
DR   BioMuta; GTF3C1; -.
DR   DMDM; 215274233; -.
DR   jPOST; Q12789; -.
DR   MassIVE; Q12789; -.
DR   PaxDb; 9606-ENSP00000348510; -.
DR   PeptideAtlas; Q12789; -.
DR   ProteomicsDB; 58924; -. [Q12789-2]
DR   ProteomicsDB; 58925; -. [Q12789-3]
DR   Pumba; Q12789; -.
DR   Antibodypedia; 26269; 41 antibodies from 11 providers.
DR   DNASU; 2975; -.
DR   Ensembl; ENST00000356183.9; ENSP00000348510.4; ENSG00000077235.18. [Q12789-2]
DR   Ensembl; ENST00000561623.5; ENSP00000455417.1; ENSG00000077235.18. [Q12789-3]
DR   GeneID; 2975; -.
DR   KEGG; hsa:2975; -.
DR   MANE-Select; ENST00000356183.9; ENSP00000348510.4; NM_001520.4; NP_001511.2.
DR   UCSC; uc002dou.4; human. [Q12789-2]
DR   AGR; HGNC:4664; -.
DR   CTD; 2975; -.
DR   DisGeNET; 2975; -.
DR   GeneCards; GTF3C1; -.
DR   HGNC; HGNC:4664; GTF3C1.
DR   HPA; ENSG00000077235; Low tissue specificity.
DR   MIM; 603246; gene.
DR   neXtProt; NX_Q12789; -.
DR   OpenTargets; ENSG00000077235; -.
DR   PharmGKB; PA29052; -.
DR   VEuPathDB; HostDB:ENSG00000077235; -.
DR   eggNOG; KOG4560; Eukaryota.
DR   GeneTree; ENSGT00390000008664; -.
DR   HOGENOM; CLU_001556_1_0_1; -.
DR   InParanoid; Q12789; -.
DR   OMA; PHKVHVE; -.
DR   OrthoDB; 72674at2759; -.
DR   PhylomeDB; Q12789; -.
DR   TreeFam; TF351624; -.
DR   PathwayCommons; Q12789; -.
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   SignaLink; Q12789; -.
DR   SIGNOR; Q12789; -.
DR   BioGRID-ORCS; 2975; 686 hits in 1148 CRISPR screens.
DR   ChiTaRS; GTF3C1; human.
DR   GeneWiki; GTF3C1; -.
DR   GenomeRNAi; 2975; -.
DR   Pharos; Q12789; Tbio.
DR   PRO; PR:Q12789; -.
DR   Proteomes; UP000005640; Chromosome 16.
DR   RNAct; Q12789; protein.
DR   Bgee; ENSG00000077235; Expressed in lower esophagus mucosa and 205 other cell types or tissues.
DR   ExpressionAtlas; Q12789; baseline and differential.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:1990904; C:ribonucleoprotein complex; IEA:Ensembl.
DR   GO; GO:0000127; C:transcription factor TFIIIC complex; IDA:HGNC-UCL.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000995; F:RNA polymerase III general transcription initiation factor activity; IDA:GO_Central.
DR   GO; GO:0042791; P:5S class rRNA transcription by RNA polymerase III; IBA:GO_Central.
DR   GO; GO:0009303; P:rRNA transcription; TAS:ProtInc.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IC:HGNC-UCL.
DR   GO; GO:0006384; P:transcription initiation at RNA polymerase III promoter; IBA:GO_Central.
DR   GO; GO:0009304; P:tRNA transcription; TAS:ProtInc.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR   CDD; cd16169; Tau138_eWH; 1.
DR   InterPro; IPR044210; Tfc3-like.
DR   InterPro; IPR035625; Tfc3-like_eWH.
DR   InterPro; IPR007309; TFIIIC_Bblock-bd.
DR   PANTHER; PTHR15180; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 1; 1.
DR   PANTHER; PTHR15180:SF1; GENERAL TRANSCRIPTION FACTOR 3C POLYPEPTIDE 1; 1.
DR   Pfam; PF04182; B-block_TFIIIC; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Direct protein sequencing; DNA-binding;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Transcription; Ubl conjugation.
FT   CHAIN           1..2109
FT                   /note="General transcription factor 3C polypeptide 1"
FT                   /id="PRO_0000209710"
FT   REGION          467..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          586..609
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          718..775
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          836..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1059..1082
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1202..1241
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1608..1631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1823..1961
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        497..515
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        744..760
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        838..852
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1063..1082
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1210..1229
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1823..1837
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1933..1949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         667
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         739
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1062
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   MOD_RES         1068
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1253
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1611
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1632
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1653
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:16964243,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1856
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1865
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1868
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1896
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8K284"
FT   MOD_RES         1911
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   MOD_RES         1969
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17525332"
FT   CROSSLNK        529
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        770
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        833
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   CROSSLNK        1142
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   VAR_SEQ         1933..1957
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_021819"
FT   VARIANT         1889
FT                   /note="Q -> E (in dbSNP:rs35233306)"
FT                   /id="VAR_047534"
FT   VARIANT         1959
FT                   /note="F -> S (in dbSNP:rs12919017)"
FT                   /id="VAR_047535"
FT   VARIANT         2077
FT                   /note="E -> K (in dbSNP:rs2228248)"
FT                   /id="VAR_047536"
FT   CONFLICT        141
FT                   /note="A -> P (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="A -> P (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        156
FT                   /note="A -> P (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        161
FT                   /note="A -> P (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        164
FT                   /note="G -> A (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        977
FT                   /note="L -> V (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1015..1018
FT                   /note="ARSS -> GRRR (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1256
FT                   /note="Q -> H (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1316
FT                   /note="V -> L (in Ref. 1; AAA17985)"
FT                   /evidence="ECO:0000305"
FT   HELIX           3..13
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           21..29
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           41..52
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          57..61
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          80..83
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            115..119
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           124..127
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          134..136
FT                   /evidence="ECO:0007829|PDB:8CLL"
FT   HELIX           138..145
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           146..148
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          149..153
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           155..163
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            164..166
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           175..185
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            186..189
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           194..199
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           206..218
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          222..230
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          236..244
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           245..247
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           254..268
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          272..275
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           276..281
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   TURN            282..284
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           287..299
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          302..309
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           310..313
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          329..335
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           368..379
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           380..382
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           386..393
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           397..409
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          412..420
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          423..430
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           431..434
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           438..455
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           612..627
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          628..631
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           634..648
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           656..668
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          673..676
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          678..681
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          684..687
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   STRAND          690..692
FT                   /evidence="ECO:0007829|PDB:8CLI"
FT   HELIX           701..714
FT                   /evidence="ECO:0007829|PDB:8CLI"
SQ   SEQUENCE   2109 AA;  238875 MW;  37A03135EFE695FC CRC64;
     MDALESLLDE VALEGLDGLC LPALWSRLET RVPPFPLPLE PCTQEFLWRA LATHPGISFY
     EEPRERPDLQ LQDRYEEIDL ETGILESRRD PVALEDVYPI HMILENKDGI QGSCRYFKER
     KNITNDIRTK SLQPRCTMVE AFDRWGKKLI IVASQAMRYR ALIGQEGDPD LKLPDFSYCI
     LERLGRSRWQ GELQRDLHTT AFKVDAGKLH YHRKILNKNG LITMQSHVIR LPTGAQQHSI
     LLLLNRFHVD RRSKYDILME KLSVMLSTRT NHIETLGKLR EELGLCERTF KRLYQYMLNA
     GLAKVVSLRL QEIHPECGPC KTKKGTDVMV RCLKLLKEFK RNDHDDDEDE EVISKTVPPV
     DIVFERDMLT QTYDLIERRG TKGISQAEIR VAMNVGKLEA RMLCRLLQRF KVVKGFMEDE
     GRQRTTKYIS CVFAEESDLS RQYQREKARS ELLTTVSLAS MQEESLLPEG EDTFLSESDS
     EEERSSSKRR GRGSQKDTRA SANLRPKTQP HHSTPTKGGW KVVNLHPLKK QPPSFPGAAE
     ERACQSLASR DSLLDTSSVS EPNVSFVSHC ADSNSGDIAV IEEVRMENPK ESSSSLKTGR
     HSSGQDKPHE TYRLLKRRNL IIEAVTNLRL IESLFTIQKM IMDQEKQEGV STKCCKKSIV
     RLVRNLSEEG LLRLYRTTVI QDGIKKKVDL VVHPSMDQND PLVRSAIEQV RFRISNSSTA
     NRVKTSQPPV PQGEAEEDSQ GKEGPSGSGD SQLSASSRSE SGRMKKSDNK MGITPLRNYH
     PIVVPGLGRS LGFLPKMPRL RVVHMFLWYL IYGHPASNTV EKPSFISERR TIKQESGRAG
     VRPSSSGSAW EACSEAPSKG SQDGVTWEAE VELATETVYV DDASWMRYIP PIPVHRDFGF
     GWALVSDILL CLPLSIFIQI VQVSYKVDNL EEFLNDPLKK HTLIRFLPRP IRQQLLYKRR
     YIFSVVENLQ RLCYMGLLQF GPTEKFQDKD QVFIFLKKNA VIVDTTICDP HYNLARSSRP
     FERRLYVLNS MQDVENYWFD LQCVCLNTPL GVVRCPRVRK NSSTDQGSDE EGSLQKEQES
     AMDKHNLERK CAMLEYTTGS REVVDEGLIP GDGLGAAGLD SSFYGHLKRN WIWTSYIINQ
     AKKENTAAEN GLTVRLQTFL SKRPMPLSAR GNSRLNIWGE ARVGSELCAG WEEQFEVDRE
     PSLDRNRRVR GGKSQKRKRL KKDPGKKIKR KKKGEFPGEK SKRLRYHDEA DQSALQRMTR
     LRVTWSMQED GLLVLCRIAS NVLNTKVKGP FVTWQVVRDI LHATFEESLD KTSHSVGRRA
     RYIVKNPQAY LNYKVCLAEV YQDKALVGDF MNRRGDYDDP KVCANEFKEF VEKLKEKFSS
     ALRNSNLEIP DTLQELFARY RVLAIGDEKD QTRKEDELNS VDDIHFLVLQ NLIQSTLALS
     DSQMKSYQSF QTFRLYREYK DHVLVKAFME CQKRSLVNRR RVNHTLGPKK NRALPFVPMS
     YQLSQTYYRI FTWRFPSTIC TESFQFLDRM RAAGKLDQPD RFSFKDQDNN EPTNDMVAFS
     LDGPGGNCVA VLTLFSLGLI SVDVRIPEQI IVVDSSMVEN EVIKSLGKDG SLEDDEDEED
     DLDEGVGGKR RSMEVKPAQA SHTNYLLMRG YYSPGIVSTR NLNPNDSIVV NSCQMKFQLR
     CTPVPARLRP AAAPLEELTM GTSCLPDTFT KLINPQENTC SLEEFVLQLE LSGYSPEDLT
     AALEILEAII ATGCFGIDKE ELRRRFSALE KAGGGRTRTF ADCIQALLEQ HQVLEVGGNT
     ARLVAMGSAW PWLLHSVRLK DREDADIQRE DPQARPLEGS SSEDSPPEGQ APPSHSPRGT
     KRRASWASEN GETDAEGTQM TPAKRPALQD SNLAPSLGPG AEDGAEAQAP SPPPALEDTA
     AAGAAQEDQE GVGEFSSPGQ EQLSGQAQPP EGSEDPRGFT ESFGAANISQ AARERDCESV
     CFIGRPWRVV DGHLNLPVCK GMMEAMLYHI MTRPGIPESS LLRHYQGVLQ PVAVLELLQG
     LESLGCIRKR WLRKPRPVSL FSTPVVEEVE VPSSLDESPM AFYEPTLDCT LRLGRVFPHE
     VNWNKWIHL
//