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DNA-directed RNA polymerase III subunit RPC7 (RNA polymerase III subunit C7) (DNA-directed RNA polymerase III subunit G) (RNA polymerase III 32 kDa apha subunit) (RPC32-alpha) (RNA polymerase III 32 kDa subunit) (RPC32)

 RPC7_HUMAN              Reviewed;         223 AA.
O15318; A8MTH0;
01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
16-DEC-2008, sequence version 2.
10-OCT-2018, entry version 131.
RecName: Full=DNA-directed RNA polymerase III subunit RPC7;
Short=RNA polymerase III subunit C7;
AltName: Full=DNA-directed RNA polymerase III subunit G;
AltName: Full=RNA polymerase III 32 kDa apha subunit;
Short=RPC32-alpha {ECO:0000303|PubMed:20154270};
AltName: Full=RNA polymerase III 32 kDa subunit;
Short=RPC32;
Name=POLR3G;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND INTERACTION WITH POLR3C AND POLR3F.
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 [LARGE SCALE MRNA].
TISSUE=Corpus callosum;
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=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[5]
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).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, 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).
[7]
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).
[8]
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).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=20154270; DOI=10.1073/pnas.0914980107;
Haurie V., Durrieu-Gaillard S., Dumay-Odelot H., Da Silva D., Rey C.,
Prochazkova M., Roeder R.G., Besser D., Teichmann M.;
"Two isoforms of human RNA polymerase III with specific functions in
cell growth and transformation.";
Proc. Natl. Acad. Sci. U.S.A. 107:4176-4181(2010).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[11]
INTERACTION WITH POLR3C.
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).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-157, AND 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).
[13]
SUBCELLULAR LOCATION, INDUCTION BY NANOG AND POU5F1, AND DEVELOPMENTAL
STAGE.
PubMed=21898682; DOI=10.1002/stem.714;
Wong R.C., Pollan S., Fong H., Ibrahim A., Smith E.L., Ho M.,
Laslett A.L., Donovan P.J.;
"A novel role for an RNA polymerase III subunit POLR3G in regulating
pluripotency in human embryonic stem cells.";
Stem Cells 29:1517-1527(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-133, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
IDENTIFICATION IN RNA POL III SUBCOMPLEXES, AND TISSUE SPECIFICITY.
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).
[16]
INTERACTION WITH POLR3C.
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).
[17]
INDUCTION.
PubMed=27339422; DOI=10.1002/stem.2444;
Jin S., Collin J., Zhu L., Montaner D., Armstrong L., Neganova I.,
Lako M.;
"A novel role for miR-1305 in regulation of pluripotency-
differentiation balance, cell cycle, and apoptosis in human
pluripotent stem cells.";
Stem Cells 34:2306-2317(2016).
[18]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=28494942; DOI=10.1016/j.stemcr.2017.04.016;
Lund R.J., Rahkonen N., Malonzo M., Kauko L., Emani M.R., Kivinen V.,
Naervae E., Kemppainen E., Laiho A., Skottman H., Hovatta O.,
Rasool O., Nykter M., Laehdesmaeki H., Lahesmaa R.;
"RNA polymerase III subunit POLR3G regulates specific subsets of
polyA(+) and smallRNA transcriptomes and splicing in human pluripotent
stem cells.";
Stem Cell Reports 8:1442-1454(2017).
-!- 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
(PubMed:20154270). May direct with other members of the
RPC3/POLR3C-RPC6/POLR3F-RPC7/POLR3G 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 (PubMed:19609254,
PubMed:19631370). {ECO:0000269|PubMed:19609254,
ECO:0000269|PubMed:19631370, ECO:0000269|PubMed:20154270}.
-!- 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. Directly
interacts with POLR3C/RPC62 (PubMed:21358628, PubMed:24107381,
PubMed:26394183). Also found a trimeric complex with POLR3C and
POLR3GL (PubMed:24107381). {ECO:0000250,
ECO:0000269|PubMed:12391170, ECO:0000269|PubMed:21358628,
ECO:0000269|PubMed:24107381, ECO:0000269|PubMed:26394183}.
-!- INTERACTION:
Q9BUI4:POLR3C; NbExp=4; IntAct=EBI-12362221, EBI-5452779;
Q9H1D9:POLR3F; NbExp=3; IntAct=EBI-12362221, EBI-710067;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20154270,
ECO:0000269|PubMed:21898682}. Cytoplasm
{ECO:0000250|UniProtKB:Q6NXY9}. Note=Excluded from nucleoli
(PubMed:21898682). In zygotes and the 2-cell stage embryos, mainly
in the cytoplasm. Starts to localize to the nucleus in the 8-16
cell stage embryo and early blastocysts (By similarity).
{ECO:0000250|UniProtKB:Q6NXY9, ECO:0000269|PubMed:21898682}.
-!- TISSUE SPECIFICITY: Barely detectable in differentiated tissues.
Expressed in embryonic stem cells and in other dividing cells,
such as some tumor cell lines. {ECO:0000269|PubMed:20154270,
ECO:0000269|PubMed:24107381, ECO:0000269|PubMed:28494942}.
-!- DEVELOPMENTAL STAGE: Down-regulated in embryonic stem cells upon
differentiation into embroid bodies (at protein level)
(PubMed:20154270, PubMed:21898682, PubMed:28494942). An analogous
down-regulation is observed during differentiation of induced
pluripotent stem cells (PubMed:21898682).
{ECO:0000269|PubMed:20154270, ECO:0000269|PubMed:21898682,
ECO:0000269|PubMed:28494942}.
-!- INDUCTION: Induced by NANOG and POU5F1/OCT4 (PubMed:21898682).
Negatively regulated by the interaction of microRNA MIR1305 with 3
miRNA responsive elements (miREs) in its 3'-UTR (PubMed:27339422).
{ECO:0000269|PubMed:21898682, ECO:0000269|PubMed:27339422}.
-!- SIMILARITY: Belongs to the eukaryotic RPC7 RNA polymerase subunit
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAB63676.1; Type=Frameshift; Positions=214; Evidence={ECO:0000305};
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EMBL; U93868; AAB63676.1; ALT_FRAME; mRNA.
EMBL; AK295434; BAG58376.1; -; mRNA.
EMBL; AC027323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC093510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471084; EAW95980.1; -; Genomic_DNA.
CCDS; CCDS43337.1; -.
RefSeq; NP_006458.2; NM_006467.2.
RefSeq; XP_005248461.1; XM_005248404.3.
RefSeq; XP_011541402.1; XM_011543100.2.
RefSeq; XP_011541403.1; XM_011543101.2.
RefSeq; XP_011541404.1; XM_011543102.2.
RefSeq; XP_016864446.1; XM_017008957.1.
UniGene; Hs.282387; -.
BioGrid; 115867; 15.
DIP; DIP-59079N; -.
IntAct; O15318; 3.
STRING; 9606.ENSP00000382058; -.
iPTMnet; O15318; -.
PhosphoSitePlus; O15318; -.
BioMuta; POLR3G; -.
EPD; O15318; -.
MaxQB; O15318; -.
PaxDb; O15318; -.
PeptideAtlas; O15318; -.
PRIDE; O15318; -.
ProteomicsDB; 48580; -.
DNASU; 10622; -.
Ensembl; ENST00000399107; ENSP00000382058; ENSG00000113356.
Ensembl; ENST00000504930; ENSP00000421637; ENSG00000113356.
GeneID; 10622; -.
KEGG; hsa:10622; -.
UCSC; uc003kjq.3; human.
CTD; 10622; -.
EuPathDB; HostDB:ENSG00000113356.10; -.
GeneCards; POLR3G; -.
HGNC; HGNC:30075; POLR3G.
HPA; CAB010109; -.
HPA; HPA052658; -.
MIM; 617456; gene.
neXtProt; NX_O15318; -.
OpenTargets; ENSG00000113356; -.
PharmGKB; PA134986024; -.
eggNOG; ENOG410IKHU; Eukaryota.
eggNOG; ENOG4112311; LUCA.
GeneTree; ENSGT00390000002422; -.
HOGENOM; HOG000293249; -.
HOVERGEN; HBG054922; -.
InParanoid; O15318; -.
KO; K03024; -.
OMA; EWIPDWR; -.
PhylomeDB; O15318; -.
TreeFam; TF103052; -.
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.
GenomeRNAi; 10622; -.
PRO; PR:O15318; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113356; Expressed in 178 organ(s), highest expression level in dorsal root ganglion.
CleanEx; HS_POLR3G; -.
ExpressionAtlas; O15318; baseline and differential.
Genevisible; O15318; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
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:0008283; P:cell proliferation; IEP:MGI.
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; IDA:UniProtKB.
InterPro; IPR024661; RNA_pol_III_Rpc31.
PANTHER; PTHR15367; PTHR15367; 1.
Pfam; PF11705; RNA_pol_3_Rpc31; 1.
PIRSF; PIRSF000777; RNA_polIII_C31; 1.
1: Evidence at protein level;
Antiviral defense; Complete proteome; Cytoplasm;
DNA-directed RNA polymerase; Immunity; Innate immunity; Nucleus;
Phosphoprotein; Reference proteome; Transcription.
CHAIN 1 223 DNA-directed RNA polymerase III subunit
RPC7.
/FTId=PRO_0000073978.
COMPBIAS 147 196 Glu-rich.
COMPBIAS 175 181 Poly-Asp.
MOD_RES 133 133 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 157 157 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CONFLICT 96 96 K -> Q (in Ref. 1; AAB63676).
{ECO:0000305}.
CONFLICT 146 146 E -> V (in Ref. 1; AAB63676).
{ECO:0000305}.
SEQUENCE 223 AA; 25914 MW; 95E506D527962DD9 CRC64;
MAGNKGRGRA AYTFNIEAVG FSKGEKLPDV VLKPPPLFPD TDYKPVPLKT GEGEEYMLAL
KQELRETMKR MPYFIETPEE RQDIERYSKR YMKVYKEEWI PDWRRLPREM MPRNKCKKAG
PKPKKAKDAG KGTPLTNTED VLKKMEELEK RGDGEKSDEE NEEKEGSKEK SKEGDDDDDD
DAAEQEEYDE EEQEEENDYI NSYFEDGDDF GADSDDNMDE ATY


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EIAAB35792 DNA-directed RNA polymerase II 140 kDa polypeptide,DNA-directed RNA polymerase II subunit B,DNA-directed RNA polymerase II subunit RPB2,Homo sapiens,Human,POLR2B,RNA polymerase II subunit 2,RNA polyme
EIAAB35794 A-152E5.7,DNA-directed RNA polymerase II 33 kDa polypeptide,DNA-directed RNA polymerase II subunit C,DNA-directed RNA polymerase II subunit RPB3,Homo sapiens,Human,POLR2C,RNA polymerase II subunit 3,R
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
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
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
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
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
EIAAB35813 C128,DNA-directed RNA polymerase III 127.6 kDa polypeptide,DNA-directed RNA polymerase III subunit B,DNA-directed RNA polymerase III subunit RPC2,Mouse,Mus musculus,Polr3b,RNA polymerase III subunit C
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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