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DNA-directed RNA polymerase III subunit RPC3 (RNA polymerase III subunit C3) (DNA-directed RNA polymerase III subunit C) (RNA polymerase III 62 kDa subunit) (RPC62)

 RPC3_HUMAN              Reviewed;         534 AA.
Q9BUI4; O15317; Q9Y3R6;
05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
01-JUN-2001, sequence version 1.
10-OCT-2018, entry version 143.
RecName: Full=DNA-directed RNA polymerase III subunit RPC3;
Short=RNA polymerase III subunit C3;
AltName: Full=DNA-directed RNA polymerase III subunit C;
AltName: Full=RNA polymerase III 62 kDa subunit;
Short=RPC62;
Name=POLR3C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH POLR3G AND POLR3F, AND
VARIANT ARG-243.
TISSUE=Cervix carcinoma;
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 [MRNA], AND IDENTIFICATION AS ANTIGEN IN SYSTEMIC
SCLEROSIS.
PubMed=12384934; DOI=10.1002/art.10521;
Kuwana M., Kimura K., Kawakami Y.;
"Identification of an immunodominant epitope on RNA polymerase III
recognized by systemic sclerosis sera: application to enzyme-linked
immunosorbent assay.";
Arthritis Rheum. 46:2742-2747(2002).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Totaro A.;
"Genomic structure of human RNA polymerase III subunit (RPC62).";
Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Ovary;
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).
[5]
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).
[6]
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-194, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[8]
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).
[9]
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).
[10]
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).
[11]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[12]
INTERACTION WITH POLR3G AND POLR3GL.
PubMed=24107381; DOI=10.1101/gr.161570.113;
Renaud M., Praz V., Vieu E., Florens L., Washburn M.P., l'Hote P.,
Hernandez N.;
"Gene duplication and neofunctionalization: POLR3G and POLR3GL.";
Genome Res. 24:37-51(2014).
[13] {ECO:0000244|PDB:2XUB, ECO:0000244|PDB:2XV4}
X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS), FUNCTION, INTERACTION WITH
POLR3F; POLR3G AND POLR3GL, AND MUTAGENESIS OF 51-LYS-LYS-52; LEU-312;
ARG-357; 364-ARG--ARG-367; LYS-389; 445-ASN--ARG-449 AND
466-ARG--ILE-470.
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).
[14] {ECO:0000244|PDB:5AFQ}
X-RAY CRYSTALLOGRAPHY (7.00 ANGSTROMS) IN COMPLEX WITH POLR3GL.
PubMed=26394183; DOI=10.1016/J.JSB.2015.09.004;
Boissier F., Dumay-Odelot H., Teichmann M., Fribourg S.;
"Structural analysis of human RPC32beta-RPC62 complex.";
J. Struct. Biol. 192:313-319(2015).
-!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription
of DNA into RNA using the four ribonucleoside triphosphates as
substrates. Specific core component of RNA polymerase III which
synthesizes small RNAs, such as 5S rRNA and tRNAs. May direct with
other members of the subcomplex RNA Pol III binding to the TFIIIB-
DNA complex via the interactions between TFIIIB and POLR3F. May be
involved either in the recruitment and stabilization of the
subcomplex within RNA polymerase III, or in stimulating catalytic
functions of other subunits during initiation. 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 single-stranded DNA (ssDNA) in a
sequence-independent manner (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 (By similarity). RPC3/POLR3C,
RPC6/POLR3F and RPC7/POLR3G form a Pol III subcomplex
(PubMed:9171375, PubMed:12391170). Directly interacts with POLR3G
and POLR3GL (PubMed:24107381, PubMed:21358628, PubMed:26394183).
Directly interacts with POLR3F/RPC39 (PubMed:26394183). Interacts
with GTF3C4 (PubMed:10523658). {ECO:0000250,
ECO:0000269|PubMed:10523658, ECO:0000269|PubMed:12391170,
ECO:0000269|PubMed:21358628, ECO:0000269|PubMed:24107381,
ECO:0000269|PubMed:26394183, ECO:0000269|PubMed:9171375}.
-!- INTERACTION:
Q96PV4:PNMA5; NbExp=3; IntAct=EBI-5452779, EBI-10171633;
Q9H1D9:POLR3F; NbExp=2; IntAct=EBI-5452779, EBI-710067;
O15318:POLR3G; NbExp=4; IntAct=EBI-5452779, EBI-12362221;
Q9BT43:POLR3GL; NbExp=6; IntAct=EBI-5452779, EBI-2855862;
Q13464:ROCK1; NbExp=3; IntAct=EBI-5452779, EBI-876651;
Q9HAT0:ROPN1; NbExp=3; IntAct=EBI-5452779, EBI-1378139;
A1L306:TNR; NbExp=3; IntAct=EBI-5452779, EBI-10182881;
P14373:TRIM27; NbExp=5; IntAct=EBI-5452779, EBI-719493;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
-!- MISCELLANEOUS: Antibodies against POLR3C have been found in the
sera of patients with systemic sclerosis (SSc).
-!- SIMILARITY: Belongs to the eukaryotic RPC3/POLR3C RNA polymerase
subunit family. {ECO:0000305}.
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EMBL; U93867; AAB63675.1; -; mRNA.
EMBL; AY091463; AAM12033.1; -; mRNA.
EMBL; AJ238221; CAB41919.1; -; Genomic_DNA.
EMBL; AJ238222; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238223; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238224; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238225; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238226; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238227; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238228; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238229; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238230; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238231; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238232; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238233; CAB41919.1; JOINED; Genomic_DNA.
EMBL; AJ238234; CAB41919.1; JOINED; Genomic_DNA.
EMBL; BC002586; AAH02586.1; -; mRNA.
CCDS; CCDS72864.1; -.
RefSeq; NP_001290385.1; NM_001303456.1.
RefSeq; NP_006459.3; NM_006468.7.
UniGene; Hs.515768; -.
UniGene; Hs.591457; -.
PDB; 2XUB; X-ray; 2.80 A; A=1-534.
PDB; 2XV4; X-ray; 2.95 A; S=1-534.
PDB; 5AFQ; X-ray; 7.00 A; A/B=1-534.
PDBsum; 2XUB; -.
PDBsum; 2XV4; -.
PDBsum; 5AFQ; -.
ProteinModelPortal; Q9BUI4; -.
SMR; Q9BUI4; -.
BioGrid; 115868; 43.
DIP; DIP-59078N; -.
IntAct; Q9BUI4; 38.
STRING; 9606.ENSP00000334564; -.
GlyConnect; 1184; -.
iPTMnet; Q9BUI4; -.
PhosphoSitePlus; Q9BUI4; -.
BioMuta; POLR3C; -.
DMDM; 60393871; -.
EPD; Q9BUI4; -.
MaxQB; Q9BUI4; -.
PaxDb; Q9BUI4; -.
PeptideAtlas; Q9BUI4; -.
PRIDE; Q9BUI4; -.
ProteomicsDB; 79088; -.
DNASU; 10623; -.
Ensembl; ENST00000334163; ENSP00000334564; ENSG00000186141.
GeneID; 10623; -.
KEGG; hsa:10623; -.
UCSC; uc001eoh.3; human.
CTD; 10623; -.
EuPathDB; HostDB:ENSG00000186141.8; -.
GeneCards; POLR3C; -.
HGNC; HGNC:30076; POLR3C.
HPA; HPA027508; -.
HPA; HPA027516; -.
MIM; 617454; gene.
neXtProt; NX_Q9BUI4; -.
OpenTargets; ENSG00000186141; -.
PharmGKB; PA134870963; -.
eggNOG; KOG2587; Eukaryota.
eggNOG; ENOG410XPVH; LUCA.
GeneTree; ENSGT00390000002799; -.
HOGENOM; HOG000046475; -.
HOVERGEN; HBG059543; -.
InParanoid; Q9BUI4; -.
KO; K03023; -.
OMA; EQCFGKV; -.
OrthoDB; EOG091G186Z; -.
PhylomeDB; Q9BUI4; -.
TreeFam; TF103048; -.
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; POLR3C; human.
EvolutionaryTrace; Q9BUI4; -.
GeneWiki; POLR3C; -.
GenomeRNAi; 10623; -.
PRO; PR:Q9BUI4; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000186141; Expressed in 208 organ(s), highest expression level in right testis.
CleanEx; HS_POLR3C; -.
ExpressionAtlas; Q9BUI4; baseline and differential.
Genevisible; Q9BUI4; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005666; C:RNA polymerase III complex; IDA:MGI.
GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; TAS:ProtInc.
GO; GO:0003697; F:single-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; TAS:ProtInc.
GO; GO:0006383; P:transcription by RNA polymerase III; IEA:GOC.
Gene3D; 1.10.10.10; -; 4.
InterPro; IPR013197; RNA_pol_III_RPC82-rel_HTH.
InterPro; IPR008806; RNA_pol_III_Rpc82_C.
InterPro; IPR036388; WH-like_DNA-bd_sf.
Pfam; PF08221; HTH_9; 1.
Pfam; PF05645; RNA_pol_Rpc82; 1.
1: Evidence at protein level;
3D-structure; Antiviral defense; Complete proteome; DNA-binding;
DNA-directed RNA polymerase; Immunity; Innate immunity; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Transcription.
CHAIN 1 534 DNA-directed RNA polymerase III subunit
RPC3.
/FTId=PRO_0000073963.
MOD_RES 194 194 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
VARIANT 243 243 H -> R (in dbSNP:rs1044697).
{ECO:0000269|PubMed:9171375}.
/FTId=VAR_019083.
MUTAGEN 51 52 KK->EE: Strongly decreased ssDNA-binding.
No effect on interaction with POLR3F,
POLR3G, nor with POLR3GL.
{ECO:0000269|PubMed:21358628}.
MUTAGEN 312 312 L->K: Loss of interaction with POLR3G and
POLR3GL. No effect on interaction with
POLR3F. {ECO:0000269|PubMed:21358628}.
MUTAGEN 357 357 R->E: Strongly decreased ssDNA-binding.
No effect on interaction with POLR3F,
POLR3G, nor with POLR3GL.
{ECO:0000269|PubMed:21358628}.
MUTAGEN 364 367 RIFR->EIFE: Strongly decreased ssDNA-
binding. No effect on interaction with
POLR3F, POLR3G, nor with POLR3GL.
{ECO:0000269|PubMed:21358628}.
MUTAGEN 389 389 K->E: Strongly decreased ssDNA-binding.
No effect on interaction with POLR3F,
POLR3G, nor with POLR3GL.
{ECO:0000269|PubMed:21358628}.
MUTAGEN 445 449 NLIER->ALIEE: Strongly decreased ssDNA-
binding. No effect on interaction with
POLR3F, POLR3G, nor with POLR3GL.
{ECO:0000269|PubMed:21358628}.
MUTAGEN 466 470 RVEAI->EVEAF: Mild decrease in ssDNA-
binding. No effect on interaction with
POLR3F, POLR3G, nor with POLR3GL.
{ECO:0000269|PubMed:21358628}.
CONFLICT 85 86 ML -> IV (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 119 120 SA -> CT (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 216 237 KRPKYTTDNKEPIPDDGIYWQA -> RDQNILQITRXPFQM
MGFIGRP (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 289 289 S -> F (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 343 343 A -> R (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 366 366 F -> C (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 387 389 PAK -> LQ (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 401 401 E -> G (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 436 437 LH -> FD (in Ref. 1; AAB63675).
{ECO:0000305}.
CONFLICT 517 517 D -> E (in Ref. 3; CAB41919).
{ECO:0000305}.
HELIX 3 31 {ECO:0000244|PDB:2XUB}.
STRAND 33 35 {ECO:0000244|PDB:2XUB}.
HELIX 36 43 {ECO:0000244|PDB:2XUB}.
HELIX 47 59 {ECO:0000244|PDB:2XUB}.
STRAND 62 68 {ECO:0000244|PDB:2XUB}.
TURN 69 71 {ECO:0000244|PDB:2XUB}.
STRAND 72 77 {ECO:0000244|PDB:2XUB}.
HELIX 79 83 {ECO:0000244|PDB:2XUB}.
HELIX 84 87 {ECO:0000244|PDB:2XUB}.
HELIX 88 113 {ECO:0000244|PDB:2XUB}.
HELIX 118 131 {ECO:0000244|PDB:2XUB}.
STRAND 133 136 {ECO:0000244|PDB:2XUB}.
HELIX 141 153 {ECO:0000244|PDB:2XUB}.
STRAND 156 159 {ECO:0000244|PDB:2XUB}.
STRAND 234 237 {ECO:0000244|PDB:2XUB}.
HELIX 239 258 {ECO:0000244|PDB:2XUB}.
HELIX 261 272 {ECO:0000244|PDB:2XUB}.
TURN 273 277 {ECO:0000244|PDB:2XUB}.
HELIX 290 295 {ECO:0000244|PDB:2XUB}.
HELIX 305 316 {ECO:0000244|PDB:2XUB}.
STRAND 323 325 {ECO:0000244|PDB:2XUB}.
STRAND 333 337 {ECO:0000244|PDB:2XUB}.
HELIX 338 358 {ECO:0000244|PDB:2XUB}.
HELIX 360 371 {ECO:0000244|PDB:2XUB}.
HELIX 377 384 {ECO:0000244|PDB:2XUB}.
HELIX 388 400 {ECO:0000244|PDB:2XUB}.
HELIX 428 456 {ECO:0000244|PDB:2XUB}.
HELIX 458 472 {ECO:0000244|PDB:2XUB}.
HELIX 485 488 {ECO:0000244|PDB:2XUB}.
HELIX 493 529 {ECO:0000244|PDB:2XUB}.
SEQUENCE 534 AA; 60612 MW; 0E4CFEE295EE1A55 CRC64;
MTQAEIKLCS LLLQEHFGEI VEKIGVHLIR TGSQPLRVIA HDTGTSLDQV KKALCVLVQH
NLVSYQVHKR GVVEYEAQCS RVLRMLRYPR YIYTTKTLYS DTGELIVEEL LLNGKLTMSA
VVKKVADRLT ETMEDGKTMD YAEVSNTFVR LADTHFVQRC PSVPTTENSD PGPPPPAPTL
VINEKDMYLV PKLSLIGKGK RRRSSDEDAA GEPKAKRPKY TTDNKEPIPD DGIYWQANLD
RFHQHFRDQA IVSAVANRMD QTSSEIVRTM LRMSEITTSS SAPFTQPLSS NEIFRSLPVG
YNISKQVLDQ YLTLLADDPL EFVGKSGDSG GGMYVINLHK ALASLATATL ESVVQERFGS
RCARIFRLVL QKKHIEQKQV EDFAMIPAKE AKDMLYKMLS ENFMSLQEIP KTPDHAPSRT
FYLYTVNILS AARMLLHRCY KSIANLIERR QFETKENKRL LEKSQRVEAI IASMQATGAE
EAQLQEIEEM ITAPERQQLE TLKRNVNKLD ASEIQVDETI FLLESYIECT MKRQ


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EIAAB35825 DNA-directed RNA polymerase III subunit F,DNA-directed RNA polymerase III subunit RPC6,Homo sapiens,Human,POLR3F,RNA polymerase III 39 kDa subunit,RNA polymerase III subunit C6,RPC39
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
EIAAB35817 DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,Mouse,Mus musculus,Polr3c,RNA polymerase III subunit C3
EIAAB35814 DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,Polr3c,Rat,Rattus norvegicus,RNA polymerase III subunit C3
EIAAB35816 Bos taurus,Bovine,DNA-directed RNA polymerase III subunit C,DNA-directed RNA polymerase III subunit RPC3,POLR3C,RNA polymerase III subunit C3
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


 

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