General Information of Target

Target ID LDTP00608
Target Name DNA-directed RNA polymerase III subunit RPC7 (POLR3G)
Gene Name POLR3G
Gene ID 10622
Synonyms
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
3D Structure
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2D Sequence (FASTA)
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3D Structure (PDB)
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Sequence
MAGNKGRGRAAYTFNIEAVGFSKGEKLPDVVLKPPPLFPDTDYKPVPLKTGEGEEYMLAL
KQELRETMKRMPYFIETPEERQDIERYSKRYMKVYKEEWIPDWRRLPREMMPRNKCKKAG
PKPKKAKDAGKGTPLTNTEDVLKKMEELEKRGDGEKSDEENEEKEGSKEKSKEGDDDDDD
DAAEQEEYDEEEQEEENDYINSYFEDGDDFGADSDDNMDEATY
Target Bioclass
Enzyme
Family
Eukaryotic RPC7 RNA polymerase subunit family
Subcellular location
Nucleus
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 (Pol III) which synthesizes small non-coding RNAs including 5S rRNA, snRNAs, tRNAs and miRNAs from at least 500 distinct genomic loci. Acts as a long tether that bridges POLR3C/RPC3-POLR3F/RPC6-POLR3G/RPC7 heterotrimer and the mobile stalk of Pol III, coordinating the dynamics of Pol III stalk and clamp modules during the transition from apo to elongation state. Pol III exists as two alternative complexes defined by the mutually exclusive incorporation of subunit POLR3G/RPC7alpha or POLR3GL/RPC7beta. POLR3G/RPC7alpha modulates Pol III transcriptome by specifically enhancing the transcription of snaR-A non-coding RNAs. At resting state, occupies the active site of apo Pol III and keeps Pol III in an autoinhibitory mode, preventing non-specific transcription. Pol III plays a key role in sensing and limiting infection by intracellular bacteria and DNA viruses. Acts as a 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.
Uniprot ID
O15318
Ensemble ID
ENST00000504930.5
HGNC ID
HGNC:30075

Probe(s) Labeling This Target

ABPP Probe
Click To Hide/Show 5 Probe Related to This Target
Probe name Structure Binding Site(Ratio) Interaction ID Ref
m-APA
 Probe Info 
15.00  LDD0402  [1]
HHS-475
 Probe Info 
Y56(1.38); Y12(1.78)  LDD0264  [2]
SF
 Probe Info 
N.A.  LDD0028  [3]
AOyne
 Probe Info 
15.00  LDD0443  [4]
HHS-465
 Probe Info 
Y56(0.00); K49(0.00)  LDD2240  [5]

Competitor(s) Related to This Target

Competitor ID Name Cell line Binding Site(Ratio) Interaction ID Ref
 LDCM0156  Aniline NCI-H1299 13.04  LDD0403  [1]
 LDCM0116  HHS-0101 DM93 Y56(1.38); Y12(1.78)  LDD0264  [2]
 LDCM0117  HHS-0201 DM93 Y12(1.06); Y43(1.12); Y56(2.75)  LDD0265  [2]
 LDCM0118  HHS-0301 DM93 Y43(5.77); Y56(5.98)  LDD0266  [2]
 LDCM0119  HHS-0401 DM93 Y12(0.66); Y56(2.02); Y43(11.86)  LDD0267  [2]
 LDCM0120  HHS-0701 DM93 Y12(0.07); Y56(3.26); Y43(3.35)  LDD0268  [2]

The Interaction Atlas With This Target

The Protein(s) Related To This Target

Enzyme
Click To Hide/Show 2 Protein(s) Interacting with This Target
Protein name Family Uniprot ID
DNA-directed RNA polymerase III subunit RPC3 (POLR3C) Eukaryotic RPC3/POLR3C RNA polymerase subunit family Q9BUI4
DNA-directed RNA polymerase III subunit RPC6 (POLR3F) Eukaryotic RPC34/RPC39 RNA polymerase subunit family Q9H1D9

References

1 Quantitative and Site-Specific Chemoproteomic Profiling of Targets of Acrolein. Chem Res Toxicol. 2019 Mar 18;32(3):467-473. doi: 10.1021/acs.chemrestox.8b00343. Epub 2019 Jan 15.
2 Discovery of a Cell-Active SuTEx Ligand of Prostaglandin Reductase 2. Chembiochem. 2021 Jun 15;22(12):2134-2139. doi: 10.1002/cbic.202000879. Epub 2021 Apr 29.
3 Solid Phase Synthesis of Fluorosulfate Containing Macrocycles for Chemoproteomic Workflows. bioRxiv [Preprint]. 2023 Feb 18:2023.02.17.529022. doi: 10.1101/2023.02.17.529022.
Mass spectrometry data entry: PXD039931
4 Chemoproteomic profiling of targets of lipid-derived electrophiles by bioorthogonal aminooxy probe. Redox Biol. 2017 Aug;12:712-718. doi: 10.1016/j.redox.2017.04.001. Epub 2017 Apr 5.
5 Global profiling identifies a stress-responsive tyrosine site on EDC3 regulating biomolecular condensate formation. Cell Chem Biol. 2022 Dec 15;29(12):1709-1720.e7. doi: 10.1016/j.chembiol.2022.11.008. Epub 2022 Dec 6.
Mass spectrometry data entry: PXD038010