RPAC1_HUMAN
ID RPAC1_HUMAN Reviewed; 346 AA.
AC O15160; O75395; Q5JTE3;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=DNA-directed RNA polymerases I and III subunit RPAC1;
DE Short=DNA-directed RNA polymerase I subunit C;
DE Short=RNA polymerases I and III subunit AC1;
DE AltName: Full=AC40;
DE AltName: Full=DNA-directed RNA polymerases I and III 40 kDa polypeptide;
DE Short=RPA40;
DE AltName: Full=RPA39;
DE AltName: Full=RPC40;
GN Name=POLR1C; Synonyms=POLR1E;
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).
RX PubMed=9540830; DOI=10.1016/s0167-4781(97)00206-6;
RA Dammann R., Pfeifer G.P.;
RT "Cloning and characterization of the human RNA polymerase I subunit
RT hRPA40.";
RL Biochim. Biophys. Acta 1396:153-157(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Umbilical cord blood;
RX PubMed=9653160; DOI=10.1073/pnas.95.14.8175;
RA Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H.,
RA He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H.,
RA Wang Y.-X., Chen S.-J., Chen Z.;
RT "Identification of genes expressed in human CD34(+) hematopoietic
RT stem/progenitor cells by expressed sequence tags and efficient full-length
RT cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 PROTEIN SEQUENCE OF 2-11; 14-22; 79-91; 110-120; 155-167 AND 225-255,
RP CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
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 [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-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-4, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 SUBCELLULAR LOCATION, SUBUNIT, FUNCTION, INVOLVEMENT IN HLD11, VARIANTS
RP HLD11 ILE-26; ILE-32; VAL-65; SER-74; ALA-94; HIS-109; ASP-132; ARG-146;
RP GLN-191; THR-262; LYS-295 DEL AND LYS-324, CHARACTERIZATION OF VARIANTS
RP HLD11 ILE-32 AND SER-74, AND CHARACTERIZATION OF VARIANT TCS3 GLN-279.
RX PubMed=26151409; DOI=10.1038/ncomms8623;
RA Thiffault I., Wolf N.I., Forget D., Guerrero K., Tran L.T., Choquet K.,
RA Lavallee-Adam M., Poitras C., Brais B., Yoon G., Sztriha L., Webster R.I.,
RA Timmann D., van de Warrenburg B.P., Seeger J., Zimmermann A., Mate A.,
RA Goizet C., Fung E., van der Knaap M.S., Fribourg S., Vanderver A.,
RA Simons C., Taft R.J., Yates J.R. III, Coulombe B., Bernard G.;
RT "Recessive mutations in POLR1C cause a leukodystrophy by impairing
RT biogenesis of RNA polymerase III.";
RL Nat. Commun. 6:7623-7632(2015).
RN [14]
RP VARIANTS TCS3 GLN-279 AND TRP-279.
RX PubMed=21131976; DOI=10.1038/ng.724;
RA Dauwerse J.G., Dixon J., Seland S., Ruivenkamp C.A., van Haeringen A.,
RA Hoefsloot L.H., Peters D.J., Boers A.C., Daumer-Haas C., Maiwald R.,
RA Zweier C., Kerr B., Cobo A.M., Toral J.F., Hoogeboom A.J., Lohmann D.R.,
RA Hehr U., Dixon M.J., Breuning M.H., Wieczorek D.;
RT "Mutations in genes encoding subunits of RNA polymerases I and III cause
RT Treacher Collins syndrome.";
RL Nat. Genet. 43:20-22(2011).
CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of
CC DNA into RNA using the four ribonucleoside triphosphates as substrates.
CC Common component of RNA polymerases I and III which synthesize
CC ribosomal RNA precursors and small RNAs, such as 5S rRNA and tRNAs,
CC respectively. RPAC1 is part of the Pol core element with the central
CC large cleft and probably a clamp element that moves to open and close
CC the cleft (By similarity). {ECO:0000250|UniProtKB:P07703,
CC ECO:0000305|PubMed:26151409}.
CC -!- SUBUNIT: Component of the RNA polymerase I (Pol I) and RNA polymerase
CC III (Pol III) complexes consisting of at least 13 and 17 subunits,
CC respectively. {ECO:0000269|PubMed:12391170,
CC ECO:0000269|PubMed:26151409}.
CC -!- INTERACTION:
CC O15160; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-1055079, EBI-10173507;
CC O15160; Q12774: ARHGEF5; NbExp=5; IntAct=EBI-1055079, EBI-602199;
CC O15160; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-1055079, EBI-747353;
CC O15160; Q5T686: AVPI1; NbExp=3; IntAct=EBI-1055079, EBI-8640233;
CC O15160; Q6PI77: BHLHB9; NbExp=3; IntAct=EBI-1055079, EBI-11519926;
CC O15160; Q9NQY0: BIN3; NbExp=3; IntAct=EBI-1055079, EBI-2653038;
CC O15160; Q96CA5: BIRC7; NbExp=6; IntAct=EBI-1055079, EBI-517623;
CC O15160; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-1055079, EBI-2548012;
CC O15160; O95561: C1orf105; NbExp=3; IntAct=EBI-1055079, EBI-10191951;
CC O15160; Q0VAL7: C21orf58; NbExp=3; IntAct=EBI-1055079, EBI-10226774;
CC O15160; Q96LM5: C4orf45; NbExp=3; IntAct=EBI-1055079, EBI-12020542;
CC O15160; Q9HC52: CBX8; NbExp=3; IntAct=EBI-1055079, EBI-712912;
CC O15160; Q8NA61-2: CBY2; NbExp=5; IntAct=EBI-1055079, EBI-11524851;
CC O15160; O75909-2: CCNK; NbExp=3; IntAct=EBI-1055079, EBI-12010594;
CC O15160; P49368: CCT3; NbExp=3; IntAct=EBI-1055079, EBI-356673;
CC O15160; Q9UFW8: CGGBP1; NbExp=3; IntAct=EBI-1055079, EBI-723153;
CC O15160; Q9BSW2: CRACR2A; NbExp=3; IntAct=EBI-1055079, EBI-739773;
CC O15160; P02489: CRYAA; NbExp=3; IntAct=EBI-1055079, EBI-6875961;
CC O15160; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-1055079, EBI-2349927;
CC O15160; A0A0A0MR80: EP400; NbExp=3; IntAct=EBI-1055079, EBI-12089140;
CC O15160; P07954: FH; NbExp=3; IntAct=EBI-1055079, EBI-1050358;
CC O15160; Q8IXW7: FMR1; NbExp=3; IntAct=EBI-1055079, EBI-11976595;
CC O15160; Q6PJQ5: FOXR2; NbExp=3; IntAct=EBI-1055079, EBI-8468543;
CC O15160; O95995: GAS8; NbExp=3; IntAct=EBI-1055079, EBI-1052570;
CC O15160; Q9Y5P6: GMPPB; NbExp=3; IntAct=EBI-1055079, EBI-750945;
CC O15160; Q9NYA3: GOLGA6A; NbExp=3; IntAct=EBI-1055079, EBI-11163335;
CC O15160; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-1055079, EBI-5916454;
CC O15160; Q9HAV7: GRPEL1; NbExp=4; IntAct=EBI-1055079, EBI-1043499;
CC O15160; Q9H4Y5: GSTO2; NbExp=3; IntAct=EBI-1055079, EBI-10194609;
CC O15160; Q7Z353: HDX; NbExp=3; IntAct=EBI-1055079, EBI-1052734;
CC O15160; P31943: HNRNPH1; NbExp=4; IntAct=EBI-1055079, EBI-351590;
CC O15160; P17482: HOXB9; NbExp=3; IntAct=EBI-1055079, EBI-745290;
CC O15160; P35452-2: HOXD12; NbExp=3; IntAct=EBI-1055079, EBI-17244356;
CC O15160; Q8IYA8: IHO1; NbExp=3; IntAct=EBI-1055079, EBI-8638439;
CC O15160; Q9UKT9: IKZF3; NbExp=9; IntAct=EBI-1055079, EBI-747204;
CC O15160; Q0VD86: INCA1; NbExp=3; IntAct=EBI-1055079, EBI-6509505;
CC O15160; Q719H9: KCTD1; NbExp=6; IntAct=EBI-1055079, EBI-9027502;
CC O15160; Q8WZ19: KCTD13; NbExp=3; IntAct=EBI-1055079, EBI-742916;
CC O15160; Q9UIH9: KLF15; NbExp=3; IntAct=EBI-1055079, EBI-2796400;
CC O15160; P08727: KRT19; NbExp=3; IntAct=EBI-1055079, EBI-742756;
CC O15160; O95678: KRT75; NbExp=3; IntAct=EBI-1055079, EBI-2949715;
CC O15160; Q01546: KRT76; NbExp=5; IntAct=EBI-1055079, EBI-2952745;
CC O15160; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-1055079, EBI-10176379;
CC O15160; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-1055079, EBI-9996449;
CC O15160; Q5T3J3: LRIF1; NbExp=3; IntAct=EBI-1055079, EBI-473196;
CC O15160; Q9Y250: LZTS1; NbExp=3; IntAct=EBI-1055079, EBI-1216080;
CC O15160; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-1055079, EBI-741037;
CC O15160; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-1055079, EBI-10182361;
CC O15160; A8MW99: MEI4; NbExp=3; IntAct=EBI-1055079, EBI-19944212;
CC O15160; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-1055079, EBI-16439278;
CC O15160; Q13064: MKRN3; NbExp=5; IntAct=EBI-1055079, EBI-2340269;
CC O15160; Q6PF18: MORN3; NbExp=3; IntAct=EBI-1055079, EBI-9675802;
CC O15160; Q9Y3D9: MRPS23; NbExp=3; IntAct=EBI-1055079, EBI-1054270;
CC O15160; O96000: NDUFB10; NbExp=3; IntAct=EBI-1055079, EBI-1246371;
CC O15160; P46934-3: NEDD4; NbExp=3; IntAct=EBI-1055079, EBI-11980721;
CC O15160; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-1055079, EBI-740897;
CC O15160; P15531: NME1; NbExp=11; IntAct=EBI-1055079, EBI-741141;
CC O15160; O00746: NME4; NbExp=5; IntAct=EBI-1055079, EBI-744871;
CC O15160; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-1055079, EBI-10232538;
CC O15160; Q8WUT1: POLDIP3; NbExp=3; IntAct=EBI-1055079, EBI-10276663;
CC O15160; P0DPB6: POLR1D; NbExp=16; IntAct=EBI-1055079, EBI-359498;
CC O15160; P62487: POLR2G; NbExp=3; IntAct=EBI-1055079, EBI-347928;
CC O15160; P52435: POLR2J; NbExp=11; IntAct=EBI-1055079, EBI-394753;
CC O15160; Q9H1A7: POLR2J3; NbExp=3; IntAct=EBI-1055079, EBI-12818681;
CC O15160; Q969Q6: PPP2R3C; NbExp=5; IntAct=EBI-1055079, EBI-2561661;
CC O15160; P25786: PSMA1; NbExp=3; IntAct=EBI-1055079, EBI-359352;
CC O15160; Q5RL73: RBM48; NbExp=3; IntAct=EBI-1055079, EBI-473821;
CC O15160; Q9UFD9: RIMBP3; NbExp=6; IntAct=EBI-1055079, EBI-10182375;
CC O15160; Q9UHP6: RSPH14; NbExp=3; IntAct=EBI-1055079, EBI-748350;
CC O15160; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-1055079, EBI-6257312;
CC O15160; Q8IYX7: SAXO1; NbExp=3; IntAct=EBI-1055079, EBI-3957636;
CC O15160; Q16637: SMN2; NbExp=6; IntAct=EBI-1055079, EBI-395421;
CC O15160; O60504: SORBS3; NbExp=3; IntAct=EBI-1055079, EBI-741237;
CC O15160; Q9H0A9-2: SPATC1L; NbExp=3; IntAct=EBI-1055079, EBI-11995806;
CC O15160; O43609: SPRY1; NbExp=3; IntAct=EBI-1055079, EBI-3866665;
CC O15160; Q9NZ72: STMN3; NbExp=3; IntAct=EBI-1055079, EBI-725557;
CC O15160; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-1055079, EBI-10172380;
CC O15160; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-1055079, EBI-529518;
CC O15160; P15884: TCF4; NbExp=3; IntAct=EBI-1055079, EBI-533224;
CC O15160; Q6ZNM6: TEX43; NbExp=3; IntAct=EBI-1055079, EBI-18115728;
CC O15160; Q9UBB9: TFIP11; NbExp=5; IntAct=EBI-1055079, EBI-1105213;
CC O15160; Q08117-2: TLE5; NbExp=3; IntAct=EBI-1055079, EBI-11741437;
CC O15160; Q9BTD3: TMEM121; NbExp=3; IntAct=EBI-1055079, EBI-12155101;
CC O15160; Q13829: TNFAIP1; NbExp=9; IntAct=EBI-1055079, EBI-2505861;
CC O15160; P19237: TNNI1; NbExp=3; IntAct=EBI-1055079, EBI-746692;
CC O15160; Q9BWF2: TRAIP; NbExp=3; IntAct=EBI-1055079, EBI-1756205;
CC O15160; Q14142: TRIM14; NbExp=3; IntAct=EBI-1055079, EBI-2820256;
CC O15160; P14373: TRIM27; NbExp=6; IntAct=EBI-1055079, EBI-719493;
CC O15160; Q9Y3Q8: TSC22D4; NbExp=6; IntAct=EBI-1055079, EBI-739485;
CC O15160; Q9H9P5-5: UNKL; NbExp=3; IntAct=EBI-1055079, EBI-12817837;
CC O15160; Q70EL1-9: USP54; NbExp=3; IntAct=EBI-1055079, EBI-11975223;
CC O15160; P23025: XPA; NbExp=3; IntAct=EBI-1055079, EBI-295222;
CC O15160; O96006: ZBED1; NbExp=3; IntAct=EBI-1055079, EBI-740037;
CC O15160; B2RXF5: ZBTB42; NbExp=3; IntAct=EBI-1055079, EBI-12287587;
CC O15160; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-1055079, EBI-14104088;
CC O15160; Q9NU63-3: ZFP57; NbExp=3; IntAct=EBI-1055079, EBI-12879708;
CC O15160; Q9NZV7: ZIM2; NbExp=5; IntAct=EBI-1055079, EBI-11962760;
CC O15160; Q8IVP9: ZNF547; NbExp=3; IntAct=EBI-1055079, EBI-12895421;
CC O15160; Q86TJ5: ZNF554; NbExp=3; IntAct=EBI-1055079, EBI-19137100;
CC O15160; Q8N720: ZNF655; NbExp=3; IntAct=EBI-1055079, EBI-625509;
CC O15160; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-1055079, EBI-4395732;
CC O15160; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-1055079, EBI-5667516;
CC O15160; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-1055079, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26151409}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O15160-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O15160-2; Sequence=VSP_005913;
CC -!- DISEASE: Treacher Collins syndrome 3 (TCS3) [MIM:248390]: A form of
CC Treacher Collins syndrome, a disorder of craniofacial development.
CC Treacher Collins syndrome is characterized by a combination of
CC bilateral downward slanting of the palpebral fissures, colobomas of the
CC lower eyelids with a paucity of eyelashes medial to the defect,
CC hypoplasia of the facial bones, cleft palate, malformation of the
CC external ears, atresia of the external auditory canals, and bilateral
CC conductive hearing loss. {ECO:0000269|PubMed:21131976,
CC ECO:0000269|PubMed:26151409}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Leukodystrophy, hypomyelinating, 11 (HLD11) [MIM:616494]: An
CC autosomal recessive neurologic disorder characterized by brain
CC hypomyelination, delayed psychomotor development, intellectual
CC disability, tremor and other neurologic symptoms. Some patients may
CC additionally manifest non-neurologic features, particularly dental
CC abnormalities and hypogonadotropic hypogonadism.
CC {ECO:0000269|PubMed:26151409}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the archaeal Rpo3/eukaryotic RPB3 RNA polymerase
CC subunit family. {ECO:0000305}.
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DR EMBL; AF008442; AAC14354.1; -; mRNA.
DR EMBL; AF047441; AAC39892.1; -; mRNA.
DR EMBL; AL355802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC008863; AAH08863.1; -; mRNA.
DR CCDS; CCDS4900.1; -. [O15160-2]
DR CCDS; CCDS4901.1; -. [O15160-1]
DR RefSeq; NP_001305805.1; NM_001318876.1. [O15160-2]
DR RefSeq; NP_976035.1; NM_203290.3. [O15160-1]
DR PDB; 7A6H; EM; 3.30 A; C=1-346.
DR PDB; 7AE1; EM; 2.80 A; C=1-346.
DR PDB; 7AE3; EM; 3.10 A; C=1-346.
DR PDB; 7AEA; EM; 3.40 A; C=1-346.
DR PDB; 7AST; EM; 4.00 A; H=1-346.
DR PDB; 7D58; EM; 2.90 A; C=1-346.
DR PDB; 7D59; EM; 3.10 A; C=1-346.
DR PDB; 7DN3; EM; 3.50 A; C=1-346.
DR PDB; 7DU2; EM; 3.35 A; C=1-346.
DR PDB; 7FJI; EM; 3.60 A; C=1-346.
DR PDB; 7FJJ; EM; 3.60 A; C=1-346.
DR PDB; 7OB9; EM; 2.70 A; C=1-346.
DR PDB; 7OBA; EM; 3.10 A; C=1-346.
DR PDB; 7OBB; EM; 3.30 A; C=1-346.
DR PDB; 7VBA; EM; 2.89 A; C=1-346.
DR PDB; 7VBB; EM; 2.81 A; C=1-346.
DR PDB; 7VBC; EM; 3.01 A; C=1-346.
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; 7OB9; -.
DR PDBsum; 7OBA; -.
DR PDBsum; 7OBB; -.
DR PDBsum; 7VBA; -.
DR PDBsum; 7VBB; -.
DR PDBsum; 7VBC; -.
DR AlphaFoldDB; O15160; -.
DR SMR; O15160; -.
DR BioGRID; 114909; 262.
DR DIP; DIP-27587N; -.
DR IntAct; O15160; 170.
DR MINT; O15160; -.
DR STRING; 9606.ENSP00000361465; -.
DR GlyGen; O15160; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15160; -.
DR MetOSite; O15160; -.
DR PhosphoSitePlus; O15160; -.
DR BioMuta; POLR1C; -.
DR REPRODUCTION-2DPAGE; IPI00217386; -.
DR SWISS-2DPAGE; O15160; -.
DR EPD; O15160; -.
DR jPOST; O15160; -.
DR MassIVE; O15160; -.
DR MaxQB; O15160; -.
DR PaxDb; O15160; -.
DR PeptideAtlas; O15160; -.
DR PRIDE; O15160; -.
DR ProteomicsDB; 48481; -. [O15160-1]
DR ProteomicsDB; 48482; -. [O15160-2]
DR Antibodypedia; 30448; 291 antibodies from 31 providers.
DR DNASU; 9533; -.
DR Ensembl; ENST00000304004.7; ENSP00000307212.3; ENSG00000171453.20. [O15160-2]
DR Ensembl; ENST00000607635.2; ENSP00000496683.1; ENSG00000171453.20. [O15160-2]
DR Ensembl; ENST00000642195.1; ENSP00000496044.1; ENSG00000171453.20. [O15160-1]
DR GeneID; 9533; -.
DR KEGG; hsa:9533; -.
DR MANE-Select; ENST00000642195.1; ENSP00000496044.1; NM_203290.4; NP_976035.1.
DR UCSC; uc003ovn.4; human. [O15160-1]
DR CTD; 9533; -.
DR DisGeNET; 9533; -.
DR GeneCards; POLR1C; -.
DR GeneReviews; POLR1C; -.
DR HGNC; HGNC:20194; POLR1C.
DR HPA; ENSG00000171453; Low tissue specificity.
DR MalaCards; POLR1C; -.
DR MIM; 248390; phenotype.
DR MIM; 610060; gene.
DR MIM; 616494; phenotype.
DR neXtProt; NX_O15160; -.
DR OpenTargets; ENSG00000171453; -.
DR Orphanet; 88637; Hypomyelination-hypogonadotropic hypogonadism-hypodontia syndrome.
DR Orphanet; 861; Treacher-Collins syndrome.
DR PharmGKB; PA134882004; -.
DR VEuPathDB; HostDB:ENSG00000171453; -.
DR eggNOG; KOG1521; Eukaryota.
DR GeneTree; ENSGT00950000183100; -.
DR HOGENOM; CLU_038421_0_1_1; -.
DR InParanoid; O15160; -.
DR OMA; ECLRHPE; -.
DR OrthoDB; 834009at2759; -.
DR PhylomeDB; O15160; -.
DR TreeFam; TF103034; -.
DR PathwayCommons; O15160; -.
DR Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
DR Reactome; R-HSA-427413; NoRC negatively regulates rRNA expression.
DR Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR Reactome; R-HSA-73772; RNA Polymerase I Promoter Escape.
DR Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
DR Reactome; R-HSA-73863; RNA Polymerase I Transcription Termination.
DR Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
DR Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
DR Reactome; R-HSA-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; O15160; -.
DR SIGNOR; O15160; -.
DR BioGRID-ORCS; 9533; 788 hits in 1089 CRISPR screens.
DR ChiTaRS; POLR1C; human.
DR GeneWiki; POLR1C; -.
DR GenomeRNAi; 9533; -.
DR Pharos; O15160; Tbio.
DR PRO; PR:O15160; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; O15160; protein.
DR Bgee; ENSG00000171453; Expressed in secondary oocyte and 196 other tissues.
DR ExpressionAtlas; O15160; baseline and differential.
DR Genevisible; O15160; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005736; C:RNA polymerase I complex; IBA:GO_Central.
DR GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR GO; GO:0001054; F:RNA polymerase I activity; IEA:InterPro.
DR GO; GO:0001056; F:RNA polymerase III activity; IEA:InterPro.
DR GO; GO:0006360; P:transcription by RNA polymerase I; TAS:ProtInc.
DR CDD; cd07032; RNAP_I_II_AC40; 1.
DR Gene3D; 2.170.120.12; -; 1.
DR Gene3D; 3.30.1360.10; -; 1.
DR HAMAP; MF_00320; RNApol_arch_Rpo3; 1.
DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS.
DR InterPro; IPR011262; DNA-dir_RNA_pol_insert.
DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3.
DR InterPro; IPR036603; RBP11-like.
DR InterPro; IPR022842; RNAP_Rpo3/Rpb3/RPAC1.
DR InterPro; IPR033901; RNAPI/III_AC40.
DR InterPro; IPR036643; RNApol_insert_sf.
DR PANTHER; PTHR11800:SF13; PTHR11800:SF13; 1.
DR Pfam; PF01000; RNA_pol_A_bac; 1.
DR Pfam; PF01193; RNA_pol_L; 1.
DR SMART; SM00662; RPOLD; 1.
DR SUPFAM; SSF55257; SSF55257; 1.
DR SUPFAM; SSF56553; SSF56553; 1.
DR PROSITE; PS00446; RNA_POL_D_30KD; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Direct protein sequencing;
KW Disease variant; DNA-directed RNA polymerase; Leukodystrophy; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..346
FT /note="DNA-directed RNA polymerases I and III subunit
FT RPAC1"
FT /id="PRO_0000132739"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|Ref.5, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 4
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 308..346
FT /note="FSVESTGVLPPDVLVSEAIKVLMGKCRRFLDELDAVQMD -> CKKDLLAAV
FT AHTCNPSTLGGQGEWITGSRERDHPG (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:9653160"
FT /id="VSP_005913"
FT VARIANT 26
FT /note="T -> I (in HLD11; dbSNP:rs796052126)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074655"
FT VARIANT 32
FT /note="N -> I (in HLD11; decreased localization to the
FT nucleus and retained in the cytoplasm; loss of association
FT with RNA polymerase III-transcribed genes; decreased
FT association with RNA polymerase III complex; probably
FT prevents RNA polymerase III complex assembly and activity;
FT dbSNP:rs796052124)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074656"
FT VARIANT 65
FT /note="M -> V (in HLD11; dbSNP:rs141471029)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074657"
FT VARIANT 74
FT /note="N -> S (in HLD11; decreased localization to the
FT nucleus and retained in the cytoplasm; loss of association
FT with RNA polymerase III-transcribed genes; decreased
FT association with RNA polymerase III complex; probably
FT prevents RNA polymerase III complex assembly and activity;
FT dbSNP:rs371802902)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074658"
FT VARIANT 94
FT /note="V -> A (in HLD11; dbSNP:rs1305006253)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074659"
FT VARIANT 109
FT /note="R -> H (in HLD11; dbSNP:rs796052127)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074660"
FT VARIANT 132
FT /note="G -> D (in HLD11; dbSNP:rs201320592)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074661"
FT VARIANT 146
FT /note="C -> R (in HLD11; dbSNP:rs796052125)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074662"
FT VARIANT 191
FT /note="R -> Q (in HLD11; dbSNP:rs373046018)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074663"
FT VARIANT 262
FT /note="I -> T (in HLD11; dbSNP:rs751006626)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074664"
FT VARIANT 279
FT /note="R -> Q (in TCS3; no effect on localization to the
FT nucleus; no effect on association with RNA polymerase I and
FT RNA polymerase III complexes; dbSNP:rs191582628)"
FT /evidence="ECO:0000269|PubMed:21131976,
FT ECO:0000269|PubMed:26151409"
FT /id="VAR_064899"
FT VARIANT 279
FT /note="R -> W (in TCS3; dbSNP:rs141156009)"
FT /evidence="ECO:0000269|PubMed:21131976"
FT /id="VAR_064900"
FT VARIANT 295
FT /note="Missing (in HLD11; dbSNP:rs875989826)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074665"
FT VARIANT 324
FT /note="E -> K (in HLD11; dbSNP:rs1582184344)"
FT /evidence="ECO:0000269|PubMed:26151409"
FT /id="VAR_074666"
FT HELIX 3..10
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 13..16
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 32..35
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 50..57
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 60..67
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 70..82
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 86..97
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 99..101
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 103..111
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 115..117
FT /evidence="ECO:0007829|PDB:7D59"
FT HELIX 119..121
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 138..145
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 150..152
FT /evidence="ECO:0007829|PDB:7D58"
FT HELIX 159..162
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 163..165
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 167..169
FT /evidence="ECO:0007829|PDB:7AE1"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 173..175
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 181..184
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 187..189
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 190..193
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 198..201
FT /evidence="ECO:0007829|PDB:7AE1"
FT STRAND 207..217
FT /evidence="ECO:0007829|PDB:7OB9"
FT TURN 219..221
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 248..255
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 261..275
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 278..280
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 286..288
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 297..312
FT /evidence="ECO:0007829|PDB:7OB9"
FT STRAND 314..316
FT /evidence="ECO:0007829|PDB:7OB9"
FT HELIX 318..343
FT /evidence="ECO:0007829|PDB:7OB9"
SQ SEQUENCE 346 AA; 39250 MW; B7D558BC8F33D92E CRC64;
MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR VDVVHMDENS
LEFDMVGIDA AIANAFRRIL LAEVPTMAVE KVLVYNNTSI VQDEILAHRL GLIPIHADPR
LFEYRNQGDE EGTEIDTLQF RLQVRCTRNP HAAKDSSDPN ELYVNHKVYT RHMTWIPLGN
QADLFPEGTI RPVHDDILIA QLRPGQEIDL LMHCVKGIGK DHAKFSPVAT ASYRLLPDIT
LLEPVEGEAA EELSRCFSPG VIEVQEVQGK KVARVANPRL DTFSREIFRN EKLKKVVRLA
RVRDHYIFSV ESTGVLPPDV LVSEAIKVLM GKCRRFLDEL DAVQMD
