Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

DNA-directed RNA polymerase III subunit RPC6

Gene

POLR3F

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.2 Publications

GO - Molecular functioni

  • DNA-directed RNA polymerase activity Source: UniProtKB

GO - Biological processi

  • defense response to virus Source: UniProtKB-KW
  • innate immune response Source: UniProtKB-KW
  • positive regulation of innate immune response Source: UniProtKB
  • positive regulation of interferon-beta production Source: UniProtKB
  • positive regulation of type I interferon production Source: Reactome
  • regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • transcription from RNA polymerase III promoter Source: GOC
Complete GO annotation...

Keywords - Biological processi

Antiviral defense, Immunity, Innate immunity, Transcription

Enzyme and pathway databases

ReactomeiR-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA-directed RNA polymerase III subunit RPC6
Short name:
RNA polymerase III subunit C6
Alternative name(s):
DNA-directed RNA polymerase III subunit F
RNA polymerase III 39 kDa subunit
Short name:
RPC39
Gene namesi
Name:POLR3F
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 20

Organism-specific databases

HGNCiHGNC:15763. POLR3F.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • DNA-directed RNA polymerase III complex Source: UniProtKB
  • nucleoplasm Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

DNA-directed RNA polymerase, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33520.

Polymorphism and mutation databases

DMDMi20139728.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources
Chaini2 – 316315DNA-directed RNA polymerase III subunit RPC6PRO_0000073972Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources
Cross-linki7 – 7Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiQ9H1D9.
MaxQBiQ9H1D9.
PaxDbiQ9H1D9.
PeptideAtlasiQ9H1D9.
PRIDEiQ9H1D9.

PTM databases

iPTMnetiQ9H1D9.
PhosphoSiteiQ9H1D9.

Expressioni

Gene expression databases

BgeeiQ9H1D9.
CleanExiHS_POLR3F.
GenevisibleiQ9H1D9. HS.

Organism-specific databases

HPAiHPA049441.
HPA050173.

Interactioni

Subunit structurei

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). Interacts with TBP and TFIIIB90 and GTF3C4.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PNRC1Q127963EBI-710067,EBI-2827376
PRPF4BQ135232EBI-710067,EBI-395940

Protein-protein interaction databases

BioGridi115866. 40 interactions.
DIPiDIP-34646N.
IntActiQ9H1D9. 28 interactions.
MINTiMINT-1377146.
STRINGi9606.ENSP00000366828.

Structurei

Secondary structure

1
316
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi73 – 764Combined sources
Beta strandi79 – 813Combined sources
Helixi92 – 10211Combined sources
Helixi109 – 1157Combined sources
Helixi120 – 13213Combined sources
Beta strandi135 – 1395Combined sources
Beta strandi149 – 1557Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK5NMR-A78-155[»]
2YU3NMR-A61-142[»]
ProteinModelPortaliQ9H1D9.
SMRiQ9H1D9. Positions 11-155.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9H1D9.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG3233. Eukaryota.
COG5111. LUCA.
GeneTreeiENSGT00390000009679.
HOGENOMiHOG000231688.
HOVERGENiHBG006817.
InParanoidiQ9H1D9.
KOiK03025.
OMAiATSHEVW.
OrthoDBiEOG7FV3R3.
PhylomeDBiQ9H1D9.
TreeFamiTF103051.

Family and domain databases

InterProiIPR007832. RNA_pol_Rpc34.
IPR016049. RNA_pol_Rpc34-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12780. PTHR12780. 1 hit.
PfamiPF05158. RNA_pol_Rpc34. 1 hit.
[Graphical view]
PIRSFiPIRSF028763. RNA_pol_Rpc34. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9H1D9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEVKVKVQP PDADPVEIEN RIIELCHQFP HGITDQVIQN EMPHIEAQQR
60 70 80 90 100
AVAINRLLSM GQLDLLRSNT GLLYRIKDSQ NAGKMKGSDN QEKLVYQIIE
110 120 130 140 150
DAGNKGIWSR DIRYKSNLPL TEINKILKNL ESKKLIKAVK SVAASKKKVY
160 170 180 190 200
MLYNLQPDRS VTGGAWYSDQ DFESEFVEVL NQQCFKFLQS KAETARESKQ
210 220 230 240 250
NPMIQRNSSF ASSHEVWKYI CELGISKVEL SMEDIETILN TLIYDGKVEM
260 270 280 290 300
TIIAAKEGTV GSVDGHMKLY RAVNPIIPPT GLVRAPCGLC PVFDDCHEGG
310
EISPSNCIYM TEWLEF
Length:316
Mass (Da):35,684
Last modified:March 1, 2001 - v1
Checksum:i49B1360AF8B365ED
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → G in AAB63677 (PubMed:9171375).Curated
Sequence conflicti44 – 5310HIEAQQRAVA → QYRSPAAGSS in AAB63677 (PubMed:9171375).Curated
Sequence conflicti255 – 29036AKEGT…PCGLC → CKRRHSWQCRWTHETVQGSQ SNHPSHRFGPGHPVDSA (PubMed:9171375).CuratedAdd
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93869 mRNA. Translation: AAB63677.1.
AK290892 mRNA. Translation: BAF83581.1.
AL121893 Genomic DNA. Translation: CAC11110.1.
CH471133 Genomic DNA. Translation: EAX10240.1.
BC012588 mRNA. Translation: AAH12588.1.
CCDSiCCDS13135.1.
RefSeqiNP_001269455.1. NM_001282526.1.
NP_006457.2. NM_006466.3.
UniGeneiHs.472227.

Genome annotation databases

EnsembliENST00000377603; ENSP00000366828; ENSG00000132664.
GeneIDi10621.
KEGGihsa:10621.
UCSCiuc002wqv.5. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U93869 mRNA. Translation: AAB63677.1.
AK290892 mRNA. Translation: BAF83581.1.
AL121893 Genomic DNA. Translation: CAC11110.1.
CH471133 Genomic DNA. Translation: EAX10240.1.
BC012588 mRNA. Translation: AAH12588.1.
CCDSiCCDS13135.1.
RefSeqiNP_001269455.1. NM_001282526.1.
NP_006457.2. NM_006466.3.
UniGeneiHs.472227.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DK5NMR-A78-155[»]
2YU3NMR-A61-142[»]
ProteinModelPortaliQ9H1D9.
SMRiQ9H1D9. Positions 11-155.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115866. 40 interactions.
DIPiDIP-34646N.
IntActiQ9H1D9. 28 interactions.
MINTiMINT-1377146.
STRINGi9606.ENSP00000366828.

PTM databases

iPTMnetiQ9H1D9.
PhosphoSiteiQ9H1D9.

Polymorphism and mutation databases

DMDMi20139728.

Proteomic databases

EPDiQ9H1D9.
MaxQBiQ9H1D9.
PaxDbiQ9H1D9.
PeptideAtlasiQ9H1D9.
PRIDEiQ9H1D9.

Protocols and materials databases

DNASUi10621.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000377603; ENSP00000366828; ENSG00000132664.
GeneIDi10621.
KEGGihsa:10621.
UCSCiuc002wqv.5. human.

Organism-specific databases

CTDi10621.
GeneCardsiPOLR3F.
HGNCiHGNC:15763. POLR3F.
HPAiHPA049441.
HPA050173.
neXtProtiNX_Q9H1D9.
PharmGKBiPA33520.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3233. Eukaryota.
COG5111. LUCA.
GeneTreeiENSGT00390000009679.
HOGENOMiHOG000231688.
HOVERGENiHBG006817.
InParanoidiQ9H1D9.
KOiK03025.
OMAiATSHEVW.
OrthoDBiEOG7FV3R3.
PhylomeDBiQ9H1D9.
TreeFamiTF103051.

Enzyme and pathway databases

ReactomeiR-HSA-1834949. Cytosolic sensors of pathogen-associated DNA.
R-HSA-73780. RNA Polymerase III Chain Elongation.
R-HSA-73980. RNA Polymerase III Transcription Termination.
R-HSA-749476. RNA Polymerase III Abortive And Retractive Initiation.
R-HSA-76061. RNA Polymerase III Transcription Initiation From Type 1 Promoter.
R-HSA-76066. RNA Polymerase III Transcription Initiation From Type 2 Promoter.
R-HSA-76071. RNA Polymerase III Transcription Initiation From Type 3 Promoter.

Miscellaneous databases

EvolutionaryTraceiQ9H1D9.
GeneWikiiPOLR3F.
GenomeRNAii10621.
PROiQ9H1D9.

Gene expression databases

BgeeiQ9H1D9.
CleanExiHS_POLR3F.
GenevisibleiQ9H1D9. HS.

Family and domain databases

InterProiIPR007832. RNA_pol_Rpc34.
IPR016049. RNA_pol_Rpc34-like.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PANTHERiPTHR12780. PTHR12780. 1 hit.
PfamiPF05158. RNA_pol_Rpc34. 1 hit.
[Graphical view]
PIRSFiPIRSF028763. RNA_pol_Rpc34. 1 hit.
SUPFAMiSSF46785. SSF46785. 2 hits.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three human RNA polymerase III-specific subunits form a subcomplex with a selective function in specific transcription initiation."
    Wang Z., Roeder R.G.
    Genes Dev. 11:1315-1326(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    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.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "The DNA sequence and comparative analysis of human chromosome 20."
    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.
    Nature 414:865-871(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  6. "The TFIIIC90 subunit of TFIIIC interacts with multiple components of the RNA polymerase III machinery and contains a histone-specific acetyltransferase activity."
    Hsieh Y.-J., Kundu T.K., Wang Z., Kovelman R., Roeder R.G.
    Mol. Cell. Biol. 19:7697-7704(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GTF3C4.
  7. "Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits."
    Hu P., Wu S., Sun Y., Yuan C.-C., Kobayashi R., Myers M.P., Hernandez N.
    Mol. Cell. Biol. 22:8044-8055(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE RNA POL III COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "SUMO-2 orchestrates chromatin modifiers in response to DNA damage."
    Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C.
    Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-7, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. "Solution structure of winged-helix domain in RNA polymerase III 39kDa polypeptide."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 60-155.
  13. "RNA polymerase III detects cytosolic DNA and induces type I interferons through the RIG-I pathway."
    Chiu Y.-H., Macmillan J.B., Chen Z.J.
    Cell 138:576-591(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  14. "RIG-I-dependent sensing of poly(dA:dT) through the induction of an RNA polymerase III-transcribed RNA intermediate."
    Ablasser A., Bauernfeind F., Hartmann G., Latz E., Fitzgerald K.A., Hornung V.
    Nat. Immunol. 10:1065-1072(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiRPC6_HUMAN
AccessioniPrimary (citable) accession number: Q9H1D9
Secondary accession number(s): A8K4C7, O15319
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: July 6, 2016
This is version 146 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 20
    Human chromosome 20: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.