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TF3C3_HUMAN
ID   TF3C3_HUMAN             Reviewed;         886 AA.
AC   Q9Y5Q9; Q4ZG48; Q86XJ8; Q8WX84; Q96B44; Q9H5I8; Q9NT97;
DT   24-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 192.
DE   RecName: Full=General transcription factor 3C polypeptide 3;
DE   AltName: Full=Transcription factor IIIC 102 kDa subunit;
DE            Short=TFIIIC 102 kDa subunit;
DE            Short=TFIIIC102;
DE   AltName: Full=Transcription factor IIIC subunit gamma;
DE            Short=TF3C-gamma;
GN   Name=GTF3C3;
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), INTERACTION WITH BRF1 AND TBP, AND
RP   IDENTIFICATION OF SUBUNITS OF TFIIIC2 COMPLEX.
RX   PubMed=10373544; DOI=10.1128/mcb.19.7.4944;
RA   Hsieh Y.-J., Wang Z., Kovelman R., Roeder R.G.;
RT   "Cloning and characterization of two evolutionarily conserved subunits
RT   (TFIIIC102 and TFIIIC63) of human TFIIIC and their involvement in
RT   functional interactions with TFIIIB and RNA polymerase III.";
RL   Mol. Cell. Biol. 19:4944-4952(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Hegde R., Alnemri E.;
RT   "Identification of a short isoform of hTFIIIC102 subunit.";
RL   Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Hepatoma, and Placenta;
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=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA   Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA   Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA   Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA   Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA   Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA   Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA   Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA   Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA   Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA   Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA   Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA   Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA   Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA   Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA   Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA   Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT   4.";
RL   Nature 434:724-731(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-70.
RC   TISSUE=Bone marrow, 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   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-886 (ISOFORM 1).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP   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   [9]
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   [10]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP   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].
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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43, AND IDENTIFICATION BY
RP   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   [13]
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=22223895; DOI=10.1074/mcp.m111.015131;
RA   Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA   Giglione C.;
RT   "Comparative large-scale characterisation of plant vs. mammal proteins
RT   reveals similar and idiosyncratic N-alpha acetylation features.";
RL   Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-43 AND SER-282, 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).
CC   -!- FUNCTION: Involved in RNA polymerase III-mediated transcription.
CC       Integral, tightly associated component of the DNA-binding TFIIIC2
CC       subcomplex that directly binds tRNA and virus-associated RNA promoters.
CC   -!- SUBUNIT: Part of the TFIIIC subcomplex TFIIIC2, consisting of six
CC       subunits, GTF3C1, GTF3C2, GTF3C3, GTF3C4, GTF3C5 and GTF3C6. Interacts
CC       with BRF1 and TBP. {ECO:0000269|PubMed:10373544}.
CC   -!- INTERACTION:
CC       Q9Y5Q9; P13928: ANXA8; NbExp=3; IntAct=EBI-1054873, EBI-2556915;
CC       Q9Y5Q9; P05067: APP; NbExp=3; IntAct=EBI-1054873, EBI-77613;
CC       Q9Y5Q9; Q6XD76: ASCL4; NbExp=3; IntAct=EBI-1054873, EBI-10254793;
CC       Q9Y5Q9; Q9H7T9: AUNIP; NbExp=3; IntAct=EBI-1054873, EBI-10693257;
CC       Q9Y5Q9; P46379-2: BAG6; NbExp=3; IntAct=EBI-1054873, EBI-10988864;
CC       Q9Y5Q9; Q8TBE0: BAHD1; NbExp=3; IntAct=EBI-1054873, EBI-742750;
CC       Q9Y5Q9; Q5H9J7: BEX5; NbExp=3; IntAct=EBI-1054873, EBI-10243741;
CC       Q9Y5Q9; Q96LL4: C8orf48; NbExp=3; IntAct=EBI-1054873, EBI-751596;
CC       Q9Y5Q9; Q13191: CBLB; NbExp=3; IntAct=EBI-1054873, EBI-744027;
CC       Q9Y5Q9; Q14781-2: CBX2; NbExp=3; IntAct=EBI-1054873, EBI-11974585;
CC       Q9Y5Q9; Q494V2-2: CFAP100; NbExp=3; IntAct=EBI-1054873, EBI-11953200;
CC       Q9Y5Q9; P48730-2: CSNK1D; NbExp=3; IntAct=EBI-1054873, EBI-9087876;
CC       Q9Y5Q9; Q5TAQ9-2: DCAF8; NbExp=3; IntAct=EBI-1054873, EBI-25842815;
CC       Q9Y5Q9; Q92782-2: DPF1; NbExp=3; IntAct=EBI-1054873, EBI-23669343;
CC       Q9Y5Q9; Q86TI2-2: DPP9; NbExp=3; IntAct=EBI-1054873, EBI-21529239;
CC       Q9Y5Q9; Q6P1L5: FAM117B; NbExp=3; IntAct=EBI-1054873, EBI-3893327;
CC       Q9Y5Q9; Q17RN3: FAM98C; NbExp=3; IntAct=EBI-1054873, EBI-5461838;
CC       Q9Y5Q9; Q96IJ6: GMPPA; NbExp=3; IntAct=EBI-1054873, EBI-750953;
CC       Q9Y5Q9; Q9HBQ8: GOLGA2P5; NbExp=3; IntAct=EBI-1054873, EBI-22000587;
CC       Q9Y5Q9; Q9Y4H4: GPSM3; NbExp=3; IntAct=EBI-1054873, EBI-347538;
CC       Q9Y5Q9; Q6NXT2: H3-5; NbExp=3; IntAct=EBI-1054873, EBI-2868501;
CC       Q9Y5Q9; Q9HCC6: HES4; NbExp=3; IntAct=EBI-1054873, EBI-2680288;
CC       Q9Y5Q9; P42858: HTT; NbExp=12; IntAct=EBI-1054873, EBI-466029;
CC       Q9Y5Q9; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-1054873, EBI-2796400;
CC       Q9Y5Q9; Q92615: LARP4B; NbExp=3; IntAct=EBI-1054873, EBI-1052558;
CC       Q9Y5Q9; A2RU56: LOC401296; NbExp=3; IntAct=EBI-1054873, EBI-9088215;
CC       Q9Y5Q9; Q14693: LPIN1; NbExp=3; IntAct=EBI-1054873, EBI-5278370;
CC       Q9Y5Q9; Q8TD91-2: MAGEC3; NbExp=3; IntAct=EBI-1054873, EBI-10694180;
CC       Q9Y5Q9; Q9H000: MKRN2; NbExp=3; IntAct=EBI-1054873, EBI-2341005;
CC       Q9Y5Q9; Q15049: MLC1; NbExp=3; IntAct=EBI-1054873, EBI-8475277;
CC       Q9Y5Q9; O95563: MPC2; NbExp=3; IntAct=EBI-1054873, EBI-719403;
CC       Q9Y5Q9; P01106: MYC; NbExp=4; IntAct=EBI-1054873, EBI-447544;
CC       Q9Y5Q9; O15381-5: NVL; NbExp=3; IntAct=EBI-1054873, EBI-18577082;
CC       Q9Y5Q9; Q8N7B6-2: PACRGL; NbExp=3; IntAct=EBI-1054873, EBI-10694433;
CC       Q9Y5Q9; Q9BYU1: PBX4; NbExp=3; IntAct=EBI-1054873, EBI-10302990;
CC       Q9Y5Q9; Q96FM1: PGAP3; NbExp=3; IntAct=EBI-1054873, EBI-22113571;
CC       Q9Y5Q9; P19388: POLR2E; NbExp=3; IntAct=EBI-1054873, EBI-395189;
CC       Q9Y5Q9; Q13332-6: PTPRS; NbExp=3; IntAct=EBI-1054873, EBI-25906956;
CC       Q9Y5Q9; Q9Y5P3: RAI2; NbExp=3; IntAct=EBI-1054873, EBI-746228;
CC       Q9Y5Q9; Q96D59: RNF183; NbExp=3; IntAct=EBI-1054873, EBI-743938;
CC       Q9Y5Q9; Q969K3: RNF34; NbExp=3; IntAct=EBI-1054873, EBI-2340642;
CC       Q9Y5Q9; Q9BUL9: RPP25; NbExp=3; IntAct=EBI-1054873, EBI-366570;
CC       Q9Y5Q9; P62701: RPS4X; NbExp=3; IntAct=EBI-1054873, EBI-354303;
CC       Q9Y5Q9; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-1054873, EBI-6257312;
CC       Q9Y5Q9; Q8N488: RYBP; NbExp=3; IntAct=EBI-1054873, EBI-752324;
CC       Q9Y5Q9; O75446: SAP30; NbExp=3; IntAct=EBI-1054873, EBI-632609;
CC       Q9Y5Q9; P60896: SEM1; NbExp=3; IntAct=EBI-1054873, EBI-79819;
CC       Q9Y5Q9; Q8NHS9: SPATA22; NbExp=3; IntAct=EBI-1054873, EBI-7067260;
CC       Q9Y5Q9; Q8TCT7-2: SPPL2B; NbExp=3; IntAct=EBI-1054873, EBI-8345366;
CC       Q9Y5Q9; Q9NRL3: STRN4; NbExp=3; IntAct=EBI-1054873, EBI-717245;
CC       Q9Y5Q9; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-1054873, EBI-747797;
CC       Q9Y5Q9; O43615: TIMM44; NbExp=3; IntAct=EBI-1054873, EBI-861737;
CC       Q9Y5Q9; O75604-3: USP2; NbExp=3; IntAct=EBI-1054873, EBI-10696113;
CC       Q9Y5Q9; P40337-2: VHL; NbExp=3; IntAct=EBI-1054873, EBI-12157263;
CC       Q9Y5Q9; P58304: VSX2; NbExp=3; IntAct=EBI-1054873, EBI-6427899;
CC       Q9Y5Q9; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-1054873, EBI-14104088;
CC       Q9Y5Q9; Q96MN9-2: ZNF488; NbExp=3; IntAct=EBI-1054873, EBI-25831733;
CC       Q9Y5Q9; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-1054873, EBI-745520;
CC       Q9Y5Q9; Q3KNS6-3: ZNF829; NbExp=3; IntAct=EBI-1054873, EBI-18036029;
CC       Q9Y5Q9; Q8NBB4-2: ZSCAN1; NbExp=3; IntAct=EBI-1054873, EBI-12021938;
CC       Q9Y5Q9; P10073: ZSCAN22; NbExp=3; IntAct=EBI-1054873, EBI-10178224;
CC       Q9Y5Q9; A0A384ME25; NbExp=3; IntAct=EBI-1054873, EBI-10211777;
CC       Q9Y5Q9; Q9H669; NbExp=3; IntAct=EBI-1054873, EBI-10307430;
CC   -!- SUBCELLULAR LOCATION: Nucleus.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9Y5Q9-1; Sequence=Displayed;
CC       Name=2; Synonyms=Short;
CC         IsoId=Q9Y5Q9-2; Sequence=VSP_010353, VSP_010354;
CC   -!- MISCELLANEOUS: [Isoform 2]: May be due to exon skipping. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAB15638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AF133123; AAD41475.1; -; mRNA.
DR   EMBL; AF465407; AAL73493.1; -; mRNA.
DR   EMBL; AK027050; BAB15638.1; ALT_INIT; mRNA.
DR   EMBL; AK314718; BAG37262.1; -; mRNA.
DR   EMBL; AC012486; AAX88853.1; -; Genomic_DNA.
DR   EMBL; CH471063; EAW70132.1; -; Genomic_DNA.
DR   EMBL; BC015995; AAH15995.1; -; mRNA.
DR   EMBL; BC043347; AAH43347.1; -; mRNA.
DR   EMBL; AL137453; CAB70745.1; -; mRNA.
DR   CCDS; CCDS2316.1; -. [Q9Y5Q9-1]
DR   CCDS; CCDS56153.1; -. [Q9Y5Q9-2]
DR   PIR; T46268; T46268.
DR   RefSeq; NP_001193703.1; NM_001206774.1. [Q9Y5Q9-2]
DR   RefSeq; NP_036218.1; NM_012086.4. [Q9Y5Q9-1]
DR   AlphaFoldDB; Q9Y5Q9; -.
DR   SMR; Q9Y5Q9; -.
DR   BioGRID; 114739; 171.
DR   CORUM; Q9Y5Q9; -.
DR   IntAct; Q9Y5Q9; 127.
DR   MINT; Q9Y5Q9; -.
DR   STRING; 9606.ENSP00000263956; -.
DR   GlyGen; Q9Y5Q9; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9Y5Q9; -.
DR   MetOSite; Q9Y5Q9; -.
DR   PhosphoSitePlus; Q9Y5Q9; -.
DR   BioMuta; GTF3C3; -.
DR   DMDM; 47606223; -.
DR   EPD; Q9Y5Q9; -.
DR   jPOST; Q9Y5Q9; -.
DR   MassIVE; Q9Y5Q9; -.
DR   MaxQB; Q9Y5Q9; -.
DR   PaxDb; Q9Y5Q9; -.
DR   PeptideAtlas; Q9Y5Q9; -.
DR   PRIDE; Q9Y5Q9; -.
DR   ProteomicsDB; 86478; -. [Q9Y5Q9-1]
DR   ProteomicsDB; 86479; -. [Q9Y5Q9-2]
DR   Antibodypedia; 19878; 253 antibodies from 27 providers.
DR   DNASU; 9330; -.
DR   Ensembl; ENST00000263956.8; ENSP00000263956.3; ENSG00000119041.11. [Q9Y5Q9-1]
DR   Ensembl; ENST00000409364.3; ENSP00000386465.3; ENSG00000119041.11. [Q9Y5Q9-2]
DR   GeneID; 9330; -.
DR   KEGG; hsa:9330; -.
DR   MANE-Select; ENST00000263956.8; ENSP00000263956.3; NM_012086.5; NP_036218.1.
DR   UCSC; uc002uts.4; human. [Q9Y5Q9-1]
DR   CTD; 9330; -.
DR   DisGeNET; 9330; -.
DR   GeneCards; GTF3C3; -.
DR   HGNC; HGNC:4666; GTF3C3.
DR   HPA; ENSG00000119041; Low tissue specificity.
DR   MIM; 604888; gene.
DR   neXtProt; NX_Q9Y5Q9; -.
DR   OpenTargets; ENSG00000119041; -.
DR   PharmGKB; PA29054; -.
DR   VEuPathDB; HostDB:ENSG00000119041; -.
DR   eggNOG; KOG2076; Eukaryota.
DR   GeneTree; ENSGT00390000016929; -.
DR   HOGENOM; CLU_002391_1_1_1; -.
DR   InParanoid; Q9Y5Q9; -.
DR   OMA; HEVAFNL; -.
DR   OrthoDB; 271586at2759; -.
DR   PhylomeDB; Q9Y5Q9; -.
DR   TreeFam; TF105955; -.
DR   PathwayCommons; Q9Y5Q9; -.
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; Q9Y5Q9; -.
DR   SIGNOR; Q9Y5Q9; -.
DR   BioGRID-ORCS; 9330; 401 hits in 1091 CRISPR screens.
DR   ChiTaRS; GTF3C3; human.
DR   GenomeRNAi; 9330; -.
DR   Pharos; Q9Y5Q9; Tdark.
DR   PRO; PR:Q9Y5Q9; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   RNAct; Q9Y5Q9; protein.
DR   Bgee; ENSG00000119041; Expressed in calcaneal tendon and 188 other tissues.
DR   ExpressionAtlas; Q9Y5Q9; baseline and differential.
DR   Genevisible; Q9Y5Q9; HS.
DR   GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
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; IC:HGNC-UCL.
DR   GO; GO:0006383; P:transcription by RNA polymerase III; IBA:GO_Central.
DR   GO; GO:0042797; P:tRNA transcription by RNA polymerase III; IC:HGNC-UCL.
DR   Gene3D; 1.25.40.10; -; 3.
DR   InterPro; IPR039340; Tfc4/TFIIIC-102/Sfc4.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_repeat.
DR   PANTHER; PTHR23082; PTHR23082; 1.
DR   Pfam; PF13181; TPR_8; 3.
DR   SMART; SM00028; TPR; 6.
DR   SUPFAM; SSF48452; SSF48452; 3.
DR   PROSITE; PS50005; TPR; 6.
DR   PROSITE; PS50293; TPR_REGION; 3.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; DNA-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Repeat; TPR repeat; Transcription.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   CHAIN           2..886
FT                   /note="General transcription factor 3C polypeptide 3"
FT                   /id="PRO_0000106363"
FT   REPEAT          149..182
FT                   /note="TPR 1"
FT   REPEAT          183..216
FT                   /note="TPR 2"
FT   REPEAT          217..250
FT                   /note="TPR 3"
FT   REPEAT          252..284
FT                   /note="TPR 4"
FT   REPEAT          290..323
FT                   /note="TPR 5"
FT   REPEAT          326..361
FT                   /note="TPR 6"
FT   REPEAT          421..454
FT                   /note="TPR 7"
FT   REPEAT          456..489
FT                   /note="TPR 8"
FT   REPEAT          491..523
FT                   /note="TPR 9"
FT   REPEAT          733..766
FT                   /note="TPR 10"
FT   REPEAT          811..844
FT                   /note="TPR 11"
FT   REGION          1..121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        13..48
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        49..65
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        66..80
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        92..115
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0007744|PubMed:22223895"
FT   MOD_RES         43
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         282
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         407..413
FT                   /note="PLLTTLV -> VCNKICT (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_010353"
FT   VAR_SEQ         414..886
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.2"
FT                   /id="VSP_010354"
FT   VARIANT         70
FT                   /note="N -> S (in dbSNP:rs11559078)"
FT                   /evidence="ECO:0000269|PubMed:15489334"
FT                   /id="VAR_061902"
FT   CONFLICT        412..413
FT                   /note="LV -> HL (in Ref. 6; AAH15995)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        589
FT                   /note="I -> M (in Ref. 3; BAB15638)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   886 AA;  101272 MW;  9B97269929F9765F CRC64;
     MSGFSPELID YLEGKISFEE FERRREERKT REKKSLQEKG KLSAEENPDD SEVPSSSGIN
     STKSQDKDVN EGETSDGVRK SVHKVFASML GENEDDEEEE EEEEEEEEEE ETPEQPTAGD
     VFVLEMVLNR ETKKMMKEKR PRSKLPRALR GLMGEANIRF ARGEREEAIL MCMEIIRQAP
     LAYEPFSTLA MIYEDQGDME KSLQFELIAA HLNPSDTEEW VRLAEMSLEQ DNIKQAIFCY
     TKALKYEPTN VRYLWERSSL YEQMGDHKMA MDGYRRILNL LSPSDGERFM QLARDMAKSY
     YEANDVTSAI NIIDEAFSKH QGLVSMEDVN IAAELYISNK QYDKALEIIT DFSGIVLEKK
     TSEEGTSEEN KAPENVTCTI PDGVPIDITV KLMVCLVHLN ILEPLNPLLT TLVEQNPEDM
     GDLYLDVAEA FLDVGEYNSA LPLLSALVCS ERYNLAVVWL RHAECLKALG YMERAAESYG
     KVVDLAPLHL DARISLSTLQ QQLGQPEKAL EALEPMYDPD TLAQDANAAQ QELKLLLHRS
     TLLFSQGKMY GYVDTLLTML AMLLKVAMNR AQVCLISSSK SGERHLYLIK VSRDKISDSN
     DQESANCDAK AIFAVLTSVL TKDDWWNLLL KAIYSLCDLS RFQEAELLVD SSLEYYSFYD
     DRQKRKELEY FGLSAAILDK NFRKAYNYIR IMVMENVNKP QLWNIFNQVT MHSQDVRHHR
     FCLRLMLKNP ENHALCVLNG HNAFVSGSFK HALGQYVQAF RTHPDEPLYS FCIGLTFIHM
     ASQKYVLRRH ALIVQGFSFL NRYLSLRGPC QESFYNLGRG LHQLGLIHLA IHYYQKALEL
     PPLVVEGIEL DQLDLRRDIA YNLSLIYQSS GNTGMAQTLL YTYCSI
 
 
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