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DNA-directed RNA polymerase III subunit RPC6 (RNA polymerase III subunit C6) (DNA-directed RNA polymerase III subunit F) (RNA polymerase III 39 kDa subunit) (RPC39)

 RPC6_HUMAN              Reviewed;         316 AA.
Q9H1D9; A8K4C7; O15319;
27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
20-JUN-2018, entry version 163.
RecName: Full=DNA-directed RNA polymerase III subunit RPC6;
Short=RNA polymerase III subunit C6;
AltName: Full=DNA-directed RNA polymerase III subunit F;
AltName: Full=RNA polymerase III 39 kDa subunit;
Short=RPC39;
Name=POLR3F;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9171375; DOI=10.1101/gad.11.10.1315;
Wang Z., Roeder R.G.;
"Three human RNA polymerase III-specific subunits form a subcomplex
with a selective function in specific transcription initiation.";
Genes Dev. 11:1315-1326(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M.,
Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H.,
Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
INTERACTION WITH GTF3C4.
PubMed=10523658; DOI=10.1128/MCB.19.11.7697;
Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.;
"The TFIIIC90 subunit of TFIIIC interacts with multiple components of
the RNA polymerase III machinery and contains a histone-specific
acetyltransferase activity.";
Mol. Cell. Biol. 19:7697-7704(1999).
[7]
IDENTIFICATION IN THE RNA POL III COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=12391170; DOI=10.1128/MCB.22.22.8044-8055.2002;
Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P.,
Hernandez N.;
"Characterization of human RNA polymerase III identifies orthologues
for Saccharomyces cerevisiae RNA polymerase III subunits.";
Mol. Cell. Biol. 22:8044-8055(2002).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[9]
FUNCTION, INTERACTION WITH POLR3C, AND MUTAGENESIS OF 137-LYS--LYS-140
AND 173-GLU--GLU-175.
PubMed=21358628; DOI=10.1038/NSMB.1996;
Lefevre S., Dumay-Odelot H., El-Ayoubi L., Budd A., Legrand P.,
Pinaud N., Teichmann M., Fribourg S.;
"Structure-function analysis of hRPC62 provides insights into RNA
polymerase III transcription initiation.";
Nat. Struct. Mol. Biol. 18:352-358(2011).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[11]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[12]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[13]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-5 AND LYS-7, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[14]
STRUCTURE BY NMR OF 60-155.
RIKEN structural genomics initiative (RSGI);
"Solution structure of winged-helix domain in RNA polymerase III 39kDa
polypeptide.";
Submitted (OCT-2006) to the PDB data bank.
[15]
FUNCTION.
PubMed=19631370; DOI=10.1016/j.cell.2009.06.015;
Chiu Y.-H., Macmillan J.B., Chen Z.J.;
"RNA polymerase III detects cytosolic DNA and induces type I
interferons through the RIG-I pathway.";
Cell 138:576-591(2009).
[16]
FUNCTION.
PubMed=19609254; DOI=10.1038/ni.1779;
Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A.,
Hornung V.;
"RIG-I-dependent sensing of poly(dA:dT) through the induction of an
RNA polymerase III-transcribed RNA intermediate.";
Nat. Immunol. 10:1065-1072(2009).
-!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
of DNA into RNA using the four ribonucleoside triphosphates as
substrates. Specific peripheric component of RNA polymerase III
which synthesizes small RNAs, such as 5S rRNA and tRNAs. May
direct RNA Pol III binding to the TFIIIB-DNA complex. Plays a key
role in sensing and limiting infection by intracellular bacteria
and DNA viruses. Acts as nuclear and cytosolic DNA sensor involved
in innate immune response. Can sense non-self dsDNA that serves as
template for transcription into dsRNA. The non-self RNA polymerase
III transcripts, such as Epstein-Barr virus-encoded RNAs (EBERs)
induce type I interferon and NF- Kappa-B through the RIG-I
pathway. Preferentially binds double-stranded DNA (dsDNA)
(PubMed:21358628). {ECO:0000269|PubMed:19609254,
ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:21358628}.
-!- SUBUNIT: Component of the RNA polymerase III (Pol III) complex
consisting of 17 subunits. RPC3/POLR3C, RPC6/POLR3F and
RPC7/POLR3G form a Pol III subcomplex (By similarity). Directly
interacts with POLR3C (PubMed:21358628). Interacts with TBP and
TFIIIB90 and GTF3C4 (By similarity) (PubMed:10523658).
{ECO:0000250, ECO:0000269|PubMed:10523658,
ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:21358628}.
-!- INTERACTION:
Q12796:PNRC1; NbExp=3; IntAct=EBI-710067, EBI-2827376;
Q9BUI4:POLR3C; NbExp=2; IntAct=EBI-710067, EBI-5452779;
O15318:POLR3G; NbExp=3; IntAct=EBI-710067, EBI-12362221;
Q9BT43:POLR3GL; NbExp=3; IntAct=EBI-710067, EBI-2855862;
Q13523:PRPF4B; NbExp=2; IntAct=EBI-710067, EBI-395940;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- SIMILARITY: Belongs to the eukaryotic RPC34/RPC39 RNA polymerase
subunit family. {ECO:0000305}.
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EMBL; U93869; AAB63677.1; -; mRNA.
EMBL; AK290892; BAF83581.1; -; mRNA.
EMBL; AL121893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471133; EAX10240.1; -; Genomic_DNA.
EMBL; BC012588; AAH12588.1; -; mRNA.
CCDS; CCDS13135.1; -.
RefSeq; NP_001269455.1; NM_001282526.1.
RefSeq; NP_006457.2; NM_006466.3.
UniGene; Hs.472227; -.
PDB; 2DK5; NMR; -; A=78-155.
PDB; 2YU3; NMR; -; A=61-142.
PDBsum; 2DK5; -.
PDBsum; 2YU3; -.
ProteinModelPortal; Q9H1D9; -.
SMR; Q9H1D9; -.
BioGrid; 115866; 41.
DIP; DIP-34646N; -.
IntAct; Q9H1D9; 33.
MINT; Q9H1D9; -.
STRING; 9606.ENSP00000366828; -.
iPTMnet; Q9H1D9; -.
PhosphoSitePlus; Q9H1D9; -.
DMDM; 20139728; -.
EPD; Q9H1D9; -.
MaxQB; Q9H1D9; -.
PaxDb; Q9H1D9; -.
PeptideAtlas; Q9H1D9; -.
PRIDE; Q9H1D9; -.
ProteomicsDB; 80402; -.
DNASU; 10621; -.
Ensembl; ENST00000377603; ENSP00000366828; ENSG00000132664.
GeneID; 10621; -.
KEGG; hsa:10621; -.
UCSC; uc002wqv.5; human.
CTD; 10621; -.
EuPathDB; HostDB:ENSG00000132664.11; -.
GeneCards; POLR3F; -.
HGNC; HGNC:15763; POLR3F.
HPA; HPA049441; -.
HPA; HPA050173; -.
HPA; HPA072298; -.
MIM; 617455; gene.
neXtProt; NX_Q9H1D9; -.
OpenTargets; ENSG00000132664; -.
PharmGKB; PA33520; -.
eggNOG; KOG3233; Eukaryota.
eggNOG; COG5111; LUCA.
GeneTree; ENSGT00390000009679; -.
HOGENOM; HOG000231688; -.
HOVERGEN; HBG006817; -.
InParanoid; Q9H1D9; -.
KO; K03025; -.
OMA; CEYMRDW; -.
OrthoDB; EOG091G0DUX; -.
PhylomeDB; Q9H1D9; -.
TreeFam; TF103051; -.
Reactome; R-HSA-1834949; Cytosolic sensors of pathogen-associated DNA.
Reactome; R-HSA-73780; RNA Polymerase III Chain Elongation.
Reactome; R-HSA-73980; RNA Polymerase III Transcription Termination.
Reactome; R-HSA-749476; RNA Polymerase III Abortive And Retractive Initiation.
Reactome; R-HSA-76061; RNA Polymerase III Transcription Initiation From Type 1 Promoter.
Reactome; R-HSA-76066; RNA Polymerase III Transcription Initiation From Type 2 Promoter.
Reactome; R-HSA-76071; RNA Polymerase III Transcription Initiation From Type 3 Promoter.
ChiTaRS; POLR3F; human.
EvolutionaryTrace; Q9H1D9; -.
GeneWiki; POLR3F; -.
GenomeRNAi; 10621; -.
PRO; PR:Q9H1D9; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000132664; -.
CleanEx; HS_POLR3F; -.
Genevisible; Q9H1D9; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005666; C:DNA-directed RNA polymerase III complex; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; NAS:UniProtKB.
GO; GO:0003690; F:double-stranded DNA binding; IDA:UniProtKB.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0045089; P:positive regulation of innate immune response; IMP:UniProtKB.
GO; GO:0032728; P:positive regulation of interferon-beta production; IMP:UniProtKB.
GO; GO:0006359; P:regulation of transcription by RNA polymerase III; NAS:UniProtKB.
GO; GO:0006383; P:transcription by RNA polymerase III; IEA:InterPro.
Gene3D; 1.10.10.10; -; 2.
InterPro; IPR007832; RNA_pol_Rpc34.
InterPro; IPR016049; RNA_pol_Rpc34-like.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
PANTHER; PTHR12780; PTHR12780; 1.
Pfam; PF05158; RNA_pol_Rpc34; 1.
PIRSF; PIRSF028763; RNA_pol_Rpc34; 1.
SUPFAM; SSF46785; SSF46785; 2.
1: Evidence at protein level;
3D-structure; Acetylation; Antiviral defense; Complete proteome;
DNA-binding; DNA-directed RNA polymerase; Immunity; Innate immunity;
Isopeptide bond; Nucleus; Reference proteome; Transcription;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378}.
CHAIN 2 316 DNA-directed RNA polymerase III subunit
RPC6.
/FTId=PRO_0000073972.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
CROSSLNK 5 5 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 7 7 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
MUTAGEN 137 140 KAVK->EAVE: Strongly impaired dsDNA-
binding. No effect on interaction with
POLR3C. {ECO:0000269|PubMed:21358628}.
MUTAGEN 173 175 ESE->KSK: Strongly impaired dsDNA-
binding. No effect on interaction with
POLR3C. {ECO:0000269|PubMed:21358628}.
CONFLICT 2 2 A -> G (in Ref. 1; AAB63677).
{ECO:0000305}.
CONFLICT 44 53 HIEAQQRAVA -> QYRSPAAGSS (in Ref. 1;
AAB63677). {ECO:0000305}.
CONFLICT 255 290 AKEGTVGSVDGHMKLYRAVNPIIPPTGLVRAPCGLC -> C
KRRHSWQCRWTHETVQGSQSNHPSHRFGPGHPVDSA (in
Ref. 1; AAB63677). {ECO:0000305}.
STRAND 73 76 {ECO:0000244|PDB:2YU3}.
STRAND 79 81 {ECO:0000244|PDB:2YU3}.
HELIX 92 102 {ECO:0000244|PDB:2DK5}.
HELIX 109 115 {ECO:0000244|PDB:2DK5}.
HELIX 120 132 {ECO:0000244|PDB:2DK5}.
STRAND 135 139 {ECO:0000244|PDB:2DK5}.
STRAND 149 155 {ECO:0000244|PDB:2DK5}.
SEQUENCE 316 AA; 35684 MW; 49B1360AF8B365ED CRC64;
MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR AVAINRLLSM
GQLDLLRSNT GLLYRIKDSQ NAGKMKGSDN QEKLVYQIIE DAGNKGIWSR DIRYKSNLPL
TEINKILKNL ESKKLIKAVK SVAASKKKVY MLYNLQPDRS VTGGAWYSDQ DFESEFVEVL
NQQCFKFLQS KAETARESKQ NPMIQRNSSF ASSHEVWKYI CELGISKVEL SMEDIETILN
TLIYDGKVEM TIIAAKEGTV GSVDGHMKLY RAVNPIIPPT GLVRAPCGLC PVFDDCHEGG
EISPSNCIYM TEWLEF


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EIAAB35823 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit F,DNA-directed RNA polymerase III subunit RPC6,POLR3F,RNA polymerase III subunit C6
EIAAB35824 DNA-directed RNA polymerase III subunit F,DNA-directed RNA polymerase III subunit RPC6,Mouse,Mus musculus,Polr3f,RNA polymerase III subunit C6
EIAAB35750 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Homo sapiens,Human,PAF53,POLR1E,PRAF1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35796 DNA-directed RNA polymerase II subunit D,DNA-directed RNA polymerase II subunit RPB4,Homo sapiens,Human,POLR2D,RNA polymerase II 16 kDa subunit,RNA polymerase II subunit B4,RPB16
EIAAB35786 DNA-directed RNA polymerase II subunit J,DNA-directed RNA polymerase II subunit RPB11,Mouse,Mus musculus,Polr2j,RNA polymerase II 13.3 kDa subunit,RNA polymerase II subunit B11,RPB14,Rpo2-4
EIAAB35815 DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,Homo sapiens,Human,POLR3C,RNA polymerase III 62 kDa subunit,RNA polymerase III subunit C3,RPC62
EIAAB35827 DNA-directed RNA polymerase III subunit G,DNA-directed RNA polymerase III subunit RPC7,Homo sapiens,Human,POLR3G,RNA polymerase III 32 kDa subunit,RNA polymerase III subunit C7,RPC32
EIAAB35802 DNA-directed RNA polymerase II subunit I,DNA-directed RNA polymerase II subunit RPB9,Homo sapiens,Human,POLR2I,RNA polymerase II 14.5 kDa subunit,RNA polymerase II subunit B9,RPB14.5
EIAAB35749 DNA-directed RNA polymerase I subunit E,DNA-directed RNA polymerase I subunit RPA49,Mouse,Mus musculus,Paf53,Polr1e,Praf1,RNA polymerase I subunit A49,RNA polymerase I-associated factor 1,RNA polymera
EIAAB35832 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit 22.9 kDa polypeptide,DNA-directed RNA polymerase III subunit H,DNA-directed RNA polymerase III subunit RPC8,POLR3H,RNA polymerase III subunit
EIAAB35793 DNA-directed RNA polymerase II 33 kDa polypeptide,DNA-directed RNA polymerase II subunit C,DNA-directed RNA polymerase II subunit RPB3,Mouse,Mus musculus,Polr2c,RNA polymerase II subunit 3,RNA polymer
EIAAB35791 DNA-directed RNA polymerase II 140 kDa polypeptide,DNA-directed RNA polymerase II subunit B,DNA-directed RNA polymerase II subunit RPB2,Mouse,Mus musculus,Polr2b,RNA polymerase II subunit 2,RNA polyme


 

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